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Conserved domains on  [gi|2108271237|gb|UCG37659|]
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arsenite methyltransferase [Candidatus Bathyarchaeota archaeon]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 1000582)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
arsM super family cl30592
arsenite methyltransferase;
1-288 1.75e-118

arsenite methyltransferase;


The actual alignment was detected with superfamily member PRK11873:

Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 341.16  E-value: 1.75e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237   1 MNVKEDVRKEVREGYAKIAKKGLPSGLSSSCC-CNSEAAEEQGMKIGYTAEDLHSVPDGANLNLGCGNPVALASLNEGET 79
Cdd:PRK11873    1 MMDADDIKEVVREKYGEIAERGGSGCSGCSCCgASANDAADPSTSLGYSEEELAAVPEGANLGLGCGNPTALAELKPGET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  80 VVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENLPVADNTADLVMSNCVINLSP 159
Cdd:PRK11873   81 VLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTNVEFRLGEIEALPVADNSVDVIISNCVINLSP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 160 SKTRVFEEAYRALKPGGRLMVSDIVLLKEIPEAIR-AGAHPASCVRGAIAKEEYLKSLREVGFRNVEILEEKQESFEDva 238
Cdd:PRK11873  161 DKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRnDAELYAGCVAGALQEEEYLAMLAEAGFVDITIQPKREYRIPD-- 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2108271237 239 sdpnakvlvanpekkseelkVVSELEGKTRDIVRQILESTASITVSATKP 288
Cdd:PRK11873  239 --------------------AREFLEDWGIAPGRQLDGYIVSATVEATKP 268
 
Name Accession Description Interval E-value
arsM PRK11873
arsenite methyltransferase;
1-288 1.75e-118

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 341.16  E-value: 1.75e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237   1 MNVKEDVRKEVREGYAKIAKKGLPSGLSSSCC-CNSEAAEEQGMKIGYTAEDLHSVPDGANLNLGCGNPVALASLNEGET 79
Cdd:PRK11873    1 MMDADDIKEVVREKYGEIAERGGSGCSGCSCCgASANDAADPSTSLGYSEEELAAVPEGANLGLGCGNPTALAELKPGET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  80 VVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENLPVADNTADLVMSNCVINLSP 159
Cdd:PRK11873   81 VLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTNVEFRLGEIEALPVADNSVDVIISNCVINLSP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 160 SKTRVFEEAYRALKPGGRLMVSDIVLLKEIPEAIR-AGAHPASCVRGAIAKEEYLKSLREVGFRNVEILEEKQESFEDva 238
Cdd:PRK11873  161 DKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRnDAELYAGCVAGALQEEEYLAMLAEAGFVDITIQPKREYRIPD-- 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2108271237 239 sdpnakvlvanpekkseelkVVSELEGKTRDIVRQILESTASITVSATKP 288
Cdd:PRK11873  239 --------------------AREFLEDWGIAPGRQLDGYIVSATVEATKP 268
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 74-220 1.83e-42

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 142.94  E-value: 1.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  74 LNEGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENLP--VADNTADLVMS 151
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPelLEDDKFDVVIS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 152 NCVINLSPSKTRVFEEAYRALKPGGRLMVSDIVLLKEIPEAIRAGA-HPASCVRGAIAKEEYLKSLREVG 220
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDStYYAGCVGGAILKKKLYELLEEAG 150
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 69-183 7.79e-35

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: 123.18  E-value: 7.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLNEGETVVDLGSGAGLDCFLAAKkvgAKGKVIGIDMTPEMIDKARKNARKSNYkNVEFRLGEIENLPVADNTADL 148
Cdd:COG2226    15 LAALGLRPGARVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFPDGSFDL 90

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2108271237 149 VMSNCVINLSPSKTRVFEEAYRALKPGGRLMVSDI 183
Cdd:COG2226    91 VISSFVLHHLPDPERALAEIARVLKPGGRLVVVDF 125
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 79-185 3.59e-20

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: 83.25  E-value: 3.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  79 TVVDLGSGAGLDCFLAAKKVGAKgkVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENLP-VADNTADLVMSNCVIN- 156
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGAR--VTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpEADESFDVIISDPPLHh 78

                          90       100
                  ....*....|....*....|....*....
gi 2108271237 157 LSPSKTRVFEEAYRALKPGGRLMVSDIVL 185
Cdd:cd02440    79 LVEDLARFLEEARRLLKPGGVLVLTLVLA 107
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 79-147 4.84e-03

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 36.52  E-value: 4.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108271237  79 TVVDLGSGAGLDCFLAAKKvGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEF-------RLGEIENLPVADNTAD 147
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARK-GAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLlnaavgdRDGELEFNVSDDDTGN 75
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
78-232 8.36e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.01  E-value: 8.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237   78 ETVVDLGSGAGLDCFLAAKKVGaKGKVIGIDMTPEMIDKARKNARKSNYKN-VEFRLGEIENLPVADnTADLVMSNCVIN 156
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHP-HLQLHGYTISPEQAEVGRERIRALGLQGrIRIFYRDSAKDPFPD-TYDLVFGFEVIH 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108271237  157 LSPSKTRVFEEAYRALKPGGRLMVSDIvllkeIPEAIRAGAHPASCVRgAIAKEEYLKSLREVGFRNVEILEEKQE 232
Cdd:smart00828  79 HIKDKMDLFSNISRHLKDGGHLVLADF-----IANLLSAIEHEETTSY-LVTREEWAELLARNNLRVVEGVDASLE 148
 
Name Accession Description Interval E-value
arsM PRK11873
arsenite methyltransferase;
1-288 1.75e-118

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 341.16  E-value: 1.75e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237   1 MNVKEDVRKEVREGYAKIAKKGLPSGLSSSCC-CNSEAAEEQGMKIGYTAEDLHSVPDGANLNLGCGNPVALASLNEGET 79
Cdd:PRK11873    1 MMDADDIKEVVREKYGEIAERGGSGCSGCSCCgASANDAADPSTSLGYSEEELAAVPEGANLGLGCGNPTALAELKPGET 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  80 VVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENLPVADNTADLVMSNCVINLSP 159
Cdd:PRK11873   81 VLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTNVEFRLGEIEALPVADNSVDVIISNCVINLSP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 160 SKTRVFEEAYRALKPGGRLMVSDIVLLKEIPEAIR-AGAHPASCVRGAIAKEEYLKSLREVGFRNVEILEEKQESFEDva 238
Cdd:PRK11873  161 DKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRnDAELYAGCVAGALQEEEYLAMLAEAGFVDITIQPKREYRIPD-- 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2108271237 239 sdpnakvlvanpekkseelkVVSELEGKTRDIVRQILESTASITVSATKP 288
Cdd:PRK11873  239 --------------------AREFLEDWGIAPGRQLDGYIVSATVEATKP 268
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 74-220 1.83e-42

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 142.94  E-value: 1.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  74 LNEGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENLP--VADNTADLVMS 151
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPelLEDDKFDVVIS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 152 NCVINLSPSKTRVFEEAYRALKPGGRLMVSDIVLLKEIPEAIRAGA-HPASCVRGAIAKEEYLKSLREVG 220
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDStYYAGCVGGAILKKKLYELLEEAG 150
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 69-183 7.79e-35

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: 123.18  E-value: 7.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLNEGETVVDLGSGAGLDCFLAAKkvgAKGKVIGIDMTPEMIDKARKNARKSNYkNVEFRLGEIENLPVADNTADL 148
Cdd:COG2226    15 LAALGLRPGARVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFPDGSFDL 90

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2108271237 149 VMSNCVINLSPSKTRVFEEAYRALKPGGRLMVSDI 183
Cdd:COG2226    91 VISSFVLHHLPDPERALAEIARVLKPGGRLVVVDF 125
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 80-176 3.13e-29

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 106.88  E-value: 3.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  80 VVDLGSGAGLDCFLAAKKVGAKgkVIGIDMTPEMIDKARKNARKSNYkNVEFRLGEIENLPVADNTADLVMSNCVINL-- 157
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGAR--VTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHlp 77

                          90
                  ....*....|....*....
gi 2108271237 158 SPSKTRVFEEAYRALKPGG 176
Cdd:pfam13649  78 DPDLEAALREIARVLKPGG 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 70-181 1.60e-24

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 97.68  E-value: 1.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  70 ALASLNEGETVVDLGSGAGLDCFLAAKKVGakGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENL-PVADNTADL 148
Cdd:COG0500    20 LLERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELdPLPAESFDL 97

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2108271237 149 VMSNCVIN-LSPSK-TRVFEEAYRALKPGGRLMVS 181
Cdd:COG0500    98 VVAFGVLHhLPPEErEALLRELARALKPGGVLLLS 132
PRK08317 PRK08317
hypothetical protein; Provisional
 70-182 6.69e-24

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 96.93  E-value: 6.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  70 ALASLNEGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARkNARKSNYKNVEFRLGEIENLPVADNTADLV 149
Cdd:PRK08317   13 ELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAK-ERAAGLGPNVEFVRGDADGLPFPDGSFDAV 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2108271237 150 MSNCVINLSPSKTRVFEEAYRALKPGGRLMVSD 182
Cdd:PRK08317   92 RSDRVLQHLEDPARALAEIARVLRPGGRVVVLD 124
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 74-183 2.00e-23

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: 92.77  E-value: 2.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  74 LNEGETVVDLGSGAGLDCFLAAKKvGAKgkVIGIDMTPEMIDKARKNARKSNyknVEFRLGEIENLPVADNTADLVMSNC 153
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARR-GAD--VTGVDISPEALEIARERAAELN---VDFVQGDLEDLPLEDGSFDLVICSE 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 2108271237 154 VINLSPSKTRVFEEAYRALKPGGRLMVSDI 183
Cdd:COG2227    96 VLEHLPDPAALLRELARLLKPGGLLLLSTP 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 81-180 5.75e-22

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 87.72  E-value: 5.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  81 VDLGSGAGLDCFLAAKKVGakgKVIGIDMTPEMIDKARKNARKSNyknVEFRLGEIENLPVADNTADLVMSNCVINLSPS 160
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA---RVTGVDISPEMLELAREKAPREG---LTFVVGDAEDLPFPDNSFDLVLSSEVLHHVED 74

                          90       100
                  ....*....|....*....|
gi 2108271237 161 KTRVFEEAYRALKPGGRLMV 180
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
76-182 3.81e-21

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 85.65  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  76 EGETVVDLGSGAGLDC-FLAAKKVGAKgkVIGIDMTPEMIDKARKNarksnYKNVEFRLGEIENLPvADNTADLVMSNCV 154
Cdd:COG4106     1 PPRRVLDLGCGTGRLTaLLAERFPGAR--VTGVDLSPEMLARARAR-----LPNVRFVVADLRDLD-PPEPFDLVVSNAA 72

                          90       100
                  ....*....|....*....|....*...
gi 2108271237 155 INLSPSKTRVFEEAYRALKPGGRLMVSD 182
Cdd:COG4106    73 LHWLPDHAALLARLAAALAPGGVLAVQV 100
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 69-180 8.83e-21

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 88.67  E-value: 8.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLNEGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNY-KNVEFRLGEIENLPVADNTAD 147
Cdd:PRK00216   44 IKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLAVGREKLRDLGLsGNVEFVQGDAEALPFPDNSFD 123

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2108271237 148 LV-MSNCVINLsPSKTRVFEEAYRALKPGGRLMV 180
Cdd:PRK00216  124 AVtIAFGLRNV-PDIDKALREMYRVLKPGGRLVI 156
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 79-185 3.59e-20

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: 83.25  E-value: 3.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  79 TVVDLGSGAGLDCFLAAKKVGAKgkVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENLP-VADNTADLVMSNCVIN- 156
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGAR--VTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpEADESFDVIISDPPLHh 78

                          90       100
                  ....*....|....*....|....*....
gi 2108271237 157 LSPSKTRVFEEAYRALKPGGRLMVSDIVL 185
Cdd:cd02440    79 LVEDLARFLEEARRLLKPGGVLVLTLVLA 107
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 69-182 3.17e-18

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 79.59  E-value: 3.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLNEGETVVDLGSGAGLDCFLAAKKVGAkgKVIGIDMTPEMIDKARKNARKSNYKN-VEFRLGEIENLPvADNTAD 147
Cdd:COG2230    44 LRKLGLKPGMRVLDIGCGWGGLALYLARRYGV--RVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDLP-ADGQFD 120

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2108271237 148 LVMSNCVINLSPSKTR--VFEEAYRALKPGGRLMVSD 182
Cdd:COG2230   121 AIVSIGMFEHVGPENYpaYFAKVARLLKPGGRLLLHT 157
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
69-181 4.16e-18

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 80.04  E-value: 4.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLNEGETVVDLGSGAGLDCFLAAKKVGakgKVIGIDMTPEMIDKARknaRKSNYknVEFRLGEIENLPVADNTADL 148
Cdd:COG4976    39 LARLPPGPFGRVLDLGCGTGLLGEALRPRGY---RLTGVDLSEEMLAKAR---EKGVY--DRLLVADLADLAEPDGRFDL 110

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2108271237 149 VMSNCVINLSPSKTRVFEEAYRALKPGGRLMVS 181
Cdd:COG4976   111 IVAADVLTYLGDLAAVFAGVARALKPGGLFIFS 143
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
76-180 2.10e-17

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 79.02  E-value: 2.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  76 EGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENLPVADNTADLVMSNCVI 155
Cdd:pfam01209  42 RGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVTISFGL 121

                          90       100
                  ....*....|....*....|....*
gi 2108271237 156 NLSPSKTRVFEEAYRALKPGGRLMV 180
Cdd:pfam01209 122 RNFPDYLKVLKEAFRVLKPGGRVVC 146
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 71-192 3.30e-15

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: 71.90  E-value: 3.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  71 LASLNEGETVVD--LGSGAGLdcfLAAKKVGAKgkVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENLPVADNTADL 148
Cdd:COG1041    21 LAGAKEGDTVLDpfCGTGTIL---IEAGLLGRR--VIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDLPLADESVDA 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2108271237 149 VmsncVINL---SPSKT----------RVFEEAYRALKPGGRL-MVSDIVLLKEIPEA 192
Cdd:COG1041    96 I----VTDPpygRSSKIsgeellelyeKALEEAARVLKPGGRVvIVTPRDIDELLEEA 149
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 69-228 3.34e-14

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: 70.57  E-value: 3.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLNEGETVVDLGSGAG-LDCFLAaKKVGAKGKVIGIDMTPEMIDKARKNARKSN-YKNVEFRLGEIENlPVADNTA 146
Cdd:COG2519    84 IARLDIFPGARVLEAGTGSGaLTLALA-RAVGPEGKVYSYERREDFAEIARKNLERFGlPDNVELKLGDIRE-GIDEGDV 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 147 DLVmsncVINLsPSKTRVFEEAYRALKPGGRLmvsdIVLLKEIPEAIRAgahpascvrgaiakeeyLKSLREVGFRNVEI 226
Cdd:COG2519   162 DAV----FLDM-PDPWEALEAVAKALKPGGVL----VAYVPTVNQVSKL-----------------VEALRESGFTDIEA 215


                  ..
gi 2108271237 227 LE 228
Cdd:COG2519   216 VE 217
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 70-178 3.29e-12

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


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 64.78  E-value: 3.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  70 ALASLNEGETVVDLGSGAGLDCFLAAKKVgAKGKVIGIDMTPEMIDKARKNARKSNYKN-VEFRLGEIENLP--VADNTA 146
Cdd:COG4123    31 AFAPVKKGGRVLDLGTGTGVIALMLAQRS-PGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDLKEFAaeLPPGSF 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2108271237 147 DLVMSN------CVINLSPSKTR-------------VFEEAYRALKPGGRL 178
Cdd:COG4123   110 DLVVSNppyfkaGSGRKSPDEARaiarhedaltledLIRAAARLLKPGGRF 160
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 74-270 6.67e-12

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 64.22  E-value: 6.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  74 LNEGETVVDLGSGAGLDCFLAAKKVGAKgkVIGIDMTPEMIDKArkNARKSNYKNVEFRLGEIENLPVADNTADLVMS-N 152
Cdd:PTZ00098   50 LNENSKVLDIGSGLGGGCKYINEKYGAH--VHGVDICEKMVNIA--KLRNSDKNKIEFEANDILKKDFPENTFDMIYSrD 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 153 CVINLS-PSKTRVFEEAYRALKPGGRLMVSDIVLLK------EIPEAIRAGAHPascvrgAIAKEEYLKSLREVGFRNV- 224
Cdd:PTZ00098  126 AILHLSyADKKKLFEKCYKWLKPNGILLITDYCADKienwdeEFKAYIKKRKYT------LIPIQEYGDLIKSCNFQNVv 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108271237 225 ---------EILEEKQESFEdvasdpnakvlvanpEKKSEELKVVSELE------GKTRDI 270
Cdd:PTZ00098  200 akdisdywlELLQVELKKLE---------------EKKEEFLKLYSEKEynslkdGWTRKI 245
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 81-178 7.77e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 60.46  E-value: 7.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  81 VDLGSGAGLDCFLAAKKVGAkGKVIGIDMTPEMIDKAR-KNARKSNYKNVEFRLGEIENLPVADNTADLVMSNCVINLSP 159
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPG-LEYTGLDISPAALEAAReRLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 2108271237 160 SKTRVFEEAYRALKPGGRL 178
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 69-182 9.56e-12

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 63.76  E-value: 9.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLNEGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKA--RKNAR-KSNYKNVEFRLGEIENLPVADNT 145
Cdd:PLN02233   66 VSWSGAKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAasRQELKaKSCYKNIEWIEGDATDLPFDDCY 145

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2108271237 146 ADLVMSNCVINLSPSKTRVFEEAYRALKPGGRLMVSD 182
Cdd:PLN02233  146 FDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILD 182
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 71-218 3.32e-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: 60.58  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  71 LASLNEGETVVDLGSGAG---LdCFLAAkkVGAKGKVIGIDMTPEMIDKARKNARKSNY-KNVEFRLGE-IENLP-VADN 144
Cdd:COG4122    11 LARLLGAKRILEIGTGTGystL-WLARA--LPDDGRLTTIEIDPERAAIARENFARAGLaDRIRLILGDaLEVLPrLADG 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108271237 145 TADLVmsncVINLSPSKT-RVFEEAYRALKPGGrLMVSDIVLLKEIPeairagAHPASCVRGAIAKEEYLKSLRE 218
Cdd:COG4122    88 PFDLV----FIDADKSNYpDYLELALPLLRPGG-LIVADNVLWHGRV------ADPARRDPSTRAIREFNEYLRE 151
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 69-149 1.45e-10

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: 60.96  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLNEGETVVDLGSGAGLDCFLAAKKVGakgKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIEN-LP--VADNT 145
Cdd:COG2265   226 LEWLDLTGGERVLDLYCGVGTFALPLARRAK---KVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEvLPelLWGGR 302


                  ....
gi 2108271237 146 ADLV 149
Cdd:COG2265   303 PDVV 306
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
74-195 2.28e-10

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 59.80  E-value: 2.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  74 LNEGETVVDLGSGAGLdcfLA--AKKVGAKgKVIGIDMTPEMIDKARKNARKSNYKN-VEFRLGEIEnlpvADNTADLVM 150
Cdd:COG2264   146 LKPGKTVLDVGCGSGI---LAiaAAKLGAK-RVLAVDIDPVAVEAARENAELNGVEDrIEVVLGDLL----EDGPYDLVV 217

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2108271237 151 SNcvINLSPSKtRVFEEAYRALKPGGRLMVSDIvLLKEIPEAIRA 195
Cdd:COG2264   218 AN--ILANPLI-ELAPDLAALLKPGGYLILSGI-LEEQADEVLAA 258
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
74-180 4.15e-10

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 58.15  E-value: 4.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  74 LNEGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEF-----RLGEIENLPVAdntadl 148
Cdd:pfam01135  71 LKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLENVIVvvgdgRQGWPEFAPYD------ 144

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2108271237 149 vmsncVINLSPSKTRVFEEAYRALKPGGRLMV 180
Cdd:pfam01135 145 -----AIHVGAAAPEIPEALIDQLKEGGRLVI 171
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 75-180 5.86e-10

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: 57.51  E-value: 5.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  75 NEGETVVDLGSGAGldcFLA--AKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENlPVADNTADLVMSN 152
Cdd:COG2813    48 PLGGRVLDLGCGYG---VIGlaLAKRNPEARVTLVDVNARAVELARANAAANGLENVEVLWSDGLS-GVPDGSFDLILSN 123

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2108271237 153 CVI--NLSPSKT---RVFEEAYRALKPGGRLMV 180
Cdd:COG2813   124 PPFhaGRAVDKEvahALIADAARHLRPGGELWL 156
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 79-226 6.02e-10

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 59.14  E-value: 6.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  79 TVVDLGSGAGLDCFLAAKKVGAKGKVIgIDMTPEMIDKARKnarKSNYKNVEFRLGEIENLPVADNTADLVMSNCVINLS 158
Cdd:PLN02490  116 KVVDVGGGTGFTTLGIVKHVDAKNVTI-LDQSPHQLAKAKQ---KEPLKECKIIEGDAEDLPFPTDYADRYVSAGSIEYW 191

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108271237 159 PSKTRVFEEAYRALKPGGRLMVSDIVllkeipeairagaHPASCVRGAIA--------KEEYLKSLREVGFRNVEI 226
Cdd:PLN02490  192 PDPQRGIKEAYRVLKIGGKACLIGPV-------------HPTFWLSRFFAdvwmlfpkEEEYIEWFTKAGFKDVKL 254
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
76-152 2.90e-09

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 55.68  E-value: 2.90e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108271237  76 EGETVVDLGSGAGldCF-LAAKKVGAKgKVIGIDMTPEMIDKARKNARKSNyKNVEFRLGEIENLPVaDNTADLVMSN 152
Cdd:COG2263    45 EGKTVLDLGCGTG--MLaIGAALLGAK-KVVGVDIDPEALEIARENAERLG-VRVDFIRADVTRIPL-GGSVDTVVMN 117
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 69-195 4.35e-09

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: 56.71  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLN--EGETVVDLGSGAG---LDCFLAAKKvgakGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGE----IENL 139
Cdd:COG2242   238 LTLAKLAlrPGDVLWDIGAGSGsvsIEAARLAPG----GRVYAIERDPERAALIRANARRFGVPNVEVVEGEapeaLADL 313

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108271237 140 PVADntadlvmsnCVI------NLSPsktrVFEEAYRALKPGGRLMVSdIVLLKEIPEAIRA 195
Cdd:COG2242   314 PDPD---------AVFiggsggNLPE----ILEACWARLRPGGRLVAN-AVTLETLALALEA 361
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 74-195 4.93e-09

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: 56.12  E-value: 4.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  74 LNEGETVVDLGSGAGLdCFLAAKKVGAKgKVIGIDMTPEMIDKARKNARKsNYKNVEFRLGEIENLPVAdnTADLVMSNC 153
Cdd:pfam06325 159 VKPGESVLDVGCGSGI-LAIAALKLGAK-KVVGVDIDPVAVRAAKENAEL-NGVEARLEVYLPGDLPKE--KADVVVANI 233

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2108271237 154 ----VINLSPsktrvfeEAYRALKPGGRLMVSDIvlLKEIPEAIRA 195
Cdd:pfam06325 234 ladpLIELAP-------DIYALVKPGGYLILSGI--LKEQAQMVAE 270
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
77-182 7.93e-09

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 55.31  E-value: 7.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  77 GETVVDLGSGAGLDCFLAAKKVGAKGKVIG-----IDMTPEMIDKARKN------ARKSNYKNVEFRLGEIENLPVA-DN 144
Cdd:COG4798    67 GMTVVEIWPGGGWYTEILAPYLGPKGKVYAanfdpDSEPPEYAKRSREAfsaklaADPALYGNVRVTAFAPPDDPIApPG 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2108271237 145 TADLVMSNCVI-NLSPSKTR--VFEEAYRALKPGGRLMVSD 182
Cdd:COG4798   147 SADLVLTFRNYhNWYRAGDAaaMFAAFFKALKPGGVLGVVD 187
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
76-229 9.77e-09

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 54.77  E-value: 9.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  76 EGETVVDLGSGAGLdcfL--AAKKVGAKgKVIGIDMTPEMIDKARKNARKsNykNVEFRLgeieNLPVADNTADLVMSNC 153
Cdd:PRK00517  119 PGKTVLDVGCGSGI---LaiAAAKLGAK-KVLAVDIDPQAVEAARENAEL-N--GVELNV----YLPQGDLKADVIVANI 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 154 V----INLSPsktrvfeEAYRALKPGGRLMVSDIvlLKEIpeairagahpascvrgaiaKEEYLKSLREVGFRNVEILEE 229
Cdd:PRK00517  188 LanplLELAP-------DLARLLKPGGRLILSGI--LEEQ-------------------ADEVLEAYEEAGFTLDEVLER 239
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 61-135 1.03e-08

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 54.25  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  61 LNLGCGNPVA----------LASLNEGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVE 130
Cdd:PRK13942   51 LEIGYGQTISaihmvaimceLLDLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKKLGYDNVE 130


                  ....*
gi 2108271237 131 FRLGE 135
Cdd:PRK13942  131 VIVGD 135
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 70-225 1.13e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 53.20  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  70 ALASLNEGETVVDLGSGAGLDCfLAAKKVGAKgkVIGIDMTPEMIDKARKNARKSNYknvefrlgEIENLPVADNTADLV 149
Cdd:pfam13489  16 LLPKLPSPGRVLDFGCGTGIFL-RLLRAQGFS--VTGVDPSPIAIERALLNVRFDQF--------DEQEAAVPAGKFDVI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108271237 150 MSNCVINLSPSKTRVFEEAYRALKPGGRLMVSDIVLLKEIPEAIRAGAHPASCVRGA--IAKEEYLKSLREVGFRNVE 225
Cdd:pfam13489  85 VAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPRNGHIslFSARSLKRLLEEAGFEVVS 162
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 69-271 1.19e-08

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 55.53  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLNEGETVVDLGSGAGLDCFLAAKKVGAKgkVIGIDMTPEMIDKA--RKNARKSNyknVEFRLGEIENLPVADNTA 146
Cdd:PLN02336  259 VDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVH--VVGIDLSVNMISFAleRAIGRKCS---VEFEVADCTKKTYPDNSF 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 147 DLVMSNCVINLSPSKTRVFEEAYRALKPGGRLMVSDIVllkeipeaiRAGAHPASCVRGAIAK--------EEYLKSLRE 218
Cdd:PLN02336  334 DVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYC---------RSPGTPSPEFAEYIKQrgydlhdvQAYGQMLKD 404

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2108271237 219 VGFRNVeILEEKQESFEDVASDPNAKVlvanpEKKSEELkvVSEL-EGKTRDIV 271
Cdd:PLN02336  405 AGFDDV-IAEDRTDQFLQVLQRELDAV-----EKEKDEF--ISDFsEEDYNDIV 450
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 78-195 1.68e-08

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 54.38  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  78 ETVVDLGSGAGLdcflAAKKVGAKG-KVIGIDMTPEMIDKARKNARKSNYknvefRLGEIENLPVADNTADLVMSNCVIN 156
Cdd:PRK10258   44 THVLDAGCGPGW----MSRYWRERGsQVTALDLSPPMLAQARQKDAADHY-----LAGDIESLPLATATFDLAWSNLAVQ 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2108271237 157 LSPSKTRVFEEAYRALKPGGRLMVSDIVL--LKEIPEAIRA 195
Cdd:PRK10258  115 WCGNLSTALRELYRVVRPGGVVAFTTLVQgsLPELHQAWQA 155
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
75-211 1.89e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 50.81  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  75 NEGETVVDLGSGAGLDCFLAAKKvGAKgKVIGIDMTPEMIDKARKNARKSNYK-NVEFrlgeIE------NLPvadNTAD 147
Cdd:COG4076    34 KPGDVVLDIGTGSGLLSMLAARA-GAK-KVYAVEVNPDIAAVARRIIAANGLSdRITV----INadatdlDLP---EKAD 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2108271237 148 LVMSNCVIN--LSPSKTRVFEEAYRA-LKPGGRLmvsdivllkeIPEAIRAGAHPASCVRGAIAKEE 211
Cdd:COG4076   105 VIISEMLDTalLDEGQVPILNHARKRlLKPGGRI----------IPERITNAAQPVESPVDAEGFED 161
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 80-229 2.00e-07

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 50.84  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  80 VVDLGSGAG-LDCFLAAKKVGAkgKVIGIDMTPEMIDKARKnarksnyKNVEFRLGEIENLPVADNTaDLVMSNCVINLS 158
Cdd:PRK14103   33 VVDLGCGPGnLTRYLARRWPGA--VIEALDSSPEMVAAARE-------RGVDARTGDVRDWKPKPDT-DVVVSNAALQWV 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2108271237 159 PSKTRVFEEAYRALKPGGRLMVsdivllkEIPEAIRAGAHPAscVRGAIAKEEYLKSLREVGFRNVEILEE 229
Cdd:PRK14103  103 PEHADLLVRWVDELAPGSWIAV-------QVPGNFDAPSHAA--VRALARREPWAKLLRDIPFRVGAVVQT 164
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 49-180 1.12e-06

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: 48.86  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  49 AEDLHSVPDGANLNLGCGNPVALAS----------LNEGETVVDLGSGA-GLDCFLAAKKVGAKgkVIGIDMTPEMIDKA 117
Cdd:cd05188    97 ADNLVPLPDGLSLEEAALLPEPLATayhalrragvLKPGDTVLVLGAGGvGLLAAQLAKAAGAR--VIVTDRSDEKLELA 174

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108271237 118 RKN--ARKSNYKNVEFrlgEIENLPVADNTADLVMsNCVINLSpsktrVFEEAYRALKPGGRLMV 180
Cdd:cd05188   175 KELgaDHVIDYKEEDL---EEELRLTGGGGADVVI-DAVGGPE-----TLAQALRLLRPGGRIVV 230
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 75-180 4.52e-06

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: 46.04  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  75 NEGETVVDLGSGAG-LDCFLAakKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGEIENlPVADNTADLVMSNC 153
Cdd:pfam05175  30 DLSGKVLDLGCGAGvLGAALA--KESPDAELTMVDINARALESARENLAANGLENGEVVASDVYS-GVEDGKFDLIISNP 106

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2108271237 154 VINlSPSKT------RVFEEAYRALKPGGRLMV 180
Cdd:pfam05175 107 PFH-AGLATtynvaqRFIADAKRHLRPGGELWI 138
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 70-228 5.29e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 47.07  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  70 ALASLNEGE--TVVDLGSGAGldCF-LAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKN-VEFRLGEI-ENLPvADN 144
Cdd:COG2890   104 ALALLPAGAppRVLDLGTGSG--AIaLALAKERPDARVTAVDISPDALAVARRNAERLGLEDrVRFLQGDLfEPLP-GDG 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 145 TADLVMSN------CVINLSPSKTRVFE------------EAYRA--------LKPGGRLMVsdivllkEI----PEAIR 194
Cdd:COG2890   181 RFDLIVSNppyipeDEIALLPPEVRDHEprlaldggedglDFYRRiiaqaprlLKPGGWLLL-------EIgedqGEAVR 253

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2108271237 195 AgahpascvrgaiakeeyLksLREVGFRNVEILE 228
Cdd:COG2890   254 A-----------------L--LEAAGFADVETHK 268
RlmE COG0293
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ...
 74-151 8.79e-06

23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440062 [Multi-domain]  Cd Length: 208  Bit Score: 45.45  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  74 LNEGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTP-EMIDkarknarksnykNVEFRLG---------EIENLpVAD 143
Cdd:COG0293    48 IKPGMRVVDLGAAPGGWSQVAAKRVGGKGRVIALDLLPmEPIP------------GVEFIQGdfredevldQLLEA-LGG 114


                  ....*...
gi 2108271237 144 NTADLVMS 151
Cdd:COG0293   115 RKVDLVLS 122
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 72-195 1.16e-05

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 45.17  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  72 ASLNEGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARK-SNYKNVEFRLGE-IENLPVADNTADLV 149
Cdd:PRK00377   36 LRLRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEKfGVLNNIVLIKGEaPEILFTINEKFDRI 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2108271237 150 MsncVINLSPSKTRVFEEAYRALKPGGRLmVSDIVLLKEIPEAIRA 195
Cdd:PRK00377  116 F---IGGGSEKLKEIISASWEIIKKGGRI-VIDAILLETVNNALSA 157
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 72-180 2.86e-05

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 44.84  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  72 ASLNEGETVVDLGSGAGLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGE----IENLPVADntad 147
Cdd:PRK13943   76 VGLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRRLGIENVIFVCGDgyygVPEFAPYD---- 151

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2108271237 148 lvmsncVINLSPSKTRVFEEAYRALKPGGRLMV 180
Cdd:PRK13943  152 ------VIFVTVGVDEVPETWFTQLKEGGRVIV 178
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
 76-200 3.90e-05

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


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 44.47  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  76 EGETVVDLGSGAGLDCFLAAKKVGAkgKVIGIDMTPEMIDKARKNARKSN-YKNVEFRLGEIENL-PVADNTADLVmsnc 153
Cdd:COG2520   180 PGERVLDMFAGVGPFSIPIAKRSGA--KVVAIDINPDAVEYLKENIRLNKvEDRVTPILGDAREVaPELEGKADRI---- 253

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2108271237 154 VINLsPSKTRVF-EEAYRALKPGGRLMVSDIV----LLKEIPEAIRAGAHPA 200
Cdd:COG2520   254 IMNL-PHSADEFlDAALRALKPGGVIHYYEIVpeedPFERAEERIEEAAEEA 304
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 76-176 4.53e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 44.74  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  76 EGETVVDLGSGAGLDCFLAAKKVGakgKVIGIDMTPEMIDKarKNARKSNYKNVEFRLGEI--ENLPVADNTADLVMSNC 153
Cdd:PLN02336   37 EGKSVLELGAGIGRFTGELAKKAG---QVIALDFIESVIKK--NESINGHYKNVKFMCADVtsPDLNISDGSVDLIFSNW 111

                          90       100
                  ....*....|....*....|....*
gi 2108271237 154 VI-NLSPSK-TRVFEEAYRALKPGG 176
Cdd:PLN02336  112 LLmYLSDKEvENLAERMVKWLKVGG 136
PLN02244 PLN02244
tocopherol O-methyltransferase
 79-180 1.09e-04

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 43.19  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  79 TVVDLGSGAGLDCFLAAKKVGAKgkVIGIDMTPEMIDKARKNARKSNYKN-VEFRLGEIENLPVADNTADLVMSNCVINL 157
Cdd:PLN02244  121 RIVDVGCGIGGSSRYLARKYGAN--VKGITLSPVQAARANALAAAQGLSDkVSFQVADALNQPFEDGQFDLVWSMESGEH 198

                          90       100
                  ....*....|....*....|...
gi 2108271237 158 SPSKTRVFEEAYRALKPGGRLMV 180
Cdd:PLN02244  199 MPDKRKFVQELARVAAPGGRIII 221
alcohol_DH_class_III cd08300
class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde ...
 55-119 1.19e-04

class III alcohol dehydrogenases; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176260 [Multi-domain]  Cd Length: 368  Bit Score: 42.99  E-value: 1.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108271237  55 VPDGANLN----LGCGNPVAL-ASLN-----EGETVVDLGSGA-GLDCFLAAKKVGAKgKVIGIDMTPEMIDKARK 119
Cdd:cd08300   155 INPEAPLDkvclLGCGVTTGYgAVLNtakvePGSTVAVFGLGAvGLAVIQGAKAAGAS-RIIGIDINPDKFELAKK 229
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 78-180 1.44e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 42.24  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  78 ETVVDLGSGAGLDCFLAAKKVGAkGKVIGIDMTPEMIDKARKnarksNYKNVEFRLGEIEN-LPVADntADLVMSNCVIN 156
Cdd:PRK01683   33 RYVVDLGCGPGNSTELLVERWPA-ARITGIDSSPAMLAEARS-----RLPDCQFVEADIASwQPPQA--LDLIFANASLQ 104

                          90       100
                  ....*....|....*....|....
gi 2108271237 157 LSPSKTRVFEEAYRALKPGGRLMV 180
Cdd:PRK01683  105 WLPDHLELFPRLVSLLAPGGVLAV 128
PRK14968 PRK14968
putative methyltransferase; Provisional
 76-193 1.86e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  76 EGETVVDLGSGAGLDCFLAAKKvgAKgKVIGIDMTPEMIDKARKNARKSNYKN--VEFRLGeieNL--PVADNTADLVMS 151
Cdd:PRK14968   23 KGDRVLEVGTGSGIVAIVAAKN--GK-KVVGVDINPYAVECAKCNAKLNNIRNngVEVIRS---DLfePFRGDKFDVILF 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108271237 152 N-------------CVINLSPS--KT------RVFEEAYRALKPGGR--LMVSDIVLLKEIPEAI 193
Cdd:PRK14968   97 NppylpteeeeewdDWLNYALSggKDgrevidRFLDEVGRYLKPGGRilLLQSSLTGEDEVLEYL 161
Methyltransf_32 pfam13679
Methyltransferase domain; This family appears to be a methyltransferase domain.
 75-149 2.43e-04

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


Pssm-ID: 379330 [Multi-domain]  Cd Length: 138  Bit Score: 40.25  E-value: 2.43e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2108271237  75 NEGETVVDLGSGAG-LDCFLAAKKVGakGKVIGIDMTPEMIDKARKNARKSNY-KNVEFRLGEIE--NLPVADNTADLV 149
Cdd:pfam13679  24 NGPITIVDHGAGKGyLGFILYYLKYG--VRVYGIDTRAELVEKANALAQKLGFnKRMSFLEGTIAgsTPVELPDRVDVV 100
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 77-139 2.74e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 41.36  E-value: 2.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2108271237  77 GETVVDLGSGAGLDCFLAAKKvGAKgkVIGIDMTPEMIDKARKNARKS-NYKNVEFRLGEIENL 139
Cdd:PRK07580   64 GLRILDAGCGVGSLSIPLARR-GAK--VVASDISPQMVEEARERAPEAgLAGNITFEVGDLESL 124
FDH_like_1 cd08283
Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified ...
 69-130 6.69e-04

Glutathione-dependent formaldehyde dehydrogenase related proteins, child 1; Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176243 [Multi-domain]  Cd Length: 386  Bit Score: 40.60  E-value: 6.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2108271237  69 VALASLNEGETVVDLGSGA-GLDCFLAAKKVGAKgKVIGIDMTPEMIDKARK--NARKSNYKNVE 130
Cdd:cd08283   177 AELAEVKPGDTVAVWGCGPvGLFAARSAKLLGAE-RVIAIDRVPERLEMARShlGAETINFEEVD 240
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 49-180 8.01e-04

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: 40.51  E-value: 8.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  49 AEDLHSVPDGANLN-------LGCG-NPVALASLNEGETVVDLGSGA-GLDCFLAAKKVGAkGKVIGIDMTPEMIDKARK 119
Cdd:COG1063   126 AANLVKVPDGLSDEaaalvepLAVAlHAVERAGVKPGDTVLVIGAGPiGLLAALAARLAGA-ARVIVVDRNPERLELARE 204

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108271237 120 -------NARKSnykNVEFRLGEIENLPVADntadlvmsnCVINLSPSKtRVFEEAYRALKPGGRLMV 180
Cdd:COG1063   205 lgadavvNPREE---DLVEAVRELTGGRGAD---------VVIEAVGAP-AALEQALDLVRPGGTVVL 259
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 70-230 8.26e-04

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


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 40.55  E-value: 8.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  70 ALASLNEGETVvdlgsgagLDCF-------LAAKKVGAKgKVIGIDMTPEMIDKARKNARKSNYK-NVEFR----LGEIE 137
Cdd:COG1092   210 RVAELAKGKRV--------LNLFsytggfsVHAAAGGAK-SVTSVDLSATALEWAKENAALNGLDdRHEFVqadaFDWLR 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 138 NLPVADNTADLVmsncVIN---LSPSKTRVF----------EEAYRALKPGGRLMVSdivllkeipeairagahpaSCVR 204
Cdd:COG1092   281 ELAREGERFDLI----ILDppaFAKSKKDLFdaqrdykdlnRLALKLLAPGGILVTS-------------------SCSR 337

                         170       180
                  ....*....|....*....|....*....
gi 2108271237 205 GaIAKEEYLKSLREVGF---RNVEILEEK 230
Cdd:COG1092   338 H-FSLDLFLEILARAARdagRRVRIIERL 365
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 69-194 8.97e-04

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 39.26  E-value: 8.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  69 VALASLNEGETVVD--LGSGA--------GLDCFLAAKKVGAKGKVIGIDMTPEMIDKARKNARKSNYKN-VEFRLGEIE 137
Cdd:pfam01170  21 VNLAGWKPGDPLLDpmCGSGTilieaalmGANIAPGKFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDlIEFVQADAA 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108271237 138 NLPVADNTADLVMSN-----------CVINLSPSKTRVFEeayRALKPGGRLmVSDIVLLKEIPEAIR 194
Cdd:pfam01170 101 DLPLLEGSVDVIVTNppygirlgskgALEALYPEFLREAK---RVLRGGGWL-VLLTAENKDFEKAAR 164
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 74-176 9.87e-04

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 39.11  E-value: 9.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  74 LNEGETVVDLGSGAG--LDCflAAKKVgaKGKVIGIDMTPEMIDKARKNARKSNYKnVEFRLGEIENL--PVADNTADLV 149
Cdd:pfam01728  19 LKPGKTVLDLGAAPGgwSQV--ALQRG--AGKVVGVDLGPMQLWKPRNDPGVTFIQ-GDIRDPETLDLleELLGRKVDLV 93

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2108271237 150 MSNCVINLSPSKTR-----------VFEEAYRALKPGG 176
Cdd:pfam01728  94 LSDGSPFISGNKVLdhlrsldlvkaALEVALELLRKGG 131
FDH_like cd05278
Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the ...
 71-178 2.04e-03

Formaldehyde dehydrogenases; Formaldehyde dehydrogenase (FDH) is a member of the zinc-dependent/medium chain alcohol dehydrogenase family. Formaldehyde dehydrogenase (aka ADH3) may be the ancestral form of alcohol dehydrogenase, which evolved to detoxify formaldehyde. This CD contains glutathione dependant FDH, glutathione independent FDH, and related alcohol dehydrogenases. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. Unlike typical FDH, Pseudomonas putida aldehyde-dismutating FDH (PFDH) is glutathione-independent. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176181 [Multi-domain]  Cd Length: 347  Bit Score: 39.18  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  71 LASLNEGETVVDLGSGA-GLDCFLAAKKVGAkGKVIGIDMTPEMIDKARKN--ARKSNYKNVEF--RLGEIENLPVADnt 145
Cdd:cd05278   162 LAGIKPGSTVAVIGAGPvGLCAVAGARLLGA-ARIIAVDSNPERLDLAKEAgaTDIINPKNGDIveQILELTGGRGVD-- 238

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2108271237 146 adlvmsnCVINLSPSKTrVFEEAYRALKPGGRL 178
Cdd:cd05278   239 -------CVIEAVGFEE-TFEQAVKVVRPGGTI 263
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
68-119 2.54e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 38.37  E-value: 2.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  68 PVAL------ASLNEGETVVD--LGSGAGLdcfLAAKKVGAKGkvIGIDMTPEMIDKARK 119
Cdd:COG0863   168 PVELlerlilASSNPGDIVLDpfAGSGTTL---VAAERLGRRF--IGIEIDPEYVEVARR 222
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
77-182 2.58e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 39.08  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  77 GETVVDLGSGAGLDCFLAAKKVGAKgKVIGIDMTPEMIDKARKnaRKSN-YKNVEFRLGEIENLP--VADNTADLVMSNC 153
Cdd:PRK06922  419 GDTIVDVGAGGGVMLDMIEEETEDK-RIYGIDISENVIDTLKK--KKQNeGRSWNVIKGDAINLSssFEKESVDTIVYSS 495

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2108271237 154 VINLSPS---------KTRVFEE----AYRALKPGGRLMVSD 182
Cdd:PRK06922  496 ILHELFSyieyegkkfNHEVIKKglqsAYEVLKPGGRIIIRD 537
Zn_ADH1 cd05279
Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H) ...
 52-118 2.59e-03

Liver alcohol dehydrogenase and related zinc-dependent alcohol dehydrogenases; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. There are 7 vertebrate ADH 7 classes, 6 of which have been identified in humans. Class III, glutathione-dependent formaldehyde dehydrogenase, has been identified as the primordial form and exists in diverse species, including plants, micro-organisms, vertebrates, and invertebrates. Class I, typified by liver dehydrogenase, is an evolving form. Gene duplication and functional specialization of ADH into ADH classes and subclasses created numerous forms in vertebrates. For example, the A, B and C (formerly alpha, beta, gamma) human class I subunits have high overall structural similarity, but differ in the substrate binding pocket and therefore in substrate specificity. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine (His-51), the ribose of NAD, a serine (Ser-48), then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of an beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.


Pssm-ID: 176182 [Multi-domain]  Cd Length: 365  Bit Score: 38.96  E-value: 2.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2108271237  52 LHSVPDGANLN----LGC------GNPVALASLNEGETVVDLGSGA-GLDCFLAAKKVGAkGKVIGIDMTPEMIDKAR 118
Cdd:cd05279   149 LAKIDPDAPLEkvclIGCgfstgyGAAVNTAKVTPGSTCAVFGLGGvGLSVIMGCKAAGA-SRIIAVDINKDKFEKAK 225
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
101-181 3.13e-03

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


Pssm-ID: 180961  Cd Length: 196  Bit Score: 38.05  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 101 KGKVIGIDMTPEMIDKARKNARKSNYKNVEFRLGeieNLPvadntadlvmsNCVINLSPSKTRV-----------FEEAY 169
Cdd:PRK07402   64 KGRVIAIERDEEVVNLIRRNCDRFGVKNVEVIEG---SAP-----------ECLAQLAPAPDRVcieggrpikeiLQAVW 129

                          90
                  ....*....|..
gi 2108271237 170 RALKPGGRLMVS 181
Cdd:PRK07402  130 QYLKPGGRLVAT 141
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 105-182 3.34e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 37.36  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237 105 IGIDMTPEMIDKA--RKNAR-KSNYKNVEFRLGEIENLPVADNTADLVMSNCVINLSPSKTRVFEEAYRALKPGGRLMVS 181
Cdd:PLN02232    1 MGLDFSSEQLAVAatRQSLKaRSCYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSIL 80


                  .
gi 2108271237 182 D 182
Cdd:PLN02232   81 D 81
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 79-147 4.84e-03

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 36.52  E-value: 4.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108271237  79 TVVDLGSGAGLDCFLAAKKvGAKGKVIGIDMTPEMIDKARKNARKSNYKNVEF-------RLGEIENLPVADNTAD 147
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARK-GAEGRVIAFEPLPDAYEILEENVKLNNLPNVVLlnaavgdRDGELEFNVSDDDTGN 75
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
94-180 5.13e-03

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 36.43  E-value: 5.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  94 AAKKVGAKgkVIGIDMTPEMIDKARKN--ARKSNYKNVEFrLGEIENLPVADNtADLVMsNCVinlspSKTRVFEEAYRA 171
Cdd:pfam00107   9 LAKAAGAK--VIAVDGSEEKLELAKELgaDHVINPKETDL-VEEIKELTGGKG-VDVVF-DCV-----GSPATLEQALKL 78


                  ....*....
gi 2108271237 172 LKPGGRLMV 180
Cdd:pfam00107  79 LRPGGRVVV 87
iditol_2_DH_like cd08235
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ...
 65-179 5.93e-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: 37.57  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  65 CGNPVALASLNEGETVVDLGSGA-GLDCFLAAKKVGAKgKVIGIDMTPEMIDKARK-------NARKSNYKNVEFRLgei 136
Cdd:cd08235   154 CINAQRKAGIKPGDTVLVIGAGPiGLLHAMLAKASGAR-KVIVSDLNEFRLEFAKKlgadytiDAAEEDLVEKVREL--- 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2108271237 137 enlpvADNT-ADLVMsncvinLSPSKTRVFEEAYRALKPGGRLM 179
Cdd:cd08235   230 -----TDGRgADVVI------VATGSPEAQAQALELVRKGGRIL 262
PRK15451 PRK15451
carboxy-S-adenosyl-L-methionine synthase CmoA;
77-182 6.63e-03

carboxy-S-adenosyl-L-methionine synthase CmoA;


Pssm-ID: 185348  Cd Length: 247  Bit Score: 37.31  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237  77 GETVVDLGSGAGLDCFLAAKKV-GAKGKVIGIDMTPEMIDKARKNArkSNYKN---VEFRLGEIENLPVaDNTADLVMSN 152
Cdd:PRK15451   57 GTQVYDLGCSLGAATLSVRRNIhHDNCKIIAIDNSPAMIERCRRHI--DAYKAptpVDVIEGDIRDIAI-ENASMVVLNF 133

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2108271237 153 CVINLSPSKTR-VFEEAYRALKPGGRLMVSD 182
Cdd:PRK15451  134 TLQFLEPSERQaLLDKIYQGLNPGGALVLSE 164
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
69-131 8.35e-03

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 37.44  E-value: 8.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2108271237  69 VALA----SLNEGETVVDLGSGAG-----LdcflaAKKVGAkgkVIGIDMTPEMIDKARKNARKSNYKNVEF 131
Cdd:PRK13168  286 VARAlewlDPQPGDRVLDLFCGLGnftlpL-----ARQAAE---VVGVEGVEAMVERARENARRNGLDNVTF 349
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
78-232 8.36e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.01  E-value: 8.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108271237   78 ETVVDLGSGAGLDCFLAAKKVGaKGKVIGIDMTPEMIDKARKNARKSNYKN-VEFRLGEIENLPVADnTADLVMSNCVIN 156
Cdd:smart00828   1 KRVLDFGCGYGSDLIDLAERHP-HLQLHGYTISPEQAEVGRERIRALGLQGrIRIFYRDSAKDPFPD-TYDLVFGFEVIH 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2108271237  157 LSPSKTRVFEEAYRALKPGGRLMVSDIvllkeIPEAIRAGAHPASCVRgAIAKEEYLKSLREVGFRNVEILEEKQE 232
Cdd:smart00828  79 HIKDKMDLFSNISRHLKDGGHLVLADF-----IANLLSAIEHEETTSY-LVTREEWAELLARNNLRVVEGVDASLE 148
 
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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