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Conserved domains on  [gi|491949657|ref|WP_005687091|]
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class I SAM-dependent methyltransferase [Lacticaseibacillus rhamnosus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11457987)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Methanocaldococcus jannaschii S-adenosylmethionine-dependent methyltransferase MJ0882

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 8-198 2.18e-73

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: 219.68  E-value: 2.18e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   8 DPDLAHDERTFDFELGGHRLRFTTDNGVFSKHTVDFGSRVLIATVlaETLPDGPILDVGAGYGPIGLALAKHFPNRQVTM 87
Cdd:COG2813    1 APAASDWPRTITVRLAGRDLTFVTLPGVFSRDRLDIGTRLLLEHL--PEPLGGRVLDLGCGYGVIGLALAKRNPEARVTL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  88 SDVNERALALAKQNAADNGITNVSIIESSMYDGIDD-QFAVVVTNPPIRAG----KAIVSGILSGAAAHLLPGGQLYAVI 162
Cdd:COG2813   79 VDVNARAVELARANAAANGLENVEVLWSDGLSGVPDgSFDLILSNPPFHAGravdKEVAHALIADAARHLRPGGELWLVA 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 491949657 163 QKKQgapSALKLMKATYANAEVIKKEHGYYILKASK 198
Cdd:COG2813  159 NRHL---PYERKLEELFGNVEVLARNKGFKVLRAVK 191
 
Name Accession Description Interval E-value
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 8-198 2.18e-73

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: 219.68  E-value: 2.18e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   8 DPDLAHDERTFDFELGGHRLRFTTDNGVFSKHTVDFGSRVLIATVlaETLPDGPILDVGAGYGPIGLALAKHFPNRQVTM 87
Cdd:COG2813    1 APAASDWPRTITVRLAGRDLTFVTLPGVFSRDRLDIGTRLLLEHL--PEPLGGRVLDLGCGYGVIGLALAKRNPEARVTL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  88 SDVNERALALAKQNAADNGITNVSIIESSMYDGIDD-QFAVVVTNPPIRAG----KAIVSGILSGAAAHLLPGGQLYAVI 162
Cdd:COG2813   79 VDVNARAVELARANAAANGLENVEVLWSDGLSGVPDgSFDLILSNPPFHAGravdKEVAHALIADAARHLRPGGELWLVA 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 491949657 163 QKKQgapSALKLMKATYANAEVIKKEHGYYILKASK 198
Cdd:COG2813  159 NRHL---PYERKLEELFGNVEVLARNKGFKVLRAVK 191
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 27-195 6.48e-56

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: 174.70  E-value: 6.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   27 LRFTTDNGVFSKHTVDFGSRVLIATVlaETLPDGPILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNG 106
Cdd:pfam05175   2 LTFKTLPGVFSHGRLDIGSRLLLEHL--PKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  107 ITNVSIIESSMYDGI-DDQFAVVVTNPPIRAGKA----IVSGILSGAAAHLLPGGQLYAVIQKKQGAPSalkLMKATYAN 181
Cdd:pfam05175  80 LENGEVVASDVYSGVeDGKFDLIISNPPFHAGLAttynVAQRFIADAKRHLRPGGELWIVANRFLGYPP---LLEELFGN 156

                         170
                  ....*....|....
gi 491949657  182 AEVIKKEHGYYILK 195
Cdd:pfam05175 157 VEVVAKTNGFKVLK 170
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 47-186 5.85e-24

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 95.23  E-value: 5.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  47 VLIATVLAETLPDGP--ILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGI-DD 123
Cdd:PRK09328  95 ELVEWALEALLLKEPlrVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEPLpGG 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657 124 QFAVVVTNPP-IRAGK---------------AIVSG---------ILSGAAAHLLPGGQLYAVIQKKQGApSALKLMKAT 178
Cdd:PRK09328 175 RFDLIVSNPPyIPEADihllqpevrdhephlALFGGedgldfyrrIIEQAPRYLKPGGWLLLEIGYDQGE-AVRALLAAA 253


                 ....*....
gi 491949657 179 -YANAEVIK 186
Cdd:PRK09328 254 gFADVETRK 262
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 62-162 9.02e-15

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: 67.07  E-value: 9.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  62 ILDVGAGYGPIGLALAKHfPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGI---DDQFAVVVTNPPIRAGK 138
Cdd:cd02440    2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpeaDESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....
gi 491949657 139 AIVSGILSGAAAHLLPGGQLYAVI 162
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTL 104
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 62-133 5.20e-14

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: 68.53  E-value: 5.20e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491949657   62 ILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGIT-NVSIIESSMYDGID-DQFAVVVTNPP 133
Cdd:TIGR00536 118 ILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEhRVEFIQSNLFEPLAgQKIDIIVSNPP 191
 
Name Accession Description Interval E-value
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 8-198 2.18e-73

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: 219.68  E-value: 2.18e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   8 DPDLAHDERTFDFELGGHRLRFTTDNGVFSKHTVDFGSRVLIATVlaETLPDGPILDVGAGYGPIGLALAKHFPNRQVTM 87
Cdd:COG2813    1 APAASDWPRTITVRLAGRDLTFVTLPGVFSRDRLDIGTRLLLEHL--PEPLGGRVLDLGCGYGVIGLALAKRNPEARVTL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  88 SDVNERALALAKQNAADNGITNVSIIESSMYDGIDD-QFAVVVTNPPIRAG----KAIVSGILSGAAAHLLPGGQLYAVI 162
Cdd:COG2813   79 VDVNARAVELARANAAANGLENVEVLWSDGLSGVPDgSFDLILSNPPFHAGravdKEVAHALIADAARHLRPGGELWLVA 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 491949657 163 QKKQgapSALKLMKATYANAEVIKKEHGYYILKASK 198
Cdd:COG2813  159 NRHL---PYERKLEELFGNVEVLARNKGFKVLRAVK 191
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 27-195 6.48e-56

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: 174.70  E-value: 6.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   27 LRFTTDNGVFSKHTVDFGSRVLIATVlaETLPDGPILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNG 106
Cdd:pfam05175   2 LTFKTLPGVFSHGRLDIGSRLLLEHL--PKDLSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  107 ITNVSIIESSMYDGI-DDQFAVVVTNPPIRAGKA----IVSGILSGAAAHLLPGGQLYAVIQKKQGAPSalkLMKATYAN 181
Cdd:pfam05175  80 LENGEVVASDVYSGVeDGKFDLIISNPPFHAGLAttynVAQRFIADAKRHLRPGGELWIVANRFLGYPP---LLEELFGN 156

                         170
                  ....*....|....
gi 491949657  182 AEVIKKEHGYYILK 195
Cdd:pfam05175 157 VEVVAKTNGFKVLK 170
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 47-186 5.85e-24

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 95.23  E-value: 5.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  47 VLIATVLAETLPDGP--ILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGI-DD 123
Cdd:PRK09328  95 ELVEWALEALLLKEPlrVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEPLpGG 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657 124 QFAVVVTNPP-IRAGK---------------AIVSG---------ILSGAAAHLLPGGQLYAVIQKKQGApSALKLMKAT 178
Cdd:PRK09328 175 RFDLIVSNPPyIPEADihllqpevrdhephlALFGGedgldfyrrIIEQAPRYLKPGGWLLLEIGYDQGE-AVRALLAAA 253


                 ....*....
gi 491949657 179 -YANAEVIK 186
Cdd:PRK09328 254 gFADVETRK 262
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 47-186 5.47e-23

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 92.91  E-value: 5.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  47 VLIATVLAETLPDGP--ILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITN-VSIIESSMYDGIDD 123
Cdd:COG2890   99 ELVELALALLPAGAPprVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDLFEPLPG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657 124 --QFAVVVTNPP-IRAGK---------------AIVSG---------ILSGAAAHLLPGGQLYAVIQKKQGaPSALKLMK 176
Cdd:COG2890  179 dgRFDLIVSNPPyIPEDEiallppevrdheprlALDGGedgldfyrrIIAQAPRLLKPGGWLLLEIGEDQG-EAVRALLE 257

                        170
                 ....*....|.
gi 491949657 177 AT-YANAEVIK 186
Cdd:COG2890  258 AAgFADVETHK 268
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
34-187 8.19e-22

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


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 90.77  E-value: 8.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  34 GVFSKHTVDFGSRVLIATVLAETlpDGPILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITNvSII 113
Cdd:PRK09489 174 GVFSRDGLDVGSQLLLSTLTPHT--KGKVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRATLAANGLEG-EVF 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657 114 ESSMYDGIDDQFAVVVTNPPIRAG-----KAiVSGILSGAAAHLLPGGQLYAViqkkqgAPSAL---KLMKATYANAEVI 185
Cdd:PRK09489 251 ASNVFSDIKGRFDMIISNPPFHDGiqtslDA-AQTLIRGAVRHLNSGGELRIV------ANAFLpypDLLDETFGSHEVL 323


                 ..
gi 491949657 186 KK 187
Cdd:PRK09489 324 AQ 325
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 62-162 9.02e-15

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: 67.07  E-value: 9.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  62 ILDVGAGYGPIGLALAKHfPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGI---DDQFAVVVTNPPIRAGK 138
Cdd:cd02440    2 VLDLGCGTGALALALASG-PGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpeaDESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....
gi 491949657 139 AIVSGILSGAAAHLLPGGQLYAVI 162
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTL 104
PRK14968 PRK14968
putative methyltransferase; Provisional
 53-189 1.21e-14

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 68.77  E-value: 1.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  53 LAETLPDGP---ILDVGAGYGPIGLALAKHfpNRQVTMSDVNERALALAKQNAADNGITN--VSIIESSMYDGI-DDQFA 126
Cdd:PRK14968  15 LAENAVDKKgdrVLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIRNngVEVIRSDLFEPFrGDKFD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657 127 VVVTNPPI--------------------RAGKAIVSGILSGAAAHLLPGGQLYAVIQKKQGAPSALKLMKATYANAEVIK 186
Cdd:PRK14968  93 VILFNPPYlpteeeeewddwlnyalsggKDGREVIDRFLDEVGRYLKPGGRILLLQSSLTGEDEVLEYLEKLGFEAEVVA 172


                 ...
gi 491949657 187 KEH 189
Cdd:PRK14968 173 EEK 175
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 11-137 2.91e-14

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: 69.82  E-value: 2.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  11 LAHDERTFDFELGGHRLRFTTDngvfskhtvDF------GSRVLIATVL--AETLPDGPILDVGAGYGPIGLALAKHFpn 82
Cdd:COG2265  187 VRAGRDYLTERLGGLTFRISPG---------SFfqvnpeQAEALYAAALewLDLTGGERVLDLYCGVGTFALPLARRA-- 255

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  83 RQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGIDDQ-----FAVVVTNPPiRAG 137
Cdd:COG2265  256 KKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLPELlwggrPDVVVLDPP-RAG 314
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 62-162 4.50e-14

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 68.25  E-value: 4.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  62 ILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITN-VSIIESSMYD----GIDDQFAVVVTNPPIR- 135
Cdd:COG4123   41 VLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDLKEfaaeLPPGSFDLVVSNPPYFk 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491949657 136 AGKAIVSG-----------------ILSGAAAHLLPGGQLYAVI 162
Cdd:COG4123  121 AGSGRKSPdearaiarhedaltledLIRAAARLLKPGGRFALIH 164
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 62-133 5.20e-14

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: 68.53  E-value: 5.20e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491949657   62 ILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGIT-NVSIIESSMYDGID-DQFAVVVTNPP 133
Cdd:TIGR00536 118 ILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQLEhRVEFIQSNLFEPLAgQKIDIIVSNPP 191
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 62-156 3.77e-11

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.19  E-value: 3.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   62 ILDVGAGYGPIGLALAKHFpNRQVTMSDVNERALALAKQNAADNGItNVSIIESSM--YDGIDDQFAVVVTNPPIRA-GK 138
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAedLPFPDGSFDLVVSSGVLHHlPD 78

                          90
                  ....*....|....*...
gi 491949657  139 AIVSGILSGAAAHLLPGG 156
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 47-166 4.43e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 59.54  E-value: 4.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  47 VLIATVLAETLPDG-PILDVGAGYGPIGLALAKHFpNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGI---D 122
Cdd:COG0500   14 LAALLALLERLPKGgRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDplpA 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491949657 123 DQFAVVV-------TNPPIRagkaivSGILSGAAAHLLPGGQLYAVIQKKQ 166
Cdd:COG0500   93 ESFDLVVafgvlhhLPPEER------EALLRELARALKPGGVLLLSASDAA 137
PRK15001 PRK15001
23S rRNA (guanine(1835)-N(2))-methyltransferase RlmG;
7-198 8.59e-11

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


Pssm-ID: 184963 [Multi-domain]  Cd Length: 378  Bit Score: 60.04  E-value: 8.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   7 NDPDLAHDERTFDFELGGHRLRFTTDNGVFSKHTVDFGSRVLIATvLAETLpDGPILDVGAGYGPIGLALAKHFPNRQVT 86
Cdd:PRK15001 179 NEPPLADAPQTVSWKLEGTDWTIHNHANVFSRTGLDIGARFFMQH-LPENL-EGEIVDLGCGNGVIGLTLLDKNPQAKVV 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  87 MSDVNERALALAKQNAADN---GITNVSIIESSMYDGIDD-QFAVVVTNPPIRAGKAIVSGILSGAAAH----LLPGGQL 158
Cdd:PRK15001 257 FVDESPMAVASSRLNVETNmpeALDRCEFMINNALSGVEPfRFNAVLCNPPFHQQHALTDNVAWEMFHHarrcLKINGEL 336

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 491949657 159 YAVIQKKQgapSALKLMKATYANAEVIKKEHGYYILKASK 198
Cdd:PRK15001 337 YIVANRHL---DYFHKLKKIFGNCTTIATNNKFVVLKAVK 373
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
58-158 1.14e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 53.29  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  58 PDGPILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAAdngitNVSIIESSMYD-GIDDQFAVVVTN----- 131
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLP-----NVRFVVADLRDlDPPEPFDLVVSNaalhw 75

                         90       100
                 ....*....|....*....|....*...
gi 491949657 132 -PPIRAgkaivsgILSGAAAHLLPGGQL 158
Cdd:COG4106   76 lPDHAA-------LLARLAAALAPGGVL 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 49-159 3.04e-09

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: 52.71  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  49 IATVLAETLPDGP-ILDVGAGYGPIGLALAKHfpNRQVTMSDVNERALALAKQNAADngiTNVSIIESSMYD--GIDDQF 125
Cdd:COG2227   14 LAALLARLLPAGGrVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAE---LNVDFVQGDLEDlpLEDGSF 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491949657 126 AVVVTN------PPIRAgkaivsgILSGAAAHLLPGGQLY 159
Cdd:COG2227   89 DLVICSevlehlPDPAA-------LLRELARLLKPGGLLL 121
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 62-133 4.79e-09

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 54.87  E-value: 4.79e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491949657  62 ILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITN-VSIIESSMYDGIDDQ-FAVVVTNPP 133
Cdd:PRK01544 142 ILELGTGSGCIAISLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDrIQIIHSNWFENIEKQkFDFIVSNPP 215
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
62-158 1.80e-08

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 51.93  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  62 ILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGIDDQFAVVVtnppIRAGKAIV 141
Cdd:PRK08287  35 LIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGNIDIIPGEAPIELPGKADAIF----IGGSGGNL 110

                         90
                 ....*....|....*..
gi 491949657 142 SGILSGAAAHLLPGGQL 158
Cdd:PRK08287 111 TAIIDWSLAHLHPGGRL 127
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 58-195 9.16e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 49.34  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   58 PDGPILDVGAGYGPIGLALA-KHFPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYD----GIDDQFAVVVTNP 132
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAeELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEElpelLEDDKFDVVISNC 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491949657  133 PIRAGKAIVSgILSGAAAHLLPGGQLYAV-IQKKQGAPSALKLMKATYAN--AEVIKKEHGYYILK 195
Cdd:pfam13847  83 VLNHIPDPDK-VLQEILRVLKPGGRLIISdPDSLAELPAHVKEDSTYYAGcvGGAILKKKLYELLE 147
PRK14967 PRK14967
putative methyltransferase; Provisional
 45-185 1.94e-07

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 49.28  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  45 SRVLIATVLAETLPDGP-ILDVGAGYGPIGLAlAKHFPNRQVTMSDVNERALALAKQNAADNGITnVSIIESSMYDGID- 122
Cdd:PRK14967  22 TQLLADALAAEGLGPGRrVLDLCTGSGALAVA-AAAAGAGSVTAVDISRRAVRSARLNALLAGVD-VDVRRGDWARAVEf 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657 123 DQFAVVVTNPPI--------------RA------GKAIVSGILSGAAAHLLPGGQLYAVIQKKQGAPSALKLMKATYANA 182
Cdd:PRK14967 100 RPFDVVVSNPPYvpappdappsrgpaRAwdagpdGRAVLDRLCDAAPALLAPGGSLLLVQSELSGVERTLTRLSEAGLDA 179


                 ...
gi 491949657 183 EVI 185
Cdd:PRK14967 180 EVV 182
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
46-161 2.13e-07

precorrin-6Y C5,15-methyltransferase subunit CbiT;


Pssm-ID: 180961  Cd Length: 196  Bit Score: 49.22  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  46 RVLIATVLAETlPDGPILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGIDDqf 125
Cdd:PRK07402  29 RLLLISQLRLE-PDSVLWDIGAGTGTIPVEAGLLCPKGRVIAIERDEEVVNLIRRNCDRFGVKNVEVIEGSAPECLAQ-- 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491949657 126 avvVTNPPIRA----GKAIvSGILSGAAAHLLPGGQLYAV 161
Cdd:PRK07402 106 ---LAPAPDRVciegGRPI-KEILQAVWQYLKPGGRLVAT 141
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 58-161 4.47e-07

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: 47.30  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  58 PDGPILDVGAGYGPIGLALAKHfpNRQVTMSDVNERALALAKQNAADNGItNVSIIESSMYDgI---DDQFAVVVTN--- 131
Cdd:COG2226   22 PGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAED-LpfpDGSFDLVISSfvl 97

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491949657 132 ---PPIRAgkaivsgILSGAAAHLLPGGQLYAV 161
Cdd:COG2226   98 hhlPDPER-------ALAEIARVLKPGGRLVVV 123
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 63-158 5.06e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 46.21  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   63 LDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGIDD---QFAVVVTN------PP 133
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELdpgSFDVVVASnvlhhlAD 80

                          90       100
                  ....*....|....*....|....*
gi 491949657  134 IRAgkaivsgILSGAAAHLLPGGQL 158
Cdd:pfam08242  81 PRA-------VLRNIRRLLKPGGVL 98
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 58-156 7.57e-07

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: 48.24  E-value: 7.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  58 PDGPILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGIDD--QFAVVVtnppIR 135
Cdd:COG2242  247 PGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPEALADlpDPDAVF----IG 322

                         90       100
                 ....*....|....*....|.
gi 491949657 136 AGKAIVSGILSGAAAHLLPGG 156
Cdd:COG2242  323 GSGGNLPEILEACWARLRPGG 343
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
49-119 3.59e-06

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 46.11  E-value: 3.59e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491949657  49 IATVLAeTLPDGP--ILDVGAGYGPIGLALAK--HfpnrQVTMSDVNERALALAKQNAADNGIT-NVSIIESSMYD 119
Cdd:PRK11036  34 LDRLLA-ELPPRPlrVLDAGGGEGQTAIKLAElgH----QVILCDLSAEMIQRAKQAAEAKGVSdNMQFIHCAAQD 104
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 48-133 3.95e-06

unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 46.23  E-value: 3.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  48 LIATVLAETLPDGPILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGiTNVSIIESSMYDG---IDDQ 124
Cdd:PRK14966 241 LVEAVLARLPENGRVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNAADLG-ARVEFAHGSWFDTdmpSEGK 319


                 ....*....
gi 491949657 125 FAVVVTNPP 133
Cdd:PRK14966 320 WDIIVSNPP 328
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 62-109 7.77e-06

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 44.25  E-value: 7.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 491949657   62 ILDVGAGYGPIGLALAKHFPNRQVTMSDVNErALALAKQNAADNGITN 109
Cdd:pfam10294  50 VLELGSGTGLVGIAVALLLPGASVTITDLEE-ALELLKKNIELNALSS 96
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
57-133 1.45e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 43.74  E-value: 1.45e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491949657  57 LPDGPILDVGAGYGPIGLAlAKHFPNRQVTMSDVNERALALAKQNAADNGiTNVSIIESSMYD-GIDDQFAVVVTNPP 133
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAIG-AALLGAKKVVGVDIDPEALEIARENAERLG-VRVDFIRADVTRiPLGGSVDTVVMNPP 119
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 53-162 2.54e-05

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: 43.01  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  53 LAETLPDGPILDVGAGYGpiGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYD--GIDDQFAVVVT 130
Cdd:COG1041   21 LAGAKEGDTVLDPFCGTG--TILIEAGLLGRRVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDlpLADESVDAIVT 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491949657 131 NPP------IRAG--KAIVSGILSGAAAHLLPGGqlYAVI 162
Cdd:COG1041   99 DPPygrsskISGEelLELYEKALEEAARVLKPGG--RVVI 136
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
57-158 3.12e-05

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 43.24  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  57 LPDGPILDVGAGYGpIgLA-LAKHFPNRQVTMSDVNERALALAKQNAADNGITN-VSIIESSMYDgiDDQFAVVVTNppi 134
Cdd:COG2264  147 KPGKTVLDVGCGSG-I-LAiAAAKLGAKRVLAVDIDPVAVEAARENAELNGVEDrIEVVLGDLLE--DGPYDLVVAN--- 219

                         90       100
                 ....*....|....*....|....*...
gi 491949657 135 ragkaIVSGIL----SGAAAHLLPGGQL 158
Cdd:COG2264  220 -----ILANPLielaPDLAALLKPGGYL 242
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 47-113 3.37e-05

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 43.37  E-value: 3.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491949657  47 VLIATVLAETLPDGPILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITNVSII 113
Cdd:PRK04338  46 VLVLRAFGPKLPRESVLDALSASGIRGIRYALETGVEKVTLNDINPDAVELIKKNLELNGLENEKVF 112
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 51-104 6.04e-05

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: 42.61  E-value: 6.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491949657  51 TVLAETLPDGPILDVGAGygPIGL---ALAKHFPNRQVTMSDVNERALALAKQNAAD 104
Cdd:cd05281  156 TVLAGDVSGKSVLITGCG--PIGLmaiAVAKAAGASLVIASDPNPYRLELAKKMGAD 210
PRK06202 PRK06202
hypothetical protein; Provisional
 8-131 7.62e-05

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 41.91  E-value: 7.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   8 DPDL---AHDeRTFDfelgghrlRFTTDNGVFSkhtvdfGSRVLIATVLAETL-PDGP--ILDVGAGYGPIGLALAkHFP 81
Cdd:PRK06202  19 DPGCdpaRLD-RTYA--------GFRRVNRIVA------GWRGLYRRLLRPALsADRPltLLDIGCGGGDLAIDLA-RWA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491949657  82 NRQ-----VTMSDVNERALALAKQNAADNGITnVSIIESSMYDGIDDQFAVVVTN 131
Cdd:PRK06202  83 RRDglrleVTAIDPDPRAVAFARANPRRPGVT-FRQAVSDELVAEGERFDVVTSN 136
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 51-111 7.74e-05

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 42.50  E-value: 7.74e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491949657  51 TVLAETLPDGPILDVGAGygPIGL---ALAKHFPNRQVTMSDVNERALALAKQNAADNGItNVS 111
Cdd:PRK05396 156 TALSFDLVGEDVLITGAG--PIGImaaAVAKHVGARHVVITDVNEYRLELARKMGATRAV-NVA 216
tRNA_U5-meth_tr pfam05958
tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC: ...
 59-137 9.26e-05

tRNA (Uracil-5-)-methyltransferase; This family consists of (Uracil-5-)-methyltransferases EC:2.1.1.35 from bacteria, archaea and eukaryotes. A 5-methyluridine (m(5)U) residue at position 54 is a conserved feature of bacterial and eukaryotic tRNAs. The methylation of U54 is catalyzed by the tRNA(m5U54)methyltransferase, which in Saccharomyces cerevisiae is encoded by the nonessential TRM2 gene. It is thought that tRNA modification enzymes might have a role in tRNA maturation not necessarily linked to their known catalytic activity.


Pssm-ID: 428692  Cd Length: 357  Bit Score: 42.04  E-value: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   59 DGPILDVGAGYGPIGLALAKHFpnRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYD---------------GID- 122
Cdd:pfam05958 202 KGDLLELYCGNGNFSLALARNF--RKVLATEIAKPSVAAAQYNIAANNIDNVQIIRMSAEEftqamngvrefnrlkGIDl 279

                          90
                  ....*....|....*..
gi 491949657  123 --DQFAVVVTNPPiRAG 137
Cdd:pfam05958 280 ksYNCSTIFVDPP-RAG 295
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
48-167 1.12e-04

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 41.14  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  48 LIATVLAE--TLPDGPILDVGAGYGPIGLALAKHFpnRQVTMSDVNERALALAKQNAADNGITNVSIIEssmYDGIDDQF 125
Cdd:COG4976   34 LAEELLARlpPGPFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKAREKGVYDRLLVADLAD---LAEPDGRF 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 491949657 126 AVVVTN---PPIRAGKAivsgILSGAAAHLLPGGQLYAVIQKKQG 167
Cdd:COG4976  109 DLIVAAdvlTYLGDLAA----VFAGVARALKPGGLFIFSVEDADG 149
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 62-182 1.50e-04

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: 41.39  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  62 ILDVGAGYGPIGLALAKHFPnRQVTMSDVNERALALAKQNAADNGI-TNVSIIES------SMYDGIDDQfaVVVTNPpi 134
Cdd:COG2520  184 VLDMFAGVGPFSIPIAKRSG-AKVVAIDINPDAVEYLKENIRLNKVeDRVTPILGdarevaPELEGKADR--IIMNLP-- 258

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 491949657 135 raGKAIvsGILSGAAAHLLPGGQL--YAVIQKKQGAPSALKLMKATYANA 182
Cdd:COG2520  259 --HSAD--EFLDAALRALKPGGVIhyYEIVPEEDPFERAEERIEEAAEEA 304
rumA TIGR00479
23S rRNA (uracil-5-)-methyltransferase RumA; This protein family was first proposed to be RNA ...
 47-139 1.63e-04

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


Pssm-ID: 129571 [Multi-domain]  Cd Length: 431  Bit Score: 41.35  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   47 VLIATVL--AETLPDGPILDVGAGYGPIGLALAKHFpnRQVTMSDVNERALALAKQNAADNGITNVSIIESSMYDGIDDQ 124
Cdd:TIGR00479 279 KLVDRALewLELQGEERVLDAYCGMGTFTLPLAKQA--KSVVGVEGVPESVEKAQQNAELNGIANVTFYHGTLETVLPKQ 356

                          90       100
                  ....*....|....*....|.
gi 491949657  125 ------FAVVVTNPPiRAGKA 139
Cdd:TIGR00479 357 pwagngFDKVLLDPP-RKGCA 376
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
58-158 2.78e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 40.40  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  58 PDGPILDVGAGYGPIGLALAKHFPnRQVTMSDVNERALALAKQNAADNGIT-NVSIIE--SSMYDgIDDQFAVVVT---- 130
Cdd:COG4076   35 PGDVVLDIGTGSGLLSMLAARAGA-KKVYAVEVNPDIAAVARRIIAANGLSdRITVINadATDLD-LPEKADVIISemld 112

                         90       100
                 ....*....|....*....|....*....
gi 491949657 131 NPPIRAGkaIVSgILSGAAAHLL-PGGQL 158
Cdd:COG4076  113 TALLDEG--QVP-ILNHARKRLLkPGGRI 138
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 49-104 3.28e-04

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


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 40.32  E-value: 3.28e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491949657  49 IATVLAETLPDGP------ILDVGAGYGPIGLALAKHFPN-RQVTMSDVNERALALAKQNAAD 104
Cdd:COG5459   65 VRAALAELAEAGPdfapltVLDVGAGPGTAAWAAADAWPSlLDATLLERSAAALALGRRLARA 127
DUF938 pfam06080
Protein of unknown function (DUF938); This family consists of several hypothetical proteins ...
 46-159 5.10e-04

Protein of unknown function (DUF938); This family consists of several hypothetical proteins from both prokaryotes and eukaryotes. The function of this family is unknown.


Pssm-ID: 253548  Cd Length: 201  Bit Score: 39.36  E-value: 5.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   46 RVLIATVLAETLPD--GPILDVGAGYGPIGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITN-------------- 109
Cdd:pfam06080  11 REPILSVLQSYFAKttERVLEIASGTGQHAVFFAPLLPNLTWQPSDPDPNLRGSIAAWADQQGLRNlrpplhldvtrppw 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 491949657  110 -VSIIESSMYDgiddqfAVVVTNPPIRAGKAIVSGILSGAAAHLLPGGQLY 159
Cdd:pfam06080  91 pVEAPAPASYD------AIFSINMIHISPWSCVEGLFRGAGRLLPPGGVLY 135
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 58-159 6.31e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 38.76  E-value: 6.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  58 PDGPILDVGAGYGPIGLALAKHFpNRQVTMSDVNERALALAKQNAADNGITN-VSIIESSMYD-GIDDQFAVVVTnppIR 135
Cdd:COG2230   51 PGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDlPADGQFDAIVS---IG 126

                         90       100
                 ....*....|....*....|....*...
gi 491949657 136 A----GKAIVSGILSGAAAHLLPGGQLY 159
Cdd:COG2230  127 MfehvGPENYPAYFAKVARLLKPGGRLL 154
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
 52-160 7.17e-04

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 38.98  E-value: 7.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  52 VLAETLPDGP--ILDVGAGYG-PiGLALAKHFPNRQVTMSDVNERALALAKQNAADNGITNVSI----IESSmydGIDDQ 124
Cdd:COG0357   59 ALLPLLPKEGarVLDVGSGAGfP-GIPLAIARPDLQVTLVDSLGKKIAFLREVVRELGLKNVTVvhgrAEEL---APREK 134

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491949657 125 FAVVVtnppIRAgkaiVS--GILSGAAAHLL-PGGQLYA 160
Cdd:COG0357  135 FDVVT----ARA----VAplPDLLELALPLLkPGGRLLA 165
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 68-107 7.21e-04

L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176197 [Multi-domain]  Cd Length: 343  Bit Score: 39.50  E-value: 7.21e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 491949657  68 GYGPIGL---ALAKHFPNRQVTMSDVNERALALAKQNAADNGI 107
Cdd:cd08235  173 GAGPIGLlhaMLAKASGARKVIVSDLNEFRLEFAKKLGADYTI 215
sorbitol_DH cd05285
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ...
 41-104 7.53e-04

Sorbitol dehydrogenase; 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. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. 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: 176188 [Multi-domain]  Cd Length: 343  Bit Score: 39.40  E-value: 7.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491949657  41 VDFGSRVLIAtvlaetlpdgpildvGAGygPIGL---ALAKHFPNRQVTMSDVNERALALAKQNAAD 104
Cdd:cd05285  160 VRPGDTVLVF---------------GAG--PIGLltaAVAKAFGATKVVVTDIDPSRLEFAKELGAT 209
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
57-158 1.10e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 38.59  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  57 LPDGPILDVGAGYGPIGLALAKhFPNRQVTMSDVNERALALAKQNAADNGITNVSIIESSmydgiDDQFAVVVTNppira 136
Cdd:PRK00517 118 LPGKTVLDVGCGSGILAIAAAK-LGAKKVLAVDIDPQAVEAARENAELNGVELNVYLPQG-----DLKADVIVAN----- 186

                         90       100
                 ....*....|....*....|....*.
gi 491949657 137 gkaIVSGIL----SGAAAHLLPGGQL 158
Cdd:PRK00517 187 ---ILANPLlelaPDLARLLKPGGRL 209
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 63-110 1.28e-03

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 36.49  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 491949657   63 LDVGAGYGPIGLALAKHFPnrQVTMSDVNERALALAKQNAADNGITNV 110
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA--RVTGVDISPEMLELAREKAPREGLTFV 46
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 41-104 3.77e-03

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: 37.43  E-value: 3.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491949657  41 VDFGSRVLIatvlaetlpdgpildVGAGygPIGL---ALAKHFPNRQVTMSDVNERALALAKQNAAD 104
Cdd:COG1063  159 VKPGDTVLV---------------IGAG--PIGLlaaLAARLAGAARVIVVDRNPERLELARELGAD 208
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 57-149 4.10e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 37.25  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657   57 LPDGPILDVGAGYGPIGLALAKhFPNRQVTMSDVNERALALAKQNAADNGITNvSIIESSMYDGIDDQFAVVVTN---PP 133
Cdd:pfam06325 160 KPGESVLDVGCGSGILAIAALK-LGAKKVVGVDIDPVAVRAAKENAELNGVEA-RLEVYLPGDLPKEKADVVVANilaDP 237

                          90       100
                  ....*....|....*....|....*...
gi 491949657  134 IRA------------GKAIVSGILSGAA 149
Cdd:pfam06325 238 LIElapdiyalvkpgGYLILSGILKEQA 265
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
68-135 5.18e-03

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 36.77  E-value: 5.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491949657  68 GYGPIGLALAKhfPNRQVTMSDVNERALALAKQNAADNGITNVSiiessmYDGIDD-QFAV--------VVTNPPIR 135
Cdd:PRK03522 183 GVGGFGLHCAT--PGMQLTGIEISAEAIACAKQSAAELGLTNVQ------FQALDStQFATaqgevpdlVLVNPPRR 251
PRK05031 PRK05031
tRNA (uracil-5-)-methyltransferase; Validated
 68-113 5.39e-03

tRNA (uracil-5-)-methyltransferase; Validated


Pssm-ID: 235332  Cd Length: 362  Bit Score: 36.73  E-value: 5.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 491949657  68 GYGPIGLALAKHFpnRQVTMSDVNERALALAKQNAADNGITNVSII 113
Cdd:PRK05031 216 GNGNFTLALARNF--RRVLATEISKPSVAAAQYNIAANGIDNVQII 259
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 83-160 6.10e-03

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 36.70  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491949657  83 RQVTMSDVNERALALAKQNAADNGIT-NVSIIES------SMYDGIDDQFAVVVTNPP--IRAGKAIVSGI-----LSGA 148
Cdd:COG1092  240 KSVTSVDLSATALEWAKENAALNGLDdRHEFVQAdafdwlRELAREGERFDLIILDPPafAKSKKDLFDAQrdykdLNRL 319

                         90
                 ....*....|...
gi 491949657 149 AAHLL-PGGQLYA 160
Cdd:COG1092  320 ALKLLaPGGILVT 332
 
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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