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Conserved domains on  [gi|1327149777|gb|PMN15670|]
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16S rRNA (guanine(966)-N(2))-methyltransferase RsmD [Vibrio lentus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
12-200 5.38e-98

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.).


The actual alignment was detected with superfamily member PRK10909:

Pssm-ID: 473071  Cd Length: 199  Bit Score: 282.38  E-value: 5.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  12 KKP---SGGFVRIISGSWRGRKLPVHDLEGLRPTIDRVKETLFNWVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLL 88
Cdd:PRK10909    3 KKPnhsGSGQIRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAPVIVDARCLDCFAGSGALGLEALSRYAAGATLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  89 EMNQKAAKQLADNAKELKADNINVVNTDAISFLKKPGTPYDMVFLDPPFRKGLLAETVELLESNGWLADNAIIYVETEKE 168
Cdd:PRK10909   83 EMDRAVAQQLIKNLATLKAGNARVVNTNALSFLAQPGTPHNVVFVDPPFRKGLLEETINLLEDNGWLADEALIYVESEVE 162
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1327149777 169 LQLEAMPENWELHRDKTTGQSSYRLFNRTTEE 200
Cdd:PRK10909  163 NGLPTVPANWQLHREKVAGQVAYRLYIREAQG 194
 
Name Accession Description Interval E-value
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
12-200 5.38e-98

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


Pssm-ID: 236793  Cd Length: 199  Bit Score: 282.38  E-value: 5.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  12 KKP---SGGFVRIISGSWRGRKLPVHDLEGLRPTIDRVKETLFNWVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLL 88
Cdd:PRK10909    3 KKPnhsGSGQIRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAPVIVDARCLDCFAGSGALGLEALSRYAAGATLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  89 EMNQKAAKQLADNAKELKADNINVVNTDAISFLKKPGTPYDMVFLDPPFRKGLLAETVELLESNGWLADNAIIYVETEKE 168
Cdd:PRK10909   83 EMDRAVAQQLIKNLATLKAGNARVVNTNALSFLAQPGTPHNVVFVDPPFRKGLLEETINLLEDNGWLADEALIYVESEVE 162
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1327149777 169 LQLEAMPENWELHRDKTTGQSSYRLFNRTTEE 200
Cdd:PRK10909  163 NGLPTVPANWQLHREKVAGQVAYRLYIREAQG 194
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
19-199 1.06e-91

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: 265.79  E-value: 1.06e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  19 VRIISGSWRGRKLPVHDLEGLRPTIDRVKETLFNWVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQL 98
Cdd:COG0742     1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNILGPDIEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAAAVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  99 ADNAKELKA-DNINVVNTDAISFLKK-PGTPYDMVFLDPPFRKGLLAETVELLESNGWLADNAIIYVETEKELQLEAMPE 176
Cdd:COG0742    81 RKNLEKLGLeDRARVIRGDALRFLKRlAGEPFDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSKREELPELPA 160
                         170       180
                  ....*....|....*....|...
gi 1327149777 177 NWELHRDKTTGQSSYRLFNRTTE 199
Cdd:COG0742   161 GLELLKERKYGDTRLSFYRREEE 183
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
19-194 3.39e-83

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 244.07  E-value: 3.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  19 VRIISGSWRGRKLPVHDLEGLRPTIDRVKETLFNWVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQL 98
Cdd:pfam03602   1 MRIIGGKARGRKLKVPPGPGTRPTTDRVREALFNWLAPYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  99 ADNAKELKADNINVVNTDAISFLKKPGT--PYDMVFLDPPFRKGLLAETVELLESNGWLADNAIIYVETEKELQLEAMPE 176
Cdd:pfam03602  81 KENLQLLGLPGAVLVMDALLALLRLAGKgpVFDIVFLDPPYAKGLIEEVLDLLAEKGWLKPNALIYVETEKRGELPEQPG 160
                         170
                  ....*....|....*...
gi 1327149777 177 NWELHRDKTTGQSSYRLF 194
Cdd:pfam03602 161 NLELVREKKYGQTTLAFY 178
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
13-194 3.79e-71

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: 214.20  E-value: 3.79e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  13 KPSGGFvRIISGSWRGRKLPVHDLEGLRPTIDRVKETLFNWVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLLEMNQ 92
Cdd:TIGR00095   5 SGSGKI-RIIGGQYRGRKLKVPPGPSTRPTTDRVRESLFNILRPDIVGAHFLDLFAGSGALGLEALSRGAASAVFVEQDR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  93 KAAKQLADNAKELKADNIN--VVNTD--AISFLKKPGTPYDMVFLDPPFRKGLLAETVELLESNGWLADNAIIYVETEKE 168
Cdd:TIGR00095  84 KVAQTLKENLSTLKKSGEQatVLNDAvrALLFLAKKQTPFDIIYLDPPFNRGLLEALLELLGENKWLNPKGLIVVEYDRE 163
                         170       180
                  ....*....|....*....|....*.
gi 1327149777 169 LQLEAMPENWELHRDKTTGQSSYRLF 194
Cdd:TIGR00095 164 NELPTVPETWSLLRQKVYGQSALRLY 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
62-155 2.64e-17

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: 73.62  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  62 TCLDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQLADNAKELKADNINVVNTDAISFLKKPGTPYDMVFLDPPF---- 137
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLhhlv 80
                          90       100
                  ....*....|....*....|
gi 1327149777 138 --RKGLLAETVELLESNGWL 155
Cdd:cd02440    81 edLARFLEEARRLLKPGGVL 100
 
Name Accession Description Interval E-value
rsmD PRK10909
16S rRNA m(2)G966-methyltransferase; Provisional
12-200 5.38e-98

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


Pssm-ID: 236793  Cd Length: 199  Bit Score: 282.38  E-value: 5.38e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  12 KKP---SGGFVRIISGSWRGRKLPVHDLEGLRPTIDRVKETLFNWVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLL 88
Cdd:PRK10909    3 KKPnhsGSGQIRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAPVIVDARCLDCFAGSGALGLEALSRYAAGATLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  89 EMNQKAAKQLADNAKELKADNINVVNTDAISFLKKPGTPYDMVFLDPPFRKGLLAETVELLESNGWLADNAIIYVETEKE 168
Cdd:PRK10909   83 EMDRAVAQQLIKNLATLKAGNARVVNTNALSFLAQPGTPHNVVFVDPPFRKGLLEETINLLEDNGWLADEALIYVESEVE 162
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1327149777 169 LQLEAMPENWELHRDKTTGQSSYRLFNRTTEE 200
Cdd:PRK10909  163 NGLPTVPANWQLHREKVAGQVAYRLYIREAQG 194
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
19-199 1.06e-91

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: 265.79  E-value: 1.06e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  19 VRIISGSWRGRKLPVHDLEGLRPTIDRVKETLFNWVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQL 98
Cdd:COG0742     1 MRIIGGKARGRKLKVPKGPGTRPTTDRVREALFNILGPDIEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAAAVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  99 ADNAKELKA-DNINVVNTDAISFLKK-PGTPYDMVFLDPPFRKGLLAETVELLESNGWLADNAIIYVETEKELQLEAMPE 176
Cdd:COG0742    81 RKNLEKLGLeDRARVIRGDALRFLKRlAGEPFDLVFLDPPYAKGLLEKALELLAENGLLAPGGLIVVEHSKREELPELPA 160
                         170       180
                  ....*....|....*....|...
gi 1327149777 177 NWELHRDKTTGQSSYRLFNRTTE 199
Cdd:COG0742   161 GLELLKERKYGDTRLSFYRREEE 183
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
19-194 3.39e-83

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 244.07  E-value: 3.39e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  19 VRIISGSWRGRKLPVHDLEGLRPTIDRVKETLFNWVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQL 98
Cdd:pfam03602   1 MRIIGGKARGRKLKVPPGPGTRPTTDRVREALFNWLAPYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQIL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  99 ADNAKELKADNINVVNTDAISFLKKPGT--PYDMVFLDPPFRKGLLAETVELLESNGWLADNAIIYVETEKELQLEAMPE 176
Cdd:pfam03602  81 KENLQLLGLPGAVLVMDALLALLRLAGKgpVFDIVFLDPPYAKGLIEEVLDLLAEKGWLKPNALIYVETEKRGELPEQPG 160
                         170
                  ....*....|....*...
gi 1327149777 177 NWELHRDKTTGQSSYRLF 194
Cdd:pfam03602 161 NLELVREKKYGQTTLAFY 178
TIGR00095 TIGR00095
16S rRNA (guanine(966)-N(2))-methyltransferase RsmD; This model represents a family of ...
13-194 3.79e-71

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: 214.20  E-value: 3.79e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  13 KPSGGFvRIISGSWRGRKLPVHDLEGLRPTIDRVKETLFNWVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLLEMNQ 92
Cdd:TIGR00095   5 SGSGKI-RIIGGQYRGRKLKVPPGPSTRPTTDRVRESLFNILRPDIVGAHFLDLFAGSGALGLEALSRGAASAVFVEQDR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  93 KAAKQLADNAKELKADNIN--VVNTD--AISFLKKPGTPYDMVFLDPPFRKGLLAETVELLESNGWLADNAIIYVETEKE 168
Cdd:TIGR00095  84 KVAQTLKENLSTLKKSGEQatVLNDAvrALLFLAKKQTPFDIIYLDPPFNRGLLEALLELLGENKWLNPKGLIVVEYDRE 163
                         170       180
                  ....*....|....*....|....*.
gi 1327149777 169 LQLEAMPENWELHRDKTTGQSSYRLF 194
Cdd:TIGR00095 164 NELPTVPETWSLLRQKVYGQSALRLY 189
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
62-155 2.64e-17

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: 73.62  E-value: 2.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  62 TCLDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQLADNAKELKADNINVVNTDAISFLKKPGTPYDMVFLDPPF---- 137
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLhhlv 80
                          90       100
                  ....*....|....*....|
gi 1327149777 138 --RKGLLAETVELLESNGWL 155
Cdd:cd02440    81 edLARFLEEARRLLKPGGVL 100
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
62-156 6.05e-08

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: 51.72  E-value: 6.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  62 TCLDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQLADNAKELK-ADNINVVNTDAISFLK---KPGTPYDMVFLDPP- 136
Cdd:COG1092   219 RVLNLFSYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNGlDDRHEFVQADAFDWLRelaREGERFDLIILDPPa 298
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1327149777 137 F---RKG----------LLAETVELLESNGWLA 156
Cdd:COG1092   299 FaksKKDlfdaqrdykdLNRLALKLLAPGGILV 331
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
50-156 1.02e-06

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: 46.87  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  50 LFNwVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVtLLEMNQKAAKQLADNAKELKADNINVVNTDAiSFLKKPGTPYD 129
Cdd:COG1041    18 LVN-LAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI-GSDIDPKMVEGARENLEHYGYEDADVIRGDA-RDLPLADESVD 94
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1327149777 130 MVFLDPPFR--------------KGLLAETVELLESNGWLA 156
Cdd:COG1041    95 AIVTDPPYGrsskisgeellelyEKALEEAARVLKPGGRVV 135
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
59-180 6.00e-06

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: 45.93  E-value: 6.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  59 PHSTCLDVFAGSGGLGFEAA--SRQAKlVTLLEMNQKAAKQLADNAKELKADNINVVNTDAISFLKKPGTPyDMVFL--D 134
Cdd:COG2242   247 PGDVLWDIGAGSGSVSIEAArlAPGGR-VYAIERDPERAALIRANARRFGVPNVEVVEGEAPEALADLPDP-DAVFIggS 324
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1327149777 135 PPFRKGLLAETVELLESNGWLADNAIIyVETEKEL--QLEAMPENWEL 180
Cdd:COG2242   325 GGNLPEILEACWARLRPGGRLVANAVT-LETLALAleALAELGYGGEL 371
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
34-139 6.52e-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: 45.14  E-value: 6.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  34 HDLEGLRPTIDRVkeTLFNWVAQDiPHSTCLDVFAGSGGLGFEAASRQAKL-VTLLEMNQKAAKQLADNAKELK-ADNIN 111
Cdd:COG4123    15 QPRCGYRFGTDAV--LLAAFAPVK-KGGRVLDLGTGTGVIALMLAQRSPGArITGVEIQPEAAELARRNVALNGlEDRIT 91
                          90       100       110
                  ....*....|....*....|....*....|
gi 1327149777 112 VVNTD--AISFLKKPGtPYDMVFLDPPFRK 139
Cdd:COG4123    92 VIHGDlkEFAAELPPG-SFDLVVSNPPYFK 120
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
55-152 1.09e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 44.64  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  55 AQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQLADNAKELK-ADNINVVNTDAISFLkkPGTPYDMV-- 131
Cdd:COG4076    31 RVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGlSDRITVINADATDLD--LPEKADVIis 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1327149777 132 ------FLDPP-------FRKGLLAE-----------TVELLESN 152
Cdd:COG4076   109 emldtaLLDEGqvpilnhARKRLLKPggriiperitnAAQPVESP 153
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
64-155 2.28e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 43.37  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  64 LDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQLADNAKELKADNINVVNTDAISFLKKPGTPYDMVF-------LDPP 136
Cdd:COG0500    31 LDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDPLPAESFDLVVafgvlhhLPPE 110
                          90
                  ....*....|....*....
gi 1327149777 137 FRKGLLAETVELLESNGWL 155
Cdd:COG0500   111 EREALLRELARALKPGGVL 129
Methyltrans_SAM pfam10672
S-adenosylmethionine-dependent methyltransferase; Members of this family are ...
53-145 4.38e-05

S-adenosylmethionine-dependent methyltransferase; Members of this family are S-adenosylmethionine-dependent methyltransferases from gamma-proteobacterial species. The diversity in the roles of methylation is matched by the almost bewildering number of methyltransferase enzymes that catalyze the methylation reaction. Although several classes of methyltransferase enzymes are known, the great majority of methylation reactions are catalyzed by the S-adenosylmethionine-dependent methyltransferases.


Pssm-ID: 287624 [Multi-domain]  Cd Length: 286  Bit Score: 42.94  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  53 WVAQDIPHSTCLDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQLADNAKeLKADNINVVNTDAISFLK-----KPGTP 127
Cdd:pfam10672 117 WVQENAKGKNVLNLFAYTCGFSVAAIAGGASQVVNVDMARGSLNKGRDNHR-LNGHDLGRVSFLGHDIFKswgkiKKLGP 195
                          90
                  ....*....|....*....
gi 1327149777 128 YDMVFLDPP-FRKGLLAET 145
Cdd:pfam10672 196 YDLVIIDPPsFQKGSFALT 214
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
48-155 4.96e-05

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: 41.16  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  48 ETLFNWVAQDIPH-STCLDVFAGSGGLGFEAASRQAKlVTLLEMNQKAAKQLADNAKELkadNINVVNTDAISfLKKPGT 126
Cdd:COG2227    12 RRLAALLARLLPAgGRVLDVGCGTGRLALALARRGAD-VTGVDISPEALEIARERAAEL---NVDFVQGDLED-LPLEDG 86
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1327149777 127 PYDMVFL--------DPpfrKGLLAETVELLESNGWL 155
Cdd:COG2227    87 SFDLVICsevlehlpDP---AALLRELARLLKPGGLL 120
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
64-155 7.24e-05

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: 41.42  E-value: 7.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  64 LDVFAGSGGLGFEAASRQAKL-VTLLEMNQKAAKQLADNAKELKADNINVVNTDAISFLKKpgTPYDMVFLDPPFRKG-- 140
Cdd:pfam05175  36 LDLGCGAGVLGAALAKESPDAeLTMVDINARALESARENLAANGLENGEVVASDVYSGVED--GKFDLIISNPPFHAGla 113
                          90       100
                  ....*....|....*....|...
gi 1327149777 141 --------LLAETVELLESNGWL 155
Cdd:pfam05175 114 ttynvaqrFIADAKRHLRPGGEL 136
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
76-160 8.30e-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: 41.32  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  76 EAASRQAKLVTLlEMNQKAAKQLADNAKELK-ADNINVVNTDAISFLKK-PGTPYDMVFLD--PPFRKGLLAETVELLES 151
Cdd:COG4122    36 RALPDDGRLTTI-EIDPERAAIARENFARAGlADRIRLILGDALEVLPRlADGPFDLVFIDadKSNYPDYLELALPLLRP 114
                          90
                  ....*....|
gi 1327149777 152 NGWL-ADNAI 160
Cdd:COG4122   115 GGLIvADNVL 124
PRK14968 PRK14968
putative methyltransferase; Provisional
54-137 1.00e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  54 VAQDIPHSTCLDVFAGSGGLGfEAASRQAKLVTLLEMNQKAAKQLADNAK--ELKADNINVVNTDAISFLKkpGTPYDMV 131
Cdd:PRK14968   18 NAVDKKGDRVLEVGTGSGIVA-IVAAKNGKKVVGVDINPYAVECAKCNAKlnNIRNNGVEVIRSDLFEPFR--GDKFDVI 94

                  ....*.
gi 1327149777 132 FLDPPF 137
Cdd:PRK14968   95 LFNPPY 100
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
52-162 1.23e-04

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


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 41.78  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  52 NWVAQDIPHSTcLDVFAGSGGLGFEAASRQAKlVTLLEMNQKA---AKQladNAKELKADNINVVNTDAISFLKKPGTPY 128
Cdd:PRK03522  167 DWVRELPPRSM-WDLFCGVGGFGLHCATPGMQ-LTGIEISAEAiacAKQ---SAAELGLTNVQFQALDSTQFATAQGEVP 241
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1327149777 129 DMVFLDPPfRKGLLAETVELLESngwLADNAIIY 162
Cdd:PRK03522  242 DLVLVNPP-RRGIGKELCDYLSQ---MAPRFILY 271
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
64-172 1.24e-04

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: 41.77  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  64 LDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQLADNAKELK-ADNINVVNTDAISFLKKPGTPYDMVFLD-PPFRKGL 141
Cdd:COG2520   185 LDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLKENIRLNKvEDRVTPILGDAREVAPELEGKADRIIMNlPHSADEF 264
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1327149777 142 LAETVELLESNGWLadnaIIYVETEKELQLE 172
Cdd:COG2520   265 LDAALRALKPGGVI----HYYEIVPEEDPFE 291
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
64-153 1.62e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.08  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  64 LDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQLADNAKELKAdNINVVNTDAISfLKKPGTPYDMVF-------LDPP 136
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAED-LPFPDGSFDLVVssgvlhhLPDP 79
                          90
                  ....*....|....*..
gi 1327149777 137 FRKGLLAETVELLESNG 153
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
59-156 8.69e-04

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: 38.05  E-value: 8.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  59 PHSTCLDVFAGSGGLGFEAASRQAKlVTLLEMNQKAAKQLADNAKElKADNINVVNTDA--ISFlkkPGTPYDMVFL--- 133
Cdd:COG2226    22 PGARVLDLGCGTGRLALALAERGAR-VTGVDISPEMLELARERAAE-AGLNVEFVVGDAedLPF---PDGSFDLVISsfv 96
                          90       100
                  ....*....|....*....|....*...
gi 1327149777 134 -----DPPfrkGLLAETVELLESNGWLA 156
Cdd:COG2226    97 lhhlpDPE---RALAEIARVLKPGGRLV 121
PRK14967 PRK14967
putative methyltransferase; Provisional
58-137 1.38e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 38.11  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  58 IPHSTCLDVFAGSGGLGFEAASRQAKLVTLLEMNQKAAKQLADNAKeLKADNINVVNTDAISFLkkPGTPYDMVFLDPPF 137
Cdd:PRK14967   35 GPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNAL-LAGVDVDVRRGDWARAV--EFRPFDVVVSNPPY 111
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
101-136 2.73e-03

Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 37.92  E-value: 2.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1327149777 101 NAKELKADNINVVNTDAISFLKKPGTPYDMVFLDPP 136
Cdd:COG4262   336 NGGALNDPRVTVVNADAFQFLRETDEKYDVIIVDLP 371
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
64-134 2.99e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 36.63  E-value: 2.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327149777  64 LDVFAGSGGLGFEAASR---QAKlVTLLEMNQKAAKQLADNAKELKADNINVVNTDAISFLK-KPGTPYDMVFLD 134
Cdd:pfam13847   8 LDLGCGTGHLSFELAEElgpNAE-VVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPElLEDDKFDVVISN 81
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
61-113 3.17e-03

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 36.90  E-value: 3.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1327149777  61 STCLDVFAGSGGLGFEAASRQAKL-VTLLEMNQKAAKQLADNAKELKADNINVV 113
Cdd:PRK08287   33 KHLIDVGAGTGSVSIEAALQFPSLqVTAIERNPDALRLIKENRQRFGCGNIDII 86
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
64-145 3.57e-03

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 37.59  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327149777  64 LDVFAGSG--GLGFEAASRQAKlVTLLEMNQKAAKQLADNAKELKADNINVVNTDAISFLKKPGtPYDMVFLDP-----P 136
Cdd:PRK04338   62 LDALSASGirGIRYALETGVEK-VTLNDINPDAVELIKKNLELNGLENEKVFNKDANALLHEER-KFDVVDIDPfgspaP 139
                          90
                  ....*....|....*...
gi 1327149777 137 F---------RKGLLAET 145
Cdd:PRK04338  140 FldsairsvkRGGLLCVT 157
 
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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