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Conserved domains on  [gi|515409154|ref|WP_016898196|]
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MULTISPECIES: 50S ribosomal protein L11 methyltransferase [Staphylococcus]

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 ...
 2-309 2.49e-120

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: 347.33  E-value: 2.49e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154    2 NWTELSIVVNHDVEFEVTEILEDHGSNGVVIEDSRDLEtpPSDKFGeiYELNPEDYPSsGVRLKAYFNELTFNDELRKSI 81
Cdd:pfam06325   1 TWLELSIHTTREAAEPVSNILEEFGALGVAIEDADLLE--DRDIFE--PGLGEERLWD-EVRVKALFDEETDALELIAQL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154   82 KNNILNvsnLDKGVLTFSEkgIAEKDWANEWKNYFRPFKASNRFTIVPSWETYtKENSDELCIELDPGMAFGTGDHPTTS 161
Cdd:pfam06325  76 AELIGG---LDSPKVTVEE--VAEEDWARAWKKYFHPVRIGERLTIVPSWEDY-PENPDALNIELDPGMAFGTGTHPTTK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  162 MCLKAIEEYVQTTDSIIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEA-VPGNLLkeeKEKY 240
Cdd:pfam06325 150 LCLEALERLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVyLPGDLP---KEKA 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515409154  241 NIVIANILAHIIEEMIEDAYNTLFEEGYFITSGIIEEKYEEIESHMKRvGFNIISVEHDNGWVCIVGQK 309
Cdd:pfam06325 227 DVVVANILADPLIELAPDIYALVKPGGYLILSGILKEQAQMVAEAYSQ-GFELITVEHREEWVCIVGKK 294
 
Name Accession Description Interval E-value
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 2-309 2.49e-120

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: 347.33  E-value: 2.49e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154    2 NWTELSIVVNHDVEFEVTEILEDHGSNGVVIEDSRDLEtpPSDKFGeiYELNPEDYPSsGVRLKAYFNELTFNDELRKSI 81
Cdd:pfam06325   1 TWLELSIHTTREAAEPVSNILEEFGALGVAIEDADLLE--DRDIFE--PGLGEERLWD-EVRVKALFDEETDALELIAQL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154   82 KNNILNvsnLDKGVLTFSEkgIAEKDWANEWKNYFRPFKASNRFTIVPSWETYtKENSDELCIELDPGMAFGTGDHPTTS 161
Cdd:pfam06325  76 AELIGG---LDSPKVTVEE--VAEEDWARAWKKYFHPVRIGERLTIVPSWEDY-PENPDALNIELDPGMAFGTGTHPTTK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  162 MCLKAIEEYVQTTDSIIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEA-VPGNLLkeeKEKY 240
Cdd:pfam06325 150 LCLEALERLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVyLPGDLP---KEKA 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515409154  241 NIVIANILAHIIEEMIEDAYNTLFEEGYFITSGIIEEKYEEIESHMKRvGFNIISVEHDNGWVCIVGQK 309
Cdd:pfam06325 227 DVVVANILADPLIELAPDIYALVKPGGYLILSGILKEQAQMVAEAYSQ-GFELITVEHREEWVCIVGKK 294
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
1-309 3.65e-106

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 310.95  E-value: 3.65e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154   1 MNWTELSIVVNHDVEFEVTEILEDHGSNGVVIEDsrdletppsdkfgeiyelnPEDYPSSGVRLKAYFNELTFNDELRKS 80
Cdd:COG2264    1 MKWIELTITTPEEAAEALSDALEELGAEGVEIED-------------------APPGLWERVGVKAYFPEDEDLEELLAA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  81 IKNNIlnvSNLDKGVLTFSEkgIAEKDWANEWKNYFRPFKASNRFTIVPSWETYTkENSDELCIELDPGMAFGTGDHPTT 160
Cdd:COG2264   62 LAEAL---GELGAPEITVEE--VEEEDWVEEWKKYFKPIRVGDRLVIVPSWEEYE-PDPGEIVIEIDPGMAFGTGTHPTT 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 161 SMCLKAIEEYVQTTDSIIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLLKEekEKY 240
Cdd:COG2264  136 RLCLEALEKLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLED--GPY 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515409154 241 NIVIANILAHIIEEMIEDAYNTLFEEGYFITSGIIEEKYEEIESHMKRVGFNIISVEHDNGWVCIVGQK 309
Cdd:COG2264  214 DLVVANILANPLIELAPDLAALLKPGGYLILSGILEEQADEVLAAYEAAGFELVERRERGEWVALVLRK 282
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
1-309 3.18e-94

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 279.34  E-value: 3.18e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154   1 MNWTELSIVVNHDVEFEVTEILEDHGSNGvviedsrdletppsdkfgeiyelnpedypssgvRLKAyfneltfndelrks 80
Cdd:PRK00517   1 MKWIELTLNTTPEAAEALSDILMELGALA---------------------------------ALAN-------------- 33

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  81 iknniLNVSNLDKGVLTFSEKGIAEKDWANEWKNYFRPFKASNRFTIVPSWETYtkENSDELCIELDPGMAFGTGDHPTT 160
Cdd:PRK00517  34 -----LAGLGLDLGEPTYTIEEVEDEDWEREWKKYFHPIRIGDRLWIVPSWEDP--PDPDEINIELDPGMAFGTGTHPTT 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 161 SMCLKAIEEYVQTTDSIIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLlkeekeKY 240
Cdd:PRK00517 107 RLCLEALEKLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNVYLPQGDL------KA 180

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515409154 241 NIVIANILAHIIEEMIEDAYNTLFEEGYFITSGIIEEKYEEIESHMKRVGFNIISVEHDNGWVCIVGQK 309
Cdd:PRK00517 181 DVIVANILANPLLELAPDLARLLKPGGRLILSGILEEQADEVLEAYEEAGFTLDEVLERGEWVALVGKK 249
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 3-273 1.55e-64

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: 205.07  E-value: 1.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154    3 WTELSIVVNHDVEFEVTEILEDHGSNGVVIEDSRDLetppsdkfgeIYeLNPeDYPSSGVRLKAY--FNELTFNDELRKS 80
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFEDDKDT----------IY-FEP-HLPGEKRLWGNLdvIALFDAETDMNNS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154   81 IKNNiLNVSNLDKGVLTFSEKGIAEKDWANEWKNYFRPFKASNRFTIVPSWETYTkENSDELCIELDPGMAFGTGDHPTT 160
Cdd:TIGR00406  69 VIPL-LEAFCLDLGRNHKIEFDEFSKDWERAWKDNFHPVQFGKRFWICPSWRDVP-SDEDALIIMLDPGLAFGTGTHPTT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  161 SMCLKAIEEYVQTTDSIIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLLKEEKEKY 240
Cdd:TIGR00406 147 SLCLEWLEDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDRLQVKLIYLEQPIEGKA 226

                         250       260       270
                  ....*....|....*....|....*....|...
gi 515409154  241 NIVIANILAHIIEEMIEDAYNTLFEEGYFITSG 273
Cdd:TIGR00406 227 DVIVANILAEVIKELYPQFSRLVKPGGWLILSG 259
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 177-272 8.44e-09

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: 52.43  E-value: 8.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 177 IIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENfKKNRCEDAIEAVPGNLLK---EEKEKYNIVIANILAHI-- 251
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEElppEADESFDVIISDPPLHHlv 80

                         90       100
                 ....*....|....*....|...
gi 515409154 252 --IEEMIEDAYNTLFEEGYFITS 272
Cdd:cd02440   81 edLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 2-309 2.49e-120

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: 347.33  E-value: 2.49e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154    2 NWTELSIVVNHDVEFEVTEILEDHGSNGVVIEDSRDLEtpPSDKFGeiYELNPEDYPSsGVRLKAYFNELTFNDELRKSI 81
Cdd:pfam06325   1 TWLELSIHTTREAAEPVSNILEEFGALGVAIEDADLLE--DRDIFE--PGLGEERLWD-EVRVKALFDEETDALELIAQL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154   82 KNNILNvsnLDKGVLTFSEkgIAEKDWANEWKNYFRPFKASNRFTIVPSWETYtKENSDELCIELDPGMAFGTGDHPTTS 161
Cdd:pfam06325  76 AELIGG---LDSPKVTVEE--VAEEDWARAWKKYFHPVRIGERLTIVPSWEDY-PENPDALNIELDPGMAFGTGTHPTTK 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  162 MCLKAIEEYVQTTDSIIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEA-VPGNLLkeeKEKY 240
Cdd:pfam06325 150 LCLEALERLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVyLPGDLP---KEKA 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515409154  241 NIVIANILAHIIEEMIEDAYNTLFEEGYFITSGIIEEKYEEIESHMKRvGFNIISVEHDNGWVCIVGQK 309
Cdd:pfam06325 227 DVVVANILADPLIELAPDIYALVKPGGYLILSGILKEQAQMVAEAYSQ-GFELITVEHREEWVCIVGKK 294
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
1-309 3.65e-106

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 310.95  E-value: 3.65e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154   1 MNWTELSIVVNHDVEFEVTEILEDHGSNGVVIEDsrdletppsdkfgeiyelnPEDYPSSGVRLKAYFNELTFNDELRKS 80
Cdd:COG2264    1 MKWIELTITTPEEAAEALSDALEELGAEGVEIED-------------------APPGLWERVGVKAYFPEDEDLEELLAA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  81 IKNNIlnvSNLDKGVLTFSEkgIAEKDWANEWKNYFRPFKASNRFTIVPSWETYTkENSDELCIELDPGMAFGTGDHPTT 160
Cdd:COG2264   62 LAEAL---GELGAPEITVEE--VEEEDWVEEWKKYFKPIRVGDRLVIVPSWEEYE-PDPGEIVIEIDPGMAFGTGTHPTT 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 161 SMCLKAIEEYVQTTDSIIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLLKEekEKY 240
Cdd:COG2264  136 RLCLEALEKLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLED--GPY 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515409154 241 NIVIANILAHIIEEMIEDAYNTLFEEGYFITSGIIEEKYEEIESHMKRVGFNIISVEHDNGWVCIVGQK 309
Cdd:COG2264  214 DLVVANILANPLIELAPDLAALLKPGGYLILSGILEEQADEVLAAYEAAGFELVERRERGEWVALVLRK 282
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
1-309 3.18e-94

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 279.34  E-value: 3.18e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154   1 MNWTELSIVVNHDVEFEVTEILEDHGSNGvviedsrdletppsdkfgeiyelnpedypssgvRLKAyfneltfndelrks 80
Cdd:PRK00517   1 MKWIELTLNTTPEAAEALSDILMELGALA---------------------------------ALAN-------------- 33

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  81 iknniLNVSNLDKGVLTFSEKGIAEKDWANEWKNYFRPFKASNRFTIVPSWETYtkENSDELCIELDPGMAFGTGDHPTT 160
Cdd:PRK00517  34 -----LAGLGLDLGEPTYTIEEVEDEDWEREWKKYFHPIRIGDRLWIVPSWEDP--PDPDEINIELDPGMAFGTGTHPTT 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 161 SMCLKAIEEYVQTTDSIIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLlkeekeKY 240
Cdd:PRK00517 107 RLCLEALEKLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELNVYLPQGDL------KA 180

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515409154 241 NIVIANILAHIIEEMIEDAYNTLFEEGYFITSGIIEEKYEEIESHMKRVGFNIISVEHDNGWVCIVGQK 309
Cdd:PRK00517 181 DVIVANILANPLLELAPDLARLLKPGGRLILSGILEEQADEVLEAYEEAGFTLDEVLERGEWVALVGKK 249
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 3-273 1.55e-64

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: 205.07  E-value: 1.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154    3 WTELSIVVNHDVEFEVTEILEDHGSNGVVIEDSRDLetppsdkfgeIYeLNPeDYPSSGVRLKAY--FNELTFNDELRKS 80
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFEDDKDT----------IY-FEP-HLPGEKRLWGNLdvIALFDAETDMNNS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154   81 IKNNiLNVSNLDKGVLTFSEKGIAEKDWANEWKNYFRPFKASNRFTIVPSWETYTkENSDELCIELDPGMAFGTGDHPTT 160
Cdd:TIGR00406  69 VIPL-LEAFCLDLGRNHKIEFDEFSKDWERAWKDNFHPVQFGKRFWICPSWRDVP-SDEDALIIMLDPGLAFGTGTHPTT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  161 SMCLKAIEEYVQTTDSIIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLLKEEKEKY 240
Cdd:TIGR00406 147 SLCLEWLEDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDRLQVKLIYLEQPIEGKA 226

                         250       260       270
                  ....*....|....*....|....*....|...
gi 515409154  241 NIVIANILAHIIEEMIEDAYNTLFEEGYFITSG 273
Cdd:TIGR00406 227 DVIVANILAEVIKELYPQFSRLVKPGGWLILSG 259
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 176-246 8.04e-12

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 64.40  E-value: 8.04e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515409154 176 SIIDVGTGSGI--LSIASHLVGVkRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLLK--EEKEKYNIVIAN 246
Cdd:COG2890  115 RVLDLGTGSGAiaLALAKERPDA-RVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFEplPGDGRFDLIVSN 188
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 145-263 4.00e-11

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: 60.97  E-value: 4.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 145 ELDPGmafgtgdhptTSMCLKAIEEyvQTTDSIIDVGTGSGILSIA-SHLVGVKRIKALDIDEMAVNVAKENFKKNRCED 223
Cdd:COG2813   33 RLDIG----------TRLLLEHLPE--PLGGRVLDLGCGYGVIGLAlAKRNPEARVTLVDVNARAVELARANAAANGLEN 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 515409154 224 AiEAVPGNLLKE-EKEKYNIVIAN--------ILAHIIEEMIEDAYNTL 263
Cdd:COG2813  101 V-EVLWSDGLSGvPDGSFDLILSNppfhagraVDKEVAHALIADAARHL 148
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
156-257 4.01e-11

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 61.59  E-value: 4.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 156 DHPTTSMCLKAIEEYVQTTDSIIDVGTGSGILS-IASHLvGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLLK 234
Cdd:COG4076   18 DVERNDAFKAAIERVVKPGDVVLDIGTGSGLLSmLAARA-GAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATD 96

                         90       100
                 ....*....|....*....|....*.
gi 515409154 235 -EEKEKYNIVIANILAH--IIEEMIE 257
Cdd:COG4076   97 lDLPEKADVIISEMLDTalLDEGQVP 122
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 171-246 3.03e-10

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: 59.39  E-value: 3.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 171 VQTTDSIIDVGTGSGILSIA-SHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLL----KEEKEKYNIVIA 245
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKefaaELPPGSFDLVVS 114


                 .
gi 515409154 246 N 246
Cdd:COG4123  115 N 115
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 177-267 4.54e-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: 4.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  177 IIDVGTGSGILSIA-SHLVGVKRIKALDIDEMAVNVAKENFKKNRCEdAIEAVPGNLLKE-EKEKYNIVIAN-------- 246
Cdd:pfam05175  35 VLDLGCGAGVLGAAlAKESPDAELTMVDINARALESARENLAANGLE-NGEVVASDVYSGvEDGKFDLIISNppfhagla 113

                          90       100
                  ....*....|....*....|.
gi 515409154  247 ILAHIIEEMIEDAYNTLFEEG 267
Cdd:pfam05175 114 TTYNVAQRFIADAKRHLRPGG 134
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 176-246 1.13e-09

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 58.25  E-value: 1.13e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515409154 176 SIIDVGTGSGI--LSIASHLVGVkRIKALDIDEMAVNVAKENFkKNRCEDAIEAVPGNLLKE-EKEKYNIVIAN 246
Cdd:PRK09328 111 RVLDLGTGSGAiaLALAKERPDA-EVTAVDISPEALAVARRNA-KHGLGARVEFLQGDWFEPlPGGRFDLIVSN 182
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 177-272 8.44e-09

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: 52.43  E-value: 8.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 177 IIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENfKKNRCEDAIEAVPGNLLK---EEKEKYNIVIANILAHI-- 251
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEElppEADESFDVIISDPPLHHlv 80

                         90       100
                 ....*....|....*....|...
gi 515409154 252 --IEEMIEDAYNTLFEEGYFITS 272
Cdd:cd02440   81 edLARFLEEARRLLKPGGVLVLT 103
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
175-246 8.79e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 54.52  E-value: 8.79e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515409154 175 DSIIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKknRCEDAIEAVPGNLLK-EEKEKYNIVIAN 246
Cdd:COG2263   47 KTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAE--RLGVRVDFIRADVTRiPLGGSVDTVVMN 117
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 167-270 1.30e-07

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: 49.63  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 167 IEEYVQTTDSIIDVGTGSGILSIASHLVGVkRIKALDIDEMAVNVAKENFKKNRcedaIEAVPGNL--LKEEKEKYNIVI 244
Cdd:COG2227   18 LARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAELN----VDFVQGDLedLPLEDGSFDLVI 92

                         90       100
                 ....*....|....*....|....*....
gi 515409154 245 A-NILAHI--IEEMIEDAYNTLFEEGYFI 270
Cdd:COG2227   93 CsEVLEHLpdPAALLRELARLLKPGGLLL 121
PRK14968 PRK14968
putative methyltransferase; Provisional
 175-246 1.80e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 50.28  E-value: 1.80e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515409154 175 DSIIDVGTGSGILSIASHLVGvKRIKALDIDEMAVNVAKENFKKNRCEDA-IEAVPGNLLKE-EKEKYNIVIAN 246
Cdd:PRK14968  25 DRVLEVGTGSGIVAIVAAKNG-KKVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLFEPfRGDKFDVILFN 97
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 172-246 5.58e-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: 50.04  E-value: 5.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515409154  172 QTTDSIIDVGTGSGILSIA-SHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLLKE-EKEKYNIVIAN 246
Cdd:TIGR00536 113 PPILHILDLGTGSGCIALAlAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLFEPlAGQKIDIIVSN 189
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 177-245 1.50e-06

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: 48.34  E-value: 1.50e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 177 IIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRceDAIEAVPGNLLK-EEKEKYNIVIA 245
Cdd:COG3897   74 VLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNG--VAITTRLGDWRDpPAAGGFDLILG 141
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 177-264 3.36e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.86  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  177 IIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEdaIEAVPGNL--LKEEKEKYNIVIAN-ILAHIIE 253
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAedLPFPDGSFDLVVSSgVLHHLPD 78

                          90
                  ....*....|.
gi 515409154  254 EMIEDAYNTLF 264
Cdd:pfam13649  79 PDLEAALREIA 89
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 174-230 4.55e-04

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


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 39.24  E-value: 4.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 515409154  174 TDSIIDVGTGSGILSI-ASHLVGVKRIKALDIDEMAVNVAKENFKKNRCeDAIEAVPG 230
Cdd:TIGR02469  20 GDVLWDIGAGTGSVTIeAARLVPNGRVYAIERNPEALDLIERNLRRFGV-SNIVIVEG 76
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 160-243 8.95e-04

tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N,N-dimethylase Trm1 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441472  Cd Length: 383  Bit Score: 40.63  E-value: 8.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 160 TSMCLKAIEEYVQTTDSIIDVGTGSGILSI-ASHLVGVKRIkALDIDEMAVNVAKENFKKNRCEDaIEAVPGN---LLKE 235
Cdd:COG1867   44 SVAALRAYRERLKREISYLDALAASGIRGLrYALEVGIKVT-LNDIDPEAVELIRENLELNGLED-VEVYNRDanaLLHE 121


                 ....*...
gi 515409154 236 EKEKYNIV 243
Cdd:COG1867  122 LGRRFDVV 129
PRK14967 PRK14967
putative methyltransferase; Provisional
 177-246 1.27e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 39.65  E-value: 1.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515409154 177 IIDVGTGSGILSIASHLVGVKRIKALDIDEMAVNVAKENFKKNRCE------DAIEAVPGnllkeekEKYNIVIAN 246
Cdd:PRK14967  40 VLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVDvdvrrgDWARAVEF-------RPFDVVVSN 108
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 175-269 2.19e-03

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 39.46  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154 175 DSIIDVGTGSGILSIaSHLVGV--KRIKALDIDEMAVNVAKENFKKNRCEDAIEAVPGNLLKE-EKEKYNIVIANILAHI 251
Cdd:PRK01544 140 LNILELGTGSGCIAI-SLLCELpnANVIATDISLDAIEVAKSNAIKYEVTDRIQIIHSNWFENiEKQKFDFIVSNPPYIS 218

                         90
                 ....*....|....*...
gi 515409154 252 IEEMIEDAYNTLFEEGYF 269
Cdd:PRK01544 219 HSEKSEMAIETINYEPSI 236
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 177-272 2.39e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.78  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515409154  177 IIDVGTGSGILS--IASHLVGVKRIKALDIDEMAVNVAKENFKKNRCEDA------IEAVPGNLlkeEKEKYNIVIANIL 248
Cdd:pfam13847   7 VLDLGCGTGHLSfeLAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVefeqgdIEELPELL---EDDKFDVVISNCV 83

                          90       100
                  ....*....|....*....|....*..
gi 515409154  249 AHIIEEM---IEDAYNTLFEEGYFITS 272
Cdd:pfam13847  84 LNHIPDPdkvLQEILRVLKPGGRLIIS 110
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
175-218 4.46e-03

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 37.88  E-value: 4.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 515409154 175 DSIIDVGTGSG----ILS-IASHLVGVKRIKALdidemaVNVAKENFKK 218
Cdd:PRK00312  80 DRVLEIGTGSGyqaaVLAhLVRRVFSVERIKTL------QWEAKRRLKQ 122
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 175-230 4.65e-03

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 37.47  E-value: 4.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515409154 175 DSIIDVGTGSGILSI-ASHLVGVK-RIKALDIDEMAVNVAKENFKKNRCEDAIEAVPG 230
Cdd:PRK00377  42 DMILDIGCGTGSVTVeASLLVGETgKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKG 99
 
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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