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Conserved domains on  [gi|499845634|ref|WP_011526368|]
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16S rRNA (guanine(966)-N(2))-methyltransferase RsmD [Lawsonia intracellularis]

Protein Classification

RsmD family RNA methyltransferase( domain architecture ID 10002368)

RsmD family RNA methyltransferase similar to 16S rRNA (guanine(966)-N(2))-methyltransferase RsmD, which specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:0003676|GO:0031167|GO:0008168

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
1-185 6.84e-72

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


:

Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 215.33  E-value: 6.84e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   1 MRIMTGSLRGRILKTIEGDGYRPATGKVREALFSMLTSRgivWDQTYILDLFAGSGSLGFEAISRGAAEVCFIENNPKAV 80
Cdd:COG0742    1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNILGPD---IEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  81 QCLYKNIEKLRLFEQVSVVEQDVIQFLNQDSLFKlYQLVFIDPPYGGNRLETTISCVVEKGWIAPEGYIIAEVETtlRIN 160
Cdd:COG0742   78 AVIRKNLEKLGLEDRARVIRGDALRFLKRLAGEP-FDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSK--REE 154
                        170       180
                 ....*....|....*....|....*
gi 499845634 161 FFQLHPQLELLSNRSYGQTRLLIWK 185
Cdd:COG0742  155 LPELPAGLELLKERKYGDTRLSFYR 179
 
Name Accession Description Interval E-value
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
1-185 6.84e-72

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 215.33  E-value: 6.84e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   1 MRIMTGSLRGRILKTIEGDGYRPATGKVREALFSMLTSRgivWDQTYILDLFAGSGSLGFEAISRGAAEVCFIENNPKAV 80
Cdd:COG0742    1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNILGPD---IEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  81 QCLYKNIEKLRLFEQVSVVEQDVIQFLNQDSLFKlYQLVFIDPPYGGNRLETTISCVVEKGWIAPEGYIIAEVETtlRIN 160
Cdd:COG0742   78 AVIRKNLEKLGLEDRARVIRGDALRFLKRLAGEP-FDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSK--REE 154
                        170       180
                 ....*....|....*....|....*
gi 499845634 161 FFQLHPQLELLSNRSYGQTRLLIWK 185
Cdd:COG0742  155 LPELPAGLELLKERKYGDTRLSFYR 179
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
1-185 3.14e-52

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 165.10  E-value: 3.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634    1 MRIMTGSLRGRILKTIEGDGYRPATGKVREALFSMLTSRGivwDQTYILDLFAGSGSLGFEAISRGAAEVCFIENNPKAV 80
Cdd:pfam03602   1 MRIIGGKARGRKLKVPPGPGTRPTTDRVREALFNWLAPYI---EGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   81 QCLYKNIEKLRLFEQVsVVEQDVIQFLNQDSLFKLYQLVFIDPPYGGNRLETTISCVVEKGWIAPEGYIIaeVETTLRIN 160
Cdd:pfam03602  78 QILKENLQLLGLPGAV-LVMDALLALLRLAGKGPVFDIVFLDPPYAKGLIEEVLDLLAEKGWLKPNALIY--VETEKRGE 154
                         170       180
                  ....*....|....*....|....*
gi 499845634  161 FFQLHPQLELLSNRSYGQTRLLIWK 185
Cdd:pfam03602 155 LPEQPGNLELVREKKYGQTTLAFYQ 179
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
2-185 2.09e-39

16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188022 [Multi-domain]  Cd Length: 190  Bit Score: 132.92  E-value: 2.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634    2 RIMTGSLRGRILKTIEGDGYRPATGKVREALFSMLtsrGIVWDQTYILDLFAGSGSLGFEAISRGAAEVCFIENNPKAVQ 81
Cdd:TIGR00095  11 RIIGGQYRGRKLKVPPGPSTRPTTDRVRESLFNIL---RPDIVGAHFLDLFAGSGALGLEALSRGAASAVFVEQDRKVAQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   82 CLYKNIEKLRL-FEQVSVVEQDVIQFLNQDSLFKLYQLVFIDPPYGGNRLETTISCVVEKGWIAPEGYIIAEVETTlrin 160
Cdd:TIGR00095  88 TLKENLSTLKKsGEQATVLNDAVRALLFLAKKQTPFDIIYLDPPFNRGLLEALLELLGENKWLNPKGLIVVEYDRE---- 163
                         170       180
                  ....*....|....*....|....*...
gi 499845634  161 fFQLHPQ---LELLSNRSYGQTRLLIWK 185
Cdd:TIGR00095 164 -NELPTVpetWSLLRQKVYGQSALRLYQ 190
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
1-157 9.65e-33

16S rRNA m(2)G966-methyltransferase; Provisional


Pssm-ID: 236793  Cd Length: 199  Bit Score: 115.97  E-value: 9.65e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   1 MRIMTGSLRGRILKTIEGDGYRPATGKVREALFSMLTSrgiVWDQTYILDLFAGSGSLGFEAISRGAAEVCFIENNPKAV 80
Cdd:PRK10909  13 IRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAP---VIVDARCLDCFAGSGALGLEALSRYAAGATLLEMDRAVA 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499845634  81 QCLYKNIEKLRLfEQVSVVEQDVIQFLNQDSlfKLYQLVFIDPPYGGNRLETTISCVVEKGWIAPEG--YIIAEVETTL 157
Cdd:PRK10909  90 QQLIKNLATLKA-GNARVVNTNALSFLAQPG--TPHNVVFVDPPFRKGLLEETINLLEDNGWLADEAliYVESEVENGL 165
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
48-155 4.17e-06

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: 43.96  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  48 ILDLFAGSGSLGFEAISRGAAEVCFIENNPKAVQCLYKNiEKLRLFEQVSVVEQDVIQFLnqDSLFKLYQLVFIDPPYGG 127
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELP--PEADESFDVIISDPPLHH 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 499845634 128 nrLETTISCVVEKGW--IAPEGYIIAEVET 155
Cdd:cd02440   79 --LVEDLARFLEEARrlLKPGGVLVLTLVL 106
 
Name Accession Description Interval E-value
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
1-185 6.84e-72

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 215.33  E-value: 6.84e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   1 MRIMTGSLRGRILKTIEGDGYRPATGKVREALFSMLTSRgivWDQTYILDLFAGSGSLGFEAISRGAAEVCFIENNPKAV 80
Cdd:COG0742    1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNILGPD---IEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  81 QCLYKNIEKLRLFEQVSVVEQDVIQFLNQDSLFKlYQLVFIDPPYGGNRLETTISCVVEKGWIAPEGYIIAEVETtlRIN 160
Cdd:COG0742   78 AVIRKNLEKLGLEDRARVIRGDALRFLKRLAGEP-FDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSK--REE 154
                        170       180
                 ....*....|....*....|....*
gi 499845634 161 FFQLHPQLELLSNRSYGQTRLLIWK 185
Cdd:COG0742  155 LPELPAGLELLKERKYGDTRLSFYR 179
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
1-185 3.14e-52

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 165.10  E-value: 3.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634    1 MRIMTGSLRGRILKTIEGDGYRPATGKVREALFSMLTSRGivwDQTYILDLFAGSGSLGFEAISRGAAEVCFIENNPKAV 80
Cdd:pfam03602   1 MRIIGGKARGRKLKVPPGPGTRPTTDRVREALFNWLAPYI---EGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   81 QCLYKNIEKLRLFEQVsVVEQDVIQFLNQDSLFKLYQLVFIDPPYGGNRLETTISCVVEKGWIAPEGYIIaeVETTLRIN 160
Cdd:pfam03602  78 QILKENLQLLGLPGAV-LVMDALLALLRLAGKGPVFDIVFLDPPYAKGLIEEVLDLLAEKGWLKPNALIY--VETEKRGE 154
                         170       180
                  ....*....|....*....|....*
gi 499845634  161 FFQLHPQLELLSNRSYGQTRLLIWK 185
Cdd:pfam03602 155 LPEQPGNLELVREKKYGQTTLAFYQ 179
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
2-185 2.09e-39

16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of uncharacterized bacterial proteins. Members are present in nearly every complete bacterial genome, always in a single copy. PSI-BLAST analysis shows homology to several families of SAM-dependent methyltransferases, including ribosomal RNA adenine dimethylases. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188022 [Multi-domain]  Cd Length: 190  Bit Score: 132.92  E-value: 2.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634    2 RIMTGSLRGRILKTIEGDGYRPATGKVREALFSMLtsrGIVWDQTYILDLFAGSGSLGFEAISRGAAEVCFIENNPKAVQ 81
Cdd:TIGR00095  11 RIIGGQYRGRKLKVPPGPSTRPTTDRVRESLFNIL---RPDIVGAHFLDLFAGSGALGLEALSRGAASAVFVEQDRKVAQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   82 CLYKNIEKLRL-FEQVSVVEQDVIQFLNQDSLFKLYQLVFIDPPYGGNRLETTISCVVEKGWIAPEGYIIAEVETTlrin 160
Cdd:TIGR00095  88 TLKENLSTLKKsGEQATVLNDAVRALLFLAKKQTPFDIIYLDPPFNRGLLEALLELLGENKWLNPKGLIVVEYDRE---- 163
                         170       180
                  ....*....|....*....|....*...
gi 499845634  161 fFQLHPQ---LELLSNRSYGQTRLLIWK 185
Cdd:TIGR00095 164 -NELPTVpetWSLLRQKVYGQSALRLYQ 190
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
1-157 9.65e-33

16S rRNA m(2)G966-methyltransferase; Provisional


Pssm-ID: 236793  Cd Length: 199  Bit Score: 115.97  E-value: 9.65e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   1 MRIMTGSLRGRILKTIEGDGYRPATGKVREALFSMLTSrgiVWDQTYILDLFAGSGSLGFEAISRGAAEVCFIENNPKAV 80
Cdd:PRK10909  13 IRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAP---VIVDARCLDCFAGSGALGLEALSRYAAGATLLEMDRAVA 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499845634  81 QCLYKNIEKLRLfEQVSVVEQDVIQFLNQDSlfKLYQLVFIDPPYGGNRLETTISCVVEKGWIAPEG--YIIAEVETTL 157
Cdd:PRK10909  90 QQLIKNLATLKA-GNARVVNTNALSFLAQPG--TPHNVVFVDPPFRKGLLEETINLLEDNGWLADEAliYVESEVENGL 165
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
48-124 5.06e-09

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: 54.41  E-value: 5.06e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499845634  48 ILDLFAGSGSLGFeAISRGAAEVCFIENNPKAVQCLYKNIEKLRLfEQVSVVEQDVIQFLNQDSLFKLYQLVFIDPP 124
Cdd:COG2265  237 VLDLYCGVGTFAL-PLARRAKKVIGVEIVPEAVEDARENARLNGL-KNVEFVAGDLEEVLPELLWGGRPDVVVLDPP 311
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
48-129 1.38e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 49.52  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  48 ILDLFAGSGSLGFEAISRGAAEVCFIENNPKAVQCLYKNIEklRLFEQVSVVEQDVIQFlnqdSLFKLYQLVFIDPPYGG 127
Cdd:COG2263   49 VLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAE--RLGVRVDFIRADVTRI----PLGGSVDTVVMNPPFGA 122

                 ..
gi 499845634 128 NR 129
Cdd:COG2263  123 QR 124
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
48-103 8.37e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 47.72  E-value: 8.37e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499845634  48 ILDLFAGSGSLGFEAISRGAAEVCFIENNPKAVQCLYKNIEKLRLFEQVSVVEQDV 103
Cdd:COG4076   39 VLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADA 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
48-155 4.17e-06

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: 43.96  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  48 ILDLFAGSGSLGFEAISRGAAEVCFIENNPKAVQCLYKNiEKLRLFEQVSVVEQDVIQFLnqDSLFKLYQLVFIDPPYGG 127
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELP--PEADESFDVIISDPPLHH 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 499845634 128 nrLETTISCVVEKGW--IAPEGYIIAEVET 155
Cdd:cd02440   79 --LVEDLARFLEEARrlLKPGGVLVLTLVL 106
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
49-124 9.47e-06

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 44.79  E-value: 9.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499845634  49 LDLFAGSGSLGFEAISRGAAEVCFIENNPKAVQCLYKNIEKLRLFEQVSVVEQDVIQFLNQ-DSLFKLYQLVFIDPP 124
Cdd:COG1092  221 LNLFSYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNGLDDRHEFVQADAFDWLRElAREGERFDLIILDPP 297
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
35-126 1.12e-04

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: 40.70  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  35 MLTSRGIVWDQTYILDLFAGSGSLGFEAISRGAAEVCfIENNPKAVQCLYKNIEKLRLfEQVSVVEQDViqfLNQDSLFK 114
Cdd:COG1041   17 ALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVIG-SDIDPKMVEGARENLEHYGY-EDADVIRGDA---RDLPLADE 91
                         90
                 ....*....|..
gi 499845634 115 LYQLVFIDPPYG 126
Cdd:COG1041   92 SVDAIVTDPPYG 103
PRK14967 PRK14967
putative methyltransferase; Provisional
21-125 2.86e-04

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 40.04  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  21 YRPATGKvrEALFSMLTSRGIVwDQTYILDLFAGSGSLGFEAISRGAAEVCFIENNPKAVQCLYKNIEKLRLfeQVSVVE 100
Cdd:PRK14967  16 YRPQEDT--QLLADALAAEGLG-PGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGV--DVDVRR 90
                         90       100
                 ....*....|....*....|....*
gi 499845634 101 QDVIQFLNqdslFKLYQLVFIDPPY 125
Cdd:PRK14967  91 GDWARAVE----FRPFDVVVSNPPY 111
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
48-125 4.21e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 39.75  E-value: 4.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  48 ILDLFAGSGSLgfeAIS----RGAAEVCFIENNPKAVQCLYKNIEKLRLFEQVSVVEQDVIQFLNQDslfKLYQLVFIDP 123
Cdd:COG2890  116 VLDLGTGSGAI---ALAlakeRPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFEPLPGD---GRFDLIVSNP 189

                 ..
gi 499845634 124 PY 125
Cdd:COG2890  190 PY 191
Cyt_C5_DNA_methylase cd00315
Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many ...
48-86 4.34e-04

Cytosine-C5 specific DNA methylases; Methyl transfer reactions play an important role in many aspects of biology. Cytosine-specific DNA methylases are found both in prokaryotes and eukaryotes. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the mammalian genome. These effects include transcriptional repression via inhibition of transcription factor binding or the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability.


Pssm-ID: 238192 [Multi-domain]  Cd Length: 275  Bit Score: 39.91  E-value: 4.34e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 499845634  48 ILDLFAGSG--SLGFEAIsrGAAEVCFIENNPKAVQCLYKN 86
Cdd:cd00315    3 VIDLFAGIGgfRLGLEKA--GFEIVAANEIDKSAAETYEAN 41
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
48-153 4.81e-04

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 39.40  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  48 ILDLFAGSGSLGFEA--ISRGAAEVCFIENNPKAVQCLYKNIEKLRLFEQVSVVEQDVIQFLNQdsLFKLYQLVFIDPpy 125
Cdd:PRK00377  44 ILDIGCGTGSVTVEAslLVGETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFT--INEKFDRIFIGG-- 119
                         90       100
                 ....*....|....*....|....*...
gi 499845634 126 GGNRLETTISCVVEKgwIAPEGYIIAEV 153
Cdd:PRK00377 120 GSEKLKEIISASWEI--IKKGGRIVIDA 145
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
22-125 1.18e-03

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 38.49  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   22 RPATGKVREALFSMLTSRGIVwdqTYILDLFAGSGSLGFE-AISRGAAEVCFIENNPKAVQCLYKNIEKLRLFEQVSVVE 100
Cdd:TIGR00536  95 RPETEELVEKALASLISQPPI---LHILDLGTGSGCIALAlAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQ 171
                          90       100
                  ....*....|....*....|....*.
gi 499845634  101 QDVIqflnqDSLFKL-YQLVFIDPPY 125
Cdd:TIGR00536 172 SNLF-----EPLAGQkIDIIVSNPPY 192
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
48-143 1.23e-03

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 38.69  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634  48 ILDLFAGSGSLGFEAISRGAAEVCFIENNPKAVQCLYKNIEKLRLFEQVSVVEQDVIQFLnqDSLFKLYQLVFIDPPYGG 127
Cdd:COG2520  184 VLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLKENIRLNKVEDRVTPILGDAREVA--PELEGKADRIIMNLPHSA 261
                         90
                 ....*....|....*..
gi 499845634 128 NR-LETTISCVVEKGWI 143
Cdd:COG2520  262 DEfLDAALRALKPGGVI 278
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
46-127 2.86e-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: 36.93  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499845634   46 TYILDLFAGSG--SLGFeaiSRGAAEVCFIENNPKAVQCLYKNIEKLRLFEQVSVVEQDVIQFLNQDSLFKL-YQLVFID 122
Cdd:pfam09445   2 TRILDVFCGGGgnTIQF---ANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFELLAKLKFEKIkYDCVFAS 78

                  ....*
gi 499845634  123 PPYGG 127
Cdd:pfam09445  79 PPWGG 83
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
48-100 3.77e-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: 37.07  E-value: 3.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499845634  48 ILDLFAGSGSLGFEA--ISRGAAeVCFIENNPKAVQCLYKNIEKLRLfEQVSVVE 100
Cdd:COG2242  251 LWDIGAGSGSVSIEAarLAPGGR-VYAIERDPERAALIRANARRFGV-PNVEVVE 303
DNA_methylase pfam00145
C-5 cytosine-specific DNA methylase;
48-86 4.82e-03

C-5 cytosine-specific DNA methylase;


Pssm-ID: 395093 [Multi-domain]  Cd Length: 324  Bit Score: 36.91  E-value: 4.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 499845634   48 ILDLFAGSG--SLGFEAIsrGAAEVCFIENNPKAVQCLYKN 86
Cdd:pfam00145   3 FIDLFAGIGgfRLGLEQA--GFECVAANEIDKSAAKTYEAN 41
 
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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