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Conserved domains on  [gi|727165219|ref|WP_033636091|]
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MULTISPECIES: 23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG [Serratia]

Protein Classification

23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG( domain architecture ID 1001309)

23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG specifically methylates the guanine in position 1835 (m2G1835) of 23S rRNA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15001 super family cl33057
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
1-379 0e+00

23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;


The actual alignment was detected with superfamily member PRK15001:

Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 568.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219   1 MSQLDLGTQQLELERYPQQEESTQLQAWEAADEYLLQQLENVDIGGrPVLIFNDNFGTLACALHAHRPYSVSDSYMSQLA 80
Cdd:PRK15001   1 MSHLDNGFRSLTLQRFPATDDVNPLQAWEAADEYLLQQLDDTEIRG-PVLILNDAFGALSCALAEHKPYSIGDSYISELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219  81 TRHNLKLNGLDPEQVTLLDSLAELPAAPAVVLIRVPKALALLEQQLRALRHVVTEDTLIVAGAKARDVHTSTMQLFEKVL 160
Cdd:PRK15001  80 TRENLRLNGIDESSVKFLDSTADYPQQPGVVLIKVPKTLALLEQQLRALRKVVTSDTRIIAGAKARDIHTSTLELFEKVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 161 GPTRTSLAWKKARLIFCQAADIVPPAAAETTDWPLDGTDWLIHNHANVFSRGSLDIGARLFMEHLPRGLNGHIVDLGCGN 240
Cdd:PRK15001 160 GPTTTTLAWKKARLINCTFNEPPLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGN 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 241 GVIGLTALAQNPEAQVTFVDESYMAVASSELNVEHNLPQELDRCQFEVNNALAGIERESVQAVLCNPPFHQQHAITDHTA 320
Cdd:PRK15001 240 GVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVA 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 727165219 321 WQMFCDAKRCLQVGGELRIVGNRHLDYHQKLKRLFGNCTLVASNKKFVILRAVKSGARR 379
Cdd:PRK15001 320 WEMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVKLGRRR 378
 
Name Accession Description Interval E-value
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
1-379 0e+00

23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 568.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219   1 MSQLDLGTQQLELERYPQQEESTQLQAWEAADEYLLQQLENVDIGGrPVLIFNDNFGTLACALHAHRPYSVSDSYMSQLA 80
Cdd:PRK15001   1 MSHLDNGFRSLTLQRFPATDDVNPLQAWEAADEYLLQQLDDTEIRG-PVLILNDAFGALSCALAEHKPYSIGDSYISELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219  81 TRHNLKLNGLDPEQVTLLDSLAELPAAPAVVLIRVPKALALLEQQLRALRHVVTEDTLIVAGAKARDVHTSTMQLFEKVL 160
Cdd:PRK15001  80 TRENLRLNGIDESSVKFLDSTADYPQQPGVVLIKVPKTLALLEQQLRALRKVVTSDTRIIAGAKARDIHTSTLELFEKVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 161 GPTRTSLAWKKARLIFCQAADIVPPAAAETTDWPLDGTDWLIHNHANVFSRGSLDIGARLFMEHLPRGLNGHIVDLGCGN 240
Cdd:PRK15001 160 GPTTTTLAWKKARLINCTFNEPPLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGN 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 241 GVIGLTALAQNPEAQVTFVDESYMAVASSELNVEHNLPQELDRCQFEVNNALAGIERESVQAVLCNPPFHQQHAITDHTA 320
Cdd:PRK15001 240 GVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVA 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 727165219 321 WQMFCDAKRCLQVGGELRIVGNRHLDYHQKLKRLFGNCTLVASNKKFVILRAVKSGARR 379
Cdd:PRK15001 320 WEMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVKLGRRR 378
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
187-374 1.72e-88

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: 265.13  E-value: 1.72e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 187 AAETTDWP------LDGTDWLIHNHANVFSRGSLDIGARLFMEHLPRGLNGHIVDLGCGNGVIGLTALAQNPEAQVTFVD 260
Cdd:COG2813    1 APAASDWPrtitvrLAGRDLTFVTLPGVFSRDRLDIGTRLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 261 ESYMAVASSELNVEHNLpqeLDRCQFEVNNALAGIERESVQAVLCNPPFHQQHAITDHTAWQMFCDAKRCLQVGGELRIV 340
Cdd:COG2813   81 VNARAVELARANAAANG---LENVEVLWSDGLSGVPDGSFDLILSNPPFHAGRAVDKEVAHALIADAARHLRPGGELWLV 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 727165219 341 GNRHLDYHQKLKRLFGNCTLVASNKKFVILRAVK 374
Cdd:COG2813  158 ANRHLPYERKLEELFGNVEVLARNKGFKVLRAVK 191
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
199-371 6.51e-73

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: 224.39  E-value: 6.51e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219  199 DWLIHNHANVFSRGSLDIGARLFMEHLPRGLNGHIVDLGCGNGVIGLTALAQNPEAQVTFVDESYMAVASSELNVEHNLp 278
Cdd:pfam05175   1 ELTFKTLPGVFSHGRLDIGSRLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANG- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219  279 qeLDRCQFEVNNALAGIERESVQAVLCNPPFHQQHAITDHTAWQMFCDAKRCLQVGGELRIVGNRHLDYHQKLKRLFGNC 358
Cdd:pfam05175  80 --LENGEVVASDVYSGVEDGKFDLIISNPPFHAGLATTYNVAQRFIADAKRHLRPGGELWIVANRFLGYPPLLEELFGNV 157
                         170
                  ....*....|...
gi 727165219  359 TLVASNKKFVILR 371
Cdd:pfam05175 158 EVVAKTNGFKVLK 170
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
232-309 2.42e-07

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: 51.59  E-value: 2.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727165219  232 HIVDLGCGNGVIGLTALAQNPEAQVTFVDESYMAVASSELNVEHNlpQELDRCQFEVNNALAGIERESVQAVLCNPPF 309
Cdd:TIGR00536 117 HILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKN--QLEHRVEFIQSNLFEPLAGQKIDIIVSNPPY 192
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
233-337 2.86e-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: 45.50  E-value: 2.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 233 IVDLGCGNGVIGLtALAQNPEAQVTFVDESYMAVASSELNVEHNLPqelDRCQFEVNNALAGIER--ESVQAVLCNPPFH 310
Cdd:cd02440    2 VLDLGCGTGALAL-ALASGPGARVTGVDISPVALELARKAAAALLA---DNVEVLKGDAEELPPEadESFDVIISDPPLH 77
                         90       100
                 ....*....|....*....|....*..
gi 727165219 311 QQHaitdHTAWQMFCDAKRCLQVGGEL 337
Cdd:cd02440   78 HLV----EDLARFLEEARRLLKPGGVL 100
 
Name Accession Description Interval E-value
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
1-379 0e+00

23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 568.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219   1 MSQLDLGTQQLELERYPQQEESTQLQAWEAADEYLLQQLENVDIGGrPVLIFNDNFGTLACALHAHRPYSVSDSYMSQLA 80
Cdd:PRK15001   1 MSHLDNGFRSLTLQRFPATDDVNPLQAWEAADEYLLQQLDDTEIRG-PVLILNDAFGALSCALAEHKPYSIGDSYISELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219  81 TRHNLKLNGLDPEQVTLLDSLAELPAAPAVVLIRVPKALALLEQQLRALRHVVTEDTLIVAGAKARDVHTSTMQLFEKVL 160
Cdd:PRK15001  80 TRENLRLNGIDESSVKFLDSTADYPQQPGVVLIKVPKTLALLEQQLRALRKVVTSDTRIIAGAKARDIHTSTLELFEKVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 161 GPTRTSLAWKKARLIFCQAADIVPPAAAETTDWPLDGTDWLIHNHANVFSRGSLDIGARLFMEHLPRGLNGHIVDLGCGN 240
Cdd:PRK15001 160 GPTTTTLAWKKARLINCTFNEPPLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGN 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 241 GVIGLTALAQNPEAQVTFVDESYMAVASSELNVEHNLPQELDRCQFEVNNALAGIERESVQAVLCNPPFHQQHAITDHTA 320
Cdd:PRK15001 240 GVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVA 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 727165219 321 WQMFCDAKRCLQVGGELRIVGNRHLDYHQKLKRLFGNCTLVASNKKFVILRAVKSGARR 379
Cdd:PRK15001 320 WEMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVKLGRRR 378
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
187-374 1.72e-88

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: 265.13  E-value: 1.72e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 187 AAETTDWP------LDGTDWLIHNHANVFSRGSLDIGARLFMEHLPRGLNGHIVDLGCGNGVIGLTALAQNPEAQVTFVD 260
Cdd:COG2813    1 APAASDWPrtitvrLAGRDLTFVTLPGVFSRDRLDIGTRLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 261 ESYMAVASSELNVEHNLpqeLDRCQFEVNNALAGIERESVQAVLCNPPFHQQHAITDHTAWQMFCDAKRCLQVGGELRIV 340
Cdd:COG2813   81 VNARAVELARANAAANG---LENVEVLWSDGLSGVPDGSFDLILSNPPFHAGRAVDKEVAHALIADAARHLRPGGELWLV 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 727165219 341 GNRHLDYHQKLKRLFGNCTLVASNKKFVILRAVK 374
Cdd:COG2813  158 ANRHLPYERKLEELFGNVEVLARNKGFKVLRAVK 191
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
199-371 6.51e-73

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: 224.39  E-value: 6.51e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219  199 DWLIHNHANVFSRGSLDIGARLFMEHLPRGLNGHIVDLGCGNGVIGLTALAQNPEAQVTFVDESYMAVASSELNVEHNLp 278
Cdd:pfam05175   1 ELTFKTLPGVFSHGRLDIGSRLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANG- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219  279 qeLDRCQFEVNNALAGIERESVQAVLCNPPFHQQHAITDHTAWQMFCDAKRCLQVGGELRIVGNRHLDYHQKLKRLFGNC 358
Cdd:pfam05175  80 --LENGEVVASDVYSGVEDGKFDLIISNPPFHAGLATTYNVAQRFIADAKRHLRPGGELWIVANRFLGYPPLLEELFGNV 157
                         170
                  ....*....|...
gi 727165219  359 TLVASNKKFVILR 371
Cdd:pfam05175 158 EVVAKTNGFKVLK 170
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
208-379 3.47e-24

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 101.55  E-value: 3.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 208 VFSRGSLDIGARLFMEHLPRGLNGHIVDLGCGNGVIGlTALA-QNPEAQVTFVDESYMAVASSELNVEHNlpqeldRCQF 286
Cdd:PRK09489 175 VFSRDGLDVGSQLLLSTLTPHTKGKVLDVGCGAGVLS-AVLArHSPKIRLTLSDVSAAALESSRATLAAN------GLEG 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 287 EV--NNALAGIErESVQAVLCNPPFHQQHAITDHTAWQMFCDAKRCLQVGGELRIVGNRHLDYHQKLKRLFGNCTLVASN 364
Cdd:PRK09489 248 EVfaSNVFSDIK-GRFDMIISNPPFHDGIQTSLDAAQTLIRGAVRHLNSGGELRIVANAFLPYPDLLDETFGSHEVLAQT 326
                        170
                 ....*....|....*
gi 727165219 365 KKFVILRAVKSGARR 379
Cdd:PRK09489 327 GRFKVYRAIMTRQAK 341
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
223-308 2.82e-10

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 60.55  E-value: 2.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 223 EHLPRGLNGHIVDLGCGNGVIGLTALAQNPEAQVTFVDESYMAVASSELNVE-HNLPqelDRCQFEVNNALAGI-ERESV 300
Cdd:COG2890  106 ALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAErLGLE---DRVRFLQGDLFEPLpGDGRF 182

                 ....*...
gi 727165219 301 QAVLCNPP 308
Cdd:COG2890  183 DLIVSNPP 190
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
223-308 3.38e-10

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 60.18  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 223 EHLPRGLNGHIVDLGCGNGVIGLTALAQNPEAQVTFVDESYMAVASSELNVEHNLpqeLDRCQFEVNNALAGIERESVQA 302
Cdd:PRK09328 102 EALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGL---GARVEFLQGDWFEPLPGGRFDL 178

                 ....*.
gi 727165219 303 VLCNPP 308
Cdd:PRK09328 179 IVSNPP 184
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
230-376 1.97e-09

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: 57.46  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 230 NGHIVDLGCGNGVIGLtALAQ-NPEAQVTFV--DESY--MAVASSELNvehNLPqelDRCQFE---VNNALAGIERESVQ 301
Cdd:COG4123   38 GGRVLDLGTGTGVIAL-MLAQrSPGARITGVeiQPEAaeLARRNVALN---GLE---DRITVIhgdLKEFAAELPPGSFD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 302 AVLCNPPFH----------QQHAI---TDHTAWQMFCD-AKRCLQVGGELRIVgnrhLDYHQ--------KLKRLFGNC- 358
Cdd:COG4123  111 LVVSNPPYFkagsgrkspdEARAIarhEDALTLEDLIRaAARLLKPGGRFALI----HPAERlaeilaalRKYGLGPKRl 186
                        170       180
                 ....*....|....*....|..
gi 727165219 359 TLVASNK----KFVILRAVKSG 376
Cdd:COG4123  187 RPVHPRPgkpaKRVLLEARKGG 208
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
232-309 2.42e-07

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: 51.59  E-value: 2.42e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727165219  232 HIVDLGCGNGVIGLTALAQNPEAQVTFVDESYMAVASSELNVEHNlpQELDRCQFEVNNALAGIERESVQAVLCNPPF 309
Cdd:TIGR00536 117 HILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKN--QLEHRVEFIQSNLFEPLAGQKIDIIVSNPPY 192
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
233-335 5.03e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 47.56  E-value: 5.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219  233 IVDLGCGNGVIGLtALAQNPEAQVTFVDESYMAVASSELNVEHNLPqeldRCQFEVNNALA-GIERESVQAVLCNPPFhq 311
Cdd:pfam13649   1 VLDLGCGTGRLTL-ALARRGGARVTGVDLSPEMLERARERAAEAGL----NVEFVQGDAEDlPFPDGSFDLVVSSGVL-- 73
                          90       100
                  ....*....|....*....|....
gi 727165219  312 qHAITDHTAWQMFCDAKRCLQVGG 335
Cdd:pfam13649  74 -HHLPDPDLEAALREIARVLKPGG 96
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
215-309 2.13e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 47.98  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 215 DIGARLFMEHLPRGL--NGHIVDLGCGNGVIGLTALAQNPEaQVTFV--DESYMAVAsselnvEHNLPQELDRCQFEVNN 290
Cdd:COG2263   29 ELAAELLHLAYLRGDieGKTVLDLGCGTGMLAIGAALLGAK-KVVGVdiDPEALEIA------RENAERLGVRVDFIRAD 101
                         90
                 ....*....|....*....
gi 727165219 291 ALAGIERESVQAVLCNPPF 309
Cdd:COG2263  102 VTRIPLGGSVDTVVMNPPF 120
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
233-337 2.86e-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: 45.50  E-value: 2.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 233 IVDLGCGNGVIGLtALAQNPEAQVTFVDESYMAVASSELNVEHNLPqelDRCQFEVNNALAGIER--ESVQAVLCNPPFH 310
Cdd:cd02440    2 VLDLGCGTGALAL-ALASGPGARVTGVDISPVALELARKAAAALLA---DNVEVLKGDAEELPPEadESFDVIISDPPLH 77
                         90       100
                 ....*....|....*....|....*..
gi 727165219 311 QQHaitdHTAWQMFCDAKRCLQVGGEL 337
Cdd:cd02440   78 HLV----EDLARFLEEARRLLKPGGVL 100
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
230-306 1.20e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 40.58  E-value: 1.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727165219 230 NGHIVDLGCGNGVIGLTALAQNPEAQVTFVDesymavaSSELNVEHnLPQELDRCQFEVNNALAGIERESVQAVLCN 306
Cdd:COG4106    2 PRRVLDLGCGTGRLTALLAERFPGARVTGVD-------LSPEMLAR-ARARLPNVRFVVADLRDLDPPEPFDLVVSN 70
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
234-306 9.36e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.12  E-value: 9.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727165219  234 VDLGCGNGVIGLTALAQNPEAQVTFVDESYMAVASSELNVEHNLPQELDRCQFEVNNALAGiERESVQAVLCN 306
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGEL-DPGSFDVVVAS 72
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
230-310 2.20e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 38.17  E-value: 2.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219  230 NGHIVDLGCGNGVIGLtALAQ--NPEAQVTFVDESYMAVASSELNVEHNlpqELDRCQFEVNNALA---GIERESVQAVL 304
Cdd:pfam13847   4 GMRVLDLGCGTGHLSF-ELAEelGPNAEVVGIDISEEAIEKARENAQKL---GFDNVEFEQGDIEElpeLLEDDKFDVVI 79

                  ....*.
gi 727165219  305 CNPPFH 310
Cdd:pfam13847  80 SNCVLN 85
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
222-308 3.35e-03

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: 39.00  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 222 MEHLPRGLNGHIVDLGCGNGVIGLtALAQnPEAQVTFVDESYMAVASSELNVEHNlpqELDRCQFEVNNALAGIERESVQ 301
Cdd:COG2265  226 LEWLDLTGGERVLDLYCGVGTFAL-PLAR-RAKKVIGVEIVPEAVEDARENARLN---GLKNVEFVAGDLEEVLPELLWG 300
                         90
                 ....*....|.
gi 727165219 302 ----AVLCNPP 308
Cdd:COG2265  301 grpdVVVLDPP 311
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
233-309 3.62e-03

bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 39.46  E-value: 3.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727165219 233 IVDLGCGNGVIGLTALAQNPEAQVTFVDESYMAVASSELN-VEHNLPqelDRCQFEVNNALAGIERESVQAVLCNPPF 309
Cdd:PRK01544 142 ILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNaIKYEVT---DRIQIIHSNWFENIEKQKFDFIVSNPPY 216
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
216-310 4.89e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 37.97  E-value: 4.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 216 IGARLFMEHLPRGlnGHIVDLGCGNGVIgLTALAQNPEAQVTFVDESYMAVAsseLNVEHNLPQELDRCQFEVNNA--LA 293
Cdd:COG0500   15 AALLALLERLPKG--GRVLDLGCGTGRN-LLALAARFGGRVIGIDLSPEAIA---LARARAAKAGLGNVEFLVADLaeLD 88
                         90
                 ....*....|....*..
gi 727165219 294 GIERESVQAVLCNPPFH 310
Cdd:COG0500   89 PLPAESFDLVVAFGVLH 105
PRK14967 PRK14967
putative methyltransferase; Provisional
233-309 7.05e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 37.72  E-value: 7.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727165219 233 IVDLGCGNGVIGLTALAQNPeAQVTFVDESYMAVASSELN-VEHNLPQELDRCQFevnnaLAGIERESVQAVLCNPPF 309
Cdd:PRK14967  40 VLDLCTGSGALAVAAAAAGA-GSVTAVDISRRAVRSARLNaLLAGVDVDVRRGDW-----ARAVEFRPFDVVVSNPPY 111
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
36-148 7.12e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 38.02  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219   36 LQQLENVDIGGRPVLIFNDNFGTLACA---LHAHRPYSVSDSYMSQLATRHNLKLNGLDPE-QVTLldsLAELPAAPAVV 111
Cdd:pfam06325 152 LEALERLVKPGESVLDVGCGSGILAIAalkLGAKKVVGVDIDPVAVRAAKENAELNGVEARlEVYL---PGDLPKEKADV 228
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 727165219  112 LIRVPKALALLEQQLRALRHVVTEDTLIVAG---AKARDV 148
Cdd:pfam06325 229 VVANILADPLIELAPDIYALVKPGGYLILSGilkEQAQMV 268
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
218-340 7.97e-03

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: 36.51  E-value: 7.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165219 218 ARLFMEHLPRGLNGHIVDLGCGNGviGLTALAQNPEAQVTFVDESYMAVAsselNVEHNLPQELDRCQFEVNNALA-GIE 296
Cdd:COG2226   11 REALLAALGLRPGARVLDLGCGTG--RLALALAERGARVTGVDISPEMLE----LARERAAEAGLNVEFVVGDAEDlPFP 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 727165219 297 RESVQAVLCNPPFhqqHAITDHTAwqMFCDAKRCLQVGGELRIV 340
Cdd:COG2226   85 DGSFDLVISSFVL---HHLPDPER--ALAEIARVLKPGGRLVVV 123
 
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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