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Conserved domains on  [gi|445940840|ref|WP_000018695|]
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MULTISPECIES: 23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG [Enterobacteriaceae]

Protein Classification

23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG( domain architecture ID 11487560)

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 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
1-378 0e+00

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


:

Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 826.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840   1 MSHLDNGFRSLTLQRFPATDDVNPLQAWEAADEYLLQQLDDTEIRGPVLILNDAFGALSCALAEHKPYSIGDSYISELAT 80
Cdd:PRK15001   1 MSHLDNGFRSLTLQRFPATDDVNPLQAWEAADEYLLQQLDDTEIRGPVLILNDAFGALSCALAEHKPYSIGDSYISELAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840  81 RENLRLNGIDESSVKFLDSTADYPQQPGVVLIKVPKTLALLEQQLRALRKVVTSDTRIIAGAKARDIHTSTLELFEKVLG 160
Cdd:PRK15001  81 RENLRLNGIDESSVKFLDSTADYPQQPGVVLIKVPKTLALLEQQLRALRKVVTSDTRIIAGAKARDIHTSTLELFEKVLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 161 PTTTTLAWKKARLINCTFNEPQLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNG 240
Cdd:PRK15001 161 PTTTTLAWKKARLINCTFNEPPLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 241 VIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAW 320
Cdd:PRK15001 241 VIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAW 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 445940840 321 EMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVKLGRRR 378
Cdd:PRK15001 321 EMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVKLGRRR 378
 
Name Accession Description Interval E-value
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
1-378 0e+00

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 826.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840   1 MSHLDNGFRSLTLQRFPATDDVNPLQAWEAADEYLLQQLDDTEIRGPVLILNDAFGALSCALAEHKPYSIGDSYISELAT 80
Cdd:PRK15001   1 MSHLDNGFRSLTLQRFPATDDVNPLQAWEAADEYLLQQLDDTEIRGPVLILNDAFGALSCALAEHKPYSIGDSYISELAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840  81 RENLRLNGIDESSVKFLDSTADYPQQPGVVLIKVPKTLALLEQQLRALRKVVTSDTRIIAGAKARDIHTSTLELFEKVLG 160
Cdd:PRK15001  81 RENLRLNGIDESSVKFLDSTADYPQQPGVVLIKVPKTLALLEQQLRALRKVVTSDTRIIAGAKARDIHTSTLELFEKVLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 161 PTTTTLAWKKARLINCTFNEPQLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNG 240
Cdd:PRK15001 161 PTTTTLAWKKARLINCTFNEPPLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 241 VIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAW 320
Cdd:PRK15001 241 VIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAW 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 445940840 321 EMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVKLGRRR 378
Cdd:PRK15001 321 EMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVKLGRRR 378
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
180-373 1.63e-91

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: 272.83  E-value: 1.63e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 180 EPQLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVD 259
Cdd:COG2813    1 APAASDWPRTITVRLAGRDLTFVTLPGVFSRDRLDIGTRLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 260 ESPMAVASSRLNVETNmpeALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAWEMFHHARRCLKINGELYIV 339
Cdd:COG2813   81 VNARAVELARANAAAN---GLENVEVLWSDGLSGVPDGSFDLILSNPPFHAGRAVDKEVAHALIADAARHLRPGGELWLV 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 445940840 340 ANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVK 373
Cdd:COG2813  158 ANRHLPYERKLEELFGNVEVLARNKGFKVLRAVK 191
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
198-370 3.49e-80

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: 242.88  E-value: 3.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840  198 DWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNmp 277
Cdd:pfam05175   1 ELTFKTLPGVFSHGRLDIGSRLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAAN-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840  278 eALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAWEMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNC 357
Cdd:pfam05175  79 -GLENGEVVASDVYSGVEDGKFDLIISNPPFHAGLATTYNVAQRFIADAKRHLRPGGELWIVANRFLGYPPLLEELFGNV 157
                         170
                  ....*....|...
gi 445940840  358 TTIATNNKFVVLK 370
Cdd:pfam05175 158 EVVAKTNGFKVLK 170
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
232-339 1.21e-07

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: 49.35  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 232 IVDLGCGNGVIGLTLLdKNPQAKVVFVDESPMAVASSRLNVETNmpeALDRCEFMINNALSGV--EPFRFNAVLCNPPFH 309
Cdd:cd02440    2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAAL---LADNVEVLKGDAEELPpeADESFDVIISDPPLH 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 445940840 310 QQHALtdnvAWEMFHHARRCLKINGELYIV 339
Cdd:cd02440   78 HLVED----LARFLEEARRLLKPGGVLVLT 103
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
231-308 2.83e-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: 2.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445940840  231 EIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEalDRCEFMINNALSGVEPFRFNAVLCNPPF 308
Cdd:TIGR00536 117 HILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLE--HRVEFIQSNLFEPLAGQKIDIIVSNPPY 192
 
Name Accession Description Interval E-value
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
1-378 0e+00

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 826.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840   1 MSHLDNGFRSLTLQRFPATDDVNPLQAWEAADEYLLQQLDDTEIRGPVLILNDAFGALSCALAEHKPYSIGDSYISELAT 80
Cdd:PRK15001   1 MSHLDNGFRSLTLQRFPATDDVNPLQAWEAADEYLLQQLDDTEIRGPVLILNDAFGALSCALAEHKPYSIGDSYISELAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840  81 RENLRLNGIDESSVKFLDSTADYPQQPGVVLIKVPKTLALLEQQLRALRKVVTSDTRIIAGAKARDIHTSTLELFEKVLG 160
Cdd:PRK15001  81 RENLRLNGIDESSVKFLDSTADYPQQPGVVLIKVPKTLALLEQQLRALRKVVTSDTRIIAGAKARDIHTSTLELFEKVLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 161 PTTTTLAWKKARLINCTFNEPQLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNG 240
Cdd:PRK15001 161 PTTTTLAWKKARLINCTFNEPPLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 241 VIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAW 320
Cdd:PRK15001 241 VIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAW 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 445940840 321 EMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVKLGRRR 378
Cdd:PRK15001 321 EMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVKLGRRR 378
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
180-373 1.63e-91

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: 272.83  E-value: 1.63e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 180 EPQLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVD 259
Cdd:COG2813    1 APAASDWPRTITVRLAGRDLTFVTLPGVFSRDRLDIGTRLLLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPEARVTLVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 260 ESPMAVASSRLNVETNmpeALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAWEMFHHARRCLKINGELYIV 339
Cdd:COG2813   81 VNARAVELARANAAAN---GLENVEVLWSDGLSGVPDGSFDLILSNPPFHAGRAVDKEVAHALIADAARHLRPGGELWLV 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 445940840 340 ANRHLDYFHKLKKIFGNCTTIATNNKFVVLKAVK 373
Cdd:COG2813  158 ANRHLPYERKLEELFGNVEVLARNKGFKVLRAVK 191
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
198-370 3.49e-80

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: 242.88  E-value: 3.49e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840  198 DWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNmp 277
Cdd:pfam05175   1 ELTFKTLPGVFSHGRLDIGSRLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAAN-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840  278 eALDRCEFMINNALSGVEPFRFNAVLCNPPFHQQHALTDNVAWEMFHHARRCLKINGELYIVANRHLDYFHKLKKIFGNC 357
Cdd:pfam05175  79 -GLENGEVVASDVYSGVEDGKFDLIISNPPFHAGLATTYNVAQRFIADAKRHLRPGGELWIVANRFLGYPPLLEELFGNV 157
                         170
                  ....*....|...
gi 445940840  358 TTIATNNKFVVLK 370
Cdd:pfam05175 158 EVVAKTNGFKVLK 170
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
198-377 3.71e-30

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 118.12  E-value: 3.71e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 198 DWTIHNHANVFSRTGLDIGARFFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMP 277
Cdd:PRK09489 166 GLTVKTLPGVFSRDGLDVGSQLLLSTLTPHTKGKVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATLAANGL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 278 EAldrcEFMINNALSGVEPfRFNAVLCNPPFHQ--QHALTdnVAWEMFHHARRCLKINGELYIVANRHLDYFHKLKKIFG 355
Cdd:PRK09489 246 EG----EVFASNVFSDIKG-RFDMIISNPPFHDgiQTSLD--AAQTLIRGAVRHLNSGGELRIVANAFLPYPDLLDETFG 318
                        170       180
                 ....*....|....*....|..
gi 445940840 356 NCTTIATNNKFVVLKAVkLGRR 377
Cdd:PRK09489 319 SHEVLAQTGRFKVYRAI-MTRQ 339
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
232-338 1.89e-13

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 69.81  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNmpeALDRCEFMINNALSGVEPFRFNAVLCNPP---F 308
Cdd:PRK09328 112 VLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHG---LGARVEFLQGDWFEPLPGGRFDLIVSNPPyipE 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 445940840 309 HQQHALTDNVA-WE-----------------MFHHARRCLKINGELYI 338
Cdd:PRK09328 189 ADIHLLQPEVRdHEphlalfggedgldfyrrIIEQAPRYLKPGGWLLL 236
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
232-352 3.79e-13

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: 68.25  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEalDRCEFM---INNALSGVEPFRFNAVLCNPPF 308
Cdd:COG4123   41 VLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLE--DRITVIhgdLKEFAAELPPGSFDLVVSNPPY 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445940840 309 HQQ---------------HALTDNVAwEMFHHARRCLKINGELYIV--ANRHLDYFHKLKK 352
Cdd:COG4123  119 FKAgsgrkspdearaiarHEDALTLE-DLIRAAARLLKPGGRFALIhpAERLAEILAALRK 178
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
222-307 5.04e-12

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 65.56  E-value: 5.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 222 QHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNmpEALDRCEFMINNALSGVEPF-RFN 300
Cdd:COG2890  106 ALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERL--GLEDRVRFLQGDLFEPLPGDgRFD 183

                 ....*..
gi 445940840 301 AVLCNPP 307
Cdd:COG2890  184 LIVSNPP 190
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
232-334 1.91e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 54.11  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840  232 IVDLGCGNGVIGLTLLDKnPQAKVVFVDESPMAVASSRLNVETNMPealdRCEFMINNALS-GVEPFRFNAVLCNPPFhq 310
Cdd:pfam13649   1 VLDLGCGTGRLTLALARR-GGARVTGVDLSPEMLERARERAAEAGL----NVEFVQGDAEDlPFPDGSFDLVVSSGVL-- 73
                          90       100
                  ....*....|....*....|....
gi 445940840  311 qHALTDNVAWEMFHHARRCLKING 334
Cdd:pfam13649  74 -HHLPDPDLEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
232-339 1.40e-08

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 51.75  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRlnvetnmpEALDRCEFMINNALSGVEPFRFNAVLCNPPFH-- 309
Cdd:COG4106    5 VLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARAR--------ARLPNVRFVVADLRDLDPPEPFDLVVSNAALHwl 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 445940840 310 QQHAltdnvawEMFHHARRCLKINGELYIV 339
Cdd:COG4106   77 PDHA-------ALLARLAAALAPGGVLAVQ 99
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
233-336 2.67e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 51.21  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840  233 VDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEALDRCEFmINNALSGVEPFRFNAVLCNppfHQQH 312
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVEL-FQLDLGELDPGSFDVVVAS---NVLH 76
                          90       100
                  ....*....|....*....|....
gi 445940840  313 ALTDnvAWEMFHHARRCLKINGEL 336
Cdd:pfam08242  77 HLAD--PRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
232-339 1.21e-07

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: 49.35  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 232 IVDLGCGNGVIGLTLLdKNPQAKVVFVDESPMAVASSRLNVETNmpeALDRCEFMINNALSGV--EPFRFNAVLCNPPFH 309
Cdd:cd02440    2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAAL---LADNVEVLKGDAEELPpeADESFDVIISDPPLH 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 445940840 310 QQHALtdnvAWEMFHHARRCLKINGELYIV 339
Cdd:cd02440   78 HLVED----LARFLEEARRLLKPGGVLVLT 103
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
231-308 2.83e-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: 2.83e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445940840  231 EIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNMPEalDRCEFMINNALSGVEPFRFNAVLCNPPF 308
Cdd:TIGR00536 117 HILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLE--HRVEFIQSNLFEPLAGQKIDIIVSNPPY 192
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
232-352 3.03e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.64  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840  232 IVDLGCGNGVIGLTLLDK-NPQAKVVFVDESPMAVASSRLNVETNmpeALDRCEFM---INNALSGVEPFRFNAVLCNPP 307
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKL---GFDNVEFEqgdIEELPELLEDDKFDVVISNCV 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 445940840  308 FHQQhALTDNVAWEMFhharRCLKINGELYIV-ANRHLDYFHKLKK 352
Cdd:pfam13847  84 LNHI-PDPDKVLQEIL----RVLKPGGRLIISdPDSLAELPAHVKE 124
PRK14968 PRK14968
putative methyltransferase; Provisional
224-308 4.81e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 46.82  E-value: 4.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 224 LPENL---EGEIV-DLGCGNGVIGLTLLDKNpqAKVVFVDESPMAVASSRLNVETNMPEALDrCEFMINNALSGVEPFRF 299
Cdd:PRK14968  15 LAENAvdkKGDRVlEVGTGSGIVAIVAAKNG--KKVVGVDINPYAVECAKCNAKLNNIRNNG-VEVIRSDLFEPFRGDKF 91

                 ....*....
gi 445940840 300 NAVLCNPPF 308
Cdd:PRK14968  92 DVILFNPPY 100
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
217-338 9.39e-06

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: 44.62  E-value: 9.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 217 ARFFMQHLPENleGEIVDLGCGNGVIGLTLLDKNpqAKVVFVDESPMAVASSRLNVETNmpealdRCEFMINNALS-GVE 295
Cdd:COG2227   15 AALLARLLPAG--GRVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIARERAAEL------NVDFVQGDLEDlPLE 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 445940840 296 PFRFNAVLCNPPFHqqHaLTDnvAWEMFHHARRCLKINGELYI 338
Cdd:COG2227   85 DGSFDLVICSEVLE--H-LPD--PAALLRELARLLKPGGLLLL 122
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
210-308 2.90e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.51  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 210 RTGLDIGARFFMQ-HLPENLEGE-IVDLGCGNGVIGLTLLDKNPQaKVVFVDESPMAVASSRLNVETNMPEAldrcEFMI 287
Cdd:COG2263   25 PTPAELAAELLHLaYLRGDIEGKtVLDLGCGTGMLAIGAALLGAK-KVVGVDIDPEALEIARENAERLGVRV----DFIR 99
                         90       100
                 ....*....|....*....|.
gi 445940840 288 NNALSGVEPFRFNAVLCNPPF 308
Cdd:COG2263  100 ADVTRIPLGGSVDTVVMNPPF 120
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
217-339 4.02e-05

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: 43.06  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 217 ARFFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNpqAKVVFVDESPMAVASSRlnveTNMPEALDRCEFMINNALSgvEP 296
Cdd:COG2226   11 REALLAALGLRPGARVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELAR----ERAAEAGLNVEFVVGDAED--LP 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 445940840 297 FR---FNAVLCNPPFhqqHALTDNVAweMFHHARRCLKINGELYIV 339
Cdd:COG2226   83 FPdgsFDLVISSFVL---HHLPDPER--ALAEIARVLKPGGRLVVV 123
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
232-307 6.28e-05

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 44.78  E-value: 6.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 232 IVDLGCGNGVIGLTLLDKnpQAKVVFVDESPMAVASSRLNVETNmpeALDRCEF-------MINNALSGvepFRFNAVLC 304
Cdd:COG2265  237 VLDLYCGVGTFALPLARR--AKKVIGVEIVPEAVEDARENARLN---GLKNVEFvagdleeVLPELLWG---GRPDVVVL 308

                 ...
gi 445940840 305 NPP 307
Cdd:COG2265  309 DPP 311
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
215-346 1.37e-04

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 42.60  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 215 IGARFFMQHLPENleGEIVDLGCGNGVIgLTLLDKNPQAKVVFVDESPMAVASSRlnvETNMPEALDRCEFmINNALSGV 294
Cdd:COG0500   15 AALLALLERLPKG--GRVLDLGCGTGRN-LLALAARFGGRVIGIDLSPEAIALAR---ARAAKAGLGNVEF-LVADLAEL 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 445940840 295 EPF---RFNAVLCNPPFH-QQHALTDnvawEMFHHARRCLKINGELYIVANRHLDY 346
Cdd:COG0500   88 DPLpaeSFDLVVAFGVLHhLPPEERE----ALLRELARALKPGGVLLLSASDAAAA 139
PRK14967 PRK14967
putative methyltransferase; Provisional
186-308 1.94e-04

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 42.35  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 186 APQTVSWKLegtdwtihnhANVFSRTGLDIGARffmqhlpenlegeIVDLGCGNGVIGLTLLDKNPqAKVVFVDESPMAV 265
Cdd:PRK14967  17 RPQEDTQLL----------ADALAAEGLGPGRR-------------VLDLCTGSGALAVAAAAAGA-GSVTAVDISRRAV 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 445940840 266 ASSRLNVETN-MPEALDRCEFminnaLSGVEPFRFNAVLCNPPF 308
Cdd:PRK14967  73 RSARLNALLAgVDVDVRRGDW-----ARAVEFRPFDVVVSNPPY 111
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
217-353 3.07e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 38.44  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 217 ARFFMQHLPENLEGEIVDLGCGNGVIGLTLLDKnpQAKVVFVDESPMAVASSRlnvETNMPEALDRCEFminNALSgVEP 296
Cdd:COG4976   35 AEELLARLPPGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKAR---EKGVYDRLLVADL---ADLA-EPD 105
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 445940840 297 FRFNAVLCNPPFHQQHALTdnvawEMFHHARRCLKINGELYIVANRH---LDYFHKLKKI 353
Cdd:COG4976  106 GRFDLIVAADVLTYLGDLA-----AVFAGVARALKPGGLFIFSVEDAdgsGRYAHSLDYV 160
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
228-275 4.09e-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: 38.79  E-value: 4.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 445940840  228 LEGEIV-DLGCGNGV--IGLTLLDKnpqAKVVFVDESPMAVASSRLNVETN 275
Cdd:pfam06325 160 KPGESVlDVGCGSGIlaIAALKLGA---KKVVGVDIDPVAVRAAKENAELN 207
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
232-308 6.53e-03

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 38.31  E-value: 6.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 445940840 232 IVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRLNVETNmpEALDRCEFMINNALSGVEPFRFNAVLCNPPF 308
Cdd:PRK01544 142 ILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKY--EVTDRIQIIHSNWFENIEKQKFDFIVSNPPY 216
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
217-289 7.99e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 37.62  E-value: 7.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445940840 217 ARFFMQHLPENLEGEIVDLGCGNGVIGLTLLDKNPQAKVVFVDESPMAVASSRlnvetnmpEALDRCEFMINN 289
Cdd:PRK01683  20 ARDLLARVPLENPRYVVDLGCGPGNSTELLVERWPAARITGIDSSPAMLAEAR--------SRLPDCQFVEAD 84
 
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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