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Conserved domains on  [gi|930454569|ref|WP_054202602|]
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MULTISPECIES: 50S ribosomal protein L11 methyltransferase [Pseudoalteromonas]

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 ...
 2-291 5.18e-129

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: 368.52  E-value: 5.18e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569    2 AWIQIRINANAATADAVSDLLMEAGSASVTFIDAK---DTPIYEPKIGTVVFWADTTVIGLFEANHDMNAVVALLKRHDE 78
Cdd:pfam06325   1 TWLELSIHTTREAAEPVSNILEEFGALGVAIEDADlleDRDIFEPGLGEERLWDEVRVKALFDEETDALELIAQLAELIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569   79 LKDNLVYKIEQLEDKDWEREWMDNFHPIQFGEKLWICPSWRDIPD-PDAVNVLLDPGLAFGTGTHATTALCLKWLESQDL 157
Cdd:pfam06325  81 GLDSPKVTVEEVAEEDWARAWKKYFHPVRIGERLTIVPSWEDYPEnPDALNIELDPGMAFGTGTHPTTKLCLEALERLVK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  158 SGKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVYLPENQPEFTADIVVANILAQPLRE 237
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLPKEKADVVVANILADPLIE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 930454569  238 LHSVILGLLKPGGKIAMSGILEEQAKSVADIYAPFIELDEIAIEGDWTRVSGIK 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 ...
 2-291 5.18e-129

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: 368.52  E-value: 5.18e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569    2 AWIQIRINANAATADAVSDLLMEAGSASVTFIDAK---DTPIYEPKIGTVVFWADTTVIGLFEANHDMNAVVALLKRHDE 78
Cdd:pfam06325   1 TWLELSIHTTREAAEPVSNILEEFGALGVAIEDADlleDRDIFEPGLGEERLWDEVRVKALFDEETDALELIAQLAELIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569   79 LKDNLVYKIEQLEDKDWEREWMDNFHPIQFGEKLWICPSWRDIPD-PDAVNVLLDPGLAFGTGTHATTALCLKWLESQDL 157
Cdd:pfam06325  81 GLDSPKVTVEEVAEEDWARAWKKYFHPVRIGERLTIVPSWEDYPEnPDALNIELDPGMAFGTGTHPTTKLCLEALERLVK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  158 SGKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVYLPENQPEFTADIVVANILAQPLRE 237
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLPKEKADVVVANILADPLIE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 930454569  238 LHSVILGLLKPGGKIAMSGILEEQAKSVADIYAPFIELDEIAIEGDWTRVSGIK 291
Cdd:pfam06325 241 LAPDIYALVKPGGYLILSGILKEQAQMVAEAYSQGFELITVEHREEWVCIVGKK 294
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
1-293 8.43e-128

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 364.88  E-value: 8.43e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569   1 MAWIQIRINANAATADAVSDLLMEAGSASVTFIDAKDTPiyepkigtvvfWADTTVIGLFEANHDMNAVVALLKRHDELK 80
Cdd:COG2264    1 MKWIELTITTPEEAAEALSDALEELGAEGVEIEDAPPGL-----------WERVGVKAYFPEDEDLEELLAALAEALGEL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  81 DNLVYKIEQLEDKDWEREWMDNFHPIQFGEKLWICPSW-RDIPDPDAVNVLLDPGLAFGTGTHATTALCLKWLESQDLSG 159
Cdd:COG2264   70 GAPEITVEEVEEEDWVEEWKKYFKPIRVGDRLVIVPSWeEYEPDPGEIVIEIDPGMAFGTGTHPTTRLCLEALEKLLKPG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 160 KTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVYLPENQPEFTADIVVANILAQPLRELH 239
Cdd:COG2264  150 KTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLEDGPYDLVVANILANPLIELA 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 930454569 240 SVILGLLKPGGKIAMSGILEEQAKSVADIYAPF-IELDEIAIEGDWTRVSGIKKA 293
Cdd:COG2264  230 PDLAALLKPGGYLILSGILEEQADEVLAAYEAAgFELVERRERGEWVALVLRKKA 284
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
1-292 1.12e-117

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 337.89  E-value: 1.12e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569   1 MAWIQIRINANAATADAVSDLLMEAGSasvtfidakdtpiyepkigtvvfwadttviglfeanhdmNAVVALLKRHDELK 80
Cdd:PRK00517   1 MKWIELTLNTTPEAAEALSDILMELGA---------------------------------------LAALANLAGLGLDL 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  81 DNLVYKIEQLEDKDWEREWMDNFHPIQFGEKLWICPSWRDIPDPDAVNVLLDPGLAFGTGTHATTALCLKWLESQDLSGK 160
Cdd:PRK00517  42 GEPTYTIEEVEDEDWEREWKKYFHPIRIGDRLWIVPSWEDPPDPDEINIELDPGMAFGTGTHPTTRLCLEALEKLVLPGK 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 161 TVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVadKLEVYLPENQPEFtaDIVVANILAQPLRELHS 240
Cdd:PRK00517 122 TVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGV--ELNVYLPQGDLKA--DVIVANILANPLLELAP 197

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 930454569 241 VILGLLKPGGKIAMSGILEEQAKSVADIYAPF-IELDEIAIEGDWTRVSGIKK 292
Cdd:PRK00517 198 DLARLLKPGGRLILSGILEEQADEVLEAYEEAgFTLDEVLERGEWVALVGKKK 250
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 3-284 3.80e-115

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: 333.34  E-value: 3.80e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569    3 WIQIRINANAATADAVSDLLMEAGSASVTFIDAKDTPIYEPKI-GTVVFWADTTVIGLFEANHDMNAVVALLKRHDELKD 81
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFEDDKDTIYFEPHLpGEKRLWGNLDVIALFDAETDMNNSVIPLLEAFCLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569   82 NLVYKIEQLE-DKDWEREWMDNFHPIQFGEKLWICPSWRDIP-DPDAVNVLLDPGLAFGTGTHATTALCLKWLESQDLSG 159
Cdd:TIGR00406  81 GRNHKIEFDEfSKDWERAWKDNFHPVQFGKRFWICPSWRDVPsDEDALIIMLDPGLAFGTGTHPTTSLCLEWLEDLDLKD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  160 KTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVYLP--ENQPEFTADIVVANILAQPLRE 237
Cdd:TIGR00406 161 KNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDRLQVKLIylEQPIEGKADVIVANILAEVIKE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 930454569  238 LHSVILGLLKPGGKIAMSGILEEQAKSVADIYAPFIELDEIAIEGDW 284
Cdd:TIGR00406 241 LYPQFSRLVKPGGWLILSGILETQAQSVCDAYEQGFTVVEIRQREEW 287
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 161-255 1.85e-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: 57.05  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 161 TVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEAsLDNANRNGVADKLEVY------LPENQPEfTADIVVANILAQP 234
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALEL-ARKAAAALLADNVEVLkgdaeeLPPEADE-SFDVIISDPPLHH 78

                         90       100
                 ....*....|....*....|....*
gi 930454569 235 LRELHSVILG----LLKPGGKIAMS 255
Cdd:cd02440   79 LVEDLARFLEearrLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 2-291 5.18e-129

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: 368.52  E-value: 5.18e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569    2 AWIQIRINANAATADAVSDLLMEAGSASVTFIDAK---DTPIYEPKIGTVVFWADTTVIGLFEANHDMNAVVALLKRHDE 78
Cdd:pfam06325   1 TWLELSIHTTREAAEPVSNILEEFGALGVAIEDADlleDRDIFEPGLGEERLWDEVRVKALFDEETDALELIAQLAELIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569   79 LKDNLVYKIEQLEDKDWEREWMDNFHPIQFGEKLWICPSWRDIPD-PDAVNVLLDPGLAFGTGTHATTALCLKWLESQDL 157
Cdd:pfam06325  81 GLDSPKVTVEEVAEEDWARAWKKYFHPVRIGERLTIVPSWEDYPEnPDALNIELDPGMAFGTGTHPTTKLCLEALERLVK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  158 SGKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVYLPENQPEFTADIVVANILAQPLRE 237
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDLPKEKADVVVANILADPLIE 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 930454569  238 LHSVILGLLKPGGKIAMSGILEEQAKSVADIYAPFIELDEIAIEGDWTRVSGIK 291
Cdd:pfam06325 241 LAPDIYALVKPGGYLILSGILKEQAQMVAEAYSQGFELITVEHREEWVCIVGKK 294
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
1-293 8.43e-128

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 364.88  E-value: 8.43e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569   1 MAWIQIRINANAATADAVSDLLMEAGSASVTFIDAKDTPiyepkigtvvfWADTTVIGLFEANHDMNAVVALLKRHDELK 80
Cdd:COG2264    1 MKWIELTITTPEEAAEALSDALEELGAEGVEIEDAPPGL-----------WERVGVKAYFPEDEDLEELLAALAEALGEL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  81 DNLVYKIEQLEDKDWEREWMDNFHPIQFGEKLWICPSW-RDIPDPDAVNVLLDPGLAFGTGTHATTALCLKWLESQDLSG 159
Cdd:COG2264   70 GAPEITVEEVEEEDWVEEWKKYFKPIRVGDRLVIVPSWeEYEPDPGEIVIEIDPGMAFGTGTHPTTRLCLEALEKLLKPG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 160 KTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVYLPENQPEFTADIVVANILAQPLRELH 239
Cdd:COG2264  150 KTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDRIEVVLGDLLEDGPYDLVVANILANPLIELA 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 930454569 240 SVILGLLKPGGKIAMSGILEEQAKSVADIYAPF-IELDEIAIEGDWTRVSGIKKA 293
Cdd:COG2264  230 PDLAALLKPGGYLILSGILEEQADEVLAAYEAAgFELVERRERGEWVALVLRKKA 284
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
1-292 1.12e-117

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 337.89  E-value: 1.12e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569   1 MAWIQIRINANAATADAVSDLLMEAGSasvtfidakdtpiyepkigtvvfwadttviglfeanhdmNAVVALLKRHDELK 80
Cdd:PRK00517   1 MKWIELTLNTTPEAAEALSDILMELGA---------------------------------------LAALANLAGLGLDL 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  81 DNLVYKIEQLEDKDWEREWMDNFHPIQFGEKLWICPSWRDIPDPDAVNVLLDPGLAFGTGTHATTALCLKWLESQDLSGK 160
Cdd:PRK00517  42 GEPTYTIEEVEDEDWEREWKKYFHPIRIGDRLWIVPSWEDPPDPDEINIELDPGMAFGTGTHPTTRLCLEALEKLVLPGK 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 161 TVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVadKLEVYLPENQPEFtaDIVVANILAQPLRELHS 240
Cdd:PRK00517 122 TVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGV--ELNVYLPQGDLKA--DVIVANILANPLLELAP 197

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 930454569 241 VILGLLKPGGKIAMSGILEEQAKSVADIYAPF-IELDEIAIEGDWTRVSGIKK 292
Cdd:PRK00517 198 DLARLLKPGGRLILSGILEEQADEVLEAYEEAgFTLDEVLERGEWVALVGKKK 250
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 3-284 3.80e-115

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: 333.34  E-value: 3.80e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569    3 WIQIRINANAATADAVSDLLMEAGSASVTFIDAKDTPIYEPKI-GTVVFWADTTVIGLFEANHDMNAVVALLKRHDELKD 81
Cdd:TIGR00406   1 WIEIRINTTKELAEATSDALEEAGAVGVTFEDDKDTIYFEPHLpGEKRLWGNLDVIALFDAETDMNNSVIPLLEAFCLDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569   82 NLVYKIEQLE-DKDWEREWMDNFHPIQFGEKLWICPSWRDIP-DPDAVNVLLDPGLAFGTGTHATTALCLKWLESQDLSG 159
Cdd:TIGR00406  81 GRNHKIEFDEfSKDWERAWKDNFHPVQFGKRFWICPSWRDVPsDEDALIIMLDPGLAFGTGTHPTTSLCLEWLEDLDLKD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  160 KTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVYLP--ENQPEFTADIVVANILAQPLRE 237
Cdd:TIGR00406 161 KNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLAVESARKNAELNQVSDRLQVKLIylEQPIEGKADVIVANILAEVIKE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 930454569  238 LHSVILGLLKPGGKIAMSGILEEQAKSVADIYAPFIELDEIAIEGDW 284
Cdd:TIGR00406 241 LYPQFSRLVKPGGWLILSGILETQAQSVCDAYEQGFTVVEIRQREEW 287
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
156-229 2.62e-15

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 72.63  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 156 DLSGKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNG------VADKLEVYLPENqpeftADIVVAN 229
Cdd:COG2263   43 DIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAERLGvrvdfiRADVTRIPLGGS-----VDTVVMN 117
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 156-244 6.57e-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: 66.45  E-value: 6.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 156 DLSGKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVAdklevylpenqpeftADIVVANILAQPL 235
Cdd:COG3897   68 EVAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVA---------------ITTRLGDWRDPPA 132


                 ....*....
gi 930454569 236 RELHSVILG 244
Cdd:COG3897  133 AGGFDLILG 141
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 150-255 1.04e-12

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: 63.88  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 150 KWLESQDLSGKTVVDFGCGSGILGIAAIKLGAeRMIGIDIDPQALEASLDNANRNGV----ADKLEVYLPENQpeftADI 225
Cdd:COG2227   16 ALLARLLPAGGRVLDVGCGTGRLALALARRGA-DVTGVDISPEALEIARERAAELNVdfvqGDLEDLPLEDGS----FDL 90

                         90       100       110
                 ....*....|....*....|....*....|...
gi 930454569 226 VVANILAQPLRELHSV---ILGLLKPGGKIAMS 255
Cdd:COG2227   91 VICSEVLEHLPDPAALlreLARLLKPGGLLLLS 123
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 158-254 1.21e-12

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: 65.94  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 158 SGKTVVDFGCGSGILGIA-AIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVY------LPENQPEFTADIVVAN- 229
Cdd:COG4123   37 KGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIhgdlkeFAAELPPGSFDLVVSNp 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 930454569 230 ---------------------ILAQPLRELHSVILGLLKPGGKIAM 254
Cdd:COG4123  117 pyfkagsgrkspdearaiarhEDALTLEDLIRAAARLLKPGGRFAL 162
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
152-252 1.36e-11

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 62.75  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 152 LESQDLSGKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVYlpeNQPEFT------ADI 225
Cdd:COG4076   29 IERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVI---NADATDldlpekADV 105

                         90       100       110
                 ....*....|....*....|....*....|...
gi 930454569 226 VVANILAQ-PLRE-----LHSVILGLLKPGGKI 252
Cdd:COG4076  106 IISEMLDTaLLDEgqvpiLNHARKRLLKPGGRI 138
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 159-251 2.01e-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: 61.74  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 159 GKTVVDFGCGSGILGIAAIKLGAE-RMIGIDIDPQALEASLDNANRNGVADkLEVYLP---ENQPEFTADIVVANI---- 230
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKRNPEaRVTLVDVNARAVELARANAAANGLEN-VEVLWSdglSGVPDGSFDLILSNPpfha 128

                         90       100
                 ....*....|....*....|....*
gi 930454569 231 -LAQPLRELHSVILG---LLKPGGK 251
Cdd:COG2813  129 gRAVDKEVAHALIADaarHLRPGGE 153
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 161-255 1.85e-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: 57.05  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 161 TVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEAsLDNANRNGVADKLEVY------LPENQPEfTADIVVANILAQP 234
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALEL-ARKAAAALLADNVEVLkgdaeeLPPEADE-SFDVIISDPPLHH 78

                         90       100
                 ....*....|....*....|....*
gi 930454569 235 LRELHSVILG----LLKPGGKIAMS 255
Cdd:cd02440   79 LVEDLARFLEearrLLKPGGVLVLT 103
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 149-229 1.97e-10

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 60.16  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 149 LKWLesQDLSGKTVVDFGCGSGILGIA-AIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVY-------LPENQpe 220
Cdd:COG2890  105 LALL--PAGAPPRVLDLGTGSGAIALAlAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLqgdlfepLPGDG-- 180


                 ....*....
gi 930454569 221 fTADIVVAN 229
Cdd:COG2890  181 -RFDLIVSN 188
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 162-250 2.24e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 56.42  E-value: 2.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  162 VVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEV----YLPEnqPEFTADIVVANI------- 230
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQgdaeDLPF--PDGSFDLVVSSGvlhhlpd 78

                          90       100
                  ....*....|....*....|..
gi 930454569  231 --LAQPLRELHSVilglLKPGG 250
Cdd:pfam13649  79 pdLEAALREIARV----LKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 159-266 5.94e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 57.62  E-value: 5.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 159 GKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNG-------VADkLEVYLPENQPEFtaDIVVAN-- 229
Cdd:COG0500   27 GGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGlgnveflVAD-LAELDPLPAESF--DLVVAFgv 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 930454569 230 ---ILAQPLRELHSVILGLLKPGGKIAMSGILEEQAKSVA 266
Cdd:COG0500  104 lhhLPPEEREALLRELARALKPGGVLLLSASDAAAALSLA 143
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 132-254 1.42e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 55.71  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 132 DPGLAFGTGTHATTALCLKWLESQDlsGKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLE 211
Cdd:COG2230   27 DPDDTLEEAQEAKLDLILRKLGLKP--GMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVE 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 930454569 212 VYL------PENQPeftADIVVAN-----ILAQPLRELHSVILGLLKPGGKIAM 254
Cdd:COG2230  105 VRLadyrdlPADGQ---FDAIVSIgmfehVGPENYPAYFAKVARLLKPGGRLLL 155
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
158-255 2.67e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 55.39  E-value: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 158 SGKTVVDFGCGSGILGIAAIKLGAeRMIGIDIDPQALEAsldnANRNGVADKLEVY-LPE-NQPEFTADIVVANILAQPL 235
Cdd:COG4976   46 PFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAK----AREKGVYDRLLVAdLADlAEPDGRFDLIVAADVLTYL 120

                         90       100
                 ....*....|....*....|...
gi 930454569 236 RELHSV---ILGLLKPGGKIAMS 255
Cdd:COG4976  121 GDLAAVfagVARALKPGGLFIFS 143
PRK14968 PRK14968
putative methyltransferase; Provisional
 159-213 4.16e-09

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 54.90  E-value: 4.16e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 930454569 159 GKTVVDFGCGSGILGIAAIKLGAeRMIGIDIDPQALEASLDNANRNGVAD-KLEVY 213
Cdd:PRK14968  24 GDRVLEVGTGSGIVAIVAAKNGK-KVVGVDINPYAVECAKCNAKLNNIRNnGVEVI 78
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 145-252 1.13e-08

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: 53.36  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  145 TALCLKWLEsQDLSGKtVVDFGCGSGILGIAAIKLGAERMI-GIDIDPQALEASLDNANRNGVaDKLEVY---LPENQPE 220
Cdd:pfam05175  20 SRLLLEHLP-KDLSGK-VLDLGCGAGVLGAALAKESPDAELtMVDINARALESARENLAANGL-ENGEVVasdVYSGVED 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 930454569  221 FTADIVVANilaQPLRELHSVILGL-----------LKPGGKI 252
Cdd:pfam05175  97 GKFDLIISN---PPFHAGLATTYNVaqrfiadakrhLRPGGEL 136
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 151-277 2.00e-08

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 53.16  E-value: 2.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 151 WLEsQDLSGKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVY------LPENQPEFTAD 224
Cdd:COG0742   35 ILG-PDIEGARVLDLFAGSGALGLEALSRGAASVVFVEKDRKAAAVIRKNLEKLGLEDRARVIrgdalrFLKRLAGEPFD 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 225 IVVA------NILAQPLRELHSviLGLLKPGGKIamsgILEEQAKS-VADIYAPFIELDE 277
Cdd:COG0742  114 LVFLdppyakGLLEKALELLAE--NGLLAPGGLI----VVEHSKREeLPELPAGLELLKE 167
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 159-255 2.26e-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: 51.92  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 159 GKTVVDFGCGSGILGIAAIKLGAeRMIGIDIDPQALEASLDNANRNG------VADKLEVYLPENqpefTADIVVANI-- 230
Cdd:COG2226   23 GARVLDLGCGTGRLALALAERGA-RVTGVDISPEMLELARERAAEAGlnvefvVGDAEDLPFPDG----SFDLVISSFvl 97

                         90       100       110
                 ....*....|....*....|....*....|
gi 930454569 231 -----LAQPLRELHSVilglLKPGGKIAMS 255
Cdd:COG2226   98 hhlpdPERALAEIARV----LKPGGRLVVV 123
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 163-252 2.31e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 50.83  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  163 VDFGCGSGILGIAAIKLGAE-RMIGIDIDPQALEASL----DNANRNGVADKLEVYLPENQPEFTADIVVANILAQPLRE 237
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGlEYTGLDISPAALEAARerlaALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 930454569  238 LHSV---ILGLLKPGGKI 252
Cdd:pfam08242  81 PRAVlrnIRRLLKPGGVL 98
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 158-292 3.21e-08

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 53.63  E-value: 3.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 158 SGKTVVDFGCGSGILGIA-AIKLGAERMIGIDIDPQALEASLDNAnRNGVADKLEVY---LPENQPEFTADIVVAN---I 230
Cdd:PRK09328 108 EPLRVLDLGTGSGAIALAlAKERPDAEVTAVDISPEALAVARRNA-KHGLGARVEFLqgdWFEPLPGGRFDLIVSNppyI 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 231 ------LAQP--------------------LRELHSVILGLLKPGGKIAMSgILEEQAKSVADIYAPFiELDEIAIEGDW 284
Cdd:PRK09328 187 peadihLLQPevrdhephlalfggedgldfYRRIIEQAPRYLKPGGWLLLE-IGYDQGEAVRALLAAA-GFADVETRKDL 264

                        170
                 ....*....|.
gi 930454569 285 T---RVSGIKK 292
Cdd:PRK09328 265 AgrdRVVLGRR 275
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 158-255 7.60e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.88  E-value: 7.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  158 SGKTVVDFGCGSGILGI-AAIKLGAE-RMIGIDIDPQALEASLDNANRNG-------VADKLEvyLPENQPEFTADIVVA 228
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFeLAEELGPNaEVVGIDISEEAIEKARENAQKLGfdnvefeQGDIEE--LPELLEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 930454569  229 N-------ILAQPLRELHSVilglLKPGGKIAMS 255
Cdd:pfam13847  81 NcvlnhipDPDKVLQEILRV----LKPGGRLIIS 110
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 149-229 8.60e-08

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: 52.87  E-value: 8.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 149 LKWLEsqDLSGKTVVDFGCGSGILGIAAIKLGAeRMIGIDIDPQALEASLDNANRNG------VADKLEVYLPENQPEFT 222
Cdd:COG2265  226 LEWLD--LTGGERVLDLYCGVGTFALPLARRAK-KVIGVEIVPEAVEDARENARLNGlknvefVAGDLEEVLPELLWGGR 302


                 ....*..
gi 930454569 223 ADIVVAN 229
Cdd:COG2265  303 PDVVVLD 309
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
159-255 1.20e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 49.05  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 159 GKTVVDFGCGSGILG--IAAIKLGAeRMIGIDIDPQALEAsldnANRNG------VADklevyLPENQPEFTADIVVANI 230
Cdd:COG4106    2 PRRVLDLGCGTGRLTalLAERFPGA-RVTGVDLSPEMLAR----ARARLpnvrfvVAD-----LRDLDPPEPFDLVVSNA 71

                         90       100
                 ....*....|....*....|....*...
gi 930454569 231 LAQPLRELHSV---ILGLLKPGGKIAMS 255
Cdd:COG4106   72 ALHWLPDHAALlarLAAALAPGGVLAVQ 99
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 142-211 1.98e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 50.61  E-value: 1.98e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930454569 142 HATT-ALCLKWL-ESQDLSGKTVVDFGCGSGILGIAAIKLGAeRMIGIDIDPQALEASLDNANRNGVADKLE 211
Cdd:PRK07580  45 HQRMrDTVLSWLpADGDLTGLRILDAGCGVGSLSIPLARRGA-KVVASDISPQMVEEARERAPEAGLAGNIT 115
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 159-292 7.76e-07

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: 48.41  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 159 GKTVVDFGCGSG-ILgIAAIKLGAeRMIGIDIDPQALEASLDNANRNG-------VADKLEVYLPENqpefTADIVV--- 227
Cdd:COG1041   27 GDTVLDPFCGTGtIL-IEAGLLGR-RVIGSDIDPKMVEGARENLEHYGyedadviRGDARDLPLADE----SVDAIVtdp 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 930454569 228 -------------ANILAQPLRELHSVilglLKPGGKIAMsgileeqaksVADIYapfieLDEIAIEGDWTRVSGIKK 292
Cdd:COG1041  101 pygrsskisgeelLELYEKALEEAARV----LKPGGRVVI----------VTPRD-----IDELLEEAGFKVLERHEQ 159
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 163-254 8.95e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 46.12  E-value: 8.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  163 VDFGCGSGILGIAAIKLGAeRMIGIDIDPQALEASLDNANRNG----VADKLEVYLPENqpefTADIVVANILAQPLREL 238
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGVDISPEMLELAREKAPREGltfvVGDAEDLPFPDN----SFDLVLSSEVLHHVEDP 75

                          90
                  ....*....|....*....
gi 930454569  239 HSV---ILGLLKPGGKIAM 254
Cdd:pfam08241  76 ERAlreIARVLKPGGILII 94
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 159-263 1.25e-06

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 47.87  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 159 GKTVVDFGCGSGILGIAAIKLGAE--RMIGIDIDPQALEASLDNANRNGVADKLEV-------YLPENQPEFTADIVVAN 229
Cdd:PRK00377  41 GDMILDIGCGTGSVTVEASLLVGEtgKVYAVDKDEKAINLTRRNAEKFGVLNNIVLikgeapeILFTINEKFDRIFIGGG 120

                         90       100       110
                 ....*....|....*....|....*....|....
gi 930454569 230 ilAQPLRELHSVILGLLKPGGKIAMSGILEEQAK 263
Cdd:PRK00377 121 --SEKLKEIISASWEIIKKGGRIVIDAILLETVN 152
PRK14967 PRK14967
putative methyltransferase; Provisional
 159-229 1.46e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 48.13  E-value: 1.46e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 930454569 159 GKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGV-ADKLEVYLPENQPEFTADIVVAN 229
Cdd:PRK14967  37 GRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVdVDVRRGDWARAVEFRPFDVVVSN 108
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
151-254 2.73e-06

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 46.85  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  151 WLEsQDLSGKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALE------ASLDNANRNGVADKLEVYL--PENQPEFt 222
Cdd:pfam03602  35 WLA-PYIEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQilkenlQLLGLPGAVLVMDALLALLrlAGKGPVF- 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 930454569  223 aDIV---------VANILAQPLRElhsviLGLLKPGGKIAM 254
Cdd:pfam03602 113 -DIVfldppyakgLIEEVLDLLAE-----KGWLKPNALIYV 147
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 154-252 1.04e-05

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 46.39  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 154 SQDLSGKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLEVYL------PENQPEfTADIVV 227
Cdd:COG2520  176 ELVKPGERVLDMFAGVGPFSIPIAKRSGAKVVAIDINPDAVEYLKENIRLNKVEDRVTPILgdarevAPELEG-KADRII 254

                         90       100
                 ....*....|....*....|....*..
gi 930454569 228 ANIlaqPLRELH--SVILGLLKPGGKI 252
Cdd:COG2520  255 MNL---PHSADEflDAALRALKPGGVI 278
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 121-257 1.27e-05

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: 45.90  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 121 IPD--PDAVNVLLDPglaFGTGTHAttalclkWLESQDLSGKTVVDFGCGS-GILGIAAIKL-GAERMIGIDIDPQALEA 196
Cdd:COG1063  132 VPDglSDEAAALVEP---LAVALHA-------VERAGVKPGDTVLVIGAGPiGLLAALAARLaGAARVIVVDRNPERLEL 201

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 930454569 197 sldnANRNGVADKL---EVYLPENQPEFT----ADIVV-----ANILAQplrelhsvILGLLKPGGKIAMSGI 257
Cdd:COG1063  202 ----ARELGADAVVnprEEDLVEAVRELTggrgADVVIeavgaPAALEQ--------ALDLVRPGGTVVLVGV 262
arsM PRK11873
arsenite methyltransferase;
159-270 1.30e-05

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 45.71  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 159 GKTVVDFGCGSGI-LGIAAIKLGAE-RMIGIDIDPQALEASLDNANRNGVAD------KLEvYLPenQPEFTADIVVANI 230
Cdd:PRK11873  78 GETVLDLGSGGGFdCFLAARRVGPTgKVIGVDMTPEMLAKARANARKAGYTNvefrlgEIE-ALP--VADNSVDVIISNC 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 930454569 231 L-------AQPLRELHSVilglLKPGGKIAMSGI-----LEEQAKSVADIYA 270
Cdd:PRK11873 155 VinlspdkERVFKEAFRV----LKPGGRFAISDVvlrgeLPEEIRNDAELYA 202
PRK08317 PRK08317
hypothetical protein; Provisional
 159-255 2.20e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 44.93  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 159 GKTVVDFGCGSGILGIA-AIKLGAE-RMIGIDIDPQAL-------EASLDNA-NRNGVADKLEVylpenqPEFTADIVVA 228
Cdd:PRK08317  20 GDRVLDVGCGPGNDARElARRVGPEgRVVGIDRSEAMLalakeraAGLGPNVeFVRGDADGLPF------PDGSFDAVRS 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 930454569 229 -NIL------AQPLRELHSVilglLKPGGKIAMS 255
Cdd:PRK08317  94 dRVLqhledpARALAEIARV----LRPGGRVVVL 123
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 158-252 2.65e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 43.57  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  158 SGKTVVDFGCGSGILGIAAIKLGAErMIGIDIDPQALEASLDNANRNGVADKLEVYLPEnqpefTADIVVANI----LAQ 233
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQGFS-VTGVDPSPIAIERALLNVRFDQFDEQEAAVPAG-----KFDVIVAREvlehVPD 95

                          90
                  ....*....|....*....
gi 930454569  234 PLRELHSvILGLLKPGGKI 252
Cdd:pfam13489  96 PPALLRQ-IAALLKPGGLL 113
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 118-182 3.46e-05

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 44.46  E-value: 3.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 930454569 118 WRDI-PDPDAVN-VLLDpglaFGTGTHATTALCLKWL-ESQDLSGKTVVDFGCGSGILGIAAIKLGAE 182
Cdd:PLN02585 105 WRKIyGETDEVNkVQLD----IRLGHAQTVEKVLLWLaEDGSLAGVTVCDAGCGTGSLAIPLALEGAI 168
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 159-285 9.50e-05

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: 43.37  E-value: 9.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 159 GKTVVDFGCGS-GILGIAAIK-LGAERMIGIDIDPQALEASLD-------NANRNGVADKLEVYlpenqPEFTADIVVAN 229
Cdd:cd08236  160 GDTVVVIGAGTiGLLAIQWLKiLGAKRVIAVDIDDEKLAVARElgaddtiNPKEEDVEKVRELT-----EGRGADLVIEA 234

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 930454569 230 ILAQPLRELhsvILGLLKPGGKIAMSGILEEQAKSVADIYAPFIeLDEIAIEGDWT 285
Cdd:cd08236  235 AGSPATIEQ---ALALARPGGKVVLVGIPYGDVTLSEEAFEKIL-RKELTIQGSWN 286
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 150-259 1.09e-04

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 42.83  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 150 KWLESQdlSGKTVVDFGCGSGILGIAAIKLGAE--RMIGIDIDPQALEASLDNANRNGVADKLEVY------LP-ENQpe 220
Cdd:PRK00216  45 KWLGVR--PGDKVLDLACGTGDLAIALAKAVGKtgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVqgdaeaLPfPDN-- 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 930454569 221 fTADIV--------VANILaQPLRELHSVilglLKPGGKIAmsgILE 259
Cdd:PRK00216 121 -SFDAVtiafglrnVPDID-KALREMYRV----LKPGGRLV---ILE 158
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 118-195 3.62e-04

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 41.45  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 118 WRDIPD-PDAVNVLLDPglaFGTGTHatTALclkwleSQDLSGKTVVDFGCGS-GILGIAAIKL-GAERMIGIDIDPQAL 194
Cdd:cd05281  133 WKNDKDiPPEIASIQEP---LGNAVH--TVL------AGDVSGKSVLITGCGPiGLMAIAVAKAaGASLVIASDPNPYRL 201


                 .
gi 930454569 195 E 195
Cdd:cd05281  202 E 202
N6_N4_Mtase pfam01555
DNA methylase; Members of this family are DNA methylases. The family contains both N-4 ...
 159-199 3.96e-04

DNA methylase; Members of this family are DNA methylases. The family contains both N-4 cytosine-specific DNA methylases and N-6 Adenine-specific DNA methylases.


Pssm-ID: 396230 [Multi-domain]  Cd Length: 221  Bit Score: 40.85  E-value: 3.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 930454569  159 GKTVVDFGCGSGILGIAAIKLGaERMIGIDIDPQALEASLD 199
Cdd:pfam01555 182 GDIVLDPFAGSGTTGAAAKELG-RNFIGIEIEEEYVEIAKE 221
liver_alcohol_DH_like cd08277
Liver alcohol dehydrogenase; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the ...
 119-195 6.35e-04

Liver alcohol dehydrogenase; 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. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48) , 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. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an 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.


Pssm-ID: 176238 [Multi-domain]  Cd Length: 365  Bit Score: 40.78  E-value: 6.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 119 RDIPDPDAVNVLldpGLAFGTGTHATtalclkWLESQDLSGKTVVDFGCGSgiLGIAAIK----LGAERMIGIDIDPQAL 194
Cdd:cd08277  154 DPAAPLEHVCLL---GCGFSTGYGAA------WNTAKVEPGSTVAVFGLGA--VGLSAIMgakiAGASRIIGVDINEDKF 222


                 .
gi 930454569 195 E 195
Cdd:cd08277  223 E 223
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 159-211 9.79e-04

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: 40.16  E-value: 9.79e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 930454569 159 GKTVVDFGCGSGILGIAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKLE 211
Cdd:COG1092  217 GKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSATALEWAKENAALNGLDDRHE 269
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 145-213 1.05e-03

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: 40.24  E-value: 1.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 145 TALCLKWLESQDLSGKTVVDFGCGSGILGI-AAIKLGAERMIGiDIDPQALEASLDNANRNGVADkLEVY 213
Cdd:COG1867   44 SVAALRAYRERLKREISYLDALAASGIRGLrYALEVGIKVTLN-DIDPEAVELIRENLELNGLED-VEVY 111
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 159-229 1.33e-03

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: 38.88  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  159 GKTVVDFGCGSGILGIAAIKLGAER------------MIGIDIDPQALEASLDNANRNGVADKLEVY------LPENQPE 220
Cdd:pfam01170  29 GDPLLDPMCGSGTILIEAALMGANIapgkfdarvrapLYGSDIDRRMVQGARLNAENAGVGDLIEFVqadaadLPLLEGS 108


                  ....*....
gi 930454569  221 FtaDIVVAN 229
Cdd:pfam01170 109 V--DVIVTN 115
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 160-228 1.60e-03

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 37.93  E-value: 1.60e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 930454569  160 KTVVDFGCGSGILG-IAAIKLGAERMIGIDIDPQALEASLDNANRNGVADKL-------EVYLPENQPEFTaDIVVA 228
Cdd:pfam13679  27 ITIVDHGAGKGYLGfILYYLKYGVRVYGIDTRAELVEKANALAQKLGFNKRMsflegtiAGSTPVELPDRV-DVVTA 102
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 159-257 1.62e-03

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: 39.54  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 159 GKTVVDFGCGSgiLGIAAI----KLGAeRMIGIDIDPQALEasldNANRNGVA------DKLEVYLPENQPEFTADIVVA 228
Cdd:cd08254  166 GETVLVIGLGG--LGLNAVqiakAMGA-AVIAVDIKEEKLE----LAKELGADevlnslDDSPKDKKAAGLGGGFDVIFD 238

                         90       100
                 ....*....|....*....|....*....
gi 930454569 229 NILAQPLRELhsvILGLLKPGGKIAMSGI 257
Cdd:cd08254  239 FVGTQPTFED---AQKAVKPGGRIVVVGL 264
PLN02672 PLN02672
methionine S-methyltransferase
 160-218 2.54e-03

methionine S-methyltransferase


Pssm-ID: 215360 [Multi-domain]  Cd Length: 1082  Bit Score: 39.37  E-value: 2.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 930454569  160 KTVVDFGCGSGILGIA-AIKLGAERMIGIDIDPQALEASLDNANRNGVADK-LEVYLPENQ 218
Cdd:PLN02672  120 KTVAELGCGNGWISIAiAEKWLPSKVYGLDINPRAVKVAWINLYLNALDDDgLPVYDGEGK 180
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 118-195 2.72e-03

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 38.65  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 118 WRdIPD--PDAVNVLLDPglaFGTGTHatTALclkwleSQDLSGKTVVDFGCGS-GILGIA-AIKLGAERMIGIDIDPQA 193
Cdd:PRK05396 133 WK-IPDdiPDDLAAIFDP---FGNAVH--TAL------SFDLVGEDVLITGAGPiGIMAAAvAKHVGARHVVITDVNEYR 200


                 ..
gi 930454569 194 LE 195
Cdd:PRK05396 201 LE 202
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 162-287 3.61e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 38.04  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569  162 VVDFGCGSGILGIAAIKLG-AERMIGIDIDPQALE--ASLDNANRNGVADKLE-VYLPENQpeftADIVVANI------- 230
Cdd:TIGR02072  38 VLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAqaKTKLSENVQFICGDAEkLPLEDSS----FDLIVSNLalqwcdd 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 930454569  231 LAQPLRELHSVilglLKPGGKIAMS----GILEEQAKSVADIYAPFIELDEI--AIEGDWTRV 287
Cdd:TIGR02072 114 LSQALSELARV----LKPGGLLAFStfgpGTLHELRQSFGQHGLRYLSLDELkaLLKNSFELL 172
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
159-199 3.65e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 37.98  E-value: 3.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 930454569 159 GKTVVDFGCGSGILGIAAIKLGAeRMIGIDIDPQALEASLD 199
Cdd:COG0863  183 GDIVLDPFAGSGTTLVAAERLGR-RFIGIEIDPEYVEVARR 222
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 183-229 6.65e-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: 37.77  E-value: 6.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 930454569 183 RMIGIDIDPQALEASLDNANRNGVADKLEVY---LPENQPEFTADIVVAN 229
Cdd:COG0116  252 PIFGSDIDPRAIEAARENAERAGVADLIEFEqadFRDLEPPAEPGLIITN 301
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 168-213 7.49e-03

N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional


Pssm-ID: 235286  Cd Length: 382  Bit Score: 37.59  E-value: 7.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 930454569 168 GSGILGI-AAIKLGAERMIGIDIDPQALEASLDNANRNGVaDKLEVY 213
Cdd:PRK04338  67 ASGIRGIrYALETGVEKVTLNDINPDAVELIKKNLELNGL-ENEKVF 112
Zn_ADH_class_III cd08279
Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, ...
 159-198 7.58e-03

Class III alcohol dehydrogenase; Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. 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. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an 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.


Pssm-ID: 176240 [Multi-domain]  Cd Length: 363  Bit Score: 37.52  E-value: 7.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 930454569 159 GKTVVDFGCGsGIlGIAAI---KL-GAERMIGIDIDPQALEASL 198
Cdd:cd08279  183 GDTVAVIGCG-GV-GLNAIqgaRIaGASRIIAVDPVPEKLELAR 224
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 119-260 8.60e-03

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have 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.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 37.25  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 930454569 119 RDIPDPDAVNVlldpGLAFGTGTHATtalclkwlESQDLS-GKTVVDFGCGS-GILGIAAIKL-GAERMIGIDIDPQALE 195
Cdd:cd05278  139 DGLPDEDALML----SDILPTGFHGA--------ELAGIKpGSTVAVIGAGPvGLCAVAGARLlGAARIIAVDSNPERLD 206

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 930454569 196 ASLDN-----ANRNGVADKLEVYLPENQPEFTADIVVA---NILAQPLRelhsvilgLLKPGGKIAMSGILEE 260
Cdd:cd05278  207 LAKEAgatdiINPKNGDIVEQILELTGGRGVDCVIEAVgfeETFEQAVK--------VVRPGGTIANVGVYGK 271
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 159-195 9.11e-03

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. 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.


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 37.13  E-value: 9.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 930454569 159 GKTVVDFGCGS-GILGIA-AIKLGAERMIGIDIDPQALE 195
Cdd:cd08283  185 GDTVAVWGCGPvGLFAARsAKLLGAERVIAIDRVPERLE 223
 
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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