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Conserved domains on  [gi|502824007|ref|WP_013058983|]
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MULTISPECIES: 16S rRNA (guanine(966)-N(2))-methyltransferase RsmD [Priestia]

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 2.51e-80

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: 236.52  E-value: 2.51e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   1 MRVVAGLYKGHALKAVPGYSTRPTTDKVKEAIFNMIGPFFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTI 80
Cdd:COG0742    1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNILGPDIEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAAAVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  81 KANLASCRLEDRAEVYRNDAERALKAIKKRelTVDLLLLDPPYKAQKLKALIETVSEENLLAKTGIIVAEHSHDVQLDNE 160
Cdd:COG0742   81 RKNLEKLGLEDRARVIRGDALRFLKRLAGE--PFDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSKREELPEL 158
                        170       180
                 ....*....|....*....|....*
gi 502824007 161 IGLFEKIKSETYGIIGVSIYTYKKE 185
Cdd:COG0742  159 PAGLELLKERKYGDTRLSFYRREEE 183
 
Name Accession Description Interval E-value
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
1-185 2.51e-80

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: 236.52  E-value: 2.51e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   1 MRVVAGLYKGHALKAVPGYSTRPTTDKVKEAIFNMIGPFFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTI 80
Cdd:COG0742    1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNILGPDIEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAAAVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  81 KANLASCRLEDRAEVYRNDAERALKAIKKRelTVDLLLLDPPYKAQKLKALIETVSEENLLAKTGIIVAEHSHDVQLDNE 160
Cdd:COG0742   81 RKNLEKLGLEDRARVIRGDALRFLKRLAGE--PFDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSKREELPEL 158
                        170       180
                 ....*....|....*....|....*
gi 502824007 161 IGLFEKIKSETYGIIGVSIYTYKKE 185
Cdd:COG0742  159 PAGLELLKERKYGDTRLSFYRREEE 183
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
1-180 7.48e-65

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 197.08  E-value: 7.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007    1 MRVVAGLYKGHALKAVPGYSTRPTTDKVKEAIFNMIGPFFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTI 80
Cdd:pfam03602   1 MRIIGGKARGRKLKVPPGPGTRPTTDRVREALFNWLAPYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   81 KANLASCRLEDRaeVYRNDAERALKAIKKRELTVDLLLLDPPYKAQKLKALIETVSEENLLAKTGIIVAEHSHDVQLDNE 160
Cdd:pfam03602  81 KENLQLLGLPGA--VLVMDALLALLRLAGKGPVFDIVFLDPPYAKGLIEEVLDLLAEKGWLKPNALIYVETEKRGELPEQ 158
                         170       180
                  ....*....|....*....|
gi 502824007  161 IGLFEKIKSETYGIIGVSIY 180
Cdd:pfam03602 159 PGNLELVREKKYGQTTLAFY 178
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
2-180 2.30e-59

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: 183.76  E-value: 2.30e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007    2 RVVAGLYKGHALKAVPGYSTRPTTDKVKEAIFNMIGPFFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTIK 81
Cdd:TIGR00095  11 RIIGGQYRGRKLKVPPGPSTRPTTDRVRESLFNILRPDIVGAHFLDLFAGSGALGLEALSRGAASAVFVEQDRKVAQTLK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   82 ANLASCRLEDRAEVYRNDAERALKAIKKRELTVDLLLLDPPYKAQKLKALIETVSEENLLAKTGIIVAEHSHDVQLDNEI 161
Cdd:TIGR00095  91 ENLSTLKKSGEQATVLNDAVRALLFLAKKQTPFDIIYLDPPFNRGLLEALLELLGENKWLNPKGLIVVEYDRENELPTVP 170
                         170
                  ....*....|....*....
gi 502824007  162 GLFEKIKSETYGIIGVSIY 180
Cdd:TIGR00095 171 ETWSLLRQKVYGQSALRLY 189
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
1-150 1.68e-19

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


Pssm-ID: 236793  Cd Length: 199  Bit Score: 81.69  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   1 MRVVAGLYKGHALKAVPGYSTRPTTDKVKEAIFNMIGPFFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTI 80
Cdd:PRK10909  13 IRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAPVIVDARCLDCFAGSGALGLEALSRYAAGATLLEMDRAVAQQL 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  81 KANLASCRlEDRAEVYRNDaerALKAIKKRELTVDLLLLDPPYKAQKLKALIETVSEENLLAKTGIIVAE 150
Cdd:PRK10909  93 IKNLATLK-AGNARVVNTN---ALSFLAQPGTPHNVVFVDPPFRKGLLEETINLLEDNGWLADEALIYVE 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
44-150 2.12e-08

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: 50.12  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  44 TALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTIKANLAsCRLEDRAEVYRNDAERALKAIKKReltVDLLLLDPPY 123
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAEELPPEADES---FDVIISDPPL 76
                         90       100
                 ....*....|....*....|....*....
gi 502824007 124 KAQK--LKALIETVSEenLLAKTGIIVAE 150
Cdd:cd02440   77 HHLVedLARFLEEARR--LLKPGGVLVLT 103
 
Name Accession Description Interval E-value
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
1-185 2.51e-80

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: 236.52  E-value: 2.51e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   1 MRVVAGLYKGHALKAVPGYSTRPTTDKVKEAIFNMIGPFFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTI 80
Cdd:COG0742    1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNILGPDIEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAAAVI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  81 KANLASCRLEDRAEVYRNDAERALKAIKKRelTVDLLLLDPPYKAQKLKALIETVSEENLLAKTGIIVAEHSHDVQLDNE 160
Cdd:COG0742   81 RKNLEKLGLEDRARVIRGDALRFLKRLAGE--PFDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSKREELPEL 158
                        170       180
                 ....*....|....*....|....*
gi 502824007 161 IGLFEKIKSETYGIIGVSIYTYKKE 185
Cdd:COG0742  159 PAGLELLKERKYGDTRLSFYRREEE 183
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
1-180 7.48e-65

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 197.08  E-value: 7.48e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007    1 MRVVAGLYKGHALKAVPGYSTRPTTDKVKEAIFNMIGPFFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTI 80
Cdd:pfam03602   1 MRIIGGKARGRKLKVPPGPGTRPTTDRVREALFNWLAPYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   81 KANLASCRLEDRaeVYRNDAERALKAIKKRELTVDLLLLDPPYKAQKLKALIETVSEENLLAKTGIIVAEHSHDVQLDNE 160
Cdd:pfam03602  81 KENLQLLGLPGA--VLVMDALLALLRLAGKGPVFDIVFLDPPYAKGLIEEVLDLLAEKGWLKPNALIYVETEKRGELPEQ 158
                         170       180
                  ....*....|....*....|
gi 502824007  161 IGLFEKIKSETYGIIGVSIY 180
Cdd:pfam03602 159 PGNLELVREKKYGQTTLAFY 178
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
2-180 2.30e-59

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: 183.76  E-value: 2.30e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007    2 RVVAGLYKGHALKAVPGYSTRPTTDKVKEAIFNMIGPFFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTIK 81
Cdd:TIGR00095  11 RIIGGQYRGRKLKVPPGPSTRPTTDRVRESLFNILRPDIVGAHFLDLFAGSGALGLEALSRGAASAVFVEQDRKVAQTLK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   82 ANLASCRLEDRAEVYRNDAERALKAIKKRELTVDLLLLDPPYKAQKLKALIETVSEENLLAKTGIIVAEHSHDVQLDNEI 161
Cdd:TIGR00095  91 ENLSTLKKSGEQATVLNDAVRALLFLAKKQTPFDIIYLDPPFNRGLLEALLELLGENKWLNPKGLIVVEYDRENELPTVP 170
                         170
                  ....*....|....*....
gi 502824007  162 GLFEKIKSETYGIIGVSIY 180
Cdd:TIGR00095 171 ETWSLLRQKVYGQSALRLY 189
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
1-150 1.68e-19

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


Pssm-ID: 236793  Cd Length: 199  Bit Score: 81.69  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   1 MRVVAGLYKGHALKAVPGYSTRPTTDKVKEAIFNMIGPFFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTI 80
Cdd:PRK10909  13 IRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAPVIVDARCLDCFAGSGALGLEALSRYAAGATLLEMDRAVAQQL 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  81 KANLASCRlEDRAEVYRNDaerALKAIKKRELTVDLLLLDPPYKAQKLKALIETVSEENLLAKTGIIVAE 150
Cdd:PRK10909  93 IKNLATLK-AGNARVVNTN---ALSFLAQPGTPHNVVFVDPPFRKGLLEETINLLEDNGWLADEALIYVE 158
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
41-148 1.31e-12

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: 62.66  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  41 EGGTALDLFGGSGGLGIEALSRGIDkVIFVDRDGKAIQTIKANLASCRLEDrAEVYRNDAERalkaIKKRELTVDLLLLD 120
Cdd:COG1041   26 EGDTVLDPFCGTGTILIEAGLLGRR-VIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARD----LPLADESVDAIVTD 99
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 502824007 121 PPY------KAQKLKALIETVSEE--NLLAKTGIIV 148
Cdd:COG1041  100 PPYgrsskiSGEELLELYEKALEEaaRVLKPGGRVV 135
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
35-122 1.47e-10

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: 59.04  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  35 MIGPFFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTIKANLASCRLEDRAEVYRNDAERALKAIKKRELTV 114
Cdd:COG1092  210 RVAELAKGKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNGLDDRHEFVQADAFDWLRELAREGERF 289

                 ....*...
gi 502824007 115 DLLLLDPP 122
Cdd:COG1092  290 DLIILDPP 297
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
41-122 1.33e-08

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: 53.26  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  41 EGGTALDLFGGSGGLGIeALSRGIDKVIFVDRDGKAIQTIKANLASCRLeDRAEVYRNDAERALKAIKKRElTVDLLLLD 120
Cdd:COG2265  233 GGERVLDLYCGVGTFAL-PLARRAKKVIGVEIVPEAVEDARENARLNGL-KNVEFVAGDLEEVLPELLWGG-RPDVVVLD 309

                 ..
gi 502824007 121 PP 122
Cdd:COG2265  310 PP 311
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
44-150 2.12e-08

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: 50.12  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  44 TALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTIKANLAsCRLEDRAEVYRNDAERALKAIKKReltVDLLLLDPPY 123
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAA-ALLADNVEVLKGDAEELPPEADES---FDVIISDPPL 76
                         90       100
                 ....*....|....*....|....*....
gi 502824007 124 KAQK--LKALIETVSEenLLAKTGIIVAE 150
Cdd:cd02440   77 HHLVedLARFLEEARR--LLKPGGVLVLT 103
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
40-127 6.15e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 50.29  E-value: 6.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  40 FEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTIKANLAscRLEDRAEVYRNDAERAlkaikKRELTVDLLLL 119
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAE--RLGVRVDFIRADVTRI-----PLGGSVDTVVM 116

                 ....*...
gi 502824007 120 DPPYKAQK 127
Cdd:COG2263  117 NPPFGAQR 124
PRK14967 PRK14967
putative methyltransferase; Provisional
5-123 8.10e-07

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 47.35  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   5 AGLYKGHALKAVPG-YstRPTTDK---VKEAIFNMIGPffeGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTI 80
Cdd:PRK14967   1 AATTPPDALLRAPGvY--RPQEDTqllADALAAEGLGP---GRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSA 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 502824007  81 KANLASCRLedRAEVYRNDAERALkaikkRELTVDLLLLDPPY 123
Cdd:PRK14967  76 RLNALLAGV--DVDVRRGDWARAV-----EFRPFDVVVSNPPY 111
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
41-123 5.94e-06

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 44.65  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   41 EGGTALDLFGGSGGLGIEA------------LSRGIDKVIFVDRDGKAIQTIKANLASCRLEDRAEVYRNDAeralKAIK 108
Cdd:pfam01170  28 PGDPLLDPMCGSGTILIEAalmganiapgkfDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADA----ADLP 103
                          90
                  ....*....|....*
gi 502824007  109 KRELTVDLLLLDPPY 123
Cdd:pfam01170 104 LLEGSVDVIVTNPPY 118
PRK15128 PRK15128
23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;
39-122 1.53e-05

23S rRNA (cytosine(1962)-C(5))-methyltransferase RlmI;


Pssm-ID: 185082 [Multi-domain]  Cd Length: 396  Bit Score: 44.44  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  39 FFEGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTIKANLASCRLE-DRAEVYRNDAERALKAIKKRELTVDLL 117
Cdd:PRK15128 218 YVENKRVLNCFSYTGGFAVSALMGGCSQVVSVDTSQEALDIARQNVELNKLDlSKAEFVRDDVFKLLRTYRDRGEKFDVI 297

                 ....*
gi 502824007 118 LLDPP 122
Cdd:PRK15128 298 VMDPP 302
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
38-126 4.42e-05

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: 42.10  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  38 PFFEGGTALDLFGGSGGLGIEALSRG-IDKVIFVDRDGKAIQTIKANLASCRLEDrAEVYRNDAERALKaikkrELTVDL 116
Cdd:COG2813   46 PEPLGGRVLDLGCGYGVIGLALAKRNpEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLSGVP-----DGSFDL 119
                         90
                 ....*....|
gi 502824007 117 LLLDPPYKAQ 126
Cdd:COG2813  120 ILSNPPFHAG 129
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
29-100 6.11e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 41.95  E-value: 6.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502824007  29 KEAIFNMIGPffeGGTALDLFGGSGGLGIEALSRGIDKVIFVDRDGKAIQTIKANLASCRLEDRAEVYRNDA 100
Cdd:COG4076   26 KAAIERVVKP---GDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADA 94
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
31-144 7.63e-04

N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional


Pssm-ID: 235286  Cd Length: 382  Bit Score: 39.13  E-value: 7.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  31 AIFNMIGPFFEGGTALDLFGGSGGLGIE-ALSRGIDKVIFVDRDGKAIQTIKANLASCRLEDRaEVYRNDAERALKAIKK 109
Cdd:PRK04338  47 LVLRAFGPKLPRESVLDALSASGIRGIRyALETGVEKVTLNDINPDAVELIKKNLELNGLENE-KVFNKDANALLHEERK 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 502824007 110 reltVDLLLLDP-----PYkaqkLKALIETVSEENLLAKT 144
Cdd:PRK04338 126 ----FDVVDIDPfgspaPF----LDSAIRSVKRGGLLCVT 157
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
40-148 8.74e-04

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 39.00  E-value: 8.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  40 FEGGTALDlFG-GSGGLGIEALSRGIDKVIFVDRDGKAIQTIKANLASCRLEDRAEVYRNDAERALKAikkreltvDLL- 117
Cdd:COG2264  147 KPGKTVLD-VGcGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLEDGPY--------DLVv 217
                         90       100       110
                 ....*....|....*....|....*....|....
gi 502824007 118 ---LLDPpykaqkLKALIETVSeeNLLAKTGIIV 148
Cdd:COG2264  218 aniLANP------LIELAPDLA--ALLKPGGYLI 243
RsmJ pfam04378
Ribosomal RNA large subunit methyltransferase D, RlmJ; RlmJ is ribosomal RNA large subunit ...
30-127 1.09e-03

Ribosomal RNA large subunit methyltransferase D, RlmJ; RlmJ is ribosomal RNA large subunit methyltransferase J is required for full methylation of 23S ribosomal RNA (rRNA) during ribosome biogenesis. The ribosomal RNA of E. coli carries 24 residues that require methylation, and this methyltransferase is the last to be described, that modifies A2030. RlmJ displays a variant of the Rossmann-like methyltransferase (MTase) fold with an inserted helical subdomain. On binding cofactor and substrate a large shift of the N-terminal motif X tail is induced in order to make it cover the cofactor-binding site and to trigger active-site changes in motifs IV and VIII.


Pssm-ID: 398191  Cd Length: 245  Bit Score: 38.60  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   30 EAIFNMIGPFFEGGTaLDLFGGSGGLGIEALsRGIDKVIFVDRDGKAIQTIKANLASCRledRAEVYRNDAERALKAIKK 109
Cdd:pfam04378  47 DRYLDVIRQLNGGGT-LRYYPGSPLLAARLL-RAQDRMVLTELHPSDYPLLRANFAPDR---RVRVHQGDGFAQVKAFLP 121
                          90
                  ....*....|....*...
gi 502824007  110 RELTVDLLLLDPPYKAQK 127
Cdd:pfam04378 122 PKERRGLVLIDPPYELAD 139
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
40-150 1.14e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 38.24  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  40 FEGGTALDLFGGSGGLGIEA--LSRGIDKVIFVDRDGKAIQTIKANLASCRLEDRAEVYRNDAERALKAIKKReltVDLL 117
Cdd:PRK00377  39 RKGDMILDIGCGTGSVTVEAslLVGETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEILFTINEK---FDRI 115
                         90       100       110
                 ....*....|....*....|....*....|...
gi 502824007 118 LLDPpyKAQKLKALIETVSEenLLAKTGIIVAE 150
Cdd:PRK00377 116 FIGG--GSEKLKEIISASWE--IIKKGGRIVID 144
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
42-127 2.46e-03

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 36.80  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   42 GGTALDLFGGSGGLGIEALSRGID-KVIFVDRDGKAIQTIKANLASCRLEDrAEVYRNDAERALKAIKkreltVDLLLLD 120
Cdd:pfam05175  32 SGKVLDLGCGAGVLGAALAKESPDaELTMVDINARALESARENLAANGLEN-GEVVASDVYSGVEDGK-----FDLIISN 105

                  ....*..
gi 502824007  121 PPYKAQK 127
Cdd:pfam05175 106 PPFHAGL 112
PRK14968 PRK14968
putative methyltransferase; Provisional
41-123 2.85e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.80  E-value: 2.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  41 EGGTALDLFGGSGGLGIEALSRGIDkVIFVDRDGKAIQTIKANLASCRLEDRA-EVYRNDAERALKAIKkreltVDLLLL 119
Cdd:PRK14968  23 KGDRVLEVGTGSGIVAIVAAKNGKK-VVGVDINPYAVECAKCNAKLNNIRNNGvEVIRSDLFEPFRGDK-----FDVILF 96

                 ....
gi 502824007 120 DPPY 123
Cdd:PRK14968  97 NPPY 100
Methyltransf_15 pfam09445
RNA cap guanine-N2 methyltransferase; RNA cap guanine-N2 methyltransferases such as ...
42-123 3.03e-03

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


Pssm-ID: 370496  Cd Length: 165  Bit Score: 36.54  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007   42 GGTALDLFGGSGGLGIeALSRGIDKVIFVDRDGKAIQTIKANLASCRLEDRAEVYRNDAERALKAIKKRELTVDLLLLDP 121
Cdd:pfam09445   1 ATRILDVFCGGGGNTI-QFANVFDSVISIDINLEHLACAQHNAEVYGVSDRIWLIHGDWFELLAKLKFEKIKYDCVFASP 79

                  ..
gi 502824007  122 PY 123
Cdd:pfam09445  80 PW 81
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
42-108 3.95e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 35.77  E-value: 3.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502824007   42 GGTALDLFGGSGGLGIEALSR-GIDKVIFVDRDGKAIQTIKANLASCRLeDRAEVYRNDAERALKAIK 108
Cdd:TIGR02469  20 GDVLWDIGAGTGSVTIEAARLvPNGRVYAIERNPEALDLIERNLRRFGV-SNIVIVEGDAPEAPEALL 86
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
41-174 5.54e-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: 36.68  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824007  41 EGGTALDLFGGSGGLGIEA--LSRGIdKVIFVDRDGKAIQTIKANLASCRLeDRAEVYRNDAERALKAikkreltvdlll 118
Cdd:COG2242  247 PGDVLWDIGAGSGSVSIEAarLAPGG-RVYAIERDPERAALIRANARRFGV-PNVEVVEGEAPEALAD------------ 312
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502824007 119 LDPPYKA------QKLKALIETVSEenLLAKTGIIVAehsHDVQLDNEIGLFEKIKSETYGI 174
Cdd:COG2242  313 LPDPDAVfiggsgGNLPEILEACWA--RLRPGGRLVA---NAVTLETLALALEALAELGYGG 369
 
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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