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Conserved domains on  [gi|488673547|ref|WP_002602333|]
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class I SAM-dependent methyltransferase [Hungatella hathewayi]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10614797)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-140 2.20e-20

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 82.61  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547   46 IADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKSLNLgnRVTGIVGSMEDLPFKKKSLDLIWSEGAIDNIG- 124
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPd 78

                          90
                  ....*....|....*...
gi 488673547  125 --FEKGISYWHDFLKKGG 140
Cdd:pfam13649  79 pdLEAALREIARVLKPGG 96
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-140 2.20e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 82.61  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547   46 IADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKSLNLgnRVTGIVGSMEDLPFKKKSLDLIWSEGAIDNIG- 124
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPd 78

                          90
                  ....*....|....*...
gi 488673547  125 --FEKGISYWHDFLKKGG 140
Cdd:pfam13649  79 pdLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 31-145 6.58e-19

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 81.89  E-value: 6.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  31 EQALGFLKPLNKFSRIADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKSLNLGNrVTGIVGSMEDL-PFKKK 109
Cdd:COG0500   15 AALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGN-VEFLVADLAELdPLPAE 93

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488673547 110 SLDLIWSEGAIDNIGFEKGISY---WHDFLKKGGFVVVT 145
Cdd:COG0500   94 SFDLVVAFGVLHHLPPEEREALlreLARALKPGGVLLLS 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-149 2.05e-15

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: 70.15  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  45 RIADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKsLNLGNRVTGIVGSMEDLPFKK-KSLDLIWSEGAIDNI 123
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAEELPPEAdESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*...
gi 488673547 124 G--FEKGISYWHDFLKKGGFVVVTCPSW 149
Cdd:cd02440   80 VedLARFLEEARRLLKPGGVLVLTLVLA 107
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 34-145 9.23e-08

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


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 51.52  E-value: 9.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547   34 LGFLKPLNKF--SRIADLGCGTGGQTIHLAQHLP-GTITGLDmFADFIEKLnenAKSLNlGNRVTGIVGSMEDLPFKKKS 110
Cdd:TIGR02072  24 LALLKEKGIFipASVLDIGCGTGYLTRALLKRFPqAEFIALD-ISAGMLAQ---AKTKL-SENVQFICGDAEKLPLEDSS 98

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 488673547  111 LDLIWSEGAI---DNigFEKGISYWHDFLKKGGFVVVT 145
Cdd:TIGR02072  99 FDLIVSNLALqwcDD--LSQALSELARVLKPGGLLAFS 134
PLN02244 PLN02244
tocopherol O-methyltransferase
 30-116 4.17e-07

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 50.13  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  30 IEQALGF----LKPLNKFSRIADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKSLNLGNRVTGIVGSMEDLP 105
Cdd:PLN02244 102 IEESLAWagvpDDDEKRPKRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQP 181

                         90
                 ....*....|.
gi 488673547 106 FKKKSLDLIWS 116
Cdd:PLN02244 182 FEDGQFDLVWS 192
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-140 2.20e-20

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 82.61  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547   46 IADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKSLNLgnRVTGIVGSMEDLPFKKKSLDLIWSEGAIDNIG- 124
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPd 78

                          90
                  ....*....|....*...
gi 488673547  125 --FEKGISYWHDFLKKGG 140
Cdd:pfam13649  79 pdLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 31-145 6.58e-19

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 81.89  E-value: 6.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  31 EQALGFLKPLNKFSRIADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKSLNLGNrVTGIVGSMEDL-PFKKK 109
Cdd:COG0500   15 AALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGN-VEFLVADLAELdPLPAE 93

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488673547 110 SLDLIWSEGAIDNIGFEKGISY---WHDFLKKGGFVVVT 145
Cdd:COG0500   94 SFDLVVAFGVLHHLPPEEREALlreLARALKPGGVLLLS 132
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 44-166 1.68e-18

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: 79.27  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  44 SRIADLGCGTGGQTIHLAQHlPGTITGLDMFADFIEKLNENAKSlnLGNRVTGIVGSMEDLPFKKKSLDLIWSEGAIDNI 123
Cdd:COG2226   24 ARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAE--AGLNVEFVVGDAEDLPFPDGSFDLVISSFVLHHL 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488673547 124 G-FEKGISYWHDFLKKGGFVVVTCPSWLTKEQpaiVEKFWSNAG 166
Cdd:COG2226  101 PdPERALAEIARVLKPGGRLVVVDFSPPDLAE---LEELLAEAG 141
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 44-147 3.88e-17

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 76.12  E-value: 3.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  44 SRIADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKSLNLGNRVTGIVGSMEDLPFkKKSLDLIWSEGAIDNI 123
Cdd:COG2230   53 MRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPA-DGQFDAIVSIGMFEHV 131

                         90       100
                 ....*....|....*....|....*..
gi 488673547 124 GFEKGISY---WHDFLKKGGFVVVTCP 147
Cdd:COG2230  132 GPENYPAYfakVARLLKPGGRLLLHTP 158
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 44-148 9.32e-16

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: 71.59  E-value: 9.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  44 SRIADLGCGTGGQTIHLAQHlpG-TITGLDMFADFIEKLNENAKSLNlgnrVTGIVGSMEDLPFKKKSLDLIWSEGAIDN 122
Cdd:COG2227   26 GRVLDVGCGTGRLALALARR--GaDVTGVDISPEALEIARERAAELN----VDFVQGDLEDLPLEDGSFDLVICSEVLEH 99

                         90       100
                 ....*....|....*....|....*..
gi 488673547 123 I-GFEKGISYWHDFLKKGGFVVVTCPS 148
Cdd:COG2227  100 LpDPAALLRELARLLKPGGLLLLSTPN 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-149 2.05e-15

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: 70.15  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  45 RIADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKsLNLGNRVTGIVGSMEDLPFKK-KSLDLIWSEGAIDNI 123
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAEELPPEAdESFDVIISDPPLHHL 79

                         90       100
                 ....*....|....*....|....*...
gi 488673547 124 G--FEKGISYWHDFLKKGGFVVVTCPSW 149
Cdd:cd02440   80 VedLARFLEEARRLLKPGGVLVLTLVLA 107
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
44-146 2.15e-14

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 67.16  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  44 SRIADLGCGTGGQTIHLAQHLPG-TITGLDMFADFIEKLNENAkslnlgNRVTGIVGSMEDLPFKKKsLDLIWSEGAIDN 122
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAERFPGaRVTGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEP-FDLVVSNAALHW 75

                         90       100
                 ....*....|....*....|....*
gi 488673547 123 IG-FEKGISYWHDFLKKGGFVVVTC 146
Cdd:COG4106   76 LPdHAALLARLAAALAPGGVLAVQV 100
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 48-144 6.44e-14

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 65.38  E-value: 6.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547   48 DLGCGTGGQTIHLAQHLPgTITGLDMFADFIEKLNENAKslnlGNRVTGIVGSMEDLPFKKKSLDLIWSEGAIDNIG-FE 126
Cdd:pfam08241   2 DVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKAP----REGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEdPE 76

                          90
                  ....*....|....*...
gi 488673547  127 KGISYWHDFLKKGGFVVV 144
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 40-160 1.93e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 63.20  E-value: 1.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547   40 LNKFSRIADLGCGTGGQTIHLAQHLP--GTITGLDMFADFIEKLNENAKSLNLGNrVTGIVGSMEDLP--FKKKSLDLIW 115
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKLGFDN-VEFEQGDIEELPelLEDDKFDVVI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 488673547  116 SEGAIDNIGF-EKGISYWHDFLKKGGFVVVTCPSWLtKEQPAIVEK 160
Cdd:pfam13847  80 SNCVLNHIPDpDKVLQEILRVLKPGGRLIISDPDSL-AELPAHVKE 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
14-148 1.17e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 56.16  E-value: 1.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  14 ETHIGLERQGPGSSEAIEQALGFLkPLNKFSRIADLGCGTGGQTIHLAQHlPGTITGLDMFADFIEKlnenAKSLNLGNR 93
Cdd:COG4976   19 DAALVEDLGYEAPALLAEELLARL-PPGPFGRVLDLGCGTGLLGEALRPR-GYRLTGVDLSEEMLAK----AREKGVYDR 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  94 VtgIVGSMEDLPFKKKSLDLIWSEGAIDNIG-----FEkGIsywHDFLKKGGFVVVTCPS 148
Cdd:COG4976   93 L--LVADLADLAEPDGRFDLIVAADVLTYLGdlaavFA-GV---ARALKPGGLFIFSVED 146
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 48-142 1.22e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.21  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547   48 DLGCGTGGQTIHLAQHLPG-TITGLDMFADFIEKLNENAKSLNLGN--RVTGIVGSMEDLPFkkKSLDLIWSEGAIDNIG 124
Cdd:pfam08242   2 EIGCGTGTLLRALLEALPGlEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELDP--GSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 488673547  125 -FEKGISYWHDFLKKGGFV 142
Cdd:pfam08242  80 dPRAVLRNIRRLLKPGGVL 98
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 34-145 9.23e-08

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


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 51.52  E-value: 9.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547   34 LGFLKPLNKF--SRIADLGCGTGGQTIHLAQHLP-GTITGLDmFADFIEKLnenAKSLNlGNRVTGIVGSMEDLPFKKKS 110
Cdd:TIGR02072  24 LALLKEKGIFipASVLDIGCGTGYLTRALLKRFPqAEFIALD-ISAGMLAQ---AKTKL-SENVQFICGDAEKLPLEDSS 98

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 488673547  111 LDLIWSEGAI---DNigFEKGISYWHDFLKKGGFVVVT 145
Cdd:TIGR02072  99 FDLIVSNLALqwcDD--LSQALSELARVLKPGGLLAFS 134
PLN02244 PLN02244
tocopherol O-methyltransferase
 30-116 4.17e-07

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 50.13  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  30 IEQALGF----LKPLNKFSRIADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKSLNLGNRVTGIVGSMEDLP 105
Cdd:PLN02244 102 IEESLAWagvpDDDEKRPKRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFQVADALNQP 181

                         90
                 ....*....|.
gi 488673547 106 FKKKSLDLIWS 116
Cdd:PLN02244 182 FEDGQFDLVWS 192
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 30-114 6.14e-07

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 49.38  E-value: 6.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  30 IEQALGFLKPlNKFSRIADLGCGTGGQTIHLAQHLPG-TITGLDMFADFIEKLNENAKSLNLGNRVTGIVGSM-EDLPFK 107
Cdd:COG2890  101 VELALALLPA-GAPPRVLDLGTGSGAIALALAKERPDaRVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLfEPLPGD 179


                 ....*..
gi 488673547 108 KKsLDLI 114
Cdd:COG2890  180 GR-FDLI 185
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 45-144 2.57e-06

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


Pssm-ID: 443298  Cd Length: 173  Bit Score: 46.33  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  45 RIADLGCGTGGQTIHLAQHLP--GTITGLDMFADFIEKLNENAKSLNLGNRVTGIVG-SMEDLP-FKKKSLDLIWsegaI 120
Cdd:COG4122   19 RILEIGTGTGYSTLWLARALPddGRLTTIEIDPERAAIARENFARAGLADRIRLILGdALEVLPrLADGPFDLVF----I 94

                         90       100
                 ....*....|....*....|....*....
gi 488673547 121 DNigfEKG--ISYWH---DFLKKGGFVVV 144
Cdd:COG4122   95 DA---DKSnyPDYLElalPLLRPGGLIVA 120
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 39-114 3.81e-06

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: 46.68  E-value: 3.81e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488673547  39 PLNKFSRIADLGCGTGGQTIHLAQHLPG-TITGLDMFADFIEKLNENAKSLNLGNRVTGIVGSMEDLP--FKKKSLDLI 114
Cdd:COG4123   34 PVKKGGRVLDLGTGTGVIALMLAQRSPGaRITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAaeLPPGSFDLV 112
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 30-114 9.33e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 45.54  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  30 IEQALGFLKPlNKFSRIADLGCGTGGQTIHLAQHLPG-TITGLDMFADFIEKLNENAKsLNLGNRVTGIVGSMEDlPFKK 108
Cdd:PRK09328  97 VEWALEALLL-KEPLRVLDLGTGSGAIALALAKERPDaEVTAVDISPEALAVARRNAK-HGLGARVEFLQGDWFE-PLPG 173


                 ....*.
gi 488673547 109 KSLDLI 114
Cdd:PRK09328 174 GRFDLI 179
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 30-103 1.01e-05

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: 45.94  E-value: 1.01e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488673547  30 IEQALGFLKPLNKfSRIADLGCGTGGQTIHLAQHLpGTITGLDMFADFIEKLNENAKSLNLGNrVTGIVGSMED 103
Cdd:COG2265  222 YAAALEWLDLTGG-ERVLDLYCGVGTFALPLARRA-KKVIGVEIVPEAVEDARENARLNGLKN-VEFVAGDLEE 292
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 44-144 2.22e-05

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 44.37  E-value: 2.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  44 SRIADLGCGTGGQTIHLAQHLP--GTITGLD----MFADFIEKLnenaKSLNLGNRVTGIVGSMEDLPFKKKSLDLIwse 117
Cdd:PRK00216  53 DKVLDLACGTGDLAIALAKAVGktGEVVGLDfsegMLAVGREKL----RDLGLSGNVEFVQGDAEALPFPDNSFDAV--- 125

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488673547 118 gaidNIGF--------EKGISYWHDFLKKGGFVVV 144
Cdd:PRK00216 126 ----TIAFglrnvpdiDKALREMYRVLKPGGRLVI 156
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 39-145 1.08e-04

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 41.71  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  39 PLNKFSRIADLGCGTGGQTIHLAQHLPG-TITGLDmfADF--IEKLNENAKSLNLGNrVTGIVGsmeDL--PFKKKSLDL 113
Cdd:COG2813   46 PEPLGGRVLDLGCGYGVIGLALAKRNPEaRVTLVD--VNAraVELARANAAANGLEN-VEVLWS---DGlsGVPDGSFDL 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488673547 114 IWSegaidN----IGF--EKGISY-----WHDFLKKGG-FVVVT 145
Cdd:COG2813  120 ILS-----NppfhAGRavDKEVAHaliadAARHLRPGGeLWLVA 158
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 24-116 1.18e-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: 42.34  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547   24 PGSSEAIEQALGFLKPLNKFSRIADLGCGTGGQTIHLAQHLPG-TITGLDMFADFIEKLNENAKSLNLGNRVTGIVGSME 102
Cdd:TIGR00536  96 PETEELVEKALASLISQPPILHILDLGTGSGCIALALAYEFPNaEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLF 175

                          90
                  ....*....|....
gi 488673547  103 DlPFKKKSLDLIWS 116
Cdd:TIGR00536 176 E-PLAGQKIDIIVS 188
PRK08317 PRK08317
hypothetical protein; Provisional
 44-149 1.32e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 42.23  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  44 SRIADLGCGTGGQTIHLAQHL--PGTITGLDMFADFIEKLNENAKSLNLgnRVTGIVGSMEDLPFKKKSLDLIWSEGA-- 119
Cdd:PRK08317  21 DRVLDVGCGPGNDARELARRVgpEGRVVGIDRSEAMLALAKERAAGLGP--NVEFVRGDADGLPFPDGSFDAVRSDRVlq 98

                         90       100       110
                 ....*....|....*....|....*....|.
gi 488673547 120 -IDNIgfEKGISYWHDFLKKGGFVVVTCPSW 149
Cdd:PRK08317  99 hLEDP--ARALAEIARVLRPGGRVVVLDTDW 127
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 45-152 3.81e-04

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 41.03  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  45 RIADLGCGTGGQTIHLAQHL-PGTITGLDMFADFIEKlnenAKSLNLGNRVTGIVGSMEDLPFKKKSLDLIWSEGAIDNI 123
Cdd:PLN02490 116 KVVDVGGGTGFTTLGIVKHVdAKNVTILDQSPHQLAK----AKQKEPLKECKIIEGDAEDLPFPTDYADRYVSAGSIEYW 191

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488673547 124 -GFEKGISYWHDFLKKGGFVVVTCPS----WLTK 152
Cdd:PLN02490 192 pDPQRGIKEAYRVLKIGGKACLIGPVhptfWLSR 225
arsM PRK11873
arsenite methyltransferase;
48-116 4.69e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 40.70  E-value: 4.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488673547  48 DLGCGtGGQTIHLAQHL---PGTITGLDMFADFIEKLNENAKSLNLGNrVTGIVGSMEDLPFKKKSLDLIWS 116
Cdd:PRK11873  83 DLGSG-GGFDCFLAARRvgpTGKVIGVDMTPEMLAKARANARKAGYTN-VEFRLGEIEALPVADNSVDVIIS 152
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
44-140 2.05e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 38.48  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488673547  44 SRIADLGCGTGGQTIHLAQHLPGTITGLDMFADFIEKLNENAKSLNLGNRVTGIVGSMEDLPFKKKSlDLIWSEgAIDNI 123
Cdd:COG4076   37 DVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLPEKA-DVIISE-MLDTA 114

                         90       100
                 ....*....|....*....|..
gi 488673547 124 GFEKGI-----SYWHDFLKKGG 140
Cdd:COG4076  115 LLDEGQvpilnHARKRLLKPGG 136
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 39-80 2.90e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 38.00  E-value: 2.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488673547  39 PLNKFSRIADLGCGTGGQTIHLAQHLPG-TITGLDMFADFIEK 80
Cdd:PRK01683  28 PLENPRYVVDLGCGPGNSTELLVERWPAaRITGIDSSPAMLAE 70
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 39-114 6.52e-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: 36.41  E-value: 6.52e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488673547   39 PLNKFSRIADLGCGTGGQTIHLAQHLP-GTITGLDMFADFIEKLNENAKsLNLGNRVTGIVGSMEDlPFKKKSLDLI 114
Cdd:pfam05175  28 PKDLSGKVLDLGCGAGVLGAALAKESPdAELTMVDINARALESARENLA-ANGLENGEVVASDVYS-GVEDGKFDLI 102
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 45-72 7.02e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 36.98  E-value: 7.02e-03
                         10        20
                 ....*....|....*....|....*....
gi 488673547  45 RIADLGCGTGGQTIHLAQHLPGT-ITGLD 72
Cdd:PRK14103  32 RVVDLGCGPGNLTRYLARRWPGAvIEALD 60
 
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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