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Conserved domains on  [gi|906388950|gb|KNB75704|]
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hypothetical protein ACR57_22380 [Bacillus subtilis]

Protein Classification

tRNA1(Val) (adenine(37)-N6)-methyltransferase( domain architecture ID 11467886)

tRNA(1)(Val) (adenine(37)-N(6))-methyltransferase is a class I SAM-dependent methyltransferase that specifically methylates the adenine in position 37 of tRNA(1)(Val)

EC:  2.1.1.223
Gene Ontology:  GO:0016430|GO:1904047|GO:0008170
PubMed:  12504684

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 8-245 2.86e-114

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: 327.10  E-value: 2.86e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950   8 ERLDYLLAEDMKIIQSPTVFAFSLDAVLLSKFAYVPiQKGKIVDLCTGNGIVPLLLSTRS-KADILGVEIQERLHDMAVR 86
Cdd:COG4123    1 ERLDGFLFKQFRIIQPRCGYRFGTDAVLLAAFAPVK-KGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEAAELARR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  87 SVEYNKLDDQIQIIHDDLKNMPEKLGHNRYDVVTCNPPYFKtPKQTEQNMNEHLRIARHEIHCTLEDVISVSSKLLKQGG 166
Cdd:COG4123   80 NVALNGLEDRITVIHGDLKEFAAELPPGSFDLVVSNPPYFK-AGSGRKSPDEARAIARHEDALTLEDLIRAAARLLKPGG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 906388950 167 KAALVHRPGRLLEIFELMKAYQIEPKRVQFVYPKQGKEANTILVEGIKGGRPDLKILPPLFVYDEQNEYTKEIRTILYG 245
Cdd:COG4123  159 RFALIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVLLEARKGGRAGLRILPPLVIHDEDGEYTPEVKALLRD 237
 
Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 8-245 2.86e-114

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: 327.10  E-value: 2.86e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950   8 ERLDYLLAEDMKIIQSPTVFAFSLDAVLLSKFAYVPiQKGKIVDLCTGNGIVPLLLSTRS-KADILGVEIQERLHDMAVR 86
Cdd:COG4123    1 ERLDGFLFKQFRIIQPRCGYRFGTDAVLLAAFAPVK-KGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEAAELARR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  87 SVEYNKLDDQIQIIHDDLKNMPEKLGHNRYDVVTCNPPYFKtPKQTEQNMNEHLRIARHEIHCTLEDVISVSSKLLKQGG 166
Cdd:COG4123   80 NVALNGLEDRITVIHGDLKEFAAELPPGSFDLVVSNPPYFK-AGSGRKSPDEARAIARHEDALTLEDLIRAAARLLKPGG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 906388950 167 KAALVHRPGRLLEIFELMKAYQIEPKRVQFVYPKQGKEANTILVEGIKGGRPDLKILPPLFVYDEQNEYTKEIRTILYG 245
Cdd:COG4123  159 RFALIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVLLEARKGGRAGLRILPPLVIHDEDGEYTPEVKALLRD 237
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 48-166 4.22e-08

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: 52.74  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950   48 KIVDLCTGNGIVPL-LLSTRSKADILGVEIQERLHDMAVRSVEYNKLDDQIQIIHDDL-KNMPeklgHNRYDVVTCNPPY 125
Cdd:TIGR00536 117 HILDLGTGSGCIALaLAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLfEPLA----GQKIDIIVSNPPY 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 906388950  126 FKtpkqtEQNMNEHLRIARHEIHCTL----------EDVISVSSKLLKQGG 166
Cdd:TIGR00536 193 ID-----EEDLADLPNVVRFEPLLALvggddglnilRQIIELAPDYLKPNG 238
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 45-170 7.86e-08

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 51.70  E-value: 7.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  45 QKGKIVDLCTGNGIVPL-LLSTRSKADILGVEIQERLHDMAVRSVEYNkLDDQIQIIHDDLknmPEKLGHNRYDVVTCNP 123
Cdd:PRK09328 108 EPLRVLDLGTGSGAIALaLAKERPDAEVTAVDISPEALAVARRNAKHG-LGARVEFLQGDW---FEPLPGGRFDLIVSNP 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 906388950 124 PYfktpkqteqnmnehlrIARHEIHCTLEDV----------------------ISVSSKLLKQGGKAAL 170
Cdd:PRK09328 184 PY----------------IPEADIHLLQPEVrdhephlalfggedgldfyrriIEQAPRYLKPGGWLLL 236
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 48-171 1.45e-07

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: 48.58  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  48 KIVDLCTGNGIVPLLLSTRSKADILGVEIQERLHDMAvRSVEYNKLDDQIQIIHDDLkNMPEKLGHNRYDVVTCNPPYfk 127
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDA-EELPPEADESFDVIISDPPL-- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 906388950 128 tpkqteqnmnehlriarHEIHCTLEDVISVSSKLLKQGGKAALV 171
Cdd:cd02440   77 -----------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 49-122 3.43e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 47.17  E-value: 3.43e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 906388950   49 IVDLCTGNGIVPLLLSTRSKADILGVEIQERLHDMAVRSVEYNKLddQIQIIHDDLKNMPekLGHNRYDVVTCN 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLP--FPDGSFDLVVSS 70
 
Name Accession Description Interval E-value
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 8-245 2.86e-114

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: 327.10  E-value: 2.86e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950   8 ERLDYLLAEDMKIIQSPTVFAFSLDAVLLSKFAYVPiQKGKIVDLCTGNGIVPLLLSTRS-KADILGVEIQERLHDMAVR 86
Cdd:COG4123    1 ERLDGFLFKQFRIIQPRCGYRFGTDAVLLAAFAPVK-KGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEAAELARR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  87 SVEYNKLDDQIQIIHDDLKNMPEKLGHNRYDVVTCNPPYFKtPKQTEQNMNEHLRIARHEIHCTLEDVISVSSKLLKQGG 166
Cdd:COG4123   80 NVALNGLEDRITVIHGDLKEFAAELPPGSFDLVVSNPPYFK-AGSGRKSPDEARAIARHEDALTLEDLIRAAARLLKPGG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 906388950 167 KAALVHRPGRLLEIFELMKAYQIEPKRVQFVYPKQGKEANTILVEGIKGGRPDLKILPPLFVYDEQNEYTKEIRTILYG 245
Cdd:COG4123  159 RFALIHPAERLAEILAALRKYGLGPKRLRPVHPRPGKPAKRVLLEARKGGRAGLRILPPLVIHDEDGEYTPEVKALLRD 237
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 45-125 1.26e-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: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  45 QKGKIVDLCTGNGIVPL-LLSTRSKADILGVEIQERLHDMAVRSVEYNKLDDQIQIIHDDL-KNMPeklGHNRYDVVTCN 122
Cdd:COG2890  112 APPRVLDLGTGSGAIALaLAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLfEPLP---GDGRFDLIVSN 188


                 ...
gi 906388950 123 PPY 125
Cdd:COG2890  189 PPY 191
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 13-125 1.23e-09

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: 55.97  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  13 LLAEDMKIIQSPTVFAF-SLD---AVLLSKFAyvPIQKGKIVDLCTGNGIVPLLLSTRS-KADILGVEIQERlhdmAVRS 87
Cdd:COG2813   15 LAGRDLTFVTLPGVFSRdRLDigtRLLLEHLP--EPLGGRVLDLGCGYGVIGLALAKRNpEARVTLVDVNAR----AVEL 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 906388950  88 ----VEYNKLDDqIQIIHDDLknmPEKLGHNRYDVVTCNPPY 125
Cdd:COG2813   89 aranAAANGLEN-VEVLWSDG---LSGVPDGSFDLILSNPPF 126
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 48-166 4.22e-08

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: 52.74  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950   48 KIVDLCTGNGIVPL-LLSTRSKADILGVEIQERLHDMAVRSVEYNKLDDQIQIIHDDL-KNMPeklgHNRYDVVTCNPPY 125
Cdd:TIGR00536 117 HILDLGTGSGCIALaLAYEFPNAEVIAVDISPDALAVAEENAEKNQLEHRVEFIQSNLfEPLA----GQKIDIIVSNPPY 192

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 906388950  126 FKtpkqtEQNMNEHLRIARHEIHCTL----------EDVISVSSKLLKQGG 166
Cdd:TIGR00536 193 ID-----EEDLADLPNVVRFEPLLALvggddglnilRQIIELAPDYLKPNG 238
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 45-170 7.86e-08

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 51.70  E-value: 7.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  45 QKGKIVDLCTGNGIVPL-LLSTRSKADILGVEIQERLHDMAVRSVEYNkLDDQIQIIHDDLknmPEKLGHNRYDVVTCNP 123
Cdd:PRK09328 108 EPLRVLDLGTGSGAIALaLAKERPDAEVTAVDISPEALAVARRNAKHG-LGARVEFLQGDW---FEPLPGGRFDLIVSNP 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 906388950 124 PYfktpkqteqnmnehlrIARHEIHCTLEDV----------------------ISVSSKLLKQGGKAAL 170
Cdd:PRK09328 184 PY----------------IPEADIHLLQPEVrdhephlalfggedgldfyrriIEQAPRYLKPGGWLLL 236
L3_gln_methyl TIGR03533
protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this ...
 49-125 1.44e-07

protein-(glutamine-N5) methyltransferase, ribosomal protein L3-specific; Members of this protein family methylate ribosomal protein L3 on a glutamine side chain. This family is related to HemK, a protein-glutamine methyltranferase for peptide chain release factors. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 274633 [Multi-domain]  Cd Length: 284  Bit Score: 50.97  E-value: 1.44e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 906388950   49 IVDLCTGNGIVPLLLSTR-SKADILGVEIQERLHDMAVRSVEYNKLDDQIQIIHDDLKnmpEKLGHNRYDVVTCNPPY 125
Cdd:TIGR03533 125 ILDLCTGSGCIAIACAYAfPEAEVDAVDISPDALAVAEINIERHGLEDRVTLIQSDLF---AALPGRKYDLIVSNPPY 199
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 48-171 1.45e-07

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: 48.58  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  48 KIVDLCTGNGIVPLLLSTRSKADILGVEIQERLHDMAvRSVEYNKLDDQIQIIHDDLkNMPEKLGHNRYDVVTCNPPYfk 127
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELA-RKAAAALLADNVEVLKGDA-EELPPEADESFDVIISDPPL-- 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 906388950 128 tpkqteqnmnehlriarHEIHCTLEDVISVSSKLLKQGGKAALV 171
Cdd:cd02440   77 -----------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 49-122 3.43e-07

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 47.17  E-value: 3.43e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 906388950   49 IVDLCTGNGIVPLLLSTRSKADILGVEIQERLHDMAVRSVEYNKLddQIQIIHDDLKNMPekLGHNRYDVVTCN 122
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLP--FPDGSFDLVVSS 70
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 17-171 7.80e-07

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: 47.59  E-value: 7.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950   17 DMKIIQSPTVFAF-SLD---AVLLSKFAyvPIQKGKIVDLCTGNGIVPLLLSTRS-KADILGVEIQERlhdmAVRSVEYN 91
Cdd:pfam05175   1 ELTFKTLPGVFSHgRLDigsRLLLEHLP--KDLSGKVLDLGCGAGVLGAALAKESpDAELTMVDINAR----ALESAREN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950   92 KLD---DQIQIIHDDLKnmpEKLGHNRYDVVTCNPPyFKTPKQTeqnmneHLRIArHEIhctledvISVSSKLLKQGGKA 168
Cdd:pfam05175  75 LAAnglENGEVVASDVY---SGVEDGKFDLIISNPP-FHAGLAT------TYNVA-QRF-------IADAKRHLRPGGEL 136


                  ...
gi 906388950  169 ALV 171
Cdd:pfam05175 137 WIV 139
PRK14967 PRK14967
putative methyltransferase; Provisional
 48-129 6.26e-06

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 45.81  E-value: 6.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  48 KIVDLCTGNGIVPLLLSTRSKADILGVEIQERlhdmAVRSVEYNKLDD--QIQIIHDDLKnmpEKLGHNRYDVVTCNPPY 125
Cdd:PRK14967  39 RVLDLCTGSGALAVAAAAAGAGSVTAVDISRR----AVRSARLNALLAgvDVDVRRGDWA---RAVEFRPFDVVVSNPPY 111


                 ....
gi 906388950 126 FKTP 129
Cdd:PRK14967 112 VPAP 115
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
33-124 7.97e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 45.28  E-value: 7.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  33 AVLLSKFAYVP--IQKGKIVDLCTGNGIVPLLLSTRSKADILGVEIQERLHDMAVRSVEynKLDDQIQIIHDDLKNMPek 110
Cdd:COG2263   31 AAELLHLAYLRgdIEGKTVLDLGCGTGMLAIGAALLGAKKVVGVDIDPEALEIARENAE--RLGVRVDFIRADVTRIP-- 106

                         90
                 ....*....|....
gi 906388950 111 lGHNRYDVVTCNPP 124
Cdd:COG2263  107 -LGGSVDTVVMNPP 119
PRK14968 PRK14968
putative methyltransferase; Provisional
 44-133 1.37e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 44.50  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  44 IQKGKIV-DLCTGNGIVPLLLSTRSKaDILGVEIQERLHDMAVRSVEYNKLDDQ-IQIIHDDLKnmpEKLGHNRYDVVTC 121
Cdd:PRK14968  21 DKKGDRVlEVGTGSGIVAIVAAKNGK-KVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSDLF---EPFRGDKFDVILF 96

                         90
                 ....*....|..
gi 906388950 122 NPPYFKTPKQTE 133
Cdd:PRK14968  97 NPPYLPTEEEEE 108
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
 44-170 2.39e-05

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


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 44.86  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  44 IQKGKIVDLCTGNGIVPL-LLSTRSKADILGVEIQERLHDMAVRSVEYNKLDDQIQIIHddlKNMPEKLGHNRYDVVTCN 122
Cdd:PRK01544 137 DKFLNILELGTGSGCIAIsLLCELPNANVIATDISLDAIEVAKSNAIKYEVTDRIQIIH---SNWFENIEKQKFDFIVSN 213

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 906388950 123 PPYFKTPKQTEQNmnehLRIARHEIHCTL---ED------VISVSSK-LLKQGGKAAL 170
Cdd:PRK01544 214 PPYISHSEKSEMA----IETINYEPSIALfaeEDglqayfIIAENAKqFLKPNGKIIL 267
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 40-124 2.45e-05

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: 44.78  E-value: 2.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  40 AYVPIQKGK-IVDLCTGNGIVPLLLSTRSKAdILGVEIQERLHDMAVRSVEYNKLDdQIQIIHDDL-KNMPEKLGHNRYD 117
Cdd:COG2265  227 EWLDLTGGErVLDLYCGVGTFALPLARRAKK-VIGVEIVPEAVEDARENARLNGLK-NVEFVAGDLeEVLPELLWGGRPD 304


                 ....*..
gi 906388950 118 VVTCNPP 124
Cdd:COG2265  305 VVVLDPP 311
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 39-186 2.88e-05

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: 42.67  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  39 FAYVPIQKG-KIVDLCTGNGIVPLLLSTRSkADILGVEIQERLHDMAVRSVEYNKLddQIQIIHDDLKNMPekLGHNRYD 117
Cdd:COG2226   15 LAALGLRPGaRVLDLGCGTGRLALALAERG-ARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLP--FPDGSFD 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950 118 VVTCNppyfktpkQTEQNMNEHLRIARhEIHctledvisvssKLLKQGGKAALV-HRPGRLLEIFELMKA 186
Cdd:COG2226   90 LVISS--------FVLHHLPDPERALA-EIA-----------RVLKPGGRLVVVdFSPPDLAELEELLAE 139
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 18-166 1.31e-04

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: 40.77  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  18 MKIIQSPTVFAFSLDAVLLSKFAyvpiQKGKIVDLCTGNGIVPLLLSTRSkADILGVEIQERLHDMAVRSVEynklDDQI 97
Cdd:COG2227    1 MSDPDARDFWDRRLAALLARLLP----AGGRVLDVGCGTGRLALALARRG-ADVTGVDISPEALEIARERAA----ELNV 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 906388950  98 QIIHDDLKNMPekLGHNRYDVVTCNppyfktpkqteqNMNEHLRiarheihcTLEDVISVSSKLLKQGG 166
Cdd:COG2227   72 DFVQGDLEDLP--LEDGSFDLVICS------------EVLEHLP--------DPAALLRELARLLKPGG 118
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
44-121 2.55e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 41.18  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  44 IQKGKIV-DLCTGNGIVPLLlSTRSKAD-ILGVEIQERLHDMAVRSVEYNKLDDQIQIIHDDLK--NMPEKLghnryDVV 119
Cdd:COG4076   33 VKPGDVVlDIGTGSGLLSML-AARAGAKkVYAVEVNPDIAAVARRIIAANGLSDRITVINADATdlDLPEKA-----DVI 106


                 ..
gi 906388950 120 TC 121
Cdd:COG4076  107 IS 108
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 45-218 1.60e-03

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 38.36  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950  45 QKGKIVDLCTGNGIVPLLLSTRSKADILGVEIQERLHDMAVRSVEYNKLdDQIQIIHDDLkNMPEKLGHNRYDVVTCNpp 124
Cdd:COG0500   26 KGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADL-AELDPLPAESFDLVVAF-- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 906388950 125 yfktpkqteqNMNEHLRIARheihctLEDVISVSSKLLKQGGKAALV-HRPGRLLEIFELMKAYQIEPKRVQFVYPKQGK 203
Cdd:COG0500  102 ----------GVLHHLPPEE------REALLRELARALKPGGVLLLSaSDAAAALSLARLLLLATASLLELLLLLRLLAL 165

                        170
                 ....*....|....*
gi 906388950 204 EANTILVEGIKGGRP 218
Cdd:COG0500  166 ELYLRALLAAAATED 180
 
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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