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Conserved domains on  [gi|357548853|gb|EHJ30709|]
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ribosomal protein L11 methyltransferase [Lacticaseibacillus rhamnosus ATCC 21052]

Protein Classification

50S ribosomal protein L11 methyltransferase( domain architecture ID 11455142)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
4-314 1.70e-112

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


:

Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 327.13  E-value: 1.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853   4 DWTALTVTTSTEAVEAVSNILMEAGAVGIQIKDAAdfkketidahgtwfdpatvPHLATGAQVIGYFEPATSLIEKRDHL 83
Cdd:COG2264    2 KWIELTITTPEEAAEALSDALEELGAEGVEIEDAP-------------------PGLWERVGVKAYFPEDEDLEELLAAL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  84 ASQVKALaqfgldpGAATVTLADVRQQDWADVWKKYYHPLRVSRFLTIVPKWEHYTPQqPDELVLTLDPGMAFGTGTHPT 163
Cdd:COG2264   63 AEALGEL-------GAPEITVEEVEEEDWVEEWKKYFKPIRVGDRLVIVPSWEEYEPD-PGEIVIEIDPGMAFGTGTHPT 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 164 TQLMLSLLESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVSH-ITVKANDLLQGLTvs 242
Cdd:COG2264  135 TRLCLEALEKLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDrIEVVLGDLLEDGP-- 212

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357548853 243 ADLIVANILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKADLIRQTLQDNGFTIAQRRDAGGWVAFDAVLKA 314
Cdd:COG2264  213 YDLVVANILANPLIELAPDLAALLKPGGYLILSGILEEQADEVLAAYEAAGFELVERRERGEWVALVLRKKA 284
 
Name Accession Description Interval E-value
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
4-314 1.70e-112

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 327.13  E-value: 1.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853   4 DWTALTVTTSTEAVEAVSNILMEAGAVGIQIKDAAdfkketidahgtwfdpatvPHLATGAQVIGYFEPATSLIEKRDHL 83
Cdd:COG2264    2 KWIELTITTPEEAAEALSDALEELGAEGVEIEDAP-------------------PGLWERVGVKAYFPEDEDLEELLAAL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  84 ASQVKALaqfgldpGAATVTLADVRQQDWADVWKKYYHPLRVSRFLTIVPKWEHYTPQqPDELVLTLDPGMAFGTGTHPT 163
Cdd:COG2264   63 AEALGEL-------GAPEITVEEVEEEDWVEEWKKYFKPIRVGDRLVIVPSWEEYEPD-PGEIVIEIDPGMAFGTGTHPT 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 164 TQLMLSLLESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVSH-ITVKANDLLQGLTvs 242
Cdd:COG2264  135 TRLCLEALEKLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDrIEVVLGDLLEDGP-- 212

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357548853 243 ADLIVANILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKADLIRQTLQDNGFTIAQRRDAGGWVAFDAVLKA 314
Cdd:COG2264  213 YDLVVANILANPLIELAPDLAALLKPGGYLILSGILEEQADEVLAAYEAAGFELVERRERGEWVALVLRKKA 284
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
3-313 1.02e-107

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 313.63  E-value: 1.02e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853   3 NDWTALTVTTSTEAVEAVSNILMEAGAVGiqikdaadfkketidahgtwfdpatvphlatgaqvigyfepatsliekrdh 82
Cdd:PRK00517   1 MKWIELTLNTTPEAAEALSDILMELGALA--------------------------------------------------- 29

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  83 lasQVKALAQFGLDPGAATVTLADVRQQDWADVWKKYYHPLRVSRFLTIVPKWEHYtpQQPDELVLTLDPGMAFGTGTHP 162
Cdd:PRK00517  30 ---ALANLAGLGLDLGEPTYTIEEVEDEDWEREWKKYFHPIRIGDRLWIVPSWEDP--PDPDEINIELDPGMAFGTGTHP 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 163 TTQLMLSLLESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVS-HITVKANDLlqgltv 241
Cdd:PRK00517 105 TTRLCLEALEKLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVElNVYLPQGDL------ 178

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357548853 242 SADLIVANILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKADLIRQTLQDNGFTIAQRRDAGGWVAFDAVLK 313
Cdd:PRK00517 179 KADVIVANILANPLLELAPDLARLLKPGGRLILSGILEEQADEVLEAYEEAGFTLDEVLERGEWVALVGKKK 250
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 5-311 2.21e-99

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: 294.17  E-value: 2.21e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853    5 WTALTVTTSTEAVEAVSNILMEAGAVGIQIKDAADFKKETIdahgtwFDPATVP-HLATGAQVIGYFEPATSLIEKRDHL 83
Cdd:pfam06325   2 WLELSIHTTREAAEPVSNILEEFGALGVAIEDADLLEDRDI------FEPGLGEeRLWDEVRVKALFDEETDALELIAQL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853   84 ASQVkalaqFGLDPGAATVTLadVRQQDWADVWKKYYHPLRVSRFLTIVPKWEHYtPQQPDELVLTLDPGMAFGTGTHPT 163
Cdd:pfam06325  76 AELI-----GGLDSPKVTVEE--VAEEDWARAWKKYFHPVRIGERLTIVPSWEDY-PENPDALNIELDPGMAFGTGTHPT 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  164 TQLMLSLLESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVS-HITVKA-NDLLQGLtv 241
Cdd:pfam06325 148 TKLCLEALERLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEaRLEVYLpGDLPKEK-- 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  242 sADLIVANILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKADLIRQTLQdNGFTIAQRRDAGGWVAFDAV 311
Cdd:pfam06325 226 -ADVVVANILADPLIELAPDIYALVKPGGYLILSGILKEQAQMVAEAYS-QGFELITVEHREEWVCIVGK 293
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 5-306 1.38e-79

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: 243.59  E-value: 1.38e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853    5 WTALTVTTSTEAVEAVSNILMEAGAVGIQIKDaadfKKETIdahgtWFDPatvpHLATGAQVIGYFEPATSLIEKRDHLA 84
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFED----DKDTI-----YFEP----HLPGEKRLWGNLDVIALFDAETDMNN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853   85 SQVKALAQFGLDPGAATVTLADVRQQDWADVWKKYYHPLRVSRFLTIVPKWEHYTPQQpDELVLTLDPGMAFGTGTHPTT 164
Cdd:TIGR00406  68 SVIPLLEAFCLDLGRNHKIEFDEFSKDWERAWKDNFHPVQFGKRFWICPSWRDVPSDE-DALIIMLDPGLAFGTGTHPTT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  165 QLMLSLLESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVSHIT-VKANDLLQGLTVSA 243
Cdd:TIGR00406 147 SLCLEWLEDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDRLqVKLIYLEQPIEGKA 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357548853  244 DLIVANILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKADLIRQTLQdNGFTIAQRRDAGGWV 306
Cdd:TIGR00406 227 DVIVANILAEVIKELYPQFSRLVKPGGWLILSGILETQAQSVCDAYE-QGFTVVEIRQREEWC 288
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 180-279 5.27e-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: 53.20  E-value: 5.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 180 TMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVSHITVKANDLLQGLTV---SADLIVANILAEVLV 256
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEadeSFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*..
gi 357548853 257 PLIPQV----PSRLNPHGHFLLAGIIA 279
Cdd:cd02440   81 EDLARFleeaRRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
4-314 1.70e-112

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 327.13  E-value: 1.70e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853   4 DWTALTVTTSTEAVEAVSNILMEAGAVGIQIKDAAdfkketidahgtwfdpatvPHLATGAQVIGYFEPATSLIEKRDHL 83
Cdd:COG2264    2 KWIELTITTPEEAAEALSDALEELGAEGVEIEDAP-------------------PGLWERVGVKAYFPEDEDLEELLAAL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  84 ASQVKALaqfgldpGAATVTLADVRQQDWADVWKKYYHPLRVSRFLTIVPKWEHYTPQqPDELVLTLDPGMAFGTGTHPT 163
Cdd:COG2264   63 AEALGEL-------GAPEITVEEVEEEDWVEEWKKYFKPIRVGDRLVIVPSWEEYEPD-PGEIVIEIDPGMAFGTGTHPT 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 164 TQLMLSLLESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVSH-ITVKANDLLQGLTvs 242
Cdd:COG2264  135 TRLCLEALEKLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDrIEVVLGDLLEDGP-- 212

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357548853 243 ADLIVANILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKADLIRQTLQDNGFTIAQRRDAGGWVAFDAVLKA 314
Cdd:COG2264  213 YDLVVANILANPLIELAPDLAALLKPGGYLILSGILEEQADEVLAAYEAAGFELVERRERGEWVALVLRKKA 284
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
3-313 1.02e-107

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 313.63  E-value: 1.02e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853   3 NDWTALTVTTSTEAVEAVSNILMEAGAVGiqikdaadfkketidahgtwfdpatvphlatgaqvigyfepatsliekrdh 82
Cdd:PRK00517   1 MKWIELTLNTTPEAAEALSDILMELGALA--------------------------------------------------- 29

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  83 lasQVKALAQFGLDPGAATVTLADVRQQDWADVWKKYYHPLRVSRFLTIVPKWEHYtpQQPDELVLTLDPGMAFGTGTHP 162
Cdd:PRK00517  30 ---ALANLAGLGLDLGEPTYTIEEVEDEDWEREWKKYFHPIRIGDRLWIVPSWEDP--PDPDEINIELDPGMAFGTGTHP 104

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 163 TTQLMLSLLESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVS-HITVKANDLlqgltv 241
Cdd:PRK00517 105 TTRLCLEALEKLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVElNVYLPQGDL------ 178

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 357548853 242 SADLIVANILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKADLIRQTLQDNGFTIAQRRDAGGWVAFDAVLK 313
Cdd:PRK00517 179 KADVIVANILANPLLELAPDLARLLKPGGRLILSGILEEQADEVLEAYEEAGFTLDEVLERGEWVALVGKKK 250
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 5-311 2.21e-99

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: 294.17  E-value: 2.21e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853    5 WTALTVTTSTEAVEAVSNILMEAGAVGIQIKDAADFKKETIdahgtwFDPATVP-HLATGAQVIGYFEPATSLIEKRDHL 83
Cdd:pfam06325   2 WLELSIHTTREAAEPVSNILEEFGALGVAIEDADLLEDRDI------FEPGLGEeRLWDEVRVKALFDEETDALELIAQL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853   84 ASQVkalaqFGLDPGAATVTLadVRQQDWADVWKKYYHPLRVSRFLTIVPKWEHYtPQQPDELVLTLDPGMAFGTGTHPT 163
Cdd:pfam06325  76 AELI-----GGLDSPKVTVEE--VAEEDWARAWKKYFHPVRIGERLTIVPSWEDY-PENPDALNIELDPGMAFGTGTHPT 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  164 TQLMLSLLESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVS-HITVKA-NDLLQGLtv 241
Cdd:pfam06325 148 TKLCLEALERLVKPGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEaRLEVYLpGDLPKEK-- 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  242 sADLIVANILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKADLIRQTLQdNGFTIAQRRDAGGWVAFDAV 311
Cdd:pfam06325 226 -ADVVVANILADPLIELAPDIYALVKPGGYLILSGILKEQAQMVAEAYS-QGFELITVEHREEWVCIVGK 293
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 5-306 1.38e-79

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: 243.59  E-value: 1.38e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853    5 WTALTVTTSTEAVEAVSNILMEAGAVGIQIKDaadfKKETIdahgtWFDPatvpHLATGAQVIGYFEPATSLIEKRDHLA 84
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFED----DKDTI-----YFEP----HLPGEKRLWGNLDVIALFDAETDMNN 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853   85 SQVKALAQFGLDPGAATVTLADVRQQDWADVWKKYYHPLRVSRFLTIVPKWEHYTPQQpDELVLTLDPGMAFGTGTHPTT 164
Cdd:TIGR00406  68 SVIPLLEAFCLDLGRNHKIEFDEFSKDWERAWKDNFHPVQFGKRFWICPSWRDVPSDE-DALIIMLDPGLAFGTGTHPTT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  165 QLMLSLLESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVSHIT-VKANDLLQGLTVSA 243
Cdd:TIGR00406 147 SLCLEWLEDLDLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDRLqVKLIYLEQPIEGKA 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357548853  244 DLIVANILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKADLIRQTLQdNGFTIAQRRDAGGWV 306
Cdd:TIGR00406 227 DVIVANILAEVIKELYPQFSRLVKPGGWLILSGILETQAQSVCDAYE-QGFTVVEIRQREEWC 288
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 150-274 2.01e-15

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: 73.30  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 150 LDPGmafgtgthptTQLMLSLLEslVRGGETMIDVGTGSGILAIA-AERLGVSQILATDVDEIAVKNAQANIALNPVSHI 228
Cdd:COG2813   34 LDIG----------TRLLLEHLP--EPLGGRVLDLGCGYGVIGLAlAKRNPEARVTLVDVNARAVELARANAAANGLENV 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 357548853 229 TVKANDLLQGL-TVSADLIVAN--------ILAEVLVPLIPQVPSRLNPHGHFLL 274
Cdd:COG2813  102 EVLWSDGLSGVpDGSFDLILSNppfhagraVDKEVAHALIADAARHLRPGGELWL 156
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 182-316 2.26e-12

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 65.94  E-value: 2.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 182 IDVGTGSGILAIA-AERLGVSQILATDVDEIAVKNAQANIALNPVSH-ITVKANDLLQGLTV--SADLIVAN-------- 249
Cdd:COG2890  117 LDLGTGSGAIALAlAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDLFEPLPGdgRFDLIVSNppyipede 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 250 ---ILAEVLV--P----------------LIPQVPSRLNPHGHFLL-AGiiAEKADLIRQTLQDNGFT-IAQRRDAGGwv 306
Cdd:COG2890  197 ialLPPEVRDhePrlaldggedgldfyrrIIAQAPRLLKPGGWLLLeIG--EDQGEAVRALLEAAGFAdVETHKDLAG-- 272

                        170
                 ....*....|
gi 357548853 307 aFDAVLKAQR 316
Cdd:COG2890  273 -RDRVVVARR 281
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 183-304 9.31e-12

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 64.41  E-value: 9.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 183 DVGTGSGI--LAIAAERLGvSQILATDVDEIAVKNAQANIALNPVSHITVKANDLLQGLT-VSADLIVAN---------- 249
Cdd:PRK09328 114 DLGTGSGAiaLALAKERPD-AEVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEPLPgGRFDLIVSNppyipeadih 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 357548853 250 -ILAEVLV------------------PLIPQVPSRLNPHGHFLLAgiIAEK-ADLIRQTLQDNGFTIAQ-RRDAGG 304
Cdd:PRK09328 193 lLQPEVRDhephlalfggedgldfyrRIIEQAPRYLKPGGWLLLE--IGYDqGEAVRALLAAAGFADVEtRKDLAG 266
PRK14968 PRK14968
putative methyltransferase; Provisional
 170-249 7.33e-11

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 60.30  E-value: 7.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 170 LLESLV-RGGETMIDVGTGSGILAIAAERLGVSqILATDVDEIAVKNAQANIALNPVSH--ITVKANDLLQGLT-VSADL 245
Cdd:PRK14968  15 LAENAVdKKGDRVLEVGTGSGIVAIVAAKNGKK-VVGVDINPYAVECAKCNAKLNNIRNngVEVIRSDLFEPFRgDKFDV 93


                 ....
gi 357548853 246 IVAN 249
Cdd:PRK14968  94 ILFN 97
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 175-249 1.59e-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: 60.16  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 175 VRGGETMIDVGTGSGILAIA-AERLGVSQILATDVDEIAVKNAQANIALNPVS-HITVKANDLLQ----GLTVSADLIVA 248
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEAAELARRNVALNGLEdRITVIHGDLKEfaaeLPPGSFDLVVS 114


                 .
gi 357548853 249 N 249
Cdd:COG4123  115 N 115
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 145-274 2.35e-09

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: 55.67  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  145 ELVLTLDPGMAFGTGTHPTTQLMLSLLESLVRGgeTMIDVGTGSGILAIA-AERLGVSQILATDVDEIAVKNAQANIALN 223
Cdd:pfam05175   1 ELTFKTLPGVFSHGRLDIGSRLLLEHLPKDLSG--KVLDLGCGAGVLGAAlAKESPDAELTMVDINARALESARENLAAN 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  224 PVSHITVKANDLLQGLTV-SADLIVAN--------ILAEVLVPLIPQVPSRLNPHGHFLL 274
Cdd:pfam05175  79 GLENGEVVASDVYSGVEDgKFDLIISNppfhaglaTTYNVAQRFIADAKRHLRPGGELWI 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 180-279 5.27e-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: 53.20  E-value: 5.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 180 TMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVSHITVKANDLLQGLTV---SADLIVANILAEVLV 256
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEadeSFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*..
gi 357548853 257 PLIPQV----PSRLNPHGHFLLAGIIA 279
Cdd:cd02440   81 EDLARFleeaRRLLKPGGVLVLTLVLA 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
171-305 4.78e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 52.73  E-value: 4.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 171 LESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVSH-ITV---KANDLLqgLTVSADLI 246
Cdd:COG4076   29 IERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDrITVinaDATDLD--LPEKADVI 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357548853 247 VANILAEVLVPLiPQVPSRLNPHGHFLLAG--IIAEKADLIRQTLQdngftiaQRRDAGGW 305
Cdd:COG4076  107 ISEMLDTALLDE-GQVPILNHARKRLLKPGgrIIPERITNAAQPVE-------SPVDAEGF 159
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 178-275 1.01e-07

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: 51.81  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 178 GETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVShITVKANDLLQG-LTVSADLIVA-NIL---- 251
Cdd:COG3897   71 GKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVA-ITTRLGDWRDPpAAGGFDLILGgDVLyerd 149

                         90       100
                 ....*....|....*....|....*
gi 357548853 252 -AEVLVPLIPQVpsrLNPHGHFLLA 275
Cdd:COG3897  150 lAEPLLPFLDRL---AAPGGEVLIG 171
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 167-275 1.63e-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: 49.25  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 167 MLSLLESLVRGGETMIDVGTGSGILAIAAERLGVsQILATDVDEIAVKNAQANIALNPVSHITVKANDLLQGLTvSADLI 246
Cdd:COG2227   14 LAALLARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAELNVDFVQGDLEDLPLEDG-SFDLV 91

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 357548853 247 VANilaEVL--VP----LIPQVPSRLNPHGHFLLA 275
Cdd:COG2227   92 ICS---EVLehLPdpaaLLRELARLLKPGGLLLLS 123
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 162-316 5.00e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.53  E-value: 5.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 162 PTTQLMLSLLESLvRGGETMIDVGTGSGILAIA-AERLGvSQILATDVDEIAVKNAQANIALNPVSHITVKANDLLQGLT 240
Cdd:COG0500   12 PGLAALLALLERL-PKGGRVLDLGCGTGRNLLAlAARFG-GRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 241 VSA---DLIVAN-----ILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKADLIRQTLQDNGFTIAQRRDAGGWVAFDAVL 312
Cdd:COG0500   90 LPAesfDLVVAFgvlhhLPPEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLATASLLELLLLLRLLALELYL 169


                 ....
gi 357548853 313 KAQR 316
Cdd:COG0500  170 RALL 173
PRK14967 PRK14967
putative methyltransferase; Provisional
 161-270 1.33e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 48.51  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 161 HPTTQLMLSLLESLVRGGETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVsHITVKANDLLQGL- 239
Cdd:PRK14967  20 EDTQLLADALAAEGLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGV-DVDVRRGDWARAVe 98

                         90       100       110
                 ....*....|....*....|....*....|.
gi 357548853 240 TVSADLIVANilaevlVPLIPQVPSRLNPHG 270
Cdd:PRK14967  99 FRPFDVVVSN------PPYVPAPPDAPPSRG 123
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 151-274 1.42e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 44.54  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 151 DPGMAFGTGTHPTTQLMLSLLEslVRGGETMIDVGTGSGILAI-AAERLGVsQILATDVDEIAVKNAQANIALNPVSH-I 228
Cdd:COG2230   27 DPDDTLEEAQEAKLDLILRKLG--LKPGMRVLDIGCGWGGLALyLARRYGV-RVTGVTLSPEQLEYARERAAEAGLADrV 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 357548853 229 TVKANDLLQ-GLTVSADLIVAN-----ILAEVLVPLIPQVPSRLNPHGHFLL 274
Cdd:COG2230  104 EVRLADYRDlPADGQFDAIVSIgmfehVGPENYPAYFAKVARLLKPGGRLLL 155
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 183-249 8.98e-05

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 40.62  E-value: 8.98e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 357548853  183 DVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANIALNPVsHITVKANDL--LQGLTVSADLIVAN 249
Cdd:pfam13649   3 DLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAedLPFPDGSFDLVVSS 70
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
178-249 9.34e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 42.58  E-value: 9.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357548853 178 GETMIDVGTGSGILAIAAERLGVSQILATDVDEIAVKNAQANiALNPVSHITVKANDLLQ-GLTVSADLIVAN 249
Cdd:COG2263   46 GKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIAREN-AERLGVRVDFIRADVTRiPLGGSVDTVVMN 117
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 176-275 2.27e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.86  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  176 RGGETMIDVGTGSGILAI-AAERLGV-SQILATDVDEIAVKNAQANIALNPVSHITVK---ANDLLQGLTV-SADLIVAN 249
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFeLAEELGPnAEVVGIDISEEAIEKARENAQKLGFDNVEFEqgdIEELPELLEDdKFDVVISN 81

                          90       100
                  ....*....|....*....|....*....
gi 357548853  250 ---ILAEVLVPLIPQVPSRLNPHGHFLLA 275
Cdd:pfam13847  82 cvlNHIPDPDKVLQEILRVLKPGGRLIIS 110
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 166-249 3.22e-04

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 40.84  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 166 LMLSLLEslVRGGETMIDVGTGSGIL-AIAAERlgVSQILATDVDEIAVKNAQANIALNPVSHITVKANDLLQGLTVSA- 243
Cdd:COG2518   57 RMLEALD--LKPGDRVLEIGTGSGYQaAVLARL--AGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAp 132


                 ....*..
gi 357548853 244 -DLIVAN 249
Cdd:COG2518  133 fDRIIVT 139
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 170-295 6.61e-04

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 39.21  E-value: 6.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 170 LLESL-VRGGETMIDVGTGSGILAIAAERLGVsQILATDVDEIAVKNAQANIALNPVsHITVKANDLLQgLTV---SADL 245
Cdd:COG2226   14 LLAALgLRPGARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAAEAGL-NVEFVVGDAED-LPFpdgSFDL 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 357548853 246 IVAN-----------ILAEVLvplipqvpSRLNPHGHFLLAGIIAEKADLIRQTLQDNGFT 295
Cdd:COG2226   91 VISSfvlhhlpdperALAEIA--------RVLKPGGRLVVVDFSPPDLAELEELLAEAGFE 143
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 135-294 7.73e-04

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 39.78  E-value: 7.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 135 WEHYTPQQPDELVLTlDPGMafgtgthPTTQ-----LMLSLLEslVRGGETMIDVGTGSGILAIAAERL--GVSQILATD 207
Cdd:PRK00377   3 WKYVIPGIPDEEFER-DEEI-------PMTKeeiraLALSKLR--LRKGDMILDIGCGTGSVTVEASLLvgETGKVYAVD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 208 VDEIAV----KNAQANIALNPVSHITVKANDLLQGLTVSADLIVANILAEVLVPLIPQVPSRLNPHGHFLLAGIIAEKAD 283
Cdd:PRK00377  73 KDEKAInltrRNAEKFGVLNNIVLIKGEAPEILFTINEKFDRIFIGGGSEKLKEIISASWEIIKKGGRIVIDAILLETVN 152

                        170
                 ....*....|.
gi 357548853 284 LIRQTLQDNGF 294
Cdd:PRK00377 153 NALSALENIGF 163
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
177-274 9.41e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 37.88  E-value: 9.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 177 GGETMIDVGTGSGILAIA-AERLGVSQILATDVDEIAVKNAQANiaLNPVSHITVKANDLLqgLTVSADLIVANilaEVL 255
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALlAERFPGARVTGVDLSPEMLARARAR--LPNVRFVVADLRDLD--PPEPFDLVVSN---AAL 73

                         90       100
                 ....*....|....*....|....*
gi 357548853 256 ------VPLIPQVPSRLNPHGHFLL 274
Cdd:COG4106   74 hwlpdhAALLARLAAALAPGGVLAV 98
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 166-296 1.06e-03

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 40.54  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 166 LMLSLLEslVRGGETMIDVGTGSGILAIAAERLGVS-QILATDVDEIAVKNAQANIALNPVSHITV---KANDLLQGLTv 241
Cdd:COG2242  238 LTLAKLA--LRPGDVLWDIGAGSGSVSIEAARLAPGgRVYAIERDPERAALIRANARRFGVPNVEVvegEAPEALADLP- 314

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 357548853 242 SADLI--------VANILAEVLvplipqvpSRLNPHGHFLLAGIIAEKADLIRQTLQDNGFTI 296
Cdd:COG2242  315 DPDAVfiggsggnLPEILEACW--------ARLRPGGRLVANAVTLETLALALEALAELGYGG 369
PRK11727 PRK11727
23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;
180-231 1.38e-03

23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;


Pssm-ID: 236964  Cd Length: 321  Bit Score: 39.85  E-value: 1.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 357548853 180 TMIDVGTG-SGILAIaaerLGVS----QILATDVDEIAVKNAQANIALNPV--SHITVK 231
Cdd:PRK11727 117 RVLDIGVGaNCIYPL----IGVHeygwRFVGSDIDPQALASAQAIISANPGlnGAIRLR 171
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
165-299 1.72e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 38.83  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853 165 QLMLSLLESLV-RGGETMIDVGTGSGILAIAAERLGvSQILATDVDEIAVKNAQANIAlnpvsHITVKANDL--LQGLTV 241
Cdd:COG4976   33 LLAEELLARLPpGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSEEMLAKAREKGV-----YDRLLVADLadLAEPDG 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 357548853 242 SADLIVAN---ILAEVLVPLIPQVPSRLNPHGHFLLA-------GIIAEKADLIRQTLQDNGFTIAQR 299
Cdd:COG4976  107 RFDLIVAAdvlTYLGDLAAVFAGVARALKPGGLFIFSvedadgsGRYAHSLDYVRDLLAAAGFEVPGL 174
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 166-270 3.82e-03

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: 36.92  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  166 LMLSLLEslVRGGETMIDVGTGSGILAI-AAERLGVSQILATDVDEIAVKNAQANIALNPVSHITV---KANDLLQGLTV 241
Cdd:TIGR02469  10 LTLAKLR--LRPGDVLWDIGAGTGSVTIeAARLVPNGRVYAIERNPEALDLIERNLRRFGVSNIVIvegDAPEAPEALLP 87

                          90       100
                  ....*....|....*....|....*....
gi 357548853  242 SADLIVANILAEVLVPLIPQVPSRLNPHG 270
Cdd:TIGR02469  88 DPDAVFVGGSGGLLQEILEAVERRLRPGG 116
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 183-249 5.34e-03

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: 38.10  E-value: 5.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357548853  183 DVGTGSGILAIA-AERLGVSQILATDVDEIAVKNAQANIALNPVSH-ITVKANDLLQGLT-VSADLIVAN 249
Cdd:TIGR00536 120 DLGTGSGCIALAlAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHrVEFIQSNLFEPLAgQKIDIIVSN 189
 
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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