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Conserved domains on  [gi|504410466|ref|WP_014597568|]
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50S ribosomal protein L11 methyltransferase [Stutzerimonas stutzeri]

Protein Classification

50S ribosomal protein L11 methyltransferase( domain architecture ID 12069797)

50S ribosomal protein L11 methyltransferase is a class I SAM-dependent methyltransferase that methylates ribosomal protein L11 using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168
PubMed:  17215866|18611379|12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 3-291 6.14e-141

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: 398.56  E-value: 6.14e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466    3 WLQIRLAITPDHAEALEDQLLQLGAVSVTFMDA---EDQPIFEPDLNTTPLWSHTHLLALFEADTDTDALLAHLQLLRGG 79
Cdd:pfam06325   2 WLELSIHTTREAAEPVSNILEEFGALGVAIEDAdllEDRDIFEPGLGEERLWDEVRVKALFDEETDALELIAQLAELIGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466   80 -DLPEHQTEVIEDQDWERSWMDNFQPMRFGHRLWIVPSWHAAPE-PDAVNLLLDPGLAFGTGTHPTTALCLEWLDAQTLD 157
Cdd:pfam06325  82 lDSPKVTVEEVAEEDWARAWKKYFHPVRIGERLTIVPSWEDYPEnPDALNIELDPGMAFGTGTHPTTKLCLEALERLVKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  158 DRSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIApERFTLYLPEQLPQEPADVVVANILAGPLVS 237
Cdd:pfam06325 162 GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVE-ARLEVYLPGDLPKEKADVVVANILADPLIE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504410466  238 LAQQITALVKPGGRLALSGILAEQADEVRAAYSGAFDLDPTADKDGWVRISGVR 291
Cdd:pfam06325 241 LAPDIYALVKPGGYLILSGILKEQAQMVAEAYSQGFELITVEHREEWVCIVGKK 294
 
Name Accession Description Interval E-value
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 3-291 6.14e-141

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: 398.56  E-value: 6.14e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466    3 WLQIRLAITPDHAEALEDQLLQLGAVSVTFMDA---EDQPIFEPDLNTTPLWSHTHLLALFEADTDTDALLAHLQLLRGG 79
Cdd:pfam06325   2 WLELSIHTTREAAEPVSNILEEFGALGVAIEDAdllEDRDIFEPGLGEERLWDEVRVKALFDEETDALELIAQLAELIGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466   80 -DLPEHQTEVIEDQDWERSWMDNFQPMRFGHRLWIVPSWHAAPE-PDAVNLLLDPGLAFGTGTHPTTALCLEWLDAQTLD 157
Cdd:pfam06325  82 lDSPKVTVEEVAEEDWARAWKKYFHPVRIGERLTIVPSWEDYPEnPDALNIELDPGMAFGTGTHPTTKLCLEALERLVKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  158 DRSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIApERFTLYLPEQLPQEPADVVVANILAGPLVS 237
Cdd:pfam06325 162 GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVE-ARLEVYLPGDLPKEKADVVVANILADPLIE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504410466  238 LAQQITALVKPGGRLALSGILAEQADEVRAAYSGAFDLDPTADKDGWVRISGVR 291
Cdd:pfam06325 241 LAPDIYALVKPGGYLILSGILKEQAQMVAEAYSQGFELITVEHREEWVCIVGKK 294
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
1-292 4.81e-136

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 386.07  E-value: 4.81e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466   1 MSWLQIRLAITPDHAEALEDQLLQLGAVSVTFMDAEDqpifepdlnttPLWSHTHLLALFEADTDTDALLAHL-QLLRGG 79
Cdd:COG2264    1 MKWIELTITTPEEAAEALSDALEELGAEGVEIEDAPP-----------GLWERVGVKAYFPEDEDLEELLAALaEALGEL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  80 DLPEHQTEVIEDQDWERSWMDNFQPMRFGHRLWIVPSWHAA-PEPDAVNLLLDPGLAFGTGTHPTTALCLEWLDAQTLDD 158
Cdd:COG2264   70 GAPEITVEEVEEEDWVEEWKKYFKPIRVGDRLVIVPSWEEYePDPGEIVIEIDPGMAFGTGTHPTTRLCLEALEKLLKPG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 159 RSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIApERFTLYLPEQLPQEPADVVVANILAGPLVSL 238
Cdd:COG2264  150 KTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVE-DRIEVVLGDLLEDGPYDLVVANILANPLIEL 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504410466 239 AQQITALVKPGGRLALSGILAEQADEVRAAYSGA-FDLDPTADKDGWVRISGVRR 292
Cdd:COG2264  229 APDLAALLKPGGYLILSGILEEQADEVLAAYEAAgFELVERRERGEWVALVLRKK 283
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
1-292 1.26e-125

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 358.31  E-value: 1.26e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466   1 MSWLQIRLAITPDHAEALEDQLLQLGAVsvtfmdaedqpifepdlnttplwshthllalfeadtdtDALLAHLQLLRGGD 80
Cdd:PRK00517   1 MKWIELTLNTTPEAAEALSDILMELGAL--------------------------------------AALANLAGLGLDLG 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  81 LPEHQTEVIEDQDWERSWMDNFQPMRFGHRLWIVPSWHAAPEPDAVNLLLDPGLAFGTGTHPTTALCLEWLDAQTLDDRS 160
Cdd:PRK00517  43 EPTYTIEEVEDEDWEREWKKYFHPIRIGDRLWIVPSWEDPPDPDEINIELDPGMAFGTGTHPTTRLCLEALEKLVLPGKT 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 161 LLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIapeRFTLYLPEQlpQEPADVVVANILAGPLVSLAQ 240
Cdd:PRK00517 123 VLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGV---ELNVYLPQG--DLKADVIVANILANPLLELAP 197

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504410466 241 QITALVKPGGRLALSGILAEQADEVRAAYSGA-FDLDPTADKDGWVRISGVRR 292
Cdd:PRK00517 198 DLARLLKPGGRLILSGILEEQADEVLEAYEEAgFTLDEVLERGEWVALVGKKK 250
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 3-285 1.20e-105

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 309.07  E-value: 1.20e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466    3 WLQIRLAITPDHAEALEDQLLQLGAVSVTFMDAEDQPIFEPDL-NTTPLWSHTHLLALFEADTDTDALLAHLQLLRGGDL 81
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFEDDKDTIYFEPHLpGEKRLWGNLDVIALFDAETDMNNSVIPLLEAFCLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466   82 PE-HQTEVIE-DQDWERSWMDNFQPMRFGHRLWIVPSWHAAPE-PDAVNLLLDPGLAFGTGTHPTTALCLEWLDAQTLDD 158
Cdd:TIGR00406  81 GRnHKIEFDEfSKDWERAWKDNFHPVQFGKRFWICPSWRDVPSdEDALIIMLDPGLAFGTGTHPTTSLCLEWLEDLDLKD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  159 RSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIaPERFTLYLP--EQLPQEPADVVVANILAGPLV 236
Cdd:TIGR00406 161 KNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQV-SDRLQVKLIylEQPIEGKADVIVANILAEVIK 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 504410466  237 SLAQQITALVKPGGRLALSGILAEQADEVRAAYSGAFDLDPTADKDGWV 285
Cdd:TIGR00406 240 ELYPQFSRLVKPGGWLILSGILETQAQSVCDAYEQGFTVVEIRQREEWC 288
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 161-259 8.38e-10

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: 55.13  E-value: 8.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 161 LLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIAPERF---TLYLPEQLPQEPADVVVANILAGPLV- 236
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVlkgDAEELPPEADESFDVIISDPPLHHLVe 81

                         90       100
                 ....*....|....*....|....*.
gi 504410466 237 ---SLAQQITALVKPGGRLALSGILA 259
Cdd:cd02440   82 dlaRFLEEARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 3-291 6.14e-141

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: 398.56  E-value: 6.14e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466    3 WLQIRLAITPDHAEALEDQLLQLGAVSVTFMDA---EDQPIFEPDLNTTPLWSHTHLLALFEADTDTDALLAHLQLLRGG 79
Cdd:pfam06325   2 WLELSIHTTREAAEPVSNILEEFGALGVAIEDAdllEDRDIFEPGLGEERLWDEVRVKALFDEETDALELIAQLAELIGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466   80 -DLPEHQTEVIEDQDWERSWMDNFQPMRFGHRLWIVPSWHAAPE-PDAVNLLLDPGLAFGTGTHPTTALCLEWLDAQTLD 157
Cdd:pfam06325  82 lDSPKVTVEEVAEEDWARAWKKYFHPVRIGERLTIVPSWEDYPEnPDALNIELDPGMAFGTGTHPTTKLCLEALERLVKP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  158 DRSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIApERFTLYLPEQLPQEPADVVVANILAGPLVS 237
Cdd:pfam06325 162 GESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVE-ARLEVYLPGDLPKEKADVVVANILADPLIE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504410466  238 LAQQITALVKPGGRLALSGILAEQADEVRAAYSGAFDLDPTADKDGWVRISGVR 291
Cdd:pfam06325 241 LAPDIYALVKPGGYLILSGILKEQAQMVAEAYSQGFELITVEHREEWVCIVGKK 294
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
1-292 4.81e-136

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 386.07  E-value: 4.81e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466   1 MSWLQIRLAITPDHAEALEDQLLQLGAVSVTFMDAEDqpifepdlnttPLWSHTHLLALFEADTDTDALLAHL-QLLRGG 79
Cdd:COG2264    1 MKWIELTITTPEEAAEALSDALEELGAEGVEIEDAPP-----------GLWERVGVKAYFPEDEDLEELLAALaEALGEL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  80 DLPEHQTEVIEDQDWERSWMDNFQPMRFGHRLWIVPSWHAA-PEPDAVNLLLDPGLAFGTGTHPTTALCLEWLDAQTLDD 158
Cdd:COG2264   70 GAPEITVEEVEEEDWVEEWKKYFKPIRVGDRLVIVPSWEEYePDPGEIVIEIDPGMAFGTGTHPTTRLCLEALEKLLKPG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 159 RSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIApERFTLYLPEQLPQEPADVVVANILAGPLVSL 238
Cdd:COG2264  150 KTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVE-DRIEVVLGDLLEDGPYDLVVANILANPLIEL 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504410466 239 AQQITALVKPGGRLALSGILAEQADEVRAAYSGA-FDLDPTADKDGWVRISGVRR 292
Cdd:COG2264  229 APDLAALLKPGGYLILSGILEEQADEVLAAYEAAgFELVERRERGEWVALVLRKK 283
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
1-292 1.26e-125

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 358.31  E-value: 1.26e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466   1 MSWLQIRLAITPDHAEALEDQLLQLGAVsvtfmdaedqpifepdlnttplwshthllalfeadtdtDALLAHLQLLRGGD 80
Cdd:PRK00517   1 MKWIELTLNTTPEAAEALSDILMELGAL--------------------------------------AALANLAGLGLDLG 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  81 LPEHQTEVIEDQDWERSWMDNFQPMRFGHRLWIVPSWHAAPEPDAVNLLLDPGLAFGTGTHPTTALCLEWLDAQTLDDRS 160
Cdd:PRK00517  43 EPTYTIEEVEDEDWEREWKKYFHPIRIGDRLWIVPSWEDPPDPDEINIELDPGMAFGTGTHPTTRLCLEALEKLVLPGKT 122

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 161 LLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIapeRFTLYLPEQlpQEPADVVVANILAGPLVSLAQ 240
Cdd:PRK00517 123 VLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGV---ELNVYLPQG--DLKADVIVANILANPLLELAP 197

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504410466 241 QITALVKPGGRLALSGILAEQADEVRAAYSGA-FDLDPTADKDGWVRISGVRR 292
Cdd:PRK00517 198 DLARLLKPGGRLILSGILEEQADEVLEAYEEAgFTLDEVLERGEWVALVGKKK 250
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 3-285 1.20e-105

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 309.07  E-value: 1.20e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466    3 WLQIRLAITPDHAEALEDQLLQLGAVSVTFMDAEDQPIFEPDL-NTTPLWSHTHLLALFEADTDTDALLAHLQLLRGGDL 81
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFEDDKDTIYFEPHLpGEKRLWGNLDVIALFDAETDMNNSVIPLLEAFCLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466   82 PE-HQTEVIE-DQDWERSWMDNFQPMRFGHRLWIVPSWHAAPE-PDAVNLLLDPGLAFGTGTHPTTALCLEWLDAQTLDD 158
Cdd:TIGR00406  81 GRnHKIEFDEfSKDWERAWKDNFHPVQFGKRFWICPSWRDVPSdEDALIIMLDPGLAFGTGTHPTTSLCLEWLEDLDLKD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  159 RSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIaPERFTLYLP--EQLPQEPADVVVANILAGPLV 236
Cdd:TIGR00406 161 KNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQV-SDRLQVKLIylEQPIEGKADVIVANILAEVIK 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 504410466  237 SLAQQITALVKPGGRLALSGILAEQADEVRAAYSGAFDLDPTADKDGWV 285
Cdd:TIGR00406 240 ELYPQFSRLVKPGGWLILSGILETQAQSVCDAYEQGFTVVEIRQREEWC 288
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 151-251 7.46e-13

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 66.06  E-value: 7.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 151 LDAQTLDDRSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIAPERFTLYLPEQLPQEPADVVVA-N 229
Cdd:COG3897   64 LDHPEVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPAAGGFDLILGgD 143

                         90       100
                 ....*....|....*....|....*..
gi 504410466 230 IL-----AGPLVSLaqqITALVKPGGR 251
Cdd:COG3897  144 VLyerdlAEPLLPF---LDRLAAPGGE 167
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 149-255 7.70e-13

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: 64.27  E-value: 7.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 149 EWLDAQTLDDRSLLDFGCGSGILAIAGLLLGaHQAVGTDIDPQALEASRDNAERNGIAPERFTLY-LPeqLPQEPADVVV 227
Cdd:COG2227   16 ALLARLLPAGGRVLDVGCGTGRLALALARRG-ADVTGVDISPEALEIARERAAELNVDFVQGDLEdLP--LEDGSFDLVI 92

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504410466 228 ANILAGPL---VSLAQQITALVKPGGRLALS 255
Cdd:COG2227   93 CSEVLEHLpdpAALLRELARLLKPGGLLLLS 123
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
156-229 2.15e-12

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 64.54  E-value: 2.15e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504410466 156 LDDRSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGiAPERFTLYLPEQLP-QEPADVVVAN 229
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAERLG-VRVDFIRADVTRIPlGGSVDTVVMN 117
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 130-252 6.12e-12

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: 63.29  E-value: 6.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 130 LDPGlafgtgthptTALCLEWLDAQtlDDRSLLDFGCGSGILAIAGLLLGAHQAV-GTDIDPQALEASRDNAERNGIAPE 208
Cdd:COG2813   34 LDIG----------TRLLLEHLPEP--LGGRVLDLGCGYGVIGLALAKRNPEARVtLVDVNARAVELARANAAANGLENV 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504410466 209 RFTL-YLPEQLPQEPADVVVAN--ILAGPLV--SLAQQI-----TALvKPGGRL 252
Cdd:COG2813  102 EVLWsDGLSGVPDGSFDLILSNppFHAGRAVdkEVAHALiadaaRHL-RPGGEL 154
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 159-268 1.06e-11

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: 63.24  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 159 RSLLDFGCGSGILAiagLLLGAH----QAVGTDIDPQALEASRDNAERNGIApERFTLY------LPEQLPQEPADVVVA 228
Cdd:COG4123   39 GRVLDLGTGTGVIA---LMLAQRspgaRITGVEIQPEAAELARRNVALNGLE-DRITVIhgdlkeFAAELPPGSFDLVVS 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504410466 229 N----------------------ILAGPLVSLAQQITALVKPGGRLALsgIL-AEQADEVRAA 268
Cdd:COG4123  115 NppyfkagsgrkspdearaiarhEDALTLEDLIRAAARLLKPGGRFAL--IHpAERLAEILAA 175
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 149-292 1.10e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 62.63  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 149 EWLDAQTLD-DRSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIAPERF---TLYLPEQLPQEPAD 224
Cdd:COG0500   17 LLALLERLPkGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFlvaDLAELDPLPAESFD 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504410466 225 VVVAN-----ILAGPLVSLAQQITALVKPGGRLALSGILAEQAdEVRAAYSGAFDLDPTADKDGWVRISGVRR 292
Cdd:COG0500   97 LVVAFgvlhhLPPEEREALLRELARALKPGGVLLLSASDAAAA-LSLARLLLLATASLLELLLLLRLLALELY 168
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 161-267 3.83e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.43  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  161 LLDFGCGSGILA--IAGLLLGAHQAVGTDIDPQALEASRDNAERNGIapERFTLY------LPEQLPQEPADVVVAN--I 230
Cdd:pfam13847   7 VLDLGCGTGHLSfeLAEELGPNAEVVGIDISEEAIEKARENAQKLGF--DNVEFEqgdieeLPELLEDDKFDVVISNcvL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 504410466  231 LAGPLVSLA-QQITALVKPGGRLALS--GILAEQADEVRA 267
Cdd:pfam13847  85 NHIPDPDKVlQEILRVLKPGGRLIISdpDSLAELPAHVKE 124
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 130-252 4.07e-10

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: 57.60  E-value: 4.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  130 LDPGlafgtgthptTALCLEWLDaqTLDDRSLLDFGCGSGILAIAGLLLGAHQAV-GTDIDPQALEASRDNAERNGIAPE 208
Cdd:pfam05175  16 LDIG----------SRLLLEHLP--KDLSGKVLDLGCGAGVLGAALAKESPDAELtMVDINARALESARENLAANGLENG 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 504410466  209 RF---TLYlpEQLPQEPADVVVAN--ILAG--PLVSLAQQITA----LVKPGGRL 252
Cdd:pfam05175  84 EVvasDVY--SGVEDGKFDLIISNppFHAGlaTTYNVAQRFIAdakrHLRPGGEL 136
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 161-259 8.38e-10

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: 55.13  E-value: 8.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 161 LLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIAPERF---TLYLPEQLPQEPADVVVANILAGPLV- 236
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVlkgDAEELPPEADESFDVIISDPPLHHLVe 81

                         90       100
                 ....*....|....*....|....*.
gi 504410466 237 ---SLAQQITALVKPGGRLALSGILA 259
Cdd:cd02440   82 dlaRFLEEARRLLKPGGVLVLTLVLA 107
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 148-293 9.52e-10

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 58.24  E-value: 9.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 148 LEWLDAQTldDRSLLDFGCGSGILAIAgLLLGAHQA--VGTDIDPQALEASRDNAERNGIApERFTLY---LPEQLPQ-E 221
Cdd:COG2890  105 LALLPAGA--PPRVLDLGTGSGAIALA-LAKERPDArvTAVDISPDALAVARRNAERLGLE-DRVRFLqgdLFEPLPGdG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 222 PADVVVAN---------------------ILAgpLVS----------LAQQITALVKPGGRLALSgILAEQADEVRAAYS 270
Cdd:COG2890  181 RFDLIVSNppyipedeiallppevrdhepRLA--LDGgedgldfyrrIIAQAPRLLKPGGWLLLE-IGEDQGEAVRALLE 257

                        170       180
                 ....*....|....*....|....*
gi 504410466 271 GAFDLDPTADKD--GWVRISGVRRS 293
Cdd:COG2890  258 AAGFADVETHKDlaGRDRVVVARRP 282
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 162-250 3.44e-09

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 52.95  E-value: 3.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  162 LDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIAPErFTLYLPEQLPQEPA--DVVVAN----ILAGP- 234
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVE-FVQGDAEDLPFPDGsfDLVVSSgvlhHLPDPd 80

                          90
                  ....*....|....*.
gi 504410466  235 LVSLAQQITALVKPGG 250
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 162-292 6.66e-09

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 55.55  E-value: 6.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 162 LDFGCGSGILAIAgLLLGAHQA--VGTDIDPQALEASRDNAERNGIApeRFTLY---LPEQLPQEPADVVVAN------- 229
Cdd:PRK09328 113 LDLGTGSGAIALA-LAKERPDAevTAVDISPEALAVARRNAKHGLGA--RVEFLqgdWFEPLPGGRFDLIVSNppyipea 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 230 ---ILAG------PLVSL-------------AQQITALVKPGGRLALSgILAEQADEVRAAYSGAFDLDPTADKD--GWV 285
Cdd:PRK09328 190 dihLLQPevrdhePHLALfggedgldfyrriIEQAPRYLKPGGWLLLE-IGYDQGEAVRALLAAAGFADVETRKDlaGRD 268


                 ....*..
gi 504410466 286 RISGVRR 292
Cdd:PRK09328 269 RVVLGRR 275
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 162-252 7.41e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 52.37  E-value: 7.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  162 LDFGCGSGIL--AIAGLLLGAHQaVGTDIDPQALEASRDNAERNG---IAPERFTLYLPEQLPQEPADVVVANIL---AG 233
Cdd:pfam08242   1 LEIGCGTGTLlrALLEALPGLEY-TGLDISPAALEAARERLAALGllnAVRVELFQLDLGELDPGSFDVVVASNVlhhLA 79

                          90
                  ....*....|....*....
gi 504410466  234 PLVSLAQQITALVKPGGRL 252
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 148-229 9.07e-09

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 55.57  E-value: 9.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 148 LEWLDAQtlDDRSLLDFGCGSGILAIAgLLLGAHQAVGTDIDPQALEASRDNAERNGIAPERF-----TLYLPEQLPQEP 222
Cdd:COG2265  226 LEWLDLT--GGERVLDLYCGVGTFALP-LARRAKKVIGVEIVPEAVEDARENARLNGLKNVEFvagdlEEVLPELLWGGR 302


                 ....*..
gi 504410466 223 ADVVVAN 229
Cdd:COG2265  303 PDVVVLD 309
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 153-254 2.05e-08

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: 52.64  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 153 AQTLDDRSLLDFGCGSGILAIAGLLLGAHqAVGTDIDPQALEASRDNAERNGIapERFTLY------LPeqLPQEPADVV 226
Cdd:COG1041   22 AGAKEGDTVLDPFCGTGTILIEAGLLGRR-VIGSDIDPKMVEGARENLEHYGY--EDADVIrgdardLP--LADESVDAI 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 504410466 227 VAN--------ILAGPLVSLAQQITA----LVKPGGRLAL 254
Cdd:COG1041   97 VTDppygrsskISGEELLELYEKALEeaarVLKPGGRVVI 136
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 148-267 4.05e-08

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: 51.15  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 148 LEWLDAQtlDDRSLLDFGCGSGILAIAgLLLGAHQAVGTDIDPQALEASRDNAERNGIAPErFTLYLPEQLPQEPA--DV 225
Cdd:COG2226   15 LAALGLR--PGARVLDLGCGTGRLALA-LAERGARVTGVDISPEMLELARERAAEAGLNVE-FVVGDAEDLPFPDGsfDL 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 504410466 226 VVAN---ILAGPLVSLAQQITALVKPGGRLALSGILAEQADEVRA 267
Cdd:COG2226   91 VISSfvlHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEE 135
PRK14968 PRK14968
putative methyltransferase; Provisional
 153-205 4.42e-08

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 52.21  E-value: 4.42e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504410466 153 AQTLDDR---SLLDFGCGSGILAIAgLLLGAHQAVGTDIDPQALEASRDNAERNGI 205
Cdd:PRK14968  16 AENAVDKkgdRVLEVGTGSGIVAIV-AAKNGKKVVGVDINPYAVECAKCNAKLNNI 70
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
158-255 2.60e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.90  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 158 DRSLLDFGCGSGIL--AIAGLLLGAHqAVGTDIDPQALEASRDNAERNGIAPERFTlylpEQLPQEPADVVVAN-IL--A 232
Cdd:COG4106    2 PRRVLDLGCGTGRLtaLLAERFPGAR-VTGVDLSPEMLARARARLPNVRFVVADLR----DLDPPEPFDLVVSNaALhwL 76

                         90       100
                 ....*....|....*....|...
gi 504410466 233 GPLVSLAQQITALVKPGGRLALS 255
Cdd:COG4106   77 PDHAALLARLAAALAPGGVLAVQ 99
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 162-254 3.38e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 47.27  E-value: 3.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  162 LDFGCGSGILAIAgLLLGAHQAVGTDIDPQALEASRDNAERNGIAPERFTLylpEQLPQEPA--DVVVANILAG---PLV 236
Cdd:pfam08241   1 LDVGCGTGLLTEL-LARLGARVTGVDISPEMLELAREKAPREGLTFVVGDA---EDLPFPDNsfDLVLSSEVLHhveDPE 76

                          90
                  ....*....|....*...
gi 504410466  237 SLAQQITALVKPGGRLAL 254
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 131-254 4.27e-07

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 48.77  E-value: 4.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 131 DPGLAFGTGTHPTTALCLEWLDAQtlDDRSLLDFGCGSGILAI-AGLLLGAHqAVGTDIDPQALEASRDNAERNGIApER 209
Cdd:COG2230   27 DPDDTLEEAQEAKLDLILRKLGLK--PGMRVLDIGCGWGGLALyLARRYGVR-VTGVTLSPEQLEYARERAAEAGLA-DR 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504410466 210 FTLYL---PEQLPQEPADVVVAN-----ILAGPLVSLAQQITALVKPGGRLAL 254
Cdd:COG2230  103 VEVRLadyRDLPADGQFDAIVSIgmfehVGPENYPAYFAKVARLLKPGGRLLL 155
arsM PRK11873
arsenite methyltransferase;
162-271 5.01e-07

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 49.95  E-value: 5.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 162 LDFGCGSGILAiaglLLGAHQ------AVGTDIDPQALEASRDNAERNGIAPERFTL----YLPeqLPQEPADVVVANI- 230
Cdd:PRK11873  82 LDLGSGGGFDC----FLAARRvgptgkVIGVDMTPEMLAKARANARKAGYTNVEFRLgeieALP--VADNSVDVIISNCv 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 504410466 231 --LAGPLVSLAQQITALVKPGGRLALSGI--LAEQADEVR---AAYSG 271
Cdd:PRK11873 156 inLSPDKERVFKEAFRVLKPGGRFAISDVvlRGELPEEIRndaELYAG 203
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
151-252 1.14e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 48.49  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 151 LDAQTLDDRSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIApER--------FTLYLPeqlpqEP 222
Cdd:COG4076   29 IERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLS-DRitvinadaTDLDLP-----EK 102

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 504410466 223 ADVVVANILAGPLVS------LAQQITALVKPGGRL 252
Cdd:COG4076  103 ADVIISEMLDTALLDegqvpiLNHARKRLLKPGGRI 138
PRK14967 PRK14967
putative methyltransferase; Provisional
 159-229 4.77e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 46.58  E-value: 4.77e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504410466 159 RSLLDFGCGSGILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIAPERFTLYLPEQLPQEPADVVVAN 229
Cdd:PRK14967  38 RRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDVDVRRGDWARAVEFRPFDVVVSN 108
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 157-255 1.10e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 44.73  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  157 DDRSLLDFGCGSGILAIaglLLGAHQAVGTDIDPqaleaSRDNAERNGIAPERFTLYLPEQL-PQEPADVVVANILAG-- 233
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLR---LLRAQGFSVTGVDP-----SPIAIERALLNVRFDQFDEQEAAvPAGKFDVIVAREVLEhv 93

                          90       100
                  ....*....|....*....|...
gi 504410466  234 -PLVSLAQQITALVKPGGRLALS 255
Cdd:pfam13489  94 pDPPALLRQIAALLKPGGLLLLS 116
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
158-255 1.13e-05

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 44.99  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 158 DRSLLDFGCGSGILAIAgLLLGAHQAVGTDIDPQALEAsrdnAERNGIAPERFTLYLPE-QLPQEPADVVVAN---ILAG 233
Cdd:COG4976   47 FGRVLDLGCGTGLLGEA-LRPRGYRLTGVDLSEEMLAK----AREKGVYDRLLVADLADlAEPDGRFDLIVAAdvlTYLG 121

                         90       100
                 ....*....|....*....|..
gi 504410466 234 PLVSLAQQITALVKPGGRLALS 255
Cdd:COG4976  122 DLAAVFAGVARALKPGGLFIFS 143
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 157-206 1.26e-05

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


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 45.04  E-value: 1.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504410466  157 DDRSLLDFGCGSGILAIAGLLLGAHQA------------VGTDIDPQALEASRDNAERNGIA 206
Cdd:pfam01170  28 PGDPLLDPMCGSGTILIEAALMGANIApgkfdarvraplYGSDIDRRMVQGARLNAENAGVG 89
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 161-262 2.81e-05

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 44.02  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 161 LLDFGCGSGILAI-AGLLLGAHQAV-GTDIDPQALEASRDNAERNGIApERFTLY---LPEQLPQEPADVVVANILAGP- 234
Cdd:PRK00377  44 ILDIGCGTGSVTVeASLLVGETGKVyAVDKDEKAINLTRRNAEKFGVL-NNIVLIkgeAPEILFTINEKFDRIFIGGGSe 122

                         90       100
                 ....*....|....*....|....*....
gi 504410466 235 -LVSLAQQITALVKPGGRLALSGILAEQA 262
Cdd:PRK00377 123 kLKEIISASWEIIKKGGRIVIDAILLETV 151
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 112-263 1.10e-04

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 43.20  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 112 WIVPSWHAAPEPDAVNL----LLDPglaFGTGTHPttalcleWLDAQTLDDRSLLDFGCGS-GILAIAGL-LLGAHQAVG 185
Cdd:COG1063  122 VRVPAANLVKVPDGLSDeaaaLVEP---LAVALHA-------VERAGVKPGDTVLVIGAGPiGLLAALAArLAGAARVIV 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 186 TDIDPQALEAsrdnAERNGI------APERFTLYLPEQLPQEPADVVvanILAGPLVSLAQQITALVKPGGRLALSGILA 259
Cdd:COG1063  192 VDRNPERLEL----ARELGAdavvnpREEDLVEAVRELTGGRGADVV---IEAVGAPAALEQALDLVRPGGTVVLVGVPG 264


                 ....
gi 504410466 260 EQAD 263
Cdd:COG1063  265 GPVP 268
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 164-263 1.16e-04

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 43.00  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 164 FGCGS-GILAIA-GLLLGAHqAVGTDIDPQALEASRD-NAERNGIAPERFTLYLPEQLPQEPADVVVANILAGPLVSLAQ 240
Cdd:cd08254  172 IGLGGlGLNAVQiAKAMGAA-VIAVDIKEEKLELAKElGADEVLNSLDDSPKDKKAAGLGGGFDVIFDFVGTQPTFEDAQ 250

                         90       100
                 ....*....|....*....|...
gi 504410466 241 QitaLVKPGGRLALSGILAEQAD 263
Cdd:cd08254  251 K---AVKPGGRIVVVGLGRDKLT 270
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 148-227 1.99e-04

23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA methyltransferases by homology to the TrmA family. The member from E. coli has now been shown to act as the 23S RNA methyltransferase for the conserved U1939. The gene is now designated rumA and was previously designated ygcA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 42.50  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466  148 LEWLDAQTLDdrSLLDFGCGSGILAIAgLLLGAHQAVGTDIDPQALEASRDNAERNGIA-PERFTLYLPEQLPQEP---- 222
Cdd:TIGR00479 285 LEWLELQGEE--RVLDAYCGMGTFTLP-LAKQAKSVVGVEGVPESVEKAQQNAELNGIAnVTFYHGTLETVLPKQPwagn 361


                  ....*.
gi 504410466  223 -ADVVV 227
Cdd:TIGR00479 362 gFDKVL 367
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 147-292 6.57e-04

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 40.71  E-value: 6.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 147 CLEWLDAQTLDDR--SLLDFGCGSG--ILAIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIAPERFTLY----LPEQL 218
Cdd:COG5459   68 ALAELAEAGPDFAplTVLDVGAGPGtaAWAAADAWPSLLDATLLERSAAALALGRRLARAAANPALETAEWrladLAAAL 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504410466 219 PQEPAD-VVVANILAGplvslaqqitalVKPGGRLALsgilaeqADEVRAAYSGAFDLDPTADKDGWVRISGVRR 292
Cdd:COG5459  148 PAPPADlVVASYVLNE------------LADAARAAL-------VDRLWLAPDGALLIVEPGTPAGSRRLLAARD 203
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 155-270 7.23e-04

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 40.67  E-value: 7.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 155 TLDDRSLLdFGCGS-GILAIAGL-LLGAHQAVGTDIDPQALEASRDNAERNGIAPERFTLYLP-EQLPQEPADVVVanIL 231
Cdd:cd08236  158 TLGDTVVV-IGAGTiGLLAIQWLkILGAKRVIAVDIDDEKLAVARELGADDTINPKEEDVEKVrELTEGRGADLVI--EA 234

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 504410466 232 AGPLVSLAQQItALVKPGGRLALSGILAEQADEVRAAYS 270
Cdd:cd08236  235 AGSPATIEQAL-ALARPGGKVVLVGIPYGDVTLSEEAFE 272
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 148-206 9.05e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 39.82  E-value: 9.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 148 LEWLDAQT-LDDRSLLDFGCGSGILAIAGLLLGAHqAVGTDIDPQALEASRDNAERNGIA 206
Cdd:PRK07580  53 LSWLPADGdLTGLRILDAGCGVGSLSIPLARRGAK-VVASDISPQMVEEARERAPEAGLA 111
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 172-255 2.05e-03

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: 39.39  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 172 AIAGLLLGAHQAVGTDIDPQALEASRDNAERNGIApERFTL-------YLpEQLPQEPA--DVVV-------------AN 229
Cdd:COG1092  231 SVHAAAGGAKSVTSVDLSATALEWAKENAALNGLD-DRHEFvqadafdWL-RELAREGErfDLIIldppafakskkdlFD 308

                         90       100
                 ....*....|....*....|....*.
gi 504410466 230 ILAGpLVSLAQQITALVKPGGRLALS 255
Cdd:COG1092  309 AQRD-YKDLNRLALKLLAPGGILVTS 333
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 158-229 3.32e-03

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 38.54  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504410466 158 DRSLLDFGCGSGILAIAGLLLGAHQA---------------------------------------VGTDIDPQALEASRD 198
Cdd:COG0116  189 DRPLVDPMCGSGTILIEAALIAANIApglnrdfafekwpdfdaelwqelreeaearikrdpplpiFGSDIDPRAIEAARE 268

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504410466 199 NAERNGIAPE-RFtlylpEQL------PQEPADVVVAN 229
Cdd:COG0116  269 NAERAGVADLiEF-----EQAdfrdlePPAEPGLIITN 301
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 148-206 6.56e-03

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 37.09  E-value: 6.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504410466  148 LEWLDAQTLDDRSLLDFGCGSGILAIAGLLLGAHqAVGTDIDPQALEASRDNAERNGIA 206
Cdd:TIGR02021  46 LDWLPKDPLKGKRVLDAGCGTGLLSIELAKRGAI-VKAVDISEQMVQMARNRAQGRDVA 103
 
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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