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Conserved domains on  [gi|166987988|sp|A7ZQI7|]
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RecName: Full=Protein-L-isoaspartate O-methyltransferase; AltName: Full=L-isoaspartyl protein carboxyl methyltransferase; AltName: Full=Protein L-isoaspartyl methyltransferase; AltName: Full=Protein-beta-aspartate methyltransferase; Short=PIMT

Protein Classification

protein-L-isoaspartate O-methyltransferase( domain architecture ID 10011370)

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

EC:  2.1.1.77
Gene Ontology:  GO:0004719|GO:0030091
PubMed:  1860862
SCOP:  4000666

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
1-208 1.63e-130

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


:

Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 365.30  E-value: 1.63e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   1 MVSRRVQALLDQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVL 80
Cdd:PRK00312   4 MESERFARLVLRLRAEGILDERVLEAIEATPRELFVPEAFKHKAYENRALPIGCGQTISQPYMVARMTELLELKPGDRVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  81 EIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMT 160
Cdd:PRK00312  84 EIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRHGDGWKGWPAYAPFDRILVTAAAPEIPRALLE 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 166987988 161 QLDEGGILVLPVG-EEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA 208
Cdd:PRK00312 164 QLKEGGILVAPVGgEEQQLLTRVRKRGGRFEREVLEEVRFVPLVKGELA 212
 
Name Accession Description Interval E-value
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
1-208 1.63e-130

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 365.30  E-value: 1.63e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   1 MVSRRVQALLDQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVL 80
Cdd:PRK00312   4 MESERFARLVLRLRAEGILDERVLEAIEATPRELFVPEAFKHKAYENRALPIGCGQTISQPYMVARMTELLELKPGDRVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  81 EIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMT 160
Cdd:PRK00312  84 EIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRHGDGWKGWPAYAPFDRILVTAAAPEIPRALLE 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 166987988 161 QLDEGGILVLPVG-EEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA 208
Cdd:PRK00312 164 QLKEGGILVAPVGgEEQQLLTRVRKRGGRFEREVLEEVRFVPLVKGELA 212
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
 1-208 1.54e-124

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: 350.67  E-value: 1.54e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988    1 MVSRRVQALLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRV 79
Cdd:TIGR00080   2 DLESQKKALIDKLINEGyIKSKRVIDALLSVPREEFVPEHFKEYAYVDTPLEIGYGQTISAPHMVAMMTELLELKPGMKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   80 LEIGTGSGYQTAILAHLVQH---VCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPT 156
Cdd:TIGR00080  82 LEIGTGSGYQAAVLAEIVGRdglVVSIERIPELAEKAERRLRKLGLDNVIVIVGDGTQGWEPLAPYDRIYVTAAGPKIPE 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166987988  157 ALMTQLDEGGILVLPVGEEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA 208
Cdd:TIGR00080 162 ALIDQLKEGGILVMPVGEYLQVLKRAEKRGGEIIIKDVEPVAFVPLVGGEGF 213
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
4-202 4.62e-107

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 305.83  E-value: 4.62e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988    4 RRVQALLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEI 82
Cdd:pfam01135   1 NRNEALIENLKNYGvIKSDKVAEAMLAVDREEFVPESFKSYAYEDIPLSIGYGQTISAPHMHAMMLELLELKPGMRVLEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   83 GTGSGYQTAILAHLVQHVC---SVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALM 159
Cdd:pfam01135  81 GSGSGYLTACFARMVGEVGrvvSIEHIPELVEIARRNLEKLGLENVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 166987988  160 TQLDEGGILVLPVGEE-HQYLKRVRRRG-GEFIIDTVEAVRFVPL 202
Cdd:pfam01135 161 DQLKEGGRLVIPVGPNgNQVLQQFDKRNdGSVVIKDLEGVRFVPL 205
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 11-205 3.64e-106

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 303.16  E-value: 3.64e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  11 DQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEIGTGSGYQT 90
Cdd:COG2518    2 QQLRPRGVTDPRVLDAMRAVPRELFVPEALRELAYADRALPIGHGQTISQPYIVARMLEALDLKPGDRVLEIGTGSGYQA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  91 AILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQLDEGGILVL 170
Cdd:COG2518   82 AVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLVA 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 166987988 171 PVGEE-HQYLKRVRRRGGEFIIDTVEAVRFVPLVKG 205
Cdd:COG2518  162 PVGEGgVQRLVLITRTGDGFERESLFEVRFVPLRGG 197
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 78-172 2.25e-05

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: 42.03  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  78 RVLEIGTGSGYQTAILA-HLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQG-WQARAPFDAIIVTAAPPEIP 155
Cdd:cd02440    1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....
gi 166987988 156 TALMTQLDE-------GGILVLPV 172
Cdd:cd02440   81 EDLARFLEEarrllkpGGVLVLTL 104
rADc smart00650
Ribosomal RNA adenine dimethylases;
63-146 8.13e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 35.56  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988    63 MVARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLqwqaRRRLKNL--DLHNVSTRHGDGWQGWQARA 140
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRL----APRLREKfaAADNLTVIHGDALKFDLPKL 76


                   ....*.
gi 166987988   141 PFDAII 146
Cdd:smart00650  77 QPYKVV 82
 
Name Accession Description Interval E-value
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
1-208 1.63e-130

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 365.30  E-value: 1.63e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   1 MVSRRVQALLDQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVL 80
Cdd:PRK00312   4 MESERFARLVLRLRAEGILDERVLEAIEATPRELFVPEAFKHKAYENRALPIGCGQTISQPYMVARMTELLELKPGDRVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  81 EIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMT 160
Cdd:PRK00312  84 EIGTGSGYQAAVLAHLVRRVFSVERIKTLQWEAKRRLKQLGLHNVSVRHGDGWKGWPAYAPFDRILVTAAAPEIPRALLE 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 166987988 161 QLDEGGILVLPVG-EEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA 208
Cdd:PRK00312 164 QLKEGGILVAPVGgEEQQLLTRVRKRGGRFEREVLEEVRFVPLVKGELA 212
pimt TIGR00080
protein-L-isoaspartate(D-aspartate) O-methyltransferase; This is an all-kingdom (but not all ...
 1-208 1.54e-124

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: 350.67  E-value: 1.54e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988    1 MVSRRVQALLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRV 79
Cdd:TIGR00080   2 DLESQKKALIDKLINEGyIKSKRVIDALLSVPREEFVPEHFKEYAYVDTPLEIGYGQTISAPHMVAMMTELLELKPGMKV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   80 LEIGTGSGYQTAILAHLVQH---VCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPT 156
Cdd:TIGR00080  82 LEIGTGSGYQAAVLAEIVGRdglVVSIERIPELAEKAERRLRKLGLDNVIVIVGDGTQGWEPLAPYDRIYVTAAGPKIPE 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166987988  157 ALMTQLDEGGILVLPVGEEHQYLKRVRRRGGEFIIDTVEAVRFVPLVKGELA 208
Cdd:TIGR00080 162 ALIDQLKEGGILVMPVGEYLQVLKRAEKRGGEIIIKDVEPVAFVPLVGGEGF 213
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
4-202 4.62e-107

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 305.83  E-value: 4.62e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988    4 RRVQALLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEI 82
Cdd:pfam01135   1 NRNEALIENLKNYGvIKSDKVAEAMLAVDREEFVPESFKSYAYEDIPLSIGYGQTISAPHMHAMMLELLELKPGMRVLEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   83 GTGSGYQTAILAHLVQHVC---SVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALM 159
Cdd:pfam01135  81 GSGSGYLTACFARMVGEVGrvvSIEHIPELVEIARRNLEKLGLENVIVVVGDGRQGWPEFAPYDAIHVGAAAPEIPEALI 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 166987988  160 TQLDEGGILVLPVGEE-HQYLKRVRRRG-GEFIIDTVEAVRFVPL 202
Cdd:pfam01135 161 DQLKEGGRLVIPVGPNgNQVLQQFDKRNdGSVVIKDLEGVRFVPL 205
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 11-205 3.64e-106

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 303.16  E-value: 3.64e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  11 DQLRAQGIQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEIGTGSGYQT 90
Cdd:COG2518    2 QQLRPRGVTDPRVLDAMRAVPRELFVPEALRELAYADRALPIGHGQTISQPYIVARMLEALDLKPGDRVLEIGTGSGYQA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  91 AILAHLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQLDEGGILVL 170
Cdd:COG2518   82 AVLARLAGRVYSVERDPELAERARERLAALGYDNVTVRVGDGALGWPEHAPFDRIIVTAAAPEVPEALLEQLAPGGRLVA 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 166987988 171 PVGEE-HQYLKRVRRRGGEFIIDTVEAVRFVPLVKG 205
Cdd:COG2518  162 PVGEGgVQRLVLITRTGDGFERESLFEVRFVPLRGG 197
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 7-203 9.48e-66

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 201.40  E-value: 9.48e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   7 QALLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEIGTG 85
Cdd:PRK13942   7 RRVIEELIREGyIKSKKVIDALLKVPRHLFVPEYLEEYAYVDTPLEIGYGQTISAIHMVAIMCELLDLKEGMKVLEIGTG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  86 SGYQTAILAHLV---QHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQL 162
Cdd:PRK13942  87 SGYHAAVVAEIVgksGKVVTIERIPELAEKAKKTLKKLGYDNVEVIVGDGTLGYEENAPYDRIYVTAAGPDIPKPLIEQL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 166987988 163 DEGGILVLPVGEEHQYLKRVRRRGGEFIIDTVEAVRFVPLV 203
Cdd:PRK13942 167 KDGGIMVIPVGSYSQELIRVEKDNGKIIKKKLGEVAFVPLI 207
PRK13944 PRK13944
protein-L-isoaspartate O-methyltransferase; Provisional
 9-202 5.85e-45

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 140001  Cd Length: 205  Bit Score: 148.42  E-value: 5.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   9 LLDQLRAQG-IQDEQVLNALAAVPREKFVDEAFEQKAWDNIALPIGQGQTISQPYMVARMTELLELTPQSRVLEIGTGSG 87
Cdd:PRK13944   5 LVEELVREGiIKSERVKKAMLSVPREEFVMPEYRMMAYEDRPLPLFAGATISAPHMVAMMCELIEPRPGMKILEVGTGSG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  88 YQTAILAHLVQH---VCSVERIKGLQWQARRRLKNLDLHN-VSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQLD 163
Cdd:PRK13944  85 YQAAVCAEAIERrgkVYTVEIVKELAIYAAQNIERLGYWGvVEVYHGDGKRGLEKHAPFDAIIVTAAASTIPSALVRQLK 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 166987988 164 EGGILVLPVGEE-HQYLKRVRRRGGEFIIDTVEAVRFVPL 202
Cdd:PRK13944 165 DGGVLVIPVEEGvGQVLYKVVKRGEKVEKRAITYVLFVPL 204
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 13-172 1.07e-23

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 96.07  E-value: 1.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  13 LRAQGIQDeQVLNALAAVPREKFVDEAFE-QKAWDNIALPIGQGQ----TISQPYMVARMTELLELTPQSRVLEIGTGSG 87
Cdd:PRK13943  14 LKKYGISD-HIAKAFLEVPREEFLTKSYPlSYVYEDIVLVSYDDGeeysTSSQPSLMALFMEWVGLDKGMRVLEIGGGTG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  88 YQTAILAHLVQH---VCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQGWQARAPFDAIIVTAAPPEIPTALMTQLDE 164
Cdd:PRK13943  93 YNAAVMSRVVGEkglVVSVEYSRKICEIAKRNVRRLGIENVIFVCGDGYYGVPEFAPYDVIFVTVGVDEVPETWFTQLKE 172


                 ....*...
gi 166987988 165 GGILVLPV 172
Cdd:PRK13943 173 GGRVIVPI 180
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 62-147 3.63e-08

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: 52.08  E-value: 3.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  62 YMVARmtelLELTPQSRVLEIGTGSGYQTAILAHLVQ---HVCSVERIKGLQWQARRRLKNLDLH-NVSTRHGDGWQGWQ 137
Cdd:COG2519   82 YIIAR----LDIFPGARVLEAGTGSGALTLALARAVGpegKVYSYERREDFAEIARKNLERFGLPdNVELKLGDIREGID 157

                         90
                 ....*....|
gi 166987988 138 ARaPFDAIIV 147
Cdd:COG2519  158 EG-DVDAVFL 166
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 65-150 9.96e-08

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 49.22  E-value: 9.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  65 ARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDLhNVSTRHGDGWQGWQARAPFDA 144
Cdd:COG2226   12 EALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDLPFPDGSFDL 90


                 ....*.
gi 166987988 145 IIVTAA 150
Cdd:COG2226   91 VISSFV 96
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 60-170 5.98e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 47.99  E-value: 5.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  60 QPYMVARMTELLELTPQSRVLEIGTGSGYQTAILA-HLVQHVC----SVERIKglqwQARRRLKNLDLHNVSTRHGDgWQ 134
Cdd:COG0500   11 LPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAaRFGGRVIgidlSPEAIA----LARARAAKAGLGNVEFLVAD-LA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 166987988 135 GWQAR--APFDAIIVTAA----PPEIPTALM----TQLDEGGILVL 170
Cdd:COG0500   86 ELDPLpaESFDLVVAFGVlhhlPPEEREALLrelaRALKPGGVLLL 131
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 60-193 2.61e-06

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 45.69  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  60 QPYMVARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHvcsveRIKGL---QWQ---ARRRLKNLDLHN-VSTRHGDg 132
Cdd:COG2230   36 QEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGV-----RVTGVtlsPEQleyARERAAEAGLADrVEVRLAD- 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166987988 133 WQGWQARAPFDAIIVTAappeiptalMTQLdeggilvlpVGEEH--QYLKRVRRR---GGEFIIDT 193
Cdd:COG2230  110 YRDLPADGQFDAIVSIG---------MFEH---------VGPENypAYFAKVARLlkpGGRLLLHT 157
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
75-170 5.05e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 43.66  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  75 PQSRVLEIGTGSGYQTAILAhlvqhvcsvERIKGLQW-----------QARRRLKNLDLHnvstrHGDGWQgWQARAPFD 143
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLA---------ERFPGARVtgvdlspemlaRARARLPNVRFV-----VADLRD-LDPPEPFD 65

                         90       100       110
                 ....*....|....*....|....*....|...
gi 166987988 144 AIIVTAA------PPEIPTALMTQLDEGGILVL 170
Cdd:COG4106   66 LVVSNAAlhwlpdHAALLARLAAALAPGGVLAV 98
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 79-158 6.21e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 43.32  E-value: 6.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   79 VLEIGTGSGYQTAILAHLVQ-HVCSVERIKGLQWQARRRLKNLDLhNVSTRHGDGWQGWQARAPFDAIIVTAA-----PP 152
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDLPFPDGSFDLVVSSGVlhhlpDP 79


                  ....*.
gi 166987988  153 EIPTAL 158
Cdd:pfam13649  80 DLEAAL 85
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 65-170 9.31e-06

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: 43.47  E-value: 9.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  65 ARMTELLE--LTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLdlhNVSTRHGDGWQGWQARAPF 142
Cdd:COG2227   12 RRLAALLArlLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDLPLEDGSF 88

                         90       100       110
                 ....*....|....*....|....*....|....
gi 166987988 143 DAIIVTAA------PPEIPTALMTQLDEGGILVL 170
Cdd:COG2227   89 DLVICSEVlehlpdPAALLRELARLLKPGGLLLL 122
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 63-164 1.36e-05

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 44.76  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  63 MVARMTELLELTPQSRVLEIGTGSGyqtAI---LAHLVQ--HVCSVERIKG-LQWqARRRLKNLDLHN-VSTRHGDGWQG 135
Cdd:COG2890  100 LVELALALLPAGAPPRVLDLGTGSG---AIalaLAKERPdaRVTAVDISPDaLAV-ARRNAERLGLEDrVRFLQGDLFEP 175

                         90       100
                 ....*....|....*....|....*....
gi 166987988 136 WQARAPFDAIIvtAAPPEIPTALMTQLDE 164
Cdd:COG2890  176 LPGDGRFDLIV--SNPPYIPEDEIALLPP 202
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
61-171 2.15e-05

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 43.89  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   61 PYMVARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLqwQARRRLKNLDLHNVSTRHGDGWQgWQ--- 137
Cdd:pfam00398  16 PKVINEIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRL--AKLLQKKLSLDENLTVIHQDFLK-FEfps 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 166987988  138 --ARAPFDAIIVTAAPPEIPTALMTQL-------DEGGILVLP 171
Cdd:pfam00398  93 lvTHIHQEFLVVGNLPYNISTPIVKQLlfesrfgIVDMLLMLQ 135
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 78-172 2.25e-05

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: 42.03  E-value: 2.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  78 RVLEIGTGSGYQTAILA-HLVQHVCSVERIKGLQWQARRRLKNLDLHNVSTRHGDGWQG-WQARAPFDAIIVTAAPPEIP 155
Cdd:cd02440    1 RVLDLGCGTGALALALAsGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELpPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....
gi 166987988 156 TALMTQLDE-------GGILVLPV 172
Cdd:cd02440   81 EDLARFLEEarrllkpGGVLVLTL 104
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 68-163 4.18e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 4.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  68 TELL--------ELTPQSRVLEIGTGSGyqtAI---LAHLVQH--VCSVERIKG-LQWqARRRLKNLDLHNVSTRHGDGW 133
Cdd:PRK09328  93 TEELvewalealLLKEPLRVLDLGTGSG---AIalaLAKERPDaeVTAVDISPEaLAV-ARRNAKHGLGARVEFLQGDWF 168

                         90       100       110
                 ....*....|....*....|....*....|
gi 166987988 134 QGwQARAPFDAIIvtAAPPEIPTALMTQLD 163
Cdd:PRK09328 169 EP-LPGGRFDLIV--SNPPYIPEADIHLLQ 195
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
64-131 1.84e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 38.34  E-value: 1.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 166987988  64 VARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLQWQARRRLKNLDlhNVSTRHGD 131
Cdd:PRK14896  18 VDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRDDEIAAG--NVEIIEGD 83
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 53-170 3.03e-03

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: 37.09  E-value: 3.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988  53 GQGQTIsqpYMVARMTElleltPQsRVLEIGTGSGYQTAILAHLVQ---HVCSVERIKGLQWQARRRLKNLDL-HNVSTR 128
Cdd:COG4122    3 EQGRLL---YLLARLLG-----AK-RILEIGTGTGYSTLWLARALPddgRLTTIEIDPERAAIARENFARAGLaDRIRLI 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 166987988 129 HGDgwqgwqAR--------APFDAIIVTAAPPEIPTAL---MTQLDEGGILVL 170
Cdd:COG4122   74 LGD------ALevlprladGPFDLVFIDADKSNYPDYLelaLPLLRPGGLIVA 120
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 78-201 3.21e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 36.63  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988   78 RVLEIGTGSGYQTAILAHLVQ---HVCSVERIKGLQWQARRRLKNLDLHNVSTRHGD--GWQGWQARAPFDaIIVTAApp 152
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDieELPELLEDDKFD-VVISNC-- 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 166987988  153 eiptALMTQLDEGGILvlpvgeehQYLKRVRRRGGEFIIDTVEAVRFVP 201
Cdd:pfam13847  83 ----VLNHIPDPDKVL--------QEILRVLKPGGRLIISDPDSLAELP 119
rADc smart00650
Ribosomal RNA adenine dimethylases;
63-146 8.13e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 35.56  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166987988    63 MVARMTELLELTPQSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLqwqaRRRLKNL--DLHNVSTRHGDGWQGWQARA 140
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRL----APRLREKfaAADNLTVIHGDALKFDLPKL 76


                   ....*.
gi 166987988   141 PFDAII 146
Cdd:smart00650  77 QPYKVV 82
 
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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