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Conserved domains on  [gi|738093883|ref|WP_036052534|]
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protein-L-isoaspartate O-methyltransferase [Burkholderia gladioli]

Protein Classification

protein-L-isoaspartate O-methyltransferase family protein( domain architecture ID 11457531)

protein-L-isoaspartate O-methyltransferase family protein may catalyze the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues

CATH:  3.55.20.10
EC:  2.1.1.77
Gene Ontology:  GO:0004719|GO:0030091|GO:0036211
PubMed:  35462043|20564550|35462043|9253175
SCOP:  4000666

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 12-209 4.85e-89

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


:

Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 260.41  E-value: 4.85e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  12 EQQIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHESILEIGAGSGYM 91
Cdd:COG2518    1 VQQLRPRGVTDPRVLDAMRAVPRELFVPEALRELAYADRALPIGHGQTISQPYIVARMLEALDLKPGDRVLEIGTGSGYQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  92 AALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQELLEQLKVGGRLA 171
Cdd:COG2518   81 AAVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLV 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 738093883 172 AFVGSRPVMKAQIITRIDDkQFRVADVFETYVDHLVNA 209
Cdd:COG2518  161 APVGEGGVQRLVLITRTGD-GFERESLFEVRFVPLRGG 197
 
Name Accession Description Interval E-value
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 12-209 4.85e-89

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 260.41  E-value: 4.85e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  12 EQQIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHESILEIGAGSGYM 91
Cdd:COG2518    1 VQQLRPRGVTDPRVLDAMRAVPRELFVPEALRELAYADRALPIGHGQTISQPYIVARMLEALDLKPGDRVLEIGTGSGYQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  92 AALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQELLEQLKVGGRLA 171
Cdd:COG2518   81 AAVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLV 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 738093883 172 AFVGSRPVMKAQIITRIDDkQFRVADVFETYVDHLVNA 209
Cdd:COG2518  161 APVGEGGVQRLVLITRTGD-GFERESLFEVRFVPLRGG 197
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
1-200 9.11e-49

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 158.44  E-value: 9.11e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   1 MNIDNARF-NMIEQqIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHE 79
Cdd:PRK00312   2 RLMESERFaRLVLR-LRAEGILDERVLEAIEATPRELFVPEAFKHKAYENRALPIGCGQTISQPYMVARMTELLELKPGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  80 SILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQE 159
Cdd:PRK00312  81 RVLEIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRHGDGWKGWPAYAPFDRILVTAAAPEIPRA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 738093883 160 LLEQLKVGGRLAAFVGSRPVmkaQIITRIDDK--QFRVADVFE 200
Cdd:PRK00312 161 LLEQLKEGGILVAPVGGEEQ---QLLTRVRKRggRFEREVLEE 200
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
10-203 1.08e-35

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 124.79  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   10 MIEQQIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHESILEIGAGSG 89
Cdd:pfam01135   6 LIENLKNYGVIKSDKVAEAMLAVDREEFVPESFKSYAYEDIPLSIGYGQTISAPHMHAMMLELLELKPGMRVLEIGSGSG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   90 YMAALLAHRGQH---VVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQELLEQLKV 166
Cdd:pfam01135  86 YLTACFARMVGEvgrVVSIEHIPELVEIARRNLEKLGLENVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALIDQLKE 165

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 738093883  167 GGRLAAFVGSRPVMKAQIITRIDDKQFRVADVFET-YV 203
Cdd:pfam01135 166 GGRLVIPVGPNGNQVLQQFDKRNDGSVVIKDLEGVrFV 203
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
 10-189 4.64e-32

protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all species) full-length ortholog enzyme for repairing aging proteins. Among the prokaryotes, the gene name is pcm. Among eukaryotes, pimt. [Protein fate, Protein modification and repair]


Pssm-ID: 272896 [Multi-domain]  Cd Length: 215  Bit Score: 115.69  E-value: 4.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   10 MIEQQIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHESILEIGAGSG 89
Cdd:TIGR00080  10 LIDKLINEGYIKSKRVIDALLSVPREEFVPEHFKEYAYVDTPLEIGYGQTISAPHMVAMMTELLELKPGMKVLEIGTGSG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   90 YMAALLAH---RGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQELLEQLKV 166
Cdd:TIGR00080  90 YQAAVLAEivgRDGLVVSIERIPELAEKAERRLRKLGLDNVIVIVGDGTQGWEPLAPYDRIYVTAAGPKIPEALIDQLKE 169

                         170       180
                  ....*....|....*....|...
gi 738093883  167 GGRLAAFVGSrpvmKAQIITRID 189
Cdd:TIGR00080 170 GGILVMPVGE----YLQVLKRAE 188
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 81-170 1.75e-11

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: 58.98  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  81 ILEIGAGSGYMAALLAHR-GQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLP-EKGPYDVICVSGGLPVVP- 157
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLVe 81

                         90
                 ....*....|....*....
gi 738093883 158 ------QELLEQLKVGGRL 170
Cdd:cd02440   82 dlarflEEARRLLKPGGVL 100
rADc smart00650
Ribosomal RNA adenine dimethylases;
68-147 3.46e-06

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 45.58  E-value: 3.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883    68 RMLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQfaadNLRD--NGVSNAEVVLADAAR-GLPEKGPY 144
Cdd:smart00650   4 KIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAP----RLREkfAAADNLTVIHGDALKfDLPKLQPY 79


                   ...
gi 738093883   145 DVI 147
Cdd:smart00650  80 KVV 82
 
Name Accession Description Interval E-value
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 12-209 4.85e-89

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 260.41  E-value: 4.85e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  12 EQQIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHESILEIGAGSGYM 91
Cdd:COG2518    1 VQQLRPRGVTDPRVLDAMRAVPRELFVPEALRELAYADRALPIGHGQTISQPYIVARMLEALDLKPGDRVLEIGTGSGYQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  92 AALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQELLEQLKVGGRLA 171
Cdd:COG2518   81 AAVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLV 160

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 738093883 172 AFVGSRPVMKAQIITRIDDkQFRVADVFETYVDHLVNA 209
Cdd:COG2518  161 APVGEGGVQRLVLITRTGD-GFERESLFEVRFVPLRGG 197
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
1-200 9.11e-49

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 158.44  E-value: 9.11e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   1 MNIDNARF-NMIEQqIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHE 79
Cdd:PRK00312   2 RLMESERFaRLVLR-LRAEGILDERVLEAIEATPRELFVPEAFKHKAYENRALPIGCGQTISQPYMVARMTELLELKPGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  80 SILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQE 159
Cdd:PRK00312  81 RVLEIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRHGDGWKGWPAYAPFDRILVTAAAPEIPRA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 738093883 160 LLEQLKVGGRLAAFVGSRPVmkaQIITRIDDK--QFRVADVFE 200
Cdd:PRK00312 161 LLEQLKEGGILVAPVGGEEQ---QLLTRVRKRggRFEREVLEE 200
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
10-203 1.08e-35

Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 124.79  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   10 MIEQQIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHESILEIGAGSG 89
Cdd:pfam01135   6 LIENLKNYGVIKSDKVAEAMLAVDREEFVPESFKSYAYEDIPLSIGYGQTISAPHMHAMMLELLELKPGMRVLEIGSGSG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   90 YMAALLAHRGQH---VVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQELLEQLKV 166
Cdd:pfam01135  86 YLTACFARMVGEvgrVVSIEHIPELVEIARRNLEKLGLENVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALIDQLKE 165

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 738093883  167 GGRLAAFVGSRPVMKAQIITRIDDKQFRVADVFET-YV 203
Cdd:pfam01135 166 GGRLVIPVGPNGNQVLQQFDKRNDGSVVIKDLEGVrFV 203
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 11-176 1.04e-34

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 122.43  E-value: 1.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  11 IEQQIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHESILEIGAGSGY 90
Cdd:PRK13942  10 IEELIREGYIKSKKVIDALLKVPRHLFVPEYLEEYAYVDTPLEIGYGQTISAIHMVAIMCELLDLKEGMKVLEIGTGSGY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  91 MAALLAH----RGqHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQELLEQLKV 166
Cdd:PRK13942  90 HAAVVAEivgkSG-KVVTIERIPELAEKAKKTLKKLGYDNVEVIVGDGTLGYEENAPYDRIYVTAAGPDIPKPLIEQLKD 168

                        170
                 ....*....|
gi 738093883 167 GGRLAAFVGS 176
Cdd:PRK13942 169 GGIMVIPVGS 178
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
 10-189 4.64e-32

protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all species) full-length ortholog enzyme for repairing aging proteins. Among the prokaryotes, the gene name is pcm. Among eukaryotes, pimt. [Protein fate, Protein modification and repair]


Pssm-ID: 272896 [Multi-domain]  Cd Length: 215  Bit Score: 115.69  E-value: 4.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   10 MIEQQIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHESILEIGAGSG 89
Cdd:TIGR00080  10 LIDKLINEGYIKSKRVIDALLSVPREEFVPEHFKEYAYVDTPLEIGYGQTISAPHMVAMMTELLELKPGMKVLEIGTGSG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   90 YMAALLAH---RGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQELLEQLKV 166
Cdd:TIGR00080  90 YQAAVLAEivgRDGLVVSIERIPELAEKAERRLRKLGLDNVIVIVGDGTQGWEPLAPYDRIYVTAAGPKIPEALIDQLKE 169

                         170       180
                  ....*....|....*....|...
gi 738093883  167 GGRLAAFVGSrpvmKAQIITRID 189
Cdd:TIGR00080 170 GGILVMPVGE----YLQVLKRAE 188
methyltran_FxLD TIGR04364
methyltransferase, FxLD system; Members of this family resemble occur regularly in the ...
 13-190 5.57e-25

methyltransferase, FxLD system; Members of this family resemble occur regularly in the vicinity of lantibiotic biosynthesis enzymes and their probable target, the FxLD family of putative ribosomal natural product precursor (TIGR04363). Members resemble protein-L-isoaspartate O-methyltransferase (TIGR00080) and a predicted methyltranserase, TIGR04188, of another putative peptide modification system.


Pssm-ID: 275158  Cd Length: 394  Bit Score: 100.52  E-value: 5.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   13 QQIRPWEVL-DPEVLSLLSVVKRELYVPSVYRDLAF-ADLELPL---PGG---QKMLAPRVEARMLQELAVKKHESILEI 84
Cdd:TIGR04364  10 DELREDGVIrSPRVEAAFRTVPRHLFAPGAPLEKAYaANRAVVTkrdEDGralSSVSAPHIQAMMLEQAGVEPGMRVLEI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   85 GAGsGYMAALLAH---RGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQELL 161
Cdd:TIGR04364  90 GSG-GYNAALLAElvgPSGEVTTVDIDEDVTDRARACLAAAGYPQVTVVLADAEAGVPELAPYDRIIVTVGAWDIPPAWL 168

                         170       180
                  ....*....|....*....|....*....
gi 738093883  162 EQLKVGGRLAAFVGSRPVMKAQIITRIDD 190
Cdd:TIGR04364 169 DQLAPGGRLVVPLRMRGLTRSIAFERAGD 197
PRK13944 PRK13944
protein-L-isoaspartate O-methyltransferase; Provisional
 6-203 1.82e-24

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 140001  Cd Length: 205  Bit Score: 95.65  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   6 ARFNMIEQQIRPWEVLDPEVLSLLSVVKRELYVPSVYRDLAFADLELPLPGGQKMLAPRVEARMLQELAVKKHESILEIG 85
Cdd:PRK13944   1 MAKRLVEELVREGIIKSERVKKAMLSVPREEFVMPEYRMMAYEDRPLPLFAGATISAPHMVAMMCELIEPRPGMKILEVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  86 AGSGYMAALLAH---RGQHVVTVDIDPALVQFAADNLRDNGVSN-AEVVLADAARGLPEKGPYDVICVSGGLPVVPQELL 161
Cdd:PRK13944  81 TGSGYQAAVCAEaieRRGKVYTVEIVKELAIYAAQNIERLGYWGvVEVYHGDGKRGLEKHAPFDAIIVTAAASTIPSALV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 738093883 162 EQLKVGGRLAAFVGSRpvmKAQIITRIDDKQFRVADVFETYV 203
Cdd:PRK13944 161 RQLKDGGVLVIPVEEG---VGQVLYKVVKRGEKVEKRAITYV 199
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 65-178 1.61e-19

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: 81.19  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  65 VEARMLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGVsNAEVVLADAARgLP-EKGP 143
Cdd:COG2226   10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAED-LPfPDGS 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 738093883 144 YDVICVSGGLPVVP------QELLEQLKVGGRLAAFVGSRP 178
Cdd:COG2226   88 FDLVISSFVLHHLPdperalAEIARVLKPGGRLVVVDFSPP 128
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 67-171 1.51e-15

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 71.11  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  67 ARMLQELAVKKHESILEIGAGSGYMAALLA-HRGQHVVTVDIDPALVQFAADNLRDNGVSN-AEVVLADaARGLPEKGPY 144
Cdd:COG2230   41 DLILRKLGLKPGMRVLDIGCGWGGLALYLArRYGVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLAD-YRDLPADGQF 119

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 738093883 145 DVICVSGGLPVVPQELLEQ--------LKVGGRLA 171
Cdd:COG2230  120 DAIVSIGMFEHVGPENYPAyfakvarlLKPGGRLL 154
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 67-170 1.89e-14

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: 67.35  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  67 ARMLQELAVKKHeSILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGVsnaEVVLADAARGLPEKGPYDV 146
Cdd:COG2227   15 AALLARLLPAGG-RVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAELNV---DFVQGDLEDLPLEDGSFDL 90

                         90       100       110
                 ....*....|....*....|....*....|
gi 738093883 147 ICVSGGLPVVP------QELLEQLKVGGRL 170
Cdd:COG2227   91 VICSEVLEHLPdpaallRELARLLKPGGLL 120
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 81-168 6.81e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 64.89  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   81 ILEIGAGSGYMAALLAHRGQHVVT-VDIDPALVQFAADNLRDNGVsNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQE 159
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTgVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 738093883  160 LLEQ--------LKVGG 168
Cdd:pfam13649  80 DLEAalreiarvLKPGG 96
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 63-170 1.04e-13

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 68.72  E-value: 1.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  63 PRVEARMLQELAVKKHESILEIGAGSGYMAALLAH---RGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLP 139
Cdd:PRK13943  66 PSLMALFMEWVGLDKGMRVLEIGGGTGYNAAVMSRvvgEKGLVVSVEYSRKICEIAKRNVRRLGIENVIFVCGDGYYGVP 145

                         90       100       110
                 ....*....|....*....|....*....|.
gi 738093883 140 EKGPYDVICVSGGLPVVPQELLEQLKVGGRL 170
Cdd:PRK13943 146 EFAPYDVIFVTVGVDEVPETWFTQLKEGGRV 176
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 69-170 2.20e-13

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: 65.98  E-value: 2.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  69 MLQELAVKKHESILEIGAGSGYMAALLAHRGQ--HVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEkGPYDV 146
Cdd:COG2813   41 LLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPeaRVTLVDVNARAVELARANAAANGLENVEVLWSDGLSGVPD-GSFDL 119

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 738093883 147 IcVS------GGLPV--VPQELLEQ----LKVGGRL 170
Cdd:COG2813  120 I-LSnppfhaGRAVDkeVAHALIADaarhLRPGGEL 154
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
79-174 3.29e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 63.30  E-value: 3.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  79 ESILEIGAGSGYMAALLAHR--GQHVVTVDIDPALVQFAADNLrdngvSNAEVVLADAARGLPEkGPYDVICVS------ 150
Cdd:COG4106    3 RRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARL-----PNVRFVVADLRDLDPP-EPFDLVVSNaalhwl 76

                         90       100
                 ....*....|....*....|....
gi 738093883 151 GGLPVVPQELLEQLKVGGRLAAFV 174
Cdd:COG4106   77 PDHAALLARLAAALAPGGVLAVQV 100
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 61-170 3.82e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 65.32  E-value: 3.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  61 LAPRVEARMLQELAVKKHESILEIGAGSGYMAALLAHR-GQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLP 139
Cdd:COG0500   10 LLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDP 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 738093883 140 EK-GPYDVICVSGGLPVVP--------QELLEQLKVGGRL 170
Cdd:COG0500   90 LPaESFDLVVAFGVLHHLPpeereallRELARALKPGGVL 129
PRK14968 PRK14968
putative methyltransferase; Provisional
 69-148 4.70e-12

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 62.22  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  69 MLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNA--EVVLADAARGLpEKGPYDV 146
Cdd:PRK14968  15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNgvEVIRSDLFEPF-RGDKFDV 93


                 ..
gi 738093883 147 IC 148
Cdd:PRK14968  94 IL 95
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 60-172 7.29e-12

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


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 60.42  E-value: 7.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   60 MLAPRVEARMLQELAVKKHESILEIGAGSGYMA--ALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARG 137
Cdd:TIGR02469   2 MTKREVRALTLAKLRLRPGDVLWDIGAGTGSVTieAARLVPNGRVYAIERNPEALDLIERNLRRFGVSNIVIVEGDAPEA 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 738093883  138 LPEKGP-YDVICVSGG---LPVVPQELLEQLKVGGRLAA 172
Cdd:TIGR02469  82 PEALLPdPDAVFVGGSgglLQEILEAVERRLRPGGRIVL 120
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 70-172 8.37e-12

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: 63.26  E-value: 8.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  70 LQELAVKKHESILEIGAGSGYMA--ALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVI 147
Cdd:COG2242  240 LAKLALRPGDVLWDIGAGSGSVSieAARLAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPEALADLPDPDAV 319

                         90       100
                 ....*....|....*....|....*...
gi 738093883 148 CVSGG---LPVVPQELLEQLKVGGRLAA 172
Cdd:COG2242  320 FIGGSggnLPEILEACWARLRPGGRLVA 347
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 81-170 1.75e-11

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: 58.98  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  81 ILEIGAGSGYMAALLAHR-GQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLP-EKGPYDVICVSGGLPVVP- 157
Cdd:cd02440    2 VLDLGCGTGALALALASGpGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLVe 81

                         90
                 ....*....|....*....
gi 738093883 158 ------QELLEQLKVGGRL 170
Cdd:cd02440   82 dlarflEEARRLLKPGGVL 100
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 64-168 5.06e-11

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 59.04  E-value: 5.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  64 RVEARMLQELA-VKKHESILEIGAGSGY----MAALLAHRGqHVVTVDIDPALVQFAADNLRDNGVSN-AEVVLADAARG 137
Cdd:COG4122    2 PEQGRLLYLLArLLGAKRILEIGTGTGYstlwLARALPDDG-RLTTIEIDPERAAIARENFARAGLADrIRLILGDALEV 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 738093883 138 LPE--KGPYDVICVSG---GLPVVPQELLEQLKVGG 168
Cdd:COG4122   81 LPRlaDGPFDLVFIDAdksNYPDYLELALPLLRPGG 116
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
64-171 8.41e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 58.47  E-value: 8.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  64 RVEARMLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAadnlRDNGVSnAEVVLADAARGLPEKGP 143
Cdd:COG4976   33 LLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA----REKGVY-DRLLVADLADLAEPDGR 107

                         90       100       110
                 ....*....|....*....|....*....|....
gi 738093883 144 YDVICVSGGLPVVP------QELLEQLKVGGRLA 171
Cdd:COG4976  108 FDLIVAADVLTYLGdlaavfAGVARALKPGGLFI 141
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 10-150 1.32e-10

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: 58.74  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  10 MIEQQIR-PWEVLDPEV--LSLLSVVKRELYVPSVYRDLAFADLELPL-----PGGQKMlaprveAR-MLQELAVKKhES 80
Cdd:COG3897    1 MSEDFIRaNTRLETVLVpeIRLHLAADAHPLWDATEEALGESGAPPPFwaflwPSGQAL------ARyLLDHPEVAG-KR 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738093883  81 ILEIGAGSGyMAALLAHR--GQHVVTVDIDPALVQFAADNLRDNGVSnAEVVLADaARGLPEKGPYDVICVS 150
Cdd:COG3897   74 VLELGCGLG-LVGIAAAKagAADVTATDYDPEALAALRLNAALNGVA-ITTRLGD-WRDPPAAGGFDLILGG 142
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 75-147 3.99e-10

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


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 57.46  E-value: 3.99e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738093883  75 VKKHESILEIGAGSGYMAALLAHR--GQHVVTVDIDPALVQFAADNLRDNGVSN-AEVVLAD--AARGLPEKGPYDVI 147
Cdd:COG4123   35 VKKGGRVLDLGTGTGVIALMLAQRspGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDlkEFAAELPPGSFDLV 112
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 76-172 5.14e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.89  E-value: 5.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   76 KKHESILEIGAGSGYMAALLAHR---GQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARgLP---EKGPYDVICV 149
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEE-LPellEDDKFDVVIS 80

                          90       100
                  ....*....|....*....|....*....
gi 738093883  150 SGGLPVVP------QELLEQLKVGGRLAA 172
Cdd:pfam13847  81 NCVLNHIPdpdkvlQEILRVLKPGGRLII 109
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 69-170 1.01e-09

HemK-related putative methylase; 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. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 55.63  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   69 MLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGVsNAEVVLADAARGLpeKGPYDVIC 148
Cdd:TIGR00537  11 LEANLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKELRENAKLNNV-GLDVVMTDLFKGV--RGKFDVIL 87

                          90       100
                  ....*....|....*....|..
gi 738093883  149 VSGglPVVPQEllEQLKVGGRL 170
Cdd:TIGR00537  88 FNP--PYLPLE--DDLRRGDWL 105
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 61-150 1.30e-09

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 56.70  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  61 LAPR------VEARmLQELAVKKHESILEIGAGSGYMAALLAHR--GQHVVTVDIDPALVQFAADNLRDNGVSN-AEVVL 131
Cdd:COG2890   91 LIPRpeteelVELA-LALLPAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVARRNAERLGLEDrVRFLQ 169

                         90
                 ....*....|....*....
gi 738093883 132 ADAARGLPEKGPYDVIcVS 150
Cdd:COG2890  170 GDLFEPLPGDGRFDLI-VS 187
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 69-195 2.07e-09

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 54.52  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   69 MLQELAVKKHESILEIGAGSGYMAALLAHRG--QHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEkGPYDV 146
Cdd:pfam05175  23 LLEHLPKDLSGKVLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGLENGEVVASDVYSGVED-GKFDL 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  147 IcVSG-----GLPVVP---QELLEQ----LKVGGRL----AAFVGSRPVMKA-----QIITRidDKQFRV 195
Cdd:pfam05175 102 I-ISNppfhaGLATTYnvaQRFIADakrhLRPGGELwivaNRFLGYPPLLEElfgnvEVVAK--TNGFKV 168
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 81-174 2.32e-09

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 55.55  E-value: 2.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  81 ILEIGAGSGYMAALLAH----RGqHVVTVDIDPALVQFAADNLRDNGVS-NAEVVLADAARGLPEkGPYDVIcvsgglpV 155
Cdd:COG2519   95 VLEAGTGSGALTLALARavgpEG-KVYSYERREDFAEIARKNLERFGLPdNVELKLGDIREGIDE-GDVDAV-------F 165

                         90       100
                 ....*....|....*....|....*..
gi 738093883 156 V----PQELLEQ----LKVGGRLAAFV 174
Cdd:COG2519  166 LdmpdPWEALEAvakaLKPGGVLVAYV 192
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 82-171 3.82e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 52.28  E-value: 3.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   82 LEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGVsnaEVVLADAARgLP-EKGPYDVICVSGGLPVVP--- 157
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGL---TFVVGDAED-LPfPDNSFDLVLSSEVLHHVEdpe 76

                          90
                  ....*....|....*..
gi 738093883  158 ---QELLEQLKVGGRLA 171
Cdd:pfam08241  77 ralREIARVLKPGGILI 93
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
69-147 6.53e-09

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 54.41  E-value: 6.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  69 MLQELA--VKKHESILEIGAGSG---YMAALLAHRgqHVVTVDIDPALVQFAADNLRDNGVSNA-EVVLADaargLPEKG 142
Cdd:COG2264  138 CLEALEklLKPGKTVLDVGCGSGilaIAAAKLGAK--RVLAVDIDPVAVEAARENAELNGVEDRiEVVLGD----LLEDG 211


                 ....*
gi 738093883 143 PYDVI 147
Cdd:COG2264  212 PYDLV 216
PRK08317 PRK08317
hypothetical protein; Provisional
 64-214 1.03e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.79  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  64 RVEARMLQELAVKKHESILEIGAGSGYMAALLAHR---GQHVVTVDIDPALVQFAADNLRDNGvSNAEVVLADAArGLP- 139
Cdd:PRK08317   6 RYRARTFELLAVQPGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLG-PNVEFVRGDAD-GLPf 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883 140 EKGPYDVICVSGGL------PVVPQELLEQLKVGGRLAAFvgsRPVMKAQIItRIDDKQfRVADVFETYVDHLVNAMEPS 213
Cdd:PRK08317  84 PDGSFDAVRSDRVLqhledpARALAEIARVLRPGGRVVVL---DTDWDTLVW-HSGDRA-LMRKILNFWSDHFADPWLGR 158


                 .
gi 738093883 214 R 214
Cdd:PRK08317 159 R 159
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 60-204 3.26e-08

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: 51.49  E-value: 3.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  60 MLAPRVeARMLQELA-VKKHESILEIGAGSGYM---AALLahrGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAA 135
Cdd:COG1041    9 SLDPRL-ARALVNLAgAKEGDTVLDPFCGTGTIlieAGLL---GRRVIGSDIDPKMVEGARENLEHYGYEDADVIRGDAR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883 136 RgLPEK-GPYDVICV-------SGGLPVVPQELLEQ--------LKVGGRLAAfvgsrpVMKAQIITRIDDKQFRVADVF 199
Cdd:COG1041   85 D-LPLAdESVDAIVTdppygrsSKISGEELLELYEKaleeaarvLKPGGRVVI------VTPRDIDELLEEAGFKVLERH 157


                 ....*
gi 738093883 200 ETYVD 204
Cdd:COG1041  158 EQRVH 162
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
72-147 3.42e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 51.96  E-value: 3.42e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738093883  72 ELAVKKHESILEIGAGSGYMAALLAHRGQ-HVVTVDIDPALVQFAADNLRDNGVS-NAEVVLADAAR-GLPEKGpyDVI 147
Cdd:COG4076   30 ERVVKPGDVVLDIGTGSGLLSMLAARAGAkKVYAVEVNPDIAAVARRIIAANGLSdRITVINADATDlDLPEKA--DVI 106
PRK03612 PRK03612
polyamine aminopropyltransferase;
74-149 2.71e-07

polyamine aminopropyltransferase;


Pssm-ID: 235139 [Multi-domain]  Cd Length: 521  Bit Score: 50.22  E-value: 2.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  74 AVKKHESILEIGAGSGyMAA--LLAHRG-QHVVTVDIDPALVQFAADN---LRDNGVS----NAEVVLADAARGLPE-KG 142
Cdd:PRK03612 294 ASARPRRVLVLGGGDG-LALreVLKYPDvEQVTLVDLDPAMTELARTSpalRALNGGAlddpRVTVVNDDAFNWLRKlAE 372


                 ....*..
gi 738093883 143 PYDVICV 149
Cdd:PRK03612 373 KFDVIIV 379
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 66-170 3.04e-07

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 48.58  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   66 EARMLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVvladaargLPEKGPYD 145
Cdd:pfam13489  11 DLLLRLLPKLPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEA--------AVPAGKFD 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 738093883  146 VICVSGGL------PVVPQELLEQLKVGGRL 170
Cdd:pfam13489  83 VIVAREVLehvpdpPALLRQIAALLKPGGLL 113
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 63-147 4.37e-07

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 48.97  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  63 PRVEARMLQELAVKKHESILEIGAGSGymaAL---LAHRGQHVVTVDIDPALVQFAADNLRDNGvsNAEVVLADA----A 135
Cdd:COG0030   23 PNIIRRIVDAAGITPGDTVLEIGPGLG---ALtraLLERAARVTAVEIDRRLAAILRETFAAYP--NLTVIEGDAlkvdL 97

                         90
                 ....*....|..
gi 738093883 136 RGLPEKGPYDVI 147
Cdd:COG0030   98 PALAAGEPLKVV 109
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
79-149 4.67e-07

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 48.29  E-value: 4.67e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738093883  79 ESILEIGAGSGYMA-ALLAHRGQ-HVVTVDIDPALVQFAADNLRDNGVSN----AEVVLADAARGLPE-KGPYDVICV 149
Cdd:COG0421   39 KRVLIIGGGDGGLArELLKHPPVeRVDVVEIDPEVVELAREYFPLLAPAFddprLRVVIGDGRAFLREaEESYDVIIV 116
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
69-147 6.44e-07

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 48.61  E-value: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  69 MLQELA--VKKHESILEIGAGSGYMAALLAHRG-QHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAArglpekgPYD 145
Cdd:PRK00517 109 CLEALEklVLPGKTVLDVGCGSGILAIAAAKLGaKKVLAVDIDPQAVEAARENAELNGVELNVYLPQGDL-------KAD 181


                 ..
gi 738093883 146 VI 147
Cdd:PRK00517 182 VI 183
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 57-154 6.80e-07

ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 48.38  E-value: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   57 GQKML-APRVEARMLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDngVSNAEVVLADAA 135
Cdd:TIGR00755   8 GQNFLvDENVIRKIVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSL--YNNLEIIEGDAL 85

                          90
                  ....*....|....*....
gi 738093883  136 RGLPEKGPYDVICVSGGLP 154
Cdd:TIGR00755  86 KFDLNELAKDLTKVVGNLP 104
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
74-180 7.24e-07

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 48.20  E-value: 7.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   74 AVKKHESILEIGAGSG-YMAALLAHRGQ--HVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARgLP-EKGPYDVICV 149
Cdd:pfam01209  39 GVKRGNKFLDVAGGTGdWTFGLSDSAGSsgKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEE-LPfEDDSFDIVTI 117

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 738093883  150 SGGLPVVP------QELLEQLKVGGRLAAFVGSRPVM 180
Cdd:pfam01209 118 SFGLRNFPdylkvlKEAFRVLKPGGRVVCLEFSKPEN 154
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 82-170 8.00e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 45.82  E-value: 8.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   82 LEIGAGSGYMAALLA--HRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVV-LADAARGLPEKGPYDVI---CVSGGLPv 155
Cdd:pfam08242   1 LEIGCGTGTLLRALLeaLPGLEYTGLDISPAALEAARERLAALGLLNAVRVeLFQLDLGELDPGSFDVVvasNVLHHLA- 79

                          90
                  ....*....|....*....
gi 738093883  156 VPQELLEQ----LKVGGRL 170
Cdd:pfam08242  80 DPRAVLRNirrlLKPGGVL 98
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 75-171 8.22e-07

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: 48.42  E-value: 8.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   75 VKKHESILEIGAGSGYM---AALLAhrGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLadAARGLPeKGPYDVIcVSG 151
Cdd:pfam06325 159 VKPGESVLDVGCGSGILaiaALKLG--AKKVVGVDIDPVAVRAAKENAELNGVEARLEVY--LPGDLP-KEKADVV-VAN 232

                          90       100
                  ....*....|....*....|....
gi 738093883  152 GLPVVPQELLEQ----LKVGGRLA 171
Cdd:pfam06325 233 ILADPLIELAPDiyalVKPGGYLI 256
PTZ00338 PTZ00338
dimethyladenosine transferase-like protein; Provisional
 57-150 1.05e-06

dimethyladenosine transferase-like protein; Provisional


Pssm-ID: 240367 [Multi-domain]  Cd Length: 294  Bit Score: 48.08  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  57 GQKMLA-PRVEARMLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALV-----QFAADNLRdngvSNAEVV 130
Cdd:PTZ00338  15 GQHILKnPLVLDKIVEKAAIKPTDTVLEIGPGTGNLTEKLLQLAKKVIAIEIDPRMVaelkkRFQNSPLA----SKLEVI 90

                         90       100
                 ....*....|....*....|
gi 738093883 131 LADAARGlpEKGPYDViCVS 150
Cdd:PTZ00338  91 EGDALKT--EFPYFDV-CVA 107
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 68-171 1.07e-06

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: 47.67  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   68 RMLQELAVKKHESILEIGAGSGYMAALLAHRG--QHVVTVDIDPALVQFAADNLRdngvSNAEVVLADAARGLPEKGPYD 145
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRALLKRFpqAEFIALDISAGMLAQAKTKLS----ENVQFICGDAEKLPLEDSSFD 100

                          90       100       110
                  ....*....|....*....|....*....|...
gi 738093883  146 VIcVS-------GGLPVVPQELLEQLKVGGRLA 171
Cdd:TIGR02072 101 LI-VSnlalqwcDDLSQALSELARVLKPGGLLA 132
COG4262 COG4262
Predicted spermidine synthase with an N-terminal membrane domain [General function prediction ...
 73-147 2.66e-06

Predicted spermidine synthase with an N-terminal membrane domain [General function prediction only];


Pssm-ID: 443404 [Multi-domain]  Cd Length: 426  Bit Score: 47.17  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  73 LAVKKHESILEIGAGSGyMAA--LLAHRG-QHVVTVDIDPALVQFAADN---LRDNGVS----NAEVVLADAARGLPE-K 141
Cdd:COG4262  282 AAHPRPRRVLVLGGGDG-LAAreVLKYPDvESVTLVDLDPEVTDLAKTNpflRELNGGAlndpRVTVVNADAFQFLREtD 360


                 ....*.
gi 738093883 142 GPYDVI 147
Cdd:COG4262  361 EKYDVI 366
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 70-150 2.99e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 46.69  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  70 LQELAVKKHESILEIGAGSGYMA-ALLAHRGQ-HVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPeKGPYDVI 147
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSGAIAlALAKERPDaEVTAVDISPEALAVARRNAKHGLGARVEFLQGDWFEPLP-GGRFDLI 179


                 ...
gi 738093883 148 cVS 150
Cdd:PRK09328 180 -VS 181
rADc smart00650
Ribosomal RNA adenine dimethylases;
68-147 3.46e-06

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 45.58  E-value: 3.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883    68 RMLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQfaadNLRD--NGVSNAEVVLADAAR-GLPEKGPY 144
Cdd:smart00650   4 KIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAP----RLREkfAAADNLTVIHGDALKfDLPKLQPY 79


                   ...
gi 738093883   145 DVI 147
Cdd:smart00650  80 KVV 82
COG3963 COG3963
Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];
63-184 3.50e-06

Phosphatidylethanolamine N-methyltransferase [Lipid transport and metabolism];


Pssm-ID: 443163  Cd Length: 193  Bit Score: 45.97  E-value: 3.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  63 PRVEARMLQELAVKKHESILEIGAGSGYM-AALLAH--RGQHVVTVDIDPALVQFaadnLRDNgVSNAEVVLADAAR--- 136
Cdd:COG3963   31 RALARAMASEVDWSGAGPVVELGPGTGVFtRAILARgvPDARLLAVEINPEFAEH----LRRR-FPRVTVVNGDAEDlae 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738093883 137 --GLPEKGPYDVIcVSgGLPVV--PQE----LLEQ----LKVGGRLAAF--VGSRPVMKAQI 184
Cdd:COG3963  106 llAEHGIGKVDAV-VS-GLPLLsfPPElrraILDAafrvLAPGGVFVQFtySPRSPVPRKLL 165
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 56-148 9.22e-06

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 44.83  E-value: 9.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  56 GGQKMLApRVEARmLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNA-EVVLADA 134
Cdd:PRK07580  44 GHQRMRD-TVLSW-LPADGDLTGLRILDAGCGVGSLSIPLARRGAKVVASDISPQMVEEARERAPEAGLAGNiTFEVGDL 121

                         90
                 ....*....|....*
gi 738093883 135 ArglPEKGPYD-VIC 148
Cdd:PRK07580 122 E---SLLGRFDtVVC 133
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 75-195 1.11e-05

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished 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 catalytic domain with distant homology to GroES. 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. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally 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. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 45.01  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  75 VKKHESILEIGAGS-GYMAALLA-HRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGpYDVICVSGG 152
Cdd:cd05188  132 LKPGDTVLVLGAGGvGLLAAQLAkAAGARVIVTDRSDEKLELAKELGADHVIDYKEEDLEEELRLTGGGG-ADVVIDAVG 210

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 738093883 153 LPVVPQELLEQLKVGGRLAAFVGSRPVMKAQIITRIDDKQFRV 195
Cdd:cd05188  211 GPETLAQALRLLRPGGRIVVVGGTSGGPPLDDLRRLLFKELTI 253
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
57-176 2.00e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 44.13  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  57 GQKMLA-----PRVEAR-MLQELAVKKHESILEIGAGSGYMAALLAHRG-QHVVTVDIDPALVQFAADN--LRDNGVSNA 127
Cdd:COG2521  106 GIHMHRikgtdPLEDARrKVKLVGVRRGDRVLDTCTGLGYTAIEALKRGaREVITVEKDPNVLELAELNpwSRELANERI 185

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738093883 128 EVVLADAA---RGLPEkGPYDVIC-------VSGGLPVVP--QELLEQLKVGGRLAAFVGS 176
Cdd:COG2521  186 KIILGDASeviKTFPD-ESFDAIIhdpprfsLAGELYSLEfyRELYRVLKPGGRLFHYTGN 245
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
63-134 3.99e-05

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 43.35  E-value: 3.99e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738093883  63 PRVEARMLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGvsNAEVVLADA 134
Cdd:PRK14896  15 DRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAG--NVEIIEGDA 84
RsmB COG0144
16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and ...
 73-147 4.48e-05

16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family [Translation, ribosomal structure and biogenesis]; 16S rRNA C967 or C1407 C5-methylase, RsmB/RsmF family is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439914 [Multi-domain]  Cd Length: 441  Bit Score: 43.46  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  73 LAVKKHESILEIGAGSG----YMAALLAHRGQhVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPE-KGPYDVI 147
Cdd:COG0144  245 LDPKPGERVLDLCAAPGgktlHLAELMGNKGR-VVAVDISEHRLKRLRENLARLGLSNVEVVVADARELLEWlPGKFDRV 323
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
57-134 5.39e-05

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 42.74  E-value: 5.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738093883   57 GQKMLA-PRVEARMLQELAVKKHESILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGvsNAEVVLADA 134
Cdd:pfam00398   9 GQNFLKdPKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKLSLDE--NLTVIHQDF 85
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
89-175 7.68e-05

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 41.05  E-value: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883   89 GYMAALLA-HRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPVVPQELLEQLKVG 167
Cdd:pfam00107   3 GLAAIQLAkAAGAKVIAVDGSEEKLELAKELGADHVINPKETDLVEEIKELTGGKGVDVVFDCVGSPATLEQALKLLRPG 82


                  ....*...
gi 738093883  168 GRLaAFVG 175
Cdd:pfam00107  83 GRV-VVVG 89
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 82-147 9.53e-05

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 40.37  E-value: 9.53e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738093883   82 LEIGAGSGYMAALLA-----HRGQHVVTVDIDPALVQFAAdNLRDNGVS-NAEVVLADAARGLP--EKGPYDVI 147
Cdd:pfam13578   1 VEIGTYSGVSTLWLAaalrdNGLGRLTAVDPDPGAEEAGA-LLRKAGLDdRVRLIVGDSREALPslADGPIDLL 73
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 74-170 3.75e-04

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished 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 catalytic domain with distant homology to GroES. The MDR group includes various 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: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 40.64  E-value: 3.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  74 AVKKHESILEIGAGSGYMAALLA--HRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSG 151
Cdd:cd08261  156 GVTAGDTVLVVGAGPIGLGVIQVakARGARVIVVDIDDERLEFARELGADDTINVGDEDVAARLRELTDGEGADVVIDAT 235

                         90
                 ....*....|....*....
gi 738093883 152 GLPVVPQELLEQLKVGGRL 170
Cdd:cd08261  236 GNPASMEEAVELVAHGGRV 254
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
67-155 4.48e-04

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 40.32  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  67 ARMLQELAVKKHESILEIGAGSGY-MAALLAH--RGQHVVTVDIDPALVQFAA--DNLRDngvSNAEVVLADAARGLPEk 141
Cdd:COG0827  105 GYLVEKFTKKEGLRILDPAVGTGNlLTTVLNQlkKKVNAYGVEVDDLLIRLAAvlANLQG---HPVELFHQDALQPLLI- 180

                         90
                 ....*....|....
gi 738093883 142 GPYDVicVSGGLPV 155
Cdd:COG0827  181 DPVDV--VISDLPV 192
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
80-170 5.11e-04

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 39.95  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  80 SILEIGAGSGYMAALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPE--KGPYDVICVSGGLPVV- 156
Cdd:PRK11036  47 RVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRAKQAAEAKGVSDNMQFIHCAAQDIAQhlETPVDLILFHAVLEWVa 126

                         90
                 ....*....|....*....
gi 738093883 157 -PQE----LLEQLKVGGRL 170
Cdd:PRK11036 127 dPKSvlqtLWSVLRPGGAL 145
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
57-170 5.12e-04

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


Pssm-ID: 181354  Cd Length: 187  Bit Score: 39.60  E-value: 5.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  57 GQK--MLAPRVEARMLQELAVKKHESILEIGAGSGYMA--ALLAHRGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLA 132
Cdd:PRK08287   9 GEKvpMTKEEVRALALSKLELHRAKHLIDVGAGTGSVSieAALQFPSLQVTAIERNPDALRLIKENRQRFGCGNIDIIPG 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 738093883 133 DAARGLPEKGpyDVICV--SGG-LPVVPQELLEQLKVGGRL 170
Cdd:PRK08287  89 EAPIELPGKA--DAIFIggSGGnLTAIIDWSLAHLHPGGRL 127
TRM1 COG1867
tRNA G26 N,N-dimethylase Trm1 [Translation, ribosomal structure and biogenesis]; tRNA G26 N, ...
 75-147 6.33e-04

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


Pssm-ID: 441472  Cd Length: 383  Bit Score: 39.86  E-value: 6.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738093883  75 VKKHESILEIGAGSGYMAALLAH-RGQHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPE-KGPYDVI 147
Cdd:COG1867   55 LKREISYLDALAASGIRGLRYALeVGIKVTLNDIDPEAVELIRENLELNGLEDVEVYNRDANALLHElGRRFDVV 129
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 74-179 7.10e-04

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished 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 catalytic domain with distant homology to GroES. 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.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 39.56  E-value: 7.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  74 AVKKHESILEIGAGS-GYMAALLAHR--GQHVVTVDIDPALVQFAADNLRDNGVsnaevvlADAARGLPEKGPYD-VICV 149
Cdd:cd08255   94 EPRLGERVAVVGLGLvGLLAAQLAKAagAREVVGVDPDAARRELAEALGPADPV-------AADTADEIGGRGADvVIEA 166

                         90       100       110
                 ....*....|....*....|....*....|..
gi 738093883 150 SGGLPVVpQELLEQLKVGGR--LAAFVGSRPV 179
Cdd:cd08255  167 SGSPSAL-ETALRLLRDRGRvvLVGWYGLKPL 197
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 67-147 1.75e-03

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: 38.69  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  67 ARMLQElaVKKHESILEIGAGSGYMAALLA-HRGQHVVTVDIDPALVQFAADNLRDNGVS-NAEVVLADAARGLPE-KGP 143
Cdd:COG2520  172 LRIAEL--VKPGERVLDMFAGVGPFSIPIAkRSGAKVVAIDINPDAVEYLKENIRLNKVEdRVTPILGDAREVAPElEGK 249


                 ....
gi 738093883 144 YDVI 147
Cdd:COG2520  250 ADRI 253
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 68-175 2.23e-03

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: 38.35  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  68 RMLQELAVKKHESILEIGAG-SGYMAALLA-HRG-QHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPY 144
Cdd:cd08235  156 NAQRKAGIKPGDTVLVIGAGpIGLLHAMLAkASGaRKVIVSDLNEFRLEFAKKLGADYTIDAAEEDLVEKVRELTDGRGA 235

                         90       100       110
                 ....*....|....*....|....*....|.
gi 738093883 145 DVICVSGGLPVVPQELLEQLKVGGRLAAFVG 175
Cdd:cd08235  236 DVVIVATGSPEAQAQALELVRKGGRILFFGG 266
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 75-175 2.88e-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: 37.81  E-value: 2.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  75 VKKHESILEIGAGS-GYMAALLA-HRG-QHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSG 151
Cdd:COG1063  159 VKPGDTVLVIGAGPiGLLAALAArLAGaARVIVVDRNPERLELARELGADAVVNPREEDLVEAVRELTGGRGADVVIEAV 238

                         90       100
                 ....*....|....*....|....
gi 738093883 152 GLPVVPQELLEQLKVGGRLaAFVG 175
Cdd:COG1063  239 GAPAALEQALDLVRPGGTV-VLVG 261
PRK14967 PRK14967
putative methyltransferase; Provisional
 49-157 3.95e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 37.34  E-value: 3.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  49 DLELPLPGgqkMLAPRVEARMLQELAVKKHE----SILEIGAGSGYMAALLAHRG-QHVVTVDIDPALVQFAADNLRDNG 123
Cdd:PRK14967   7 DALLRAPG---VYRPQEDTQLLADALAAEGLgpgrRVLDLCTGSGALAVAAAAAGaGSVTAVDISRRAVRSARLNALLAG 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 738093883 124 VsNAEVVLADAARGLPEkGPYDVICVSGglPVVP 157
Cdd:PRK14967  84 V-DVDVRRGDWARAVEF-RPFDVVVSNP--PYVP 113
tdh PRK05396
L-threonine 3-dehydrogenase; Validated
 79-171 7.91e-03

L-threonine 3-dehydrogenase; Validated


Pssm-ID: 180054 [Multi-domain]  Cd Length: 341  Bit Score: 36.73  E-value: 7.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093883  79 ESILEIGAGS-GYMAALLA-HRG-QHVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVICVSGGLPV 155
Cdd:PRK05396 165 EDVLITGAGPiGIMAAAVAkHVGaRHVVITDVNEYRLELARKMGATRAVNVAKEDLRDVMAELGMTEGFDVGLEMSGAPS 244

                         90
                 ....*....|....*.
gi 738093883 156 VPQELLEQLKVGGRLA 171
Cdd:PRK05396 245 AFRQMLDNMNHGGRIA 260
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 101-147 9.00e-03

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


Pssm-ID: 235286  Cd Length: 382  Bit Score: 36.43  E-value: 9.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 738093883 101 HVVTVDIDPALVQFAADNLRDNGVSNAEVVLADAARGLPEKGPYDVI 147
Cdd:PRK04338  83 KVTLNDINPDAVELIKKNLELNGLENEKVFNKDANALLHEERKFDVV 129
 
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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