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Conserved domains on  [gi|223718169|ref|NP_001138782|]
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transmembrane O-methyltransferase isoform LRTOMT2b [Homo sapiens]

Protein Classification

O-methyltransferase( domain architecture ID 11467877)

O-methyltransferase of the class I-like SAM-binding methyltransferase superfamily, such as catechol O-methyltransferases that can use various catechol-like compounds

CATH:  2.20.25.110
EC:  2.1.1.-|2.1.-.-
Gene Ontology:  GO:0008757|GO:0032259|GO:1904047|GO:0008168|GO:0008171
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 77-209 4.81e-29

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: 107.58  E-value: 4.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169  77 PVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDEHmVELIVGSSEDV 156
Cdd:COG4122    2 PEQGRLLYLLARLLGAKRILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADR-IRLILGDALEV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223718169 157 IPCLRT-QYqlsraDLVLLAHRPRCYLRDLQLLEahALLPAGATVLADHVLFPG 209
Cdd:COG4122   81 LPRLADgPF-----DLVFIDADKSNYPDYLELAL--PLLRPGGLIVADNVLWHG 127
 
Name Accession Description Interval E-value
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 77-209 4.81e-29

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: 107.58  E-value: 4.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169  77 PVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDEHmVELIVGSSEDV 156
Cdd:COG4122    2 PEQGRLLYLLARLLGAKRILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADR-IRLILGDALEV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223718169 157 IPCLRT-QYqlsraDLVLLAHRPRCYLRDLQLLEahALLPAGATVLADHVLFPG 209
Cdd:COG4122   81 LPRLADgPF-----DLVFIDADKSNYPDYLELAL--PLLRPGGLIVADNVLWHG 127
Methyltransf_3 pfam01596
O-methyltransferase; Members of this family are O-methyltransferases. The family includes ...
 71-212 1.95e-14

O-methyltransferase; Members of this family are O-methyltransferases. The family includes catechol o-methyltransferase, caffeoyl-CoA O-methyltransferase and a family of bacterial O-methyltransferases that may be involved in antibiotic production.


Pssm-ID: 396257 [Multi-domain]  Cd Length: 203  Bit Score: 69.83  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169   71 YLSHM--GPVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDeHMVEL 148
Cdd:pfam01596  21 PLAPMqvSPDEGQFLGMLVKLTGAKNVLEIGVFTGYSALAMALALPEDGKITAIDIDPEAYEIAKKFIQKAGVA-HKISF 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223718169  149 IVGSSEDVIPCLRTQYQLSRADLVLL----AHRPRCYLRDLQLLEAHALLPAGATVLADHVLFPGAPR 212
Cdd:pfam01596 100 ILGPALKVLEQLTQDKPLPEFDFIFIdadkSNYPNYYERLLELLKVGGLMAIDNTLWHGKVTEPDDQE 167
PLN02476 PLN02476
O-methyltransferase
 74-209 3.07e-11

O-methyltransferase


Pssm-ID: 178094  Cd Length: 278  Bit Score: 62.00  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169  74 HMGPVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFdEHMVELIVGSS 153
Cdd:PLN02476 101 QVSPDQAQLLAMLVQILGAERCIEVGVYTGYSSLAVALVLPESGCLVACERDSNSLEVAKRYYELAGV-SHKVNVKHGLA 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223718169 154 EDVIPCLRTQYQLSRADLVLLAHRPRCYLRDLQLLeaHALLPAGATVLADHVLFPG 209
Cdd:PLN02476 180 AESLKSMIQNGEGSSYDFAFVDADKRMYQDYFELL--LQLVRVGGVIVMDNVLWHG 233
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 95-207 2.19e-06

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: 45.11  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169  95 VLELGTYCGYSTLLIARAlpPGGRLLTVERDPRTAAVAEKLIRLAGFDEhmVELIVGSSEDVIPCLRTQYqlsraDLVLL 174
Cdd:cd02440    2 VLDLGCGTGALALALASG--PGARVTGVDISPVALELARKAAAALLADN--VEVLKGDAEELPPEADESF-----DVIIS 72

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 223718169 175 AHrPRCYLRDLQ---LLEAHALLPAGATVLADHVLF 207
Cdd:cd02440   73 DP-PLHHLVEDLarfLEEARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 77-209 4.81e-29

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: 107.58  E-value: 4.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169  77 PVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDEHmVELIVGSSEDV 156
Cdd:COG4122    2 PEQGRLLYLLARLLGAKRILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADR-IRLILGDALEV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 223718169 157 IPCLRT-QYqlsraDLVLLAHRPRCYLRDLQLLEahALLPAGATVLADHVLFPG 209
Cdd:COG4122   81 LPRLADgPF-----DLVFIDADKSNYPDYLELAL--PLLRPGGLIVADNVLWHG 127
Methyltransf_3 pfam01596
O-methyltransferase; Members of this family are O-methyltransferases. The family includes ...
 71-212 1.95e-14

O-methyltransferase; Members of this family are O-methyltransferases. The family includes catechol o-methyltransferase, caffeoyl-CoA O-methyltransferase and a family of bacterial O-methyltransferases that may be involved in antibiotic production.


Pssm-ID: 396257 [Multi-domain]  Cd Length: 203  Bit Score: 69.83  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169   71 YLSHM--GPVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDeHMVEL 148
Cdd:pfam01596  21 PLAPMqvSPDEGQFLGMLVKLTGAKNVLEIGVFTGYSALAMALALPEDGKITAIDIDPEAYEIAKKFIQKAGVA-HKISF 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223718169  149 IVGSSEDVIPCLRTQYQLSRADLVLL----AHRPRCYLRDLQLLEAHALLPAGATVLADHVLFPGAPR 212
Cdd:pfam01596 100 ILGPALKVLEQLTQDKPLPEFDFIFIdadkSNYPNYYERLLELLKVGGLMAIDNTLWHGKVTEPDDQE 167
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 96-203 1.44e-12

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 62.33  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169   96 LELGTYCGYSTLLIARALPPGG--RLLTVERDPRTAAVAEkLIRLAGFDEHmVELIVGSSEDVIPclrtQYQLSRADLVL 173
Cdd:pfam13578   1 VEIGTYSGVSTLWLAAALRDNGlgRLTAVDPDPGAEEAGA-LLRKAGLDDR-VRLIVGDSREALP----SLADGPIDLLF 74

                          90       100       110
                  ....*....|....*....|....*....|..
gi 223718169  174 L--AHRPRCYLRDLQLLEAHalLPAGATVLAD 203
Cdd:pfam13578  75 IdgDHTYEAVLNDLELWLPR--LAPGGVILFH 104
PLN02476 PLN02476
O-methyltransferase
 74-209 3.07e-11

O-methyltransferase


Pssm-ID: 178094  Cd Length: 278  Bit Score: 62.00  E-value: 3.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169  74 HMGPVKGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFdEHMVELIVGSS 153
Cdd:PLN02476 101 QVSPDQAQLLAMLVQILGAERCIEVGVYTGYSSLAVALVLPESGCLVACERDSNSLEVAKRYYELAGV-SHKVNVKHGLA 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 223718169 154 EDVIPCLRTQYQLSRADLVLLAHRPRCYLRDLQLLeaHALLPAGATVLADHVLFPG 209
Cdd:PLN02476 180 AESLKSMIQNGEGSSYDFAFVDADKRMYQDYFELL--LQLVRVGGVIVMDNVLWHG 233
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 80-158 1.23e-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: 54.01  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169  80 GQILMRLveEKAP-ACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDEHmVELIVGSSEDVIP 158
Cdd:COG2519   81 GYIIARL--DIFPgARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDN-VELKLGDIREGID 157
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 95-207 2.19e-06

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: 45.11  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169  95 VLELGTYCGYSTLLIARAlpPGGRLLTVERDPRTAAVAEKLIRLAGFDEhmVELIVGSSEDVIPCLRTQYqlsraDLVLL 174
Cdd:cd02440    2 VLDLGCGTGALALALASG--PGARVTGVDISPVALELARKAAAALLADN--VEVLKGDAEELPPEADESF-----DVIIS 72

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 223718169 175 AHrPRCYLRDLQ---LLEAHALLPAGATVLADHVLF 207
Cdd:cd02440   73 DP-PLHHLVEDLarfLEEARRLLKPGGVLVLTLVLA 107
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
83-173 2.30e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 47.34  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169  83 LMRLVEEKApaCVLELGTYCGYSTLLIARALPpgGRLLTVERDPRTAAVAEKLIRLAGFDEHMvelivgsseDVIPCLRT 162
Cdd:COG4076   29 IERVVKPGD--VVLDIGTGSGLLSMLAARAGA--KKVYAVEVNPDIAAVARRIIAANGLSDRI---------TVINADAT 95

                         90
                 ....*....|..
gi 223718169 163 QYQLS-RADLVL 173
Cdd:COG4076   96 DLDLPeKADVII 107
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 95-151 8.86e-06

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 45.08  E-value: 8.86e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223718169  95 VLELGTYCGYSTLLIARAlppGGRLLTVERDPRTAAVAEKLIRLAGFDEhmVELIVG 151
Cdd:COG2518   70 VLEIGTGSGYQAAVLARL---AGRVYSVERDPELAERARERLAALGYDN--VTVRVG 121
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 95-151 2.42e-05

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 43.85  E-value: 2.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 223718169  95 VLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDEhmVELIVG 151
Cdd:PRK13942  80 VLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKKLGYDN--VEVIVG 134
PLN02781 PLN02781
Probable caffeoyl-CoA O-methyltransferase
 72-143 2.03e-04

Probable caffeoyl-CoA O-methyltransferase


Pssm-ID: 215417  Cd Length: 234  Bit Score: 41.34  E-value: 2.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 223718169  72 LSHMG-PV-KGQILMRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDE 143
Cdd:PLN02781  47 LSEMEvPVdEGLFLSMLVKIMNAKNTLEIGVFTGYSLLTTALALPEDGRITAIDIDKEAYEVGLEFIKKAGVDH 120
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
84-151 1.23e-03

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 38.89  E-value: 1.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 223718169   84 MRLVEEKAPACVLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDEhmVELIVG 151
Cdd:pfam01135  66 LELLELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLEN--VIVVVG 131
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 95-205 1.58e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.78  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169   95 VLELGTYCGYSTLLIARALPPGGRLLTVERDPRTAAVAEKLIRLAGFDEhmVELIVGSSEDvipcLRTQYQLSRADLVlL 174
Cdd:pfam13847   7 VLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDN--VEFEQGDIEE----LPELLEDDKFDVV-I 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 223718169  175 AHRPRCYLRDLQ--LLEAHALL-PAGATVLADHV 205
Cdd:pfam13847  80 SNCVLNHIPDPDkvLQEILRVLkPGGRLIISDPD 113
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 83-221 2.42e-03

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: 37.28  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223718169  83 LMRLVEEKAPACVLELGTYCGYSTLLIARAlppGGRLLTVERDPRTAAVAEKLIRLAGFDehmVELIVGSSEDvIPclrt 162
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERAAEAGLN---VEFVVGDAED-LP---- 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 223718169 163 qYQLSRADLVLLAHrPRCYLRDLQ--LLEAHALLPAGATVLADHVLFPGAPRFLQYAKSCG 221
Cdd:COG2226   83 -FPDGSFDLVISSF-VLHHLPDPEraLAEIARVLKPGGRLVVVDFSPPDLAELEELLAEAG 141
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 109-141 8.20e-03

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: 35.74  E-value: 8.20e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 223718169 109 IARALPPGGRLLTVERDPRTAAVAEKLIRLAGF 141
Cdd:COG2226  110 IARVLKPGGRLVVVDFSPPDLAELEELLAEAGF 142
 
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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