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Conserved domains on  [gi|1004371618|gb|AMO70681|]
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methyltransferase type 11 [Sphingorhabdus sp. M41]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 44-174 1.48e-24

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: 96.22  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  44 DALLARADYQDGEMVIDLGCGGGATTIAIATAvapSGKVMGVDISPDLIAASRKRAMKSGAtNIDFTCADASTVKLPEAP 123
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFPDGS 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1004371618 124 YDRLFSRFGSMFFEDPVSAFSNLHALVRKGGRIDLAVWGPPrENLWMMEMM 174
Cdd:COG2226    88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPP-DLAELEELL 137
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 44-174 1.48e-24

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: 96.22  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  44 DALLARADYQDGEMVIDLGCGGGATTIAIATAvapSGKVMGVDISPDLIAASRKRAMKSGAtNIDFTCADASTVKLPEAP 123
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFPDGS 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1004371618 124 YDRLFSRFGSMFFEDPVSAFSNLHALVRKGGRIDLAVWGPPrENLWMMEMM 174
Cdd:COG2226    88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPP-DLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 58-154 1.14e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 81.46  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  58 VIDLGCGGGATTIAIATAVapSGKVMGVDISPDLIAASRKRAMKSGAtNIDFTCADASTVKLPEAPYDRLFSRFGSMFFE 137
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG--GARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLP 77

                          90
                  ....*....|....*....
gi 1004371618 138 DP--VSAFSNLHALVRKGG 154
Cdd:pfam13649  78 DPdlEAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 39-216 4.94e-17

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 78.44  E-value: 4.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  39 IAPIGDALLARADYQDGEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRKRAmKSGATNIDFTCADASTVK 118
Cdd:PRK08317    4 FRRYRARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERA-AGLGPNVEFVRGDADGLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618 119 LPEAPYDRLFSRFGSMFFEDPVSAFSNLHALVRKGGRI-------DLAVWGPPRENLwMMEMMGVVRNHVEiPPAVPRap 191
Cdd:PRK08317   83 FPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVvvldtdwDTLVWHSGDRAL-MRKILNFWSDHFA-DPWLGR-- 158

                         170       180
                  ....*....|....*....|....*
gi 1004371618 192 gpfafedleYLGEILDSSGFTDVDI 216
Cdd:PRK08317  159 ---------RLPGLFREAGLTDIEV 174
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 58-156 1.34e-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: 65.53  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  58 VIDLGCGGGATTIAIAtaVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADAST-VKLPEAPYDRLFSRF-GSMF 135
Cdd:cd02440     2 VLDLGCGTGALALALA--SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEElPPEADESFDVIISDPpLHHL 79

                          90       100
                  ....*....|....*....|.
gi 1004371618 136 FEDPVSAFSNLHALVRKGGRI 156
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVL 100
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 58-106 7.95e-04

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: 40.41  E-value: 7.95e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1004371618  58 VIDLGCGGGATTIAIATAVaPSGKVMGVDISPDLIAASRKRAMKSGATN 106
Cdd:TIGR00536 118 ILDLGTGSGCIALALAYEF-PNAEVIAVDISPDALAVAEENAEKNQLEH 165
rADc smart00650
Ribosomal RNA adenine dimethylases;
44-129 3.71e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.49  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618   44 DALLARADYQDGEMVIDLGCGGGATTIAIATAVApsgKVMGVDISPDLIAASRKRAmkSGATNIDFTCADASTVKLPEAP 123
Cdd:smart00650   3 DKIVRAANLRPGDTVLEIGPGKGALTEELLERAK---RVTAIEIDPRLAPRLREKF--AAADNLTVIHGDALKFDLPKLQ 77


                   ....*.
gi 1004371618  124 YDRLFS 129
Cdd:smart00650  78 PYKVVG 83
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 44-174 1.48e-24

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: 96.22  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  44 DALLARADYQDGEMVIDLGCGGGATTIAIATAvapSGKVMGVDISPDLIAASRKRAMKSGAtNIDFTCADASTVKLPEAP 123
Cdd:COG2226    12 EALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFPDGS 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1004371618 124 YDRLFSRFGSMFFEDPVSAFSNLHALVRKGGRIDLAVWGPPrENLWMMEMM 174
Cdd:COG2226    88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPP-DLAELEELL 137
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 58-154 1.14e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 81.46  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  58 VIDLGCGGGATTIAIATAVapSGKVMGVDISPDLIAASRKRAMKSGAtNIDFTCADASTVKLPEAPYDRLFSRFGSMFFE 137
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG--GARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLP 77

                          90
                  ....*....|....*....
gi 1004371618 138 DP--VSAFSNLHALVRKGG 154
Cdd:pfam13649  78 DPdlEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
58-161 3.71e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 74.86  E-value: 3.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  58 VIDLGCGGGATTIAIATAVaPSGKVMGVDISPDLIAASRKRAmksgaTNIDFTCADASTVKLPEaPYDRLFSRFGSMFFE 137
Cdd:COG4106     5 VLDLGCGTGRLTALLAERF-PGARVTGVDLSPEMLARARARL-----PNVRFVVADLRDLDPPE-PFDLVVSNAALHWLP 77

                          90       100
                  ....*....|....*....|....
gi 1004371618 138 DPVSAFSNLHALVRKGGRidLAVW 161
Cdd:COG4106    78 DHAALLARLAAALAPGGV--LAVQ 99
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 58-156 4.30e-17

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: 75.82  E-value: 4.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  58 VIDLGCGGGATTIAIATAVApsgKVMGVDISPDLIAASRKRAmksGATNIDFTCADASTVKLPEAPYDRLFSRFGSMFFE 137
Cdd:COG2227    28 VLDVGCGTGRLALALARRGA---DVTGVDISPEALEIARERA---AELNVDFVQGDLEDLPLEDGSFDLVICSEVLEHLP 101

                          90
                  ....*....|....*....
gi 1004371618 138 DPVSAFSNLHALVRKGGRI 156
Cdd:COG2227   102 DPAALLRELARLLKPGGLL 120
PRK08317 PRK08317
hypothetical protein; Provisional
 39-216 4.94e-17

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 78.44  E-value: 4.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  39 IAPIGDALLARADYQDGEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRKRAmKSGATNIDFTCADASTVK 118
Cdd:PRK08317    4 FRRYRARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERA-AGLGPNVEFVRGDADGLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618 119 LPEAPYDRLFSRFGSMFFEDPVSAFSNLHALVRKGGRI-------DLAVWGPPRENLwMMEMMGVVRNHVEiPPAVPRap 191
Cdd:PRK08317   83 FPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVvvldtdwDTLVWHSGDRAL-MRKILNFWSDHFA-DPWLGR-- 158

                         170       180
                  ....*....|....*....|....*
gi 1004371618 192 gpfafedleYLGEILDSSGFTDVDI 216
Cdd:PRK08317  159 ---------RLPGLFREAGLTDIEV 174
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 33-168 2.12e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 73.03  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  33 SLFEEMIAPIGDALLARADY-QDGEMVIDLGCGGGATTIAIATAvaPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTC 111
Cdd:COG0500     4 SYYSDELLPGLAALLALLERlPKGGRVLDLGCGTGRNLLALAAR--FGGRVIGIDLSPEAIALARARAAKAGLGNVEFLV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004371618 112 ADAS-TVKLPEAPYDRLFSrFGSMFFEDP---VSAFSNLHALVRKGGRIDLAVWGPPRENL 168
Cdd:COG0500    82 ADLAeLDPLPAESFDLVVA-FGVLHHLPPeerEALLRELARALKPGGVLLLSASDAAAALS 141
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 59-156 4.78e-15

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 69.23  E-value: 4.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  59 IDLGCGGGATTIAIATAVApsgKVMGVDISPDLIAASRKRAMKSGatnIDFTCADASTVKLPEAPYDRLFSRFGSMFFED 138
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA---RVTGVDISPEMLELAREKAPREG---LTFVVGDAEDLPFPDNSFDLVLSSEVLHHVED 74

                          90
                  ....*....|....*...
gi 1004371618 139 PVSAFSNLHALVRKGGRI 156
Cdd:pfam08241  75 PERALREIARVLKPGGIL 92
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 54-156 7.82e-15

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 70.14  E-value: 7.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  54 DGEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADAStvKLPEA----PYDRLFS 129
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIE--ELPELleddKFDVVIS 80

                          90       100
                  ....*....|....*....|....*..
gi 1004371618 130 RFGSMFFEDPVSAFSNLHALVRKGGRI 156
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRL 107
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 58-156 1.34e-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: 65.53  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  58 VIDLGCGGGATTIAIAtaVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADAST-VKLPEAPYDRLFSRF-GSMF 135
Cdd:cd02440     2 VLDLGCGTGALALALA--SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEElPPEADESFDVIISDPpLHHL 79

                          90       100
                  ....*....|....*....|.
gi 1004371618 136 FEDPVSAFSNLHALVRKGGRI 156
Cdd:cd02440    80 VEDLARFLEEARRLLKPGGVL 100
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
55-156 4.66e-13

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 67.08  E-value: 4.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  55 GEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADASTVKLPEAPYDRLFSRFGSM 134
Cdd:pfam01209  43 GNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVTISFGLR 122

                          90       100
                  ....*....|....*....|..
gi 1004371618 135 FFEDPVSAFSNLHALVRKGGRI 156
Cdd:pfam01209 123 NFPDYLKVLKEAFRVLKPGGRV 144
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
37-156 1.08e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 65.02  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  37 EMIAPIGDALLARADYQDGEMVIDLGCGGGATTIAIATAVapsGKVMGVDISPDLIAASRKRamksgATNIDFTCADAST 116
Cdd:COG4976    29 EAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG---YRLTGVDLSEEMLAKAREK-----GVYDRLLVADLAD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1004371618 117 VKLPEAPYDRLFSrFGSM-FFEDPVSAFSNLHALVRKGGRI 156
Cdd:COG4976   101 LAEPDGRFDLIVA-ADVLtYLGDLAAVFAGVARALKPGGLF 140
arsM PRK11873
arsenite methyltransferase;
47-109 3.02e-12

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 65.35  E-value: 3.02e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004371618  47 LARADYQDGEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDF 109
Cdd:PRK11873   70 TALAELKPGETVLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTNVEF 132
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 44-156 3.84e-12

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 63.02  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  44 DALLARADYQDGEMVIDLGCGGGATTIAIATAVapSGKVMGVDISPDLIAASRKRAMKSGATN-IDFTCADASTVKLPEa 122
Cdd:COG2230    41 DLILRKLGLKPGMRVLDIGCGWGGLALYLARRY--GVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDLPADG- 117

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1004371618 123 PYDRLFSrFGsMFF----EDPVSAFSNLHALVRKGGRI 156
Cdd:COG2230   118 QFDAIVS-IG-MFEhvgpENYPAYFAKVARLLKPGGRL 153
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 59-156 1.35e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 59.69  E-value: 1.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  59 IDLGCGGGATTIAIATAvAPSGKVMGVDISPDLIAASRKRAMKSG---ATNIDFTCADAStvKLPEAPYDRLFSRFGSMF 135
Cdd:pfam08242   1 LEIGCGTGTLLRALLEA-LPGLEYTGLDISPAALEAARERLAALGllnAVRVELFQLDLG--ELDPGSFDVVVASNVLHH 77

                          90       100
                  ....*....|....*....|.
gi 1004371618 136 FEDPVSAFSNLHALVRKGGRI 156
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
40-123 3.08e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 55.68  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  40 APIGDALLARADYQ---DGEMVIDLGCGGGatTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSGAtNIDFTCADAST 116
Cdd:COG2263    28 AELAAELLHLAYLRgdiEGKTVLDLGCGTG--MLAIGAALLGAKKVVGVDIDPEALEIARENAERLGV-RVDFIRADVTR 104


                  ....*..
gi 1004371618 117 VKLPEAP 123
Cdd:COG2263   105 IPLGGSV 111
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 47-156 3.33e-09

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 56.32  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  47 LARADYQDGEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRK---RAMKSGatNIDFTCADASTvKLPEAP 123
Cdd:COG2519    84 IARLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKnleRFGLPD--NVELKLGDIRE-GIDEGD 160

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1004371618 124 YDRLFsrfgsMFFEDPVSAFSNLHALVRKGGRI 156
Cdd:COG2519   161 VDAVF-----LDMPDPWEALEAVAKALKPGGVL 188
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
55-128 3.55e-09

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 55.45  E-value: 3.55e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1004371618  55 GEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADASTVKLPEAPYDRLF 128
Cdd:pfam01135  74 GMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLENVIVVVGDGRQGWPEFAPYDAIH 147
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 44-155 7.31e-08

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 52.08  E-value: 7.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  44 DALLARADYQDGEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSG-ATNIDFTCADASTVKLPEA 122
Cdd:PRK00216   41 RKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLAVGREKLRDLGlSGNVEFVQGDAEALPFPDN 120

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1004371618 123 PYDRLFSRFGSMFFEDPVSAFSNLHALVRKGGR 155
Cdd:PRK00216  121 SFDAVTIAFGLRNVPDIDKALREMYRVLKPGGR 153
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 45-125 1.68e-07

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: 50.57  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  45 ALLARADYQDGEMVIDLGCGGGATTIAIATAvAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADAsTVKLPEAPY 124
Cdd:COG2813    40 LLLEHLPEPLGGRVLDLGCGYGVIGLALAKR-NPEARVTLVDVNARAVELARANAAANGLENVEVLWSDG-LSGVPDGSF 117


                  .
gi 1004371618 125 D 125
Cdd:COG2813   118 D 118
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 47-156 2.92e-07

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 49.80  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  47 LARADYQDGEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSG-ATNIDFTCADASTVkLPEAP-- 123
Cdd:PRK00377   33 LSKLRLRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEKFGvLNNIVLIKGEAPEI-LFTINek 111

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1004371618 124 YDRLFSRFGSMFFEDPVSAFSNlhaLVRKGGRI 156
Cdd:PRK00377  112 FDRIFIGGGSEKLKEIISASWE---IIKKGGRI 141
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 36-214 5.67e-07

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 48.58  E-value: 5.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  36 EEMIAPIGDALLARADYQDGEM-VIDLGCGGGATTIAIATAVApsgKVMGVDISPDLIAASRKramksgatNIDFTCADA 114
Cdd:pfam13489   3 HQRERLLADLLLRLLPKLPSPGrVLDFGCGTGIFLRLLRAQGF---SVTGVDPSPIAIERALL--------NVRFDQFDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618 115 STVKLPEAPYDrlfsrFGSMF-----FEDPVSAFSNLHALVRKGGRIDLAVWGPPRENLWMMEmmgvvrnhvEIPPAVPR 189
Cdd:pfam13489  72 QEAAVPAGKFD-----VIVARevlehVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLL---------EWPYLRPR 137

                         170       180
                  ....*....|....*....|....*
gi 1004371618 190 APGpFAFEDLEYLGEILDSSGFTDV 214
Cdd:pfam13489 138 NGH-ISLFSARSLKRLLEEAGFEVV 161
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 47-156 5.75e-07

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: 48.41  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  47 LARAdyQDGEMVIDLGCGGGATTIAIATAVApsgKVMGVDISPDLIAASRKRAMKSGATNIDFTCADASTVKLP------ 120
Cdd:COG1041    21 LAGA--KEGDTVLDPFCGTGTILIEAGLLGR---RVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDLPLAdesvda 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1004371618 121 ---EAPYDRlFSRFGSMFFEDPVS-AFSNLHALVRKGGRI 156
Cdd:COG1041    96 ivtDPPYGR-SSKISGEELLELYEkALEEAARVLKPGGRV 134
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
55-156 7.24e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 49.26  E-value: 7.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  55 GEMVIDLGCGGGATTIAIATAVApsGKVMGVDISPDLIAASRKRAMKSG-ATNIDFTCADASTVKLPEaPYDRLFSR-FG 132
Cdd:COG4076    36 GDVVLDIGTGSGLLSMLAARAGA--KKVYAVEVNPDIAAVARRIIAANGlSDRITVINADATDLDLPE-KADVIISEmLD 112

                          90       100
                  ....*....|....*....|....*.
gi 1004371618 133 S-MFFEDPVSAFSNLHA-LVRKGGRI 156
Cdd:COG4076   113 TaLLDEGQVPILNHARKrLLKPGGRI 138
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 28-129 8.25e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 49.17  E-value: 8.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  28 WLASLSL-FE-EMIAPIGDaLLARADYQDGEMVIDLGCGGGATTiAIATAVAPSGKVMGVDISPDLIAASRKRamksgAT 105
Cdd:PRK01683    4 WNPSLYLkFEdERTRPARD-LLARVPLENPRYVVDLGCGPGNST-ELLVERWPAARITGIDSSPAMLAEARSR-----LP 76

                          90       100
                  ....*....|....*....|....
gi 1004371618 106 NIDFTCADASTVKlPEAPYDRLFS 129
Cdd:PRK01683   77 DCQFVEADIASWQ-PPQALDLIFA 99
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 54-139 9.02e-07

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 48.60  E-value: 9.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  54 DGEMVIDLGCGGGATTIAIATAvAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADASTV--KLPEAPYDRLFsrf 131
Cdd:COG0220    32 DAPLVLEIGFGKGEFLVELAAA-NPDINFIGIEVHEPGVAKALKKAEEEGLTNVRLLRGDAVELleLFPDGSLDRIY--- 107


                  ....*...
gi 1004371618 132 gsMFFEDP 139
Cdd:COG0220   108 --LNFPDP 113
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 45-126 1.58e-06

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 48.85  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  45 ALLARA-DYQDGEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADASTV-KLPEA 122
Cdd:COG0144   239 QLVALLlDPKPGERVLDLCAAPGGKTLHLAELMGNKGRVVAVDISEHRLKRLRENLARLGLSNVEVVVADARELlEWLPG 318


                  ....
gi 1004371618 123 PYDR 126
Cdd:COG0144   319 KFDR 322
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 55-118 1.63e-06

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 47.91  E-value: 1.63e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1004371618  55 GEMVIDLGCGGGATTIAIATAVApsgKVMGVDISPDLIAASRKRAMKSG-ATNIDFTCADASTVK 118
Cdd:PRK07580   64 GLRILDAGCGVGSLSIPLARRGA---KVVASDISPQMVEEARERAPEAGlAGNITFEVGDLESLL 125
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 38-128 5.83e-06

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 46.16  E-value: 5.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  38 MIAPIGDALlaraDYQDGEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADASTV 117
Cdd:PRK13942   64 MVAIMCELL----DLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKKLGYDNVEVIVGDGTLG 139

                          90
                  ....*....|.
gi 1004371618 118 KLPEAPYDRLF 128
Cdd:PRK13942  140 YEENAPYDRIY 150
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 41-129 6.59e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 46.61  E-value: 6.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  41 PIGDaLLARADYQDGEMVIDLGCGGGATTIAIATAvAPSGKVMGVDISPDLIAASRKRAmksgatnIDFTCADASTVKlP 120
Cdd:PRK14103   17 PFYD-LLARVGAERARRVVDLGCGPGNLTRYLARR-WPGAVIEALDSSPEMVAAARERG-------VDARTGDVRDWK-P 86


                  ....*....
gi 1004371618 121 EAPYDRLFS 129
Cdd:PRK14103   87 KPDTDVVVS 95
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 36-113 1.05e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 45.91  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  36 EEMIapigDALLARADYQDGEMVIDLGCGGGAttIAIATAVA-PSGKVMGVDISPDLIAASRKRAMKSGATN-IDFTCAD 113
Cdd:COG2890    98 EELV----ELALALLPAGAPPRVLDLGTGSGA--IALALAKErPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGD 171
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 44-113 1.11e-05

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 45.92  E-value: 1.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  44 DALLARADYQDGEMVIDLGCGGGATTIAIATAVaPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCAD 113
Cdd:PRK09328   98 EWALEALLLKEPLRVLDLGTGSGAIALALAKER-PDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGD 166
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 41-126 2.90e-05

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 43.92  E-value: 2.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  41 PIGD-------ALLAR----ADYQDGEMVIDLGCGGGATTiAIATAVApsGKVMGVDISPDLIAASRKRAMKSGATNIDF 109
Cdd:COG2518    42 PIGHgqtisqpYIVARmleaLDLKPGDRVLEIGTGSGYQA-AVLARLA--GRVYSVERDPELAERARERLAALGYDNVTV 118

                          90
                  ....*....|....*..
gi 1004371618 110 TCADASTVKLPEAPYDR 126
Cdd:COG2518   119 RVGDGALGWPEHAPFDR 135
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 44-170 4.35e-05

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 44.50  E-value: 4.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  44 DALLARADYQDGEM-VIDLGCGGGATTIAIATAVAPsGKVMGVDISPDLIAASRKRAMKSGATNIDftcADASTVKLPEA 122
Cdd:PLN02490  102 DDALEPADLSDRNLkVVDVGGGTGFTTLGIVKHVDA-KNVTILDQSPHQLAKAKQKEPLKECKIIE---GDAEDLPFPTD 177

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1004371618 123 PYDRLFSRFGSMFFEDPVSAFSNLHALVRKGGRIdlAVWGPPRENLWM 170
Cdd:PLN02490  178 YADRYVSAGSIEYWPDPQRGIKEAYRVLKIGGKA--CLIGPVHPTFWL 223
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 47-214 4.79e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 44.36  E-value: 4.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  47 LARADYQDGEMVIDLGCGGGATTIAIATAVapSGKVMGVDISPDLIAASRKRAMKSGATnIDFTCADASTVKLPEAPYDR 126
Cdd:PLN02336  259 VDKLDLKPGQKVLDVGCGIGGGDFYMAENF--DVHVVGIDLSVNMISFALERAIGRKCS-VEFEVADCTKKTYPDNSFDV 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618 127 LFSRFGSMFFEDPVSAFSNLHALVRKGGRIDLAVW----GPPREnlwmmEMMGVVRNHveippavprapgPFAFEDLEYL 202
Cdd:PLN02336  336 IYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYcrspGTPSP-----EFAEYIKQR------------GYDLHDVQAY 398

                         170
                  ....*....|..
gi 1004371618 203 GEILDSSGFTDV 214
Cdd:PLN02336  399 GQMLKDAGFDDV 410
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
 53-139 1.72e-04

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 41.69  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  53 QDGEMVIDLGCGGGATTIAIAtAVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADASTV---KLPEAPYDRLFs 129
Cdd:PRK00121   39 NDAPIHLEIGFGKGEFLVEMA-KANPDINFIGIEVHEPGVGKALKKIEEEGLTNLRLLCGDAVEVlldMFPDGSLDRIY- 116

                          90
                  ....*....|
gi 1004371618 130 rfgsMFFEDP 139
Cdd:PRK00121  117 ----LNFPDP 122
PRK14967 PRK14967
putative methyltransferase; Provisional
 47-125 1.99e-04

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 41.58  E-value: 1.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1004371618  47 LARADYQDGEMVIDLGCGGGAttIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSGATnIDFTCADASTVkLPEAPYD 125
Cdd:PRK14967   29 LAAEGLGPGRRVLDLCTGSGA--LAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVD-VDVRRGDWARA-VEFRPFD 103
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 55-158 2.33e-04

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 41.80  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  55 GEMVIDLGCGGGATTIAIATAVAPSGKVMGVDISPD--LIAASRKRAM-KSGATNIDFTCADASTVKLPEAPYDRLFSRF 131
Cdd:PLN02233   74 GDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEqlAVAASRQELKaKSCYKNIEWIEGDATDLPFDDCYFDAITMGY 153

                          90       100
                  ....*....|....*....|....*..
gi 1004371618 132 GSMFFEDPVSAFSNLHALVRKGGRIDL 158
Cdd:PLN02233  154 GLRNVVDRLKAMQEMYRVLKPGSRVSI 180
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 42-122 2.49e-04

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 41.24  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  42 IGDALLARADYQDGEMVIDLGCGGGATTIAIATAVaPSGKVMGVDIsPDLIAASRKRAMKSGATNIDFTCADASTVKLPE 121
Cdd:pfam00891  48 IGKDVLTAFDLSGFRSLVDVGGGTGALAQAIVSLY-PGCKGIVFDL-PHVVEAAPTHFSAGEEPRVTFHGGDFFKDSLPE 125


                  .
gi 1004371618 122 A 122
Cdd:pfam00891 126 A 126
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 58-106 7.95e-04

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: 40.41  E-value: 7.95e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1004371618  58 VIDLGCGGGATTIAIATAVaPSGKVMGVDISPDLIAASRKRAMKSGATN 106
Cdd:TIGR00536 118 ILDLGTGSGCIALALAYEF-PNAEVIAVDISPDALAVAEENAEKNQLEH 165
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 44-125 8.81e-04

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: 39.74  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  44 DA-LLAR-ADYQDGEMVIDLGCGGGAttIAIATAV-APSGKVMGVDISPDLIAASRKRAMKSG-ATNIDFTCADASTVK- 118
Cdd:COG4123    25 DAvLLAAfAPVKKGGRVLDLGTGTGV--IALMLAQrSPGARITGVEIQPEAAELARRNVALNGlEDRITVIHGDLKEFAa 102


                  ....*...
gi 1004371618 119 -LPEAPYD 125
Cdd:COG4123   103 eLPPGSFD 110
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 47-128 1.29e-03

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 39.76  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  47 LARADYQDGEMVIDLGCGGGATTIAIATAvAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADASTV--KLPEApy 124
Cdd:COG2242   240 LAKLALRPGDVLWDIGAGSGSVSIEAARL-APGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPEAlaDLPDP-- 316


                  ....
gi 1004371618 125 DRLF 128
Cdd:COG2242   317 DAVF 320
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 44-156 2.08e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 38.97  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  44 DALLARADYQDGEMVIDLGCGGGATTIAIATAVApsgKVMGVDISPDLIAASRKRamksGATNiDFTCADASTVKLPEAP 123
Cdd:PRK10258   32 DALLAMLPQRKFTHVLDAGCGPGWMSRYWRERGS---QVTALDLSPPMLAQARQK----DAAD-HYLAGDIESLPLATAT 103

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1004371618 124 YDRLFSRFGSMFFEDPVSAFSNLHALVRKGGRI 156
Cdd:PRK10258  104 FDLAWSNLAVQWCGNLSTALRELYRVVRPGGVV 136
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
60-115 2.46e-03

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 38.70  E-value: 2.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1004371618  60 DLGCGGGATTIAIATavaPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADAS 115
Cdd:PRK03522  179 DLFCGVGGFGLHCAT---PGMQLTGIEISAEAIACAKQSAAELGLTNVQFQALDST 231
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 53-125 3.57e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 38.40  E-value: 3.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1004371618  53 QDGEMVIDLGCGGGatTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADAStvkLPEAPYD 125
Cdd:pfam06325 160 KPGESVLDVGCGSG--ILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGD---LPKEKAD 227
rADc smart00650
Ribosomal RNA adenine dimethylases;
44-129 3.71e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.49  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618   44 DALLARADYQDGEMVIDLGCGGGATTIAIATAVApsgKVMGVDISPDLIAASRKRAmkSGATNIDFTCADASTVKLPEAP 123
Cdd:smart00650   3 DKIVRAANLRPGDTVLEIGPGKGALTEELLERAK---RVTAIEIDPRLAPRLREKF--AAADNLTVIHGDALKFDLPKLQ 77


                   ....*.
gi 1004371618  124 YDRLFS 129
Cdd:smart00650  78 PYKVVG 83
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 35-105 3.86e-03

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 36.78  E-value: 3.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1004371618  35 FEEMIAPIGDALLARadyQDGEMVIDLGCGGGATTIAIAtAVAPSGKVMGVDISPDLIAASRKRAMKSGAT 105
Cdd:pfam13679   9 LAEFIAPLLKELLDE---NGPITIVDHGAGKGYLGFILY-YLKYGVRVYGIDTRAELVEKANALAQKLGFN 75
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
50-105 4.33e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 38.70  E-value: 4.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1004371618  50 ADYQDGEMVIDLGCGGGaTTIAIATAVAPSGKVMGVDISPDLIAASRKRAMKSGAT 105
Cdd:PRK06922  414 LDYIKGDTIVDVGAGGG-VMLDMIEEETEDKRIYGIDISENVIDTLKKKKQNEGRS 468
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 45-97 4.68e-03

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 37.97  E-value: 4.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1004371618  45 ALLARADYQDGEMVIDLGCGG-GATTIAIATAVApsGKVMGVDISPDLIAASRK 97
Cdd:cd08260   156 ALVHQARVKPGEWVAVHGCGGvGLSAVMIASALG--ARVIAVDIDDDKLELARE 207
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 42-129 5.46e-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: 36.80  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  42 IGDALLARA-DYQDGEMVIDLGCGGGATTIAIAtAVAPSGKVMGVDISPDLIAASRKRAMKSGATNIDFTCADA-STVkl 119
Cdd:pfam05175  18 IGSRLLLEHlPKDLSGKVLDLGCGAGVLGAALA-KESPDAELTMVDINARALESARENLAANGLENGEVVASDVySGV-- 94

                          90
                  ....*....|
gi 1004371618 120 PEAPYDRLFS 129
Cdd:pfam05175  95 EDGKFDLIIS 104
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 30-155 5.64e-03

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 37.69  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1004371618  30 ASLSLFEEMIAPIgDALLARADYQDGEMVIDLGCGGGATTIaiaTAVAPSG-KVMGVDISPDLIAASRKRAMKSGAtnid 108
Cdd:pfam02353  38 PDMTLEEAQQAKL-DLILDKLGLKPGMTLLDIGCGWGGLMR---RAAERYDvNVVGLTLSKNQYKLARKRVAAEGL---- 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1004371618 109 ftcADASTVKL------PEaPYDR-----LFSRFGsmfFEDPVSAFSNLHALVRKGGR 155
Cdd:pfam02353 110 ---ARKVEVLLqdyrdfDE-PFDRivsvgMFEHVG---HENYDTFFKKLYNLLPPGGL 160
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
 55-128 7.19e-03

RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as Schizosaccharomyces pombe Tgs1 and Giardia lamblia Tgs2 catalyze methylation of the exocyclic N2 amine of 7-methylguanosine.


Pssm-ID: 370496  Cd Length: 165  Bit Score: 36.54  E-value: 7.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1004371618  55 GEMVIDLGCGGGATTIAIATAVApsgKVMGVDISPDLIAASRKRAMKSG-ATNIDFTCAD----ASTVKLPEAPYDRLF 128
Cdd:pfam09445   1 ATRILDVFCGGGGNTIQFANVFD---SVISIDINLEHLACAQHNAEVYGvSDRIWLIHGDwfelLAKLKFEKIKYDCVF 76
PLN02672 PLN02672
methionine S-methyltransferase
 58-101 7.32e-03

methionine S-methyltransferase


Pssm-ID: 215360 [Multi-domain]  Cd Length: 1082  Bit Score: 37.83  E-value: 7.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1004371618   58 VIDLGCGGGATTIAIATAVAPSgKVMGVDISPdliaasrkRAMK 101
Cdd:PLN02672   122 VAELGCGNGWISIAIAEKWLPS-KVYGLDINP--------RAVK 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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