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Conserved domains on  [gi|1194009329|gb|OTY11540|]
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methyltransferase [Bacillus thuringiensis serovar muju]

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

CATH:  2.20.25.110
EC:  2.1.-.-|2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0008168|GO:1904047
PubMed:  12504684|12826405

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.
 88-182 3.56e-19

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 80.30  E-value: 3.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  88 ILDFGCGWGRIIRFFFKDVRDEnLLGIDVDPAMINICNEtlgrgiyKTANPQPPVEFI---------SDNSLDIIFAYSV 158
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR-VTGVDLSPEMLERARE-------RAAEAGLNVEFVqgdaedlpfPDGSFDLVVSSGV 72

                          90       100
                  ....*....|....*....|....
gi 1194009329 159 FSHLSEETAEHWIKEFSRILRPGG 182
Cdd:pfam13649  73 LHHLPDPDLEAALREIARVLKPGG 96
YhdJ super family cl43301
DNA modification methylase [Replication, recombination and repair];
170-214 5.88e-03

DNA modification methylase [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG0863:

Pssm-ID: 440623  Cd Length: 236  Bit Score: 37.21  E-value: 5.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1194009329 170 WIKEFSRILRPGG---IFIATTQARYFLDYCQQ--FQEHPEFIqtgWHKT 214
Cdd:COG0863    57 WLAECYRVLKPGGslyVNIGDRYISRLIAALRDagFKLRNEII---WRKP 103
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 88-182 3.56e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 80.30  E-value: 3.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  88 ILDFGCGWGRIIRFFFKDVRDEnLLGIDVDPAMINICNEtlgrgiyKTANPQPPVEFI---------SDNSLDIIFAYSV 158
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR-VTGVDLSPEMLERARE-------RAAEAGLNVEFVqgdaedlpfPDGSFDLVVSSGV 72

                          90       100
                  ....*....|....*....|....
gi 1194009329 159 FSHLSEETAEHWIKEFSRILRPGG 182
Cdd:pfam13649  73 LHHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 80-188 1.72e-16

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: 74.65  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  80 VPLNKERKILDFGCGWGRIIRFFFKdvRDENLLGIDVDPAMINICNEtlgrgiyKTANPQPPVEFI---------SDNSL 150
Cdd:COG2226    18 LGLRPGARVLDLGCGTGRLALALAE--RGARVTGVDISPEMLELARE-------RAAEAGLNVEFVvgdaedlpfPDGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1194009329 151 DIIFAYSVFSHLSEetAEHWIKEFSRILRPGGIFIATT 188
Cdd:COG2226    89 DLVISSFVLHHLPD--PERALAEIARVLKPGGRLVVVD 124
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 87-187 3.86e-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: 55.90  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  87 KILDFGCGWGRIIRFFFKDVrDENLLGIDVDPAMINICNEtlgrgiYKTANPQPPVEFI----------SDNSLDIIFAY 156
Cdd:cd02440     1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARK------AAAALLADNVEVLkgdaeelppeADESFDVIISD 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1194009329 157 SVFSHLsEETAEHWIKEFSRILRPGGIFIAT 187
Cdd:cd02440    74 PPLHHL-VEDLARFLEEARRLLKPGGVLVLT 103
PRK08317 PRK08317
hypothetical protein; Provisional
 87-182 7.22e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.16  E-value: 7.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  87 KILDFGCGWGRIIRFFFKDVRDEN-LLGIDVDPAMINICNEtlgrgiyKTANPQPPVEFIS---------DNSLDIIFAY 156
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRVGPEGrVVGIDRSEAMLALAKE-------RAAGLGPNVEFVRgdadglpfpDGSFDAVRSD 94

                          90       100
                  ....*....|....*....|....*.
gi 1194009329 157 SVFSHLseETAEHWIKEFSRILRPGG 182
Cdd:PRK08317   95 RVLQHL--EDPARALAEIARVLRPGG 118
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
 83-230 1.95e-06

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 47.36  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  83 NKERKILDFGCGWGRIIRFFFKDVRDENLLGIDVDPAMINICNETLGRGIYKTAN------PQPPVEFISDNSLDIIFAY 156
Cdd:TIGR00091  15 NKAPLHLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKNLHvlcgdaNELLDKFFPDGSLSKVFLN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329 157 svFS--------HLSEETAEHWIKEFSRILRPGG-IFIATTQARYFLDYCQQFQEHPEFIQTgwHKTlsqafPDIN---- 223
Cdd:TIGR00091  95 --FPdpwpkkrhNKRRITQPHFLKEYANVLKKGGvIHFKTDNEPLFEDMLKVLSENDLFENT--SKS-----TDLNnspl 165

                         170
                  ....*....|
gi 1194009329 224 ---RAISDYE 230
Cdd:TIGR00091 166 srpRNMTEYE 175
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
170-214 5.88e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 37.21  E-value: 5.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1194009329 170 WIKEFSRILRPGG---IFIATTQARYFLDYCQQ--FQEHPEFIqtgWHKT 214
Cdd:COG0863    57 WLAECYRVLKPGGslyVNIGDRYISRLIAALRDagFKLRNEII---WRKP 103
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 88-182 3.56e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 80.30  E-value: 3.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  88 ILDFGCGWGRIIRFFFKDVRDEnLLGIDVDPAMINICNEtlgrgiyKTANPQPPVEFI---------SDNSLDIIFAYSV 158
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR-VTGVDLSPEMLERARE-------RAAEAGLNVEFVqgdaedlpfPDGSFDLVVSSGV 72

                          90       100
                  ....*....|....*....|....
gi 1194009329 159 FSHLSEETAEHWIKEFSRILRPGG 182
Cdd:pfam13649  73 LHHLPDPDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 80-188 1.72e-16

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: 74.65  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  80 VPLNKERKILDFGCGWGRIIRFFFKdvRDENLLGIDVDPAMINICNEtlgrgiyKTANPQPPVEFI---------SDNSL 150
Cdd:COG2226    18 LGLRPGARVLDLGCGTGRLALALAE--RGARVTGVDISPEMLELARE-------RAAEAGLNVEFVvgdaedlpfPDGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1194009329 151 DIIFAYSVFSHLSEetAEHWIKEFSRILRPGGIFIATT 188
Cdd:COG2226    89 DLVISSFVLHHLPD--PERALAEIARVLKPGGRLVVVD 124
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 89-184 3.74e-16

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 72.40  E-value: 3.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  89 LDFGCGWGRIIRFFFKDVRDENLLGIDVDPAMINICNETL-GRGIYKTANPQPPVEFISD---NSLDIIFAYSVFSHLse 164
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLaALGLLNAVRVELFQLDLGEldpGSFDVVVASNVLHHL-- 78

                          90       100
                  ....*....|....*....|
gi 1194009329 165 ETAEHWIKEFSRILRPGGIF 184
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
55-208 7.93e-15

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 70.80  E-value: 7.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  55 ASYEHALYEAyLFYRHVKTYAQNL--GVPLNKERKILDFGCGWGRIIRFFFKDVRDenLLGIDVDPAMINICNEtlgRGI 132
Cdd:COG4976    16 DSYDAALVED-LGYEAPALLAEELlaRLPPGPFGRVLDLGCGTGLLGEALRPRGYR--LTGVDLSEEMLAKARE---KGV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329 133 YktanpqppVEFI---------SDNSLDIIFAYSVFSHLsEETAEHwIKEFSRILRPGGIFIATTQAryfLDYCQQFQEH 203
Cdd:COG4976    90 Y--------DRLLvadladlaePDGRFDLIVAADVLTYL-GDLAAV-FAGVARALKPGGLFIFSVED---ADGSGRYAHS 156


                  ....*
gi 1194009329 204 PEFIQ 208
Cdd:COG4976   157 LDYVR 161
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 82-188 1.46e-14

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: 68.89  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  82 LNKERKILDFGCGWGRIIRFFFKdvRDENLLGIDVDPAMINICNETLgrgiyktanPQPPVEFI---------SDNSLDI 152
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALAR--RGADVTGVDISPEALEIARERA---------AELNVDFVqgdledlplEDGSFDL 90

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1194009329 153 IFAYSVFSHLSEetAEHWIKEFSRILRPGGIFIATT 188
Cdd:COG2227    91 VICSEVLEHLPD--PAALLRELARLLKPGGLLLLST 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 89-185 2.54e-14

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 67.30  E-value: 2.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  89 LDFGCGWGRIIRFFFKDVRdeNLLGIDVDPAMINICnetlgrgiyKTANPQPPVEFI---------SDNSLDIIFAYSVF 159
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELA---------REKAPREGLTFVvgdaedlpfPDNSFDLVLSSEVL 69

                          90       100
                  ....*....|....*....|....*..
gi 1194009329 160 SHLSE-ETAehwIKEFSRILRPGGIFI 185
Cdd:pfam08241  70 HHVEDpERA---LREIARVLKPGGILI 93
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 82-187 3.92e-14

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 69.56  E-value: 3.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  82 LNKERKILDFGCGWGRIIRFFFKDVRDeNLLGIDVDPAMINICNETLGRgiYKTANpqppVEFISDN----------SLD 151
Cdd:COG0500    24 LPKGGRVLDLGCGTGRNLLALAARFGG-RVIGIDLSPEAIALARARAAK--AGLGN----VEFLVADlaeldplpaeSFD 96

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1194009329 152 IIFAYSVFSHLSEETAEHWIKEFSRILRPGGIFIAT 187
Cdd:COG0500    97 LVVAFGVLHHLPPEEREALLRELARALKPGGVLLLS 132
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
86-188 1.13e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 62.92  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  86 RKILDFGCGWGRIIRFFFKDVRDENLLGIDVDPAMINICNETLgrgiyktanpqPPVEFI--------SDNSLDIIFAYS 157
Cdd:COG4106     3 RRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL-----------PNVRFVvadlrdldPPEPFDLVVSNA 71

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1194009329 158 VFSHLSE--ETAEHWIkefsRILRPGGIFIATT 188
Cdd:COG4106    72 ALHWLPDhaALLARLA----AALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 87-187 3.86e-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: 55.90  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  87 KILDFGCGWGRIIRFFFKDVrDENLLGIDVDPAMINICNEtlgrgiYKTANPQPPVEFI----------SDNSLDIIFAY 156
Cdd:cd02440     1 RVLDLGCGTGALALALASGP-GARVTGVDISPVALELARK------AAAALLADNVEVLkgdaeelppeADESFDVIISD 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1194009329 157 SVFSHLsEETAEHWIKEFSRILRPGGIFIAT 187
Cdd:cd02440    74 PPLHHL-VEDLARFLEEARRLLKPGGVLVLT 103
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
89-188 8.51e-10

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 56.41  E-value: 8.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  89 LDFGCGwgriirfffkDVRDENLLGIDVDPAMIN--ICNETlgrgiyktaNPQPpvefISDNSLDIIFAYSVFSHLSEET 166
Cdd:COG4627     7 LNIGCG----------PKRLPGWLNVDIVPAPGVdiVGDLT---------DPLP----FPDNSVDAIYSSHVLEHLDYEE 63

                          90       100
                  ....*....|....*....|..
gi 1194009329 167 AEHWIKEFSRILRPGGIFIATT 188
Cdd:COG4627    64 APLALKECYRVLKPGGILRIVV 85
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 81-188 4.77e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 54.17  E-value: 4.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  81 PLNKERKILDFGCGWGRIIRFFFKDvRDENLLGIDVDPAMINICNETLgrgiyKTANPQPPVEFI--------SDNSLDI 152
Cdd:COG2230    48 GLKPGMRVLDIGCGWGGLALYLARR-YGVRVTGVTLSPEQLEYARERA-----AEAGLADRVEVRladyrdlpADGQFDA 121

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1194009329 153 IFAYSVFSHLSEETAEHWIKEFSRILRPGGIFIATT 188
Cdd:COG2230   122 IVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
PRK08317 PRK08317
hypothetical protein; Provisional
 87-182 7.22e-07

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.16  E-value: 7.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  87 KILDFGCGWGRIIRFFFKDVRDEN-LLGIDVDPAMINICNEtlgrgiyKTANPQPPVEFIS---------DNSLDIIFAY 156
Cdd:PRK08317   22 RVLDVGCGPGNDARELARRVGPEGrVVGIDRSEAMLALAKE-------RAAGLGPNVEFVRgdadglpfpDGSFDAVRSD 94

                          90       100
                  ....*....|....*....|....*.
gi 1194009329 157 SVFSHLseETAEHWIKEFSRILRPGG 182
Cdd:PRK08317   95 RVLQHL--EDPARALAEIARVLRPGG 118
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
 83-230 1.95e-06

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 47.36  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  83 NKERKILDFGCGWGRIIRFFFKDVRDENLLGIDVDPAMINICNETLGRGIYKTAN------PQPPVEFISDNSLDIIFAY 156
Cdd:TIGR00091  15 NKAPLHLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKNLHvlcgdaNELLDKFFPDGSLSKVFLN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329 157 svFS--------HLSEETAEHWIKEFSRILRPGG-IFIATTQARYFLDYCQQFQEHPEFIQTgwHKTlsqafPDIN---- 223
Cdd:TIGR00091  95 --FPdpwpkkrhNKRRITQPHFLKEYANVLKKGGvIHFKTDNEPLFEDMLKVLSENDLFENT--SKS-----TDLNnspl 165

                         170
                  ....*....|
gi 1194009329 224 ---RAISDYE 230
Cdd:TIGR00091 166 srpRNMTEYE 175
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 82-188 3.99e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 45.87  E-value: 3.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  82 LNKERKILDFGCGWGRIIRFFFKDVRDE-NLLGIDVDPAMINICNETLGRGIYKTanpqppVEFI-----------SDNS 149
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNaEVVGIDISEEAIEKARENAQKLGFDN------VEFEqgdieelpellEDDK 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1194009329 150 LDIIFAYSVFSHLSEETAEhwIKEFSRILRPGGIFIATT 188
Cdd:pfam13847  75 FDVVISNCVLNHIPDPDKV--LQEILRVLKPGGRLIISD 111
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 87-188 3.97e-05

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 43.81  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  87 KILDFGCGWGRIIRFFFKDVRDENLLGIDVDPAMINICNETLGrgiyktanpqPPVEFI---------SDNSLDIIFAYS 157
Cdd:TIGR02072  37 SVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS----------ENVQFIcgdaeklplEDSSFDLIVSNL 106

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1194009329 158 VFshlseetaeHW-------IKEFSRILRPGGIFIATT 188
Cdd:TIGR02072 107 AL---------QWcddlsqaLSELARVLKPGGLLAFST 135
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 87-184 7.37e-05

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 43.22  E-value: 7.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  87 KILDFGCGWGRIIRFFFKDVRD-ENLLGIDVDPAMINIcnetlGRGIYKTANPQPPVEFI---------SDNSLDII-FA 155
Cdd:PRK00216   54 KVLDLACGTGDLAIALAKAVGKtGEVVGLDFSEGMLAV-----GREKLRDLGLSGNVEFVqgdaealpfPDNSFDAVtIA 128

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1194009329 156 YSV--FSHLseETAehwIKEFSRILRPGGIF 184
Cdd:PRK00216  129 FGLrnVPDI--DKA---LREMYRVLKPGGRL 154
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 80-183 1.86e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 42.24  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  80 VPLNKERKILDFGCGWGRIIRFFFKDVRDENLLGIDVDPAMINICNETLgrgiyktanpqPPVEFISDN--------SLD 151
Cdd:PRK01683   27 VPLENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEARSRL-----------PDCQFVEADiaswqppqALD 95

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1194009329 152 IIFAYSVFSHLseetAEHwIKEFSRI---LRPGGI 183
Cdd:PRK01683   96 LIFANASLQWL----PDH-LELFPRLvslLAPGGV 125
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 80-196 3.63e-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: 40.56  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  80 VPLNKERKILDFGCGWGRIIRFFFKDVRDENLLGIDVDPAMINICNETLgrgiykTANPQPPVEFISDNSLDIIFAYS-- 157
Cdd:COG2813    45 LPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANA------AANGLENVEVLWSDGLSGVPDGSfd 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1194009329 158 -VFS--------HLSEETAEHWIKEFSRILRPGGIFIATTQAryFLDY 196
Cdd:COG2813   119 lILSnppfhagrAVDKEVAHALIADAARHLRPGGELWLVANR--HLPY 164
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 86-196 6.71e-04

mRNA capping enzyme; This family of enzymes are related to pfam03919.


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 40.49  E-value: 6.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  86 RKILDFGCGWGRIIRFFFKdVRDENLLGIDVDPAMINICNE--TLGRGIYKTANPQPPVEFISDNS-------------- 149
Cdd:pfam03291  65 RKVLDLGCGKGGDLEKWFK-GGISQLIGTDIAEVSIEQCREryNKLRSGNKSKYYKFDAEFITGDCfvsslrevfedpfg 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1194009329 150 -LDII---FAYSvFSHLSEETAEHWIKEFSRILRPGGIFIATTQARYFLDY 196
Cdd:pfam03291 144 kFDIVscqFAIH-YSFESEEKARTMLRNVAELLASGGVFIGTTPDSDFISA 193
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 88-230 1.39e-03

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 38.81  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  88 ILDFGCGWGRIIRFFFKDVRDENLLGIDVDPAMINICNETLGRGIYKT-----ANPQPPV-EFISDNSLDIIFAYsvFS- 160
Cdd:pfam02390   5 FLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQNlrilcGNALDVLpNYFPPGSLQKIFIN--FPd 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329 161 -------HLSEETAEHWIKEFSRILRPGG-IFIATTQARYFLDYCQQFQEHPEFIQTgwHKTLSQAFPDIN--RAISDYE 230
Cdd:pfam02390  83 pwpkkrhHKRRLLQPEFLKEYARVLKPGGvLHLATDVEEYAEEMLKHLAEHPLFERL--DLENDLAPGPLSplRPATEYE 160
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
86-235 1.49e-03

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 38.66  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  86 RKILDFGCGWGRIIRFFFKDVRDENLLGIDVDPAMINICNETLGrgIYKTANPQPPVEFI----------SDNSLDIIF- 154
Cdd:COG0421    39 KRVLIIGGGDGGLARELLKHPPVERVDVVEIDPEVVELAREYFP--LLAPAFDDPRLRVVigdgraflreAEESYDVIIv 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329 155 --------AYSVFShlseetaehwiKEF----SRILRPGGIFIATTQARYFldycqqfqeHPEFIQTgWHKTLSQAFPD- 221
Cdd:COG0421   117 dltdpvgpAEGLFT-----------REFyedcRRALKPGGVLVVNLGSPFY---------GLDLLRR-VLATLREVFPHv 175

                         170
                  ....*....|....*.
gi 1194009329 222 --INRAISDYESGNFV 235
Cdd:COG0421   176 vlYAAPVPTYGGGNVF 191
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 86-206 1.52e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 39.73  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  86 RKILDFGCGWGRiIRFFFKDVRDENLLGIDVDPAMINIcneTLGRGIYKTANpqppVEF---------ISDNSLDIIFAY 156
Cdd:PLN02336  268 QKVLDVGCGIGG-GDFYMAENFDVHVVGIDLSVNMISF---ALERAIGRKCS----VEFevadctkktYPDNSFDVIYSR 339

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1194009329 157 SVFSHLSEETAehWIKEFSRILRPGGIFIATtqaryflDYCQQFQE-HPEF 206
Cdd:PLN02336  340 DTILHIQDKPA--LFRSFFKWLKPGGKVLIS-------DYCRSPGTpSPEF 381
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 80-197 2.38e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 38.80  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  80 VPLNKERKILDFGCGWGRIIRFFfKDVRDENLLGIDVDPAMINICNETLG--RGIYKTANPQPPVEFiSDNSLDIIFAYS 157
Cdd:PTZ00098   48 IELNENSKVLDIGSGLGGGCKYI-NEKYGAHVHGVDICEKMVNIAKLRNSdkNKIEFEANDILKKDF-PENTFDMIYSRD 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1194009329 158 VFSHLSEETAEHWIKEFSRILRPGGIFIATtqaryflDYC 197
Cdd:PTZ00098  126 AILHLSYADKKKLFEKCYKWLKPNGILLIT-------DYC 158
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 81-196 3.63e-03

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: 37.57  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  81 PLNKERKILDFGCGWGRIIRFFFKDVRDENLLGIDVDPAMINICNETLgrgiykTANPQPPVEFI--------SDNSLDI 152
Cdd:pfam05175  28 PKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENL------AANGLENGEVVasdvysgvEDGKFDL 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1194009329 153 IFAYSVF---SHLSEETAEHWIKEFSRILRPGGIFIATTQAryFLDY 196
Cdd:pfam05175 102 IISNPPFhagLATTYNVAQRFIADAKRHLRPGGELWIVANR--FLGY 146
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 62-193 4.77e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 37.02  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194009329  62 YEAYLFYRHVKTYAQNLGvPLNKERKILDFGCG---WGRIIRFFFKDVrdenlLGIDVDPAMINICNETLGRGIYKTANP 138
Cdd:pfam13489   1 YAHQRERLLADLLLRLLP-KLPSPGRVLDFGCGtgiFLRLLRAQGFSV-----TGVDPSPIAIERALLNVRFDQFDEQEA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1194009329 139 QPPvefisDNSLDIIFAYSVFSHLSEETAehWIKEFSRILRPGGIFIATTQARYF 193
Cdd:pfam13489  75 AVP-----AGKFDVIVAREVLEHVPDPPA--LLRQIAALLKPGGLLLLSTPLASD 122
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
170-214 5.88e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 37.21  E-value: 5.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1194009329 170 WIKEFSRILRPGG---IFIATTQARYFLDYCQQ--FQEHPEFIqtgWHKT 214
Cdd:COG0863    57 WLAECYRVLKPGGslyVNIGDRYISRLIAALRDagFKLRNEII---WRKP 103
 
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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