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Conserved domains on  [gi|1517860081|gb|ROZ60907|]
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class I SAM-dependent methyltransferase [Rhodococcus sp. WS1]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 53-154 2.17e-28

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: 103.94  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  53 LEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHveGEGVDIEWLEADLTKWDPQGRSFDLVSAqfFHMLE 132
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER--AAELNVDFVQGDLEDLPLEDGSFDLVIC--SEVLE 98

                          90       100
                  ....*....|....*....|....
gi 1517860081 133 --PARGELFRALGDLVAPGGHLLI 154
Cdd:COG2227    99 hlPDPAALLRELARLLKPGGLLLL 122
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 53-154 2.17e-28

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: 103.94  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  53 LEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHveGEGVDIEWLEADLTKWDPQGRSFDLVSAqfFHMLE 132
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER--AAELNVDFVQGDLEDLPLEDGSFDLVIC--SEVLE 98

                          90       100
                  ....*....|....*....|....
gi 1517860081 133 --PARGELFRALGDLVAPGGHLLI 154
Cdd:COG2227    99 hlPDPAALLRELARLLKPGGLLLL 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 59-150 1.35e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 95.71  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  59 LDVGCGEGADALWLARR-GWKVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTKWDPQGRSFDLV--SAQFFHMLEPAR 135
Cdd:pfam13649   2 LDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVvsSGVLHHLPDPDL 81

                          90
                  ....*....|....*
gi 1517860081 136 GELFRALGDLVAPGG 150
Cdd:pfam13649  82 EAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 57-155 5.01e-18

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: 76.31  E-value: 5.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  57 TALDVGCGEGADALWLARR-GWKVTGTDISSVALGRA-QAHVEGEGVDIEWLEADLTKWDPQ-GRSFDLV-SAQFFHMLE 132
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELArKAAAALLADNVEVLKGDAEELPPEaDESFDVIiSDPPLHHLV 80

                          90       100
                  ....*....|....*....|...
gi 1517860081 133 PARGELFRALGDLVAPGGHLLIV 155
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLT 103
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 46-155 1.50e-11

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 62.27  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  46 LIAEASDLEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTKWDPQGRsFDL-VS 124
Cdd:PRK12335  112 VLEAVQTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIRTGLYDINSASIQEE-YDFiLS 190

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1517860081 125 AQFFHMLEPAR-GELFRALGDLVAPGGHLLIV 155
Cdd:PRK12335  191 TVVLMFLNRERiPAIIKNMQEHTNPGGYNLIV 222
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
59-154 3.92e-06

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 46.26  E-value: 3.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081   59 LDVGCGEGADALWLARR--GWKVTGTDISS--VALGRAQahVEGEGVD--IEWLEADLTKwDPQGRSFDLV-SAQFFHML 131
Cdd:smart00828   4 LDFGCGYGSDLIDLAERhpHLQLHGYTISPeqAEVGRER--IRALGLQgrIRIFYRDSAK-DPFPDTYDLVfGFEVIHHI 80

                           90       100
                   ....*....|....*....|...
gi 1517860081  132 ePARGELFRALGDLVAPGGHLLI 154
Cdd:smart00828  81 -KDKMDLFSNISRHLKDGGHLVL 102
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 57-125 6.57e-03

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 36.70  E-value: 6.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1517860081  57 TALDVGCGEGADALWLARRGWKVTGTDISS--VALGRAQAHVEGEGVDIEWLEADLTKWDPQgrsFDLVSA 125
Cdd:TIGR02021  58 RVLDAGCGTGLLSIELAKRGAIVKAVDISEqmVQMARNRAQGRDVAGNVEFEVNDLLSLCGE---FDIVVC 125
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 53-154 2.17e-28

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: 103.94  E-value: 2.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  53 LEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHveGEGVDIEWLEADLTKWDPQGRSFDLVSAqfFHMLE 132
Cdd:COG2227    23 PAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARER--AAELNVDFVQGDLEDLPLEDGSFDLVIC--SEVLE 98

                          90       100
                  ....*....|....*....|....
gi 1517860081 133 --PARGELFRALGDLVAPGGHLLI 154
Cdd:COG2227    99 hlPDPAALLRELARLLKPGGLLLL 122
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 45-159 9.84e-27

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 100.39  E-value: 9.84e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  45 QLIAEASDLEPG-TALDVGCGEGADALWLARR-GWKVTGTDISSVALGRAQAHVEGEGVD--IEWLEADLTKWDPQGRsF 120
Cdd:COG2230    41 DLILRKLGLKPGmRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLAdrVEVRLADYRDLPADGQ-F 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1517860081 121 DLVSAQ--FFHMLEPARGELFRALGDLVAPGGHLLIvgHSP 159
Cdd:COG2230   120 DAIVSIgmFEHVGPENYPAYFAKVARLLKPGGRLLL--HTP 158
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 45-163 7.51e-26

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: 97.76  E-value: 7.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  45 QLIAEASDLEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTKWDPQGRSFDLV- 123
Cdd:COG2226    13 ALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGSFDLVi 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1517860081 124 SAQFFHMLE-PARG--ELFRALgdlvAPGGHLLIVGHSPHESP 163
Cdd:COG2226    93 SSFVLHHLPdPERAlaEIARVL----KPGGRLVVVDFSPPDLA 131
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 59-150 1.35e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 95.71  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  59 LDVGCGEGADALWLARR-GWKVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTKWDPQGRSFDLV--SAQFFHMLEPAR 135
Cdd:pfam13649   2 LDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVvsSGVLHHLPDPDL 81

                          90
                  ....*....|....*
gi 1517860081 136 GELFRALGDLVAPGG 150
Cdd:pfam13649  82 EAALREIARVLKPGG 96
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
19-187 1.02e-24

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 95.84  E-value: 1.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  19 YAKA-DAQFWNSLYEERPARWSGnpnpQLIAEASDLEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHve 97
Cdd:COG4976    14 YADSyDAALVEDLGYEAPALLAE----ELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  98 geGVDIEWLEADLTKWDPQGRSFDLVSA----QFFHMLEPargeLFRALGDLVAPGGHLLIvghSPHESPTEHHRAmlHT 173
Cdd:COG4976    88 --GVYDRLLVADLADLAEPDGRFDLIVAadvlTYLGDLAA----VFAGVARALKPGGLFIF---SVEDADGSGRYA--HS 156

                         170
                  ....*....|....*
gi 1517860081 174 PEYVESLFTD-GWKV 187
Cdd:COG4976   157 LDYVRDLLAAaGFEV 171
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 26-158 1.48e-24

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 96.14  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  26 FWNSLYEERParwsgnpNPQLIAEASDLE----PGTALDVGCGEGADALWLARR-GWKVTGTDISSVALGRAQAHVEGEG 100
Cdd:COG0500     1 PWDSYYSDEL-------LPGLAALLALLErlpkGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAG 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1517860081 101 VD-IEWLEADLTKWDP-QGRSFDLVSAQF-FHMLEPA-RGELFRALGDLVAPGGHLLIVGHS 158
Cdd:COG0500    74 LGnVEFLVADLAELDPlPAESFDLVVAFGvLHHLPPEeREALLRELARALKPGGVLLLSASD 135
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
54-155 1.58e-22

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 87.57  E-value: 1.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  54 EPGTALDVGCGEGADALWLARR--GWKVTGTDISSVALGRAQAHVEgegvDIEWLEADLTKWDPQGRsFDLV--SAQFFH 129
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLP----NVRFVVADLRDLDPPEP-FDLVvsNAALHW 75

                          90       100
                  ....*....|....*....|....*.
gi 1517860081 130 MLEPARgeLFRALGDLVAPGGHLLIV 155
Cdd:COG4106    76 LPDHAA--LLARLAAALAPGGVLAVQ 99
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 57-155 5.01e-18

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: 76.31  E-value: 5.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  57 TALDVGCGEGADALWLARR-GWKVTGTDISSVALGRA-QAHVEGEGVDIEWLEADLTKWDPQ-GRSFDLV-SAQFFHMLE 132
Cdd:cd02440     1 RVLDLGCGTGALALALASGpGARVTGVDISPVALELArKAAAALLADNVEVLKGDAEELPPEaDESFDVIiSDPPLHHLV 80

                          90       100
                  ....*....|....*....|...
gi 1517860081 133 PARGELFRALGDLVAPGGHLLIV 155
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLT 103
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 59-154 6.06e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 70.39  E-value: 6.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  59 LDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVdiEWLEADLTKWDPQGRSFDLVSAQ--FFHMLEPAR- 135
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGL--TFVVGDAEDLPFPDNSFDLVLSSevLHHVEDPERa 78

                          90       100
                  ....*....|....*....|
gi 1517860081 136 -GELFRALgdlvAPGGHLLI 154
Cdd:pfam08241  79 lREIARVL----KPGGILII 94
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 32-154 1.57e-14

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 68.61  E-value: 1.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  32 EERPARWSgnpnpQLIAEASDL--EPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVDIEwlead 109
Cdd:pfam13489   3 HQRERLLA-----DLLLRLLPKlpSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQ----- 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1517860081 110 ltKWDPQGRSFDLVSAqfFHMLE--PARGELFRALGDLVAPGGHLLI 154
Cdd:pfam13489  73 --EAAVPAGKFDVIVA--REVLEhvPDPPALLRQIAALLKPGGLLLL 115
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 59-152 5.43e-13

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 62.77  E-value: 5.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  59 LDVGCGEGADALWLAR--RGWKVTGTDISSVALGRAQAHVEGEGVD----IEWLEADLTkwDPQGRSFDLVSA-QFFHML 131
Cdd:pfam08242   1 LEIGCGTGTLLRALLEalPGLEYTGLDISPAALEAARERLAALGLLnavrVELFQLDLG--ELDPGSFDVVVAsNVLHHL 78

                          90       100
                  ....*....|....*....|.
gi 1517860081 132 EPARgELFRALGDLVAPGGHL 152
Cdd:pfam08242  79 ADPR-AVLRNIRRLLKPGGVL 98
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
 46-155 1.50e-11

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 62.27  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  46 LIAEASDLEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTKWDPQGRsFDL-VS 124
Cdd:PRK12335  112 VLEAVQTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDINQQSLENLQEIAEKENLNIRTGLYDINSASIQEE-YDFiLS 190

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1517860081 125 AQFFHMLEPAR-GELFRALGDLVAPGGHLLIV 155
Cdd:PRK12335  191 TVVLMFLNRERiPAIIKNMQEHTNPGGYNLIV 222
PRK08317 PRK08317
hypothetical protein; Provisional
 49-155 3.60e-11

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 60.72  E-value: 3.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  49 EASDLEPG-TALDVGCGEGADALWLARR---GWKVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTKWDPQGRSFDLV- 123
Cdd:PRK08317   13 ELLAVQPGdRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDAVr 92

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1517860081 124 SAQFF-HMLEPARG--ELFRALgdlvAPGGHLLIV 155
Cdd:PRK08317   93 SDRVLqHLEDPARAlaEIARVL----RPGGRVVVL 123
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
42-155 5.13e-10

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 57.05  E-value: 5.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  42 PNPQLIAEASDLEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVD-IEWLEADLTKWDPQGrSF 120
Cdd:PRK11207   18 THSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLERIKAAENLDnLHTAVVDLNNLTFDG-EY 96

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1517860081 121 DLVSAQFFHM-LEPAR-GELFRALGDLVAPGGHLLIV 155
Cdd:PRK11207   97 DFILSTVVLMfLEAKTiPGLIANMQRCTKPGGYNLIV 133
TPMT pfam05724
Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase ...
 22-202 6.90e-10

Thiopurine S-methyltransferase (TPMT); This family consists of thiopurine S-methyltransferase proteins from both eukaryotes and prokaryotes. Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyzes S-methylation of aromatic and heterocyclic sulfhydryl compounds, including anticancer and immunosuppressive thiopurines.


Pssm-ID: 399030  Cd Length: 218  Bit Score: 56.67  E-value: 6.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  22 ADAQFWNSLYEERPARW---SGNPNPQLIAEASDLEPGT-ALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQA-HV 96
Cdd:pfam05724   1 VDPDFWLKRWVEGQTPFhqeGVNPLLVRHWDALKLPPGLrVLVPLCGKALDMVWLAEQGHFVVGVEISELAVEKFFAeAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  97 EGEGVD------------IEWLEADLTKWDPQG-RSFDLV-SAQFFHMLEPA-RGELFRALGDLVAPGGH-LLIVGHSPh 160
Cdd:pfam05724  81 LSPPITelsgfkeyssgnISLYCGDFFTLPREElGKFDLIyDRAALCALPPEmRPRYAKQMYELLPPGGRgLLITLDYP- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1517860081 161 esPTEHHRAMLHTPE-YVESLFTDGWKVLVSEsRERDLPANPE 202
Cdd:pfam05724 160 --QTDHEGPPFSVPAaELEALFGGGWKVAELE-REDALVPEPR 199
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 46-156 1.40e-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: 55.58  E-value: 1.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  46 LIAEASDLEPGTALDVGCGEGADALWLARRGW--KVTGTDISSVALGRAQAHVEGEGVD-IEWLEADLTKwDPQGRSFDL 122
Cdd:COG2813    41 LLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPeaRVTLVDVNARAVELARANAAANGLEnVEVLWSDGLS-GVPDGSFDL 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1517860081 123 V------SAQFFHMLEPARgELFRALGDLVAPGGHLLIVG 156
Cdd:COG2813   120 IlsnppfHAGRAVDKEVAH-ALIADAARHLRPGGELWLVA 158
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 47-145 3.49e-09

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 54.84  E-value: 3.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  47 IAEASDLEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVD--IEWLEADLtkwDPQGRSFDLVS 124
Cdd:PRK07580   56 LPADGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAgnITFEVGDL---ESLLGRFDTVV 132

                          90       100
                  ....*....|....*....|...
gi 1517860081 125 A--QFFHMLEPARGELFRALGDL 145
Cdd:PRK07580  133 CldVLIHYPQEDAARMLAHLASL 155
PRK14968 PRK14968
putative methyltransferase; Provisional
 46-123 4.70e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 51.05  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  46 LIAEASDLEPG-TALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGV---DIEWLEADLTkwDP-QGRSF 120
Cdd:PRK14968   14 LLAENAVDKKGdRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIrnnGVEVIRSDLF--EPfRGDKF 91


                  ...
gi 1517860081 121 DLV 123
Cdd:PRK14968   92 DVI 94
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 45-155 6.75e-08

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 51.88  E-value: 6.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  45 QLIAEASDLEPGTALDVGCGEGAdALWLARRGWK----VTGTDISSVA--LGR--AQAHVEGEGVDIEWLEADLTKWDPQ 116
Cdd:COG5459    71 ELAEAGPDFAPLTVLDVGAGPGT-AAWAAADAWPslldATLLERSAAAlaLGRrlARAAANPALETAEWRLADLAAALPA 149

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1517860081 117 GRsFDLVSAQffHML----EPARGELFRALgdLVAPGGHLLIV 155
Cdd:COG5459   150 PP-ADLVVAS--YVLnelaDAARAALVDRL--WLAPDGALLIV 187
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 57-186 2.83e-07

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 48.57  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  57 TALDVGCGEGADALWLARR---GWKVTGTDISSVALGRAQAHVEGEGVD-IEWLEADLTKWDP--QGRSFDLVSAQFFHM 130
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEELPEllEDDKFDVVISNCVLN 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1517860081 131 LEPARGELFRALGDLVAPGGHLLIVGHSPHESPTEHHRAMLhtPEYVESLFTDGWK 186
Cdd:pfam13847  86 HIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDS--TYYAGCVGGAILK 139
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 45-123 3.80e-07

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 49.79  E-value: 3.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  45 QLIAEASDLEPG-TALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVD-IEWLEADLTKWDPQ---GRS 119
Cdd:COG2265   223 AAALEWLDLTGGeRVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLNGLKnVEFVAGDLEEVLPEllwGGR 302


                  ....
gi 1517860081 120 FDLV 123
Cdd:COG2265   303 PDVV 306
PLN02244 PLN02244
tocopherol O-methyltransferase
 33-156 5.68e-07

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 49.36  E-value: 5.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  33 ERPARWSGNPNpqliaeASDLEPGTALDVGCGEGADALWLARR-GWKVTGTDISSVALGRAQAHVEGEGVD--IEWLEAD 109
Cdd:PLN02244  103 EESLAWAGVPD------DDEKRPKRIVDVGCGIGGSSRYLARKyGANVKGITLSPVQAARANALAAAQGLSdkVSFQVAD 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1517860081 110 -LTKWDPQGrSFDLV----SAQffHMlePARGELFRALGDLVAPGGHLLIVG 156
Cdd:PLN02244  177 aLNQPFEDG-QFDLVwsmeSGE--HM--PDKRKFVQELARVAAPGGRIIIVT 223
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
52-123 8.88e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.59  E-value: 8.88e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1517860081  52 DLEPGTALDVGCGEGADALWLARRGW-KVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTKWDPQGrSFDLV 123
Cdd:COG2263    43 DIEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIPLGG-SVDTV 114
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 49-154 9.02e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 48.23  E-value: 9.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  49 EASDLEPG-TALDVGCGEGADALWLARRGWK---VTGTDISS--VALGRAQAHVEGEGVDIEWLEADLTKWDPQGRSFDL 122
Cdd:PRK00216   45 KWLGVRPGdKVLDLACGTGDLAIALAKAVGKtgeVVGLDFSEgmLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDA 124

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1517860081 123 VSAQF----FHMLEPARGELFRALgdlvAPGGHLLI 154
Cdd:PRK00216  125 VTIAFglrnVPDIDKALREMYRVL----KPGGRLVI 156
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 59-154 9.65e-07

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 48.58  E-value: 9.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  59 LDVGCGEGADALWLARRGWKVTGTDI--SSVALGRAQAHVEGEGVDIEWLEADLTKWDPQGRSFDLVSAQ--FFHMLEPA 134
Cdd:PLN02396  136 IDIGCGGGLLSEPLARMGATVTGVDAvdKNVKIARLHADMDPVTSTIEYLCTTAEKLADEGRKFDAVLSLevIEHVANPA 215

                          90       100
                  ....*....|....*....|
gi 1517860081 135 rgELFRALGDLVAPGGHLLI 154
Cdd:PLN02396  216 --EFCKSLSALTIPNGATVL 233
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 56-156 1.01e-06

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: 47.20  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  56 GTALDVGCGEGADALWLARRG--WKVTGTDISSVALGRAQAHVEGEGVD-IEWLEADLTKwDPQGRSFDLV--------- 123
Cdd:pfam05175  33 GKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLEnGEVVASDVYS-GVEDGKFDLIisnppfhag 111

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1517860081 124 SAQFFHMLEpargELFRALGDLVAPGGHLLIVG 156
Cdd:pfam05175 112 LATTYNVAQ----RFIADAKRHLRPGGELWIVA 140
Pox_MCEL pfam03291
mRNA capping enzyme; This family of enzymes are related to pfam03919.
 45-154 2.04e-06

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


Pssm-ID: 281307 [Multi-domain]  Cd Length: 332  Bit Score: 47.43  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  45 QLIAEASDLEPG--TALDVGCGEGADAL-WLARRGWKVTGTDISSVALGRAQA--HVEGEGV-------DIEWLEADLTK 112
Cdd:pfam03291  52 SLYASKTFQNSNkrKVLDLGCGKGGDLEkWFKGGISQLIGTDIAEVSIEQCREryNKLRSGNkskyykfDAEFITGDCFV 131

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1517860081 113 -------WDPQGRsFDLVSAQF-----FHMLEPARgELFRALGDLVAPGGHLLI 154
Cdd:pfam03291 132 sslrevfEDPFGK-FDIVSCQFaihysFESEEKAR-TMLRNVAELLASGGVFIG 183
PRK14967 PRK14967
putative methyltransferase; Provisional
 45-158 3.86e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 46.20  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  45 QLIAEA---SDLEPGT-ALDVGCGEGADALWLARRG-WKVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTKWDPqGRS 119
Cdd:PRK14967   23 QLLADAlaaEGLGPGRrVLDLCTGSGALAVAAAAAGaGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVE-FRP 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081 120 FDLVSAQFFH-----MLEPARG----------------ELFRALGDLVAPGGHLLIVgHS 158
Cdd:PRK14967  102 FDVVVSNPPYvpappDAPPSRGparawdagpdgravldRLCDAAPALLAPGGSLLLV-QS 160
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
59-154 3.92e-06

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 46.26  E-value: 3.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081   59 LDVGCGEGADALWLARR--GWKVTGTDISS--VALGRAQahVEGEGVD--IEWLEADLTKwDPQGRSFDLV-SAQFFHML 131
Cdd:smart00828   4 LDFGCGYGSDLIDLAERhpHLQLHGYTISPeqAEVGRER--IRALGLQgrIRIFYRDSAK-DPFPDTYDLVfGFEVIHHI 80

                           90       100
                   ....*....|....*....|...
gi 1517860081  132 ePARGELFRALGDLVAPGGHLLI 154
Cdd:smart00828  81 -KDKMDLFSNISRHLKDGGHLVL 102
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 34-152 7.47e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 45.70  E-value: 7.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  34 RPARwsgnpnpQLIAEASDLEPGTALDVGCGEGADALWLARRgW---KVTGTDISSVALGRAQAHVEgegvDIEWLEADL 110
Cdd:PRK01683   18 RPAR-------DLLARVPLENPRYVVDLGCGPGNSTELLVER-WpaaRITGIDSSPAMLAEARSRLP----DCQFVEADI 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1517860081 111 TKWDPQGRSfDLVSAQ-FFHMLePARGELFRALGDLVAPGGHL 152
Cdd:PRK01683   86 ASWQPPQAL-DLIFANaSLQWL-PDHLELFPRLVSLLAPGGVL 126
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 52-154 9.32e-06

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 45.90  E-value: 9.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  52 DLEPG-TALDVGCGEGADALWLARR-GWKVTGTDIS----SVALGRAQahveGEGVDIEWLEADLTKWDPQGRSFDLVSA 125
Cdd:PLN02336  263 DLKPGqKVLDVGCGIGGGDFYMAENfDVHVVGIDLSvnmiSFALERAI----GRKCSVEFEVADCTKKTYPDNSFDVIYS 338

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1517860081 126 Q--FFHMLE-PArgeLFRALGDLVAPGGHLLI 154
Cdd:PLN02336  339 RdtILHIQDkPA---LFRSFFKWLKPGGKVLI 367
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
45-101 1.54e-05

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 44.57  E-value: 1.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1517860081  45 QLIAEASDlEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGV 101
Cdd:PRK11036   36 RLLAELPP-RPLRVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGV 91
TehB pfam03848
Tellurite resistance protein TehB;
45-155 1.97e-05

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 43.68  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  45 QLIAEASDLEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVD-IEWLEADLTKWDPQGRSFDLV 123
Cdd:pfam03848  21 EVLEAVKIVKPGKVLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQRIKEKENLDnIHTALYDINNATIDENYDFIL 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1517860081 124 SAQFFHMLEPAR-GELFRALGDLVAPGGHLLIV 155
Cdd:pfam03848 101 STVVLMFLEPERiPGIIANMQECTNPGGYNLIV 133
YqjQ COG0300
Short-chain dehydrogenase [General function prediction only];
53-112 2.61e-05

Short-chain dehydrogenase [General function prediction only];


Pssm-ID: 440069 [Multi-domain]  Cd Length: 252  Bit Score: 43.70  E-value: 2.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1517860081  53 LEPGTALDVGCGEG---ADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTK 112
Cdd:COG0300     3 LTGKTVLITGASSGigrALARALAARGARVVLVARDAERLEALAAELRAAGARVEVVALDVTD 65
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 55-161 4.98e-05

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: 42.82  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  55 PGTALDVGCGEGADALWLARR--GWKVTGTDISSVALGRAQAHVEGEGVD--IEWLEADLTKWDP--QGRSFDLVSAQ-- 126
Cdd:COG4123    38 GGRVLDLGTGTGVIALMLAQRspGARITGVEIQPEAAELARRNVALNGLEdrITVIHGDLKEFAAelPPGSFDLVVSNpp 117

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1517860081 127 FFH----------MLEPARGE-------LFRALGDLVAPGGHLLIVgHSPHE 161
Cdd:COG4123   118 YFKagsgrkspdeARAIARHEdaltledLIRAAARLLKPGGRFALI-HPAER 168
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 55-154 7.86e-05

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: 41.71  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  55 PGTALDVGCGEGADALWLAR---RGWKVTGTDISSVALGRAQAHVEGEGVD--IEWLEADLTKWDPQ--GRSFDLV---- 123
Cdd:COG4122    17 AKRILEIGTGTGYSTLWLARalpDDGRLTTIEIDPERAAIARENFARAGLAdrIRLILGDALEVLPRlaDGPFDLVfida 96

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1517860081 124 ----SAQFFHMLEPargelfralgdLVAPGGHLLI 154
Cdd:COG4122    97 dksnYPDYLELALP-----------LLRPGGLIVA 120
PRK06202 PRK06202
hypothetical protein; Provisional
 55-147 8.81e-05

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 42.29  E-value: 8.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  55 PGTALDVGCGeGAD-----ALWLARRGWK--VTGTDISSVALGRAQAHVEGEGVDIEWLEADltKWDPQGRSFDLV-SAQ 126
Cdd:PRK06202   61 PLTLLDIGCG-GGDlaidlARWARRDGLRleVTAIDPDPRAVAFARANPRRPGVTFRQAVSD--ELVAEGERFDVVtSNH 137

                          90       100
                  ....*....|....*....|.
gi 1517860081 127 FFHMLEPArgELFRALGDLVA 147
Cdd:PRK06202  138 FLHHLDDA--EVVRLLADSAA 156
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 46-94 1.00e-04

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 42.54  E-value: 1.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1517860081  46 LIAEASDLEPGTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQA 94
Cdd:PLN02585  136 WLAEDGSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVAEAER 184
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 46-170 1.23e-04

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: 41.93  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  46 LIAEASDLEPG-TALDVGCGEGADALWLARR-GWKVTGTDISSVALGRAQAHVEGEGVDiEWLEADLTKWDPQGRSFD-L 122
Cdd:pfam02353  52 LILDKLGLKPGmTLLDIGCGWGGLMRRAAERyDVNVVGLTLSKNQYKLARKRVAAEGLA-RKVEVLLQDYRDFDEPFDrI 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1517860081 123 VSAQFFHMLEPARGEL-FRALGDLVAPGGHLLIvghspHESPTEHHRAM 170
Cdd:pfam02353 131 VSVGMFEHVGHENYDTfFKKLYNLLPPGGLMLL-----HTITGLHPDET 174
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
46-109 4.70e-04

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 40.60  E-value: 4.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1517860081  46 LIAEASDLEPG-TALDVGCGEGADALWLARR-GWKVTGTDISS--VALGRAQAhvegEGVDIEWLEAD 109
Cdd:PRK11705  158 LICRKLQLKPGmRVLDIGCGWGGLARYAAEHyGVSVVGVTISAeqQKLAQERC----AGLPVEIRLQD 221
FabG COG1028
NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and ...
 69-127 4.73e-04

NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family [Lipid transport and metabolism]; NAD(P)-dependent dehydrogenase, short-chain alcohol dehydrogenase family is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440651 [Multi-domain]  Cd Length: 249  Bit Score: 40.15  E-value: 4.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1517860081  69 ALWLARRGWKVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTKWDPQGRSFDLVSAQF 127
Cdd:COG1028    23 ARALAAEGARVVITDRDAEALEAAAAELRAAGGRALAVAADVTDEAAVEALVAAAVAAF 81
NodS pfam05401
Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The ...
 56-153 7.26e-04

Nodulation protein S (NodS); This family consists of nodulation S (NodS) proteins. The products of the rhizobial nodulation genes are involved in the biosynthesis of lipochitin oligosaccharides (LCOs), which are host-specific signal molecules required for nodule formation. NodS is an S-adenosyl-L-methionine (SAM)-dependent methyltransferase involved in N methylation of LCOs. NodS uses N-deacetylated chitooligosaccharides, the products of the NodBC proteins, as its methyl acceptors.


Pssm-ID: 428457  Cd Length: 201  Bit Score: 39.22  E-value: 7.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  56 GTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVeGEGVDIEWLEADLTKWDPQGRsFDLVSAQ----FFHML 131
Cdd:pfam05401  45 ADALEIGCAAGAFTEMLAILCERLTVVDLMPEAIAKAQERT-GKWSDIIWHECDICQFDLNAK-FDLIICAevlyYIHDK 122

                          90       100
                  ....*....|....*....|..
gi 1517860081 132 EPARGELfRALGDLVAPGGHLL 153
Cdd:pfam05401 123 EELHAAI-ENIVQLLAPDEQFI 143
arsM PRK11873
arsenite methyltransferase;
43-154 1.33e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 38.78  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  43 NPQLIAEasdLEPG-TALDVGCGEGADALWLARR----GwKVTGTDISSVALGRAQAHVEGEGVD-IEWLEADLTKWDPQ 116
Cdd:PRK11873   68 NPTALAE---LKPGeTVLDLGSGGGFDCFLAARRvgptG-KVIGVDMTPEMLAKARANARKAGYTnVEFRLGEIEALPVA 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1517860081 117 GRSFDLVSAQFFHMLEPAR----GELFRALgdlvAPGGHLLI 154
Cdd:PRK11873  144 DNSVDVIISNCVINLSPDKervfKEAFRVL----KPGGRFAI 181
CheR COG1352
Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];
72-170 1.41e-03

Methylase of chemotaxis methyl-accepting proteins [Signal transduction mechanisms];


Pssm-ID: 440963 [Multi-domain]  Cd Length: 272  Bit Score: 38.61  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  72 LARRGWKVTGTDISSVALGRAQAhveG-------EGVDIEWLEA------------------------DLTKWDPQGRSF 120
Cdd:COG1352   131 LAGWRVEILATDISEEALEKARA---GiyperslRGLPPEYLSRyftkeggryrikpelremvtfaqhNLLDDPPPFGRF 207

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1517860081 121 DLVSAQffHML----EPARGELFRALGDLVAPGGHLLIvGHSphESPTEHHRAM 170
Cdd:COG1352   208 DLIFCR--NVLiyfdPELQRRVLRRFHDSLAPGGYLFL-GHS--ESLGGLSDLF 256
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 57-150 4.32e-03

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 37.43  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  57 TALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQAHVEGEgvdiEWLEADLTKWDPQGRSFDLV----SAQFFHMLE 132
Cdd:PRK10258   45 HVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAAD----HYLAGDIESLPLATATFDLAwsnlAVQWCGNLS 120

                          90
                  ....*....|....*...
gi 1517860081 133 PARGELFRalgdLVAPGG 150
Cdd:PRK10258  121 TALRELYR----VVRPGG 134
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 40-170 6.50e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 36.59  E-value: 6.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  40 GNPNPQLIAEASDLEPGTALDVGCGEGADALWLARR--GWKVTGTDISSVALGRAQahveGEGVDIEwlEADLTKWDPQG 117
Cdd:PRK14103   15 GRPFYDLLARVGAERARRVVDLGCGPGNLTRYLARRwpGAVIEALDSSPEMVAAAR----ERGVDAR--TGDVRDWKPKP 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1517860081 118 RSFDLVSAQFFHMLePARGELFRALGDLVAPGGHLLIVGHSPHESPTehHRAM 170
Cdd:PRK14103   89 DTDVVVSNAALQWV-PEHADLLVRWVDELAPGSWIAVQVPGNFDAPS--HAAV 138
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 57-125 6.57e-03

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 36.70  E-value: 6.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1517860081  57 TALDVGCGEGADALWLARRGWKVTGTDISS--VALGRAQAHVEGEGVDIEWLEADLTKWDPQgrsFDLVSA 125
Cdd:TIGR02021  58 RVLDAGCGTGLLSIELAKRGAIVKAVDISEqmVQMARNRAQGRDVAGNVEFEVNDLLSLCGE---FDIVVC 125
ovoA_Cterm TIGR04345
putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. ...
 56-161 6.69e-03

putative 4-mercaptohistidine N1-methyltranferase; Ovothiol A is N1-methyl-4-mercaptohistidine. In the absence of S-adenosylmethione, a methyl donor, the intermediate produced is 4-mercaptohistidine. In both Erwinia tasmaniensis and Trypanosoma cruzi, a protein occurs with 5-histidylcysteine sulfoxide synthase activity, but these two enzymes and most homologs share an additional C-terminal methyltransferase domain. Thus OvoA may be a bifunctional enzyme with 5-histidylcysteine sulfoxide synthase and 4-mercaptohistidine N1-methyltranferase activity. This model describes C-terminal putative 4-mercaptohistidine N1-methyltranferase domain. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 275141  Cd Length: 242  Bit Score: 36.81  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1517860081  56 GTALDVGCGEGADALWLARRGWKVTGTDISSVALGRAQA--------HV---EGEGVD-----------------IEWLE 107
Cdd:TIGR04345  43 KRALDIGCAVGRASFELARYFDEVDGIDFSARFIRPAVAlkergslrYAlkeEGELVSfkevtlsdlgldevrdrVSFFQ 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1517860081 108 ADLTKWDPQGRSFDLVSAQffHMLE----PARgeLFRALGDLVAPGGhLLIVGhSPHE 161
Cdd:TIGR04345 123 GDACNLKPHFTGYDLILAA--NLLDrlydPAA--FLSSIHERLNPGG-LLVIA-SPYT 174
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 45-92 8.72e-03

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 36.43  E-value: 8.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1517860081  45 QLIAEASDLEPGTALDVGCGEG------ADALwLARRGWKVTGTDISSVALGRA 92
Cdd:PRK11088   76 NLLAERLDEKATALLDIGCGEGyythalADAL-PEITTMQLFGLDISKVAIKYA 128
Ga5DH-like_SDR_c cd05347
gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent ...
 52-127 9.79e-03

gluconate 5-dehydrogenase (Ga5DH)-like, classical (c) SDRs; Ga5DH catalyzes the NADP-dependent conversion of carbon source D-gluconate and 5-keto-D-gluconate. This SDR subgroup has a classical Gly-rich NAD(P)-binding motif and a conserved active site tetrad pattern. However, it has been proposed that Arg104 (Streptococcus suis Ga5DH numbering), as well as an active site Ca2+, play a critical role in catalysis. In addition to Ga5DHs this subgroup contains Erwinia chrysanthemi KduD which is involved in pectin degradation, and is a putative 2,5-diketo-3-deoxygluconate dehydrogenase. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107,15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187605 [Multi-domain]  Cd Length: 248  Bit Score: 36.18  E-value: 9.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1517860081  52 DLEPGTALDVGCGEG---ADALWLARRGWKVTGTDISSVALGRAQAHVEGEGVDIEWLEADLTKWDPQGRSFDLVSAQF 127
Cdd:cd05347     2 SLKGKVALVTGASRGigfGIASGLAEAGANIVINSRNEEKAEEAQQLIEKEGVEATAFTCDVSDEEAIKAAVEAIEEDF 80
 
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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