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Conserved domains on  [gi|109389364|ref|NP_065733|]
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arsenite methyltransferase [Homo sapiens]

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;
6-254 5.92e-49

arsenite methyltransferase;


The actual alignment was detected with superfamily member PRK11873:

Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 166.28  E-value: 5.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   6 DAEIQKDVQTYYGQVLKRSAD--LQTNGCVTTARPVPKHIR------EALQNVHEEVALRYyGCGL--VIPEHLENCWIL 75
Cdd:PRK11873   4 ADDIKEVVREKYGEIAERGGSgcSGCSCCGASANDAADPSTslgyseEELAAVPEGANLGL-GCGNptALAELKPGETVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  76 DLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKyldyHMEKYGFqaSNVTFIHGYIEKLGeagIKNESHDIVVSN 155
Cdd:PRK11873  83 DLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARA----NARKAGY--TNVEFRLGEIEALP---VADNSVDVIISN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364 156 CVINLVPDKQQVLQEAYRVLKHGGELYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFcpprlvtANl 235
Cdd:PRK11873 154 CVINLSPDKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRNDAELYAGCVAGALQEEEYLAMLAEAGF-------VD- 225

                        250
                 ....*....|....*....
gi 109389364 236 ITIQNKELERVIGDCRFVS 254
Cdd:PRK11873 226 ITIQPKREYRIPDAREFLE 244
 
Name Accession Description Interval E-value
arsM PRK11873
arsenite methyltransferase;
6-254 5.92e-49

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 166.28  E-value: 5.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   6 DAEIQKDVQTYYGQVLKRSAD--LQTNGCVTTARPVPKHIR------EALQNVHEEVALRYyGCGL--VIPEHLENCWIL 75
Cdd:PRK11873   4 ADDIKEVVREKYGEIAERGGSgcSGCSCCGASANDAADPSTslgyseEELAAVPEGANLGL-GCGNptALAELKPGETVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  76 DLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKyldyHMEKYGFqaSNVTFIHGYIEKLGeagIKNESHDIVVSN 155
Cdd:PRK11873  83 DLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARA----NARKAGY--TNVEFRLGEIEALP---VADNSVDVIISN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364 156 CVINLVPDKQQVLQEAYRVLKHGGELYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFcpprlvtANl 235
Cdd:PRK11873 154 CVINLSPDKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRNDAELYAGCVAGALQEEEYLAMLAEAGF-------VD- 225

                        250
                 ....*....|....*....
gi 109389364 236 ITIQNKELERVIGDCRFVS 254
Cdd:PRK11873 226 ITIQPKREYRIPDAREFLE 244
methyl_ArsM NF040538
arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) ...
 44-335 4.00e-46

arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) biosynthesis can act as a typical arsenite methyltransferase, acting on inorganic arsenite, methylarsenicals, and aromatic arsenicals. In arsinothricin biosynthesis, the radical SAM enzyme ArsL acts first, synthesizing hydroxyarsinothricin (AST-OH) by adding 3-amino-3-carboxypropyl derived from S-adenosylmethionine (SAM) to As(III). This ArsM then methylates AST-OH, producing the naturally occurring arsenical antibiotic arsinothricin. Other forms of ArsM would not be expected to have this specific activity.


Pssm-ID: 439748  Cd Length: 352  Bit Score: 161.17  E-value: 4.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  44 REALQNVHEEVALRYYGCGLVIPEHLENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLDYHMEKYG 123
Cdd:NF040538  35 AQLLKNIPKRIIDADFGCGNPTKYVREGDVVLDLGSGSGKICYILAQIVGPQGAVIGVDINPSMLQLARSEQKAFQEATG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364 124 FqaSNVTFIHGYI-----------EKLGEAGIKN-----------------------ESHDIVVSNCVINLV--PDKQQV 167
Cdd:NF040538 115 S--ANLRFFRASIsdlktdlelaeERLSGESCENlaswknfeqflsdsrqsnpliadNSIDLVVSNCVINLVgtTEKQNV 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364 168 LQEAYRVLKHGGELYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFcpprlvTANLITIQNKELERVI 247
Cdd:NF040538 193 FAEIFRVLRPGGRIAISDNVSNIAVPEELKNDTELWSACYSGVLQEQEFYRQLQDVGF------TGLTIEARNDAPTKRI 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364 248 GDCRFVSATFRLFK--HSKTGPTKRCQVIYNGGITghekELMFDANFTFKEGEIVEVDEETAAILKNSRFAQDFLIRPIG 325
Cdd:NF040538 267 GSVEFYSVTVTATKplEAVVGSGDMTTVIYRGPWT----EVTDDSGNQYKRGKITLVPTELAAQDRYLSFQEHLFVLDGQ 342

                        330
                 ....*....|
gi 109389364 326 EKLPTSGGCS 335
Cdd:NF040538 343 PGSNGKSCCG 352
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 70-216 1.47e-32

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 119.44  E-value: 1.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   70 ENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKyldyHMEKYGFqaSNVTFIHGYIEKLGEAgIKNESH 149
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARE----NAQKLGF--DNVEFEQGDIEELPEL-LEDDKF 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109389364  150 DIVVSNCVINLVPDKQQVLQEAYRVLKHGGELYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKEL 216
Cdd:pfam13847  76 DVVISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAILKKKL 142
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 74-185 1.83e-23

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: 94.68  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGekgHVTGIDMTKGQVEVAEkyldyhmEKYGFQASNVTFIHGYIEKLGeagIKNESHDIVV 153
Cdd:COG2226   26 VLDLGCGTGRLALALAERGA---RVTGVDISPEMLELAR-------ERAAEAGLNVEFVVGDAEDLP---FPDGSFDLVI 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 109389364 154 SNCVINLVPDKQQVLQEAYRVLKHGGELYFSD 185
Cdd:COG2226   93 SSFVLHHLPDPERALAEIARVLKPGGRLVVVD 124
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-187 7.36e-16

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: 72.85  E-value: 7.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQlvGEKGHVTGIDMTKGQVEVAEKYLDYHmekygfQASNVTFIHGYIEKLGEagIKNESHDIVV 153
Cdd:cd02440    2 VLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAAL------LADNVEVLKGDAEELPP--EADESFDVII 71

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 109389364 154 SNCVIN-LVPDKQQVLQEAYRVLKHGGELYFSDVY 187
Cdd:cd02440   72 SDPPLHhLVEDLARFLEEARRLLKPGGVLVLTLVL 106
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 74-185 1.41e-09

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 58.07  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   74 ILDLGSGSGrdcYVLSQLV--GEKGHVTGIDMTKGQVEVAEKYLdyhmekygfqASNVTFIHGYIEKLGEAGiknESHDI 151
Cdd:TIGR02072  38 VLDIGCGTG---YLTRALLkrFPQAEFIALDISAGMLAQAKTKL----------SENVQFICGDAEKLPLED---SSFDL 101

                          90       100       110
                  ....*....|....*....|....*....|....
gi 109389364  152 VVSNCVINLVPDKQQVLQEAYRVLKHGGELYFSD 185
Cdd:TIGR02072 102 IVSNLALQWCDDLSQALSELARVLKPGGLLAFST 135
 
Name Accession Description Interval E-value
arsM PRK11873
arsenite methyltransferase;
6-254 5.92e-49

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 166.28  E-value: 5.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   6 DAEIQKDVQTYYGQVLKRSAD--LQTNGCVTTARPVPKHIR------EALQNVHEEVALRYyGCGL--VIPEHLENCWIL 75
Cdd:PRK11873   4 ADDIKEVVREKYGEIAERGGSgcSGCSCCGASANDAADPSTslgyseEELAAVPEGANLGL-GCGNptALAELKPGETVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  76 DLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKyldyHMEKYGFqaSNVTFIHGYIEKLGeagIKNESHDIVVSN 155
Cdd:PRK11873  83 DLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARA----NARKAGY--TNVEFRLGEIEALP---VADNSVDVIISN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364 156 CVINLVPDKQQVLQEAYRVLKHGGELYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFcpprlvtANl 235
Cdd:PRK11873 154 CVINLSPDKERVFKEAFRVLKPGGRFAISDVVLRGELPEEIRNDAELYAGCVAGALQEEEYLAMLAEAGF-------VD- 225

                        250
                 ....*....|....*....
gi 109389364 236 ITIQNKELERVIGDCRFVS 254
Cdd:PRK11873 226 ITIQPKREYRIPDAREFLE 244
methyl_ArsM NF040538
arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) ...
 44-335 4.00e-46

arsinothricin biosynthesis methyltransferase ArsM; The ArsM found in the arsinothricin (AST) biosynthesis can act as a typical arsenite methyltransferase, acting on inorganic arsenite, methylarsenicals, and aromatic arsenicals. In arsinothricin biosynthesis, the radical SAM enzyme ArsL acts first, synthesizing hydroxyarsinothricin (AST-OH) by adding 3-amino-3-carboxypropyl derived from S-adenosylmethionine (SAM) to As(III). This ArsM then methylates AST-OH, producing the naturally occurring arsenical antibiotic arsinothricin. Other forms of ArsM would not be expected to have this specific activity.


Pssm-ID: 439748  Cd Length: 352  Bit Score: 161.17  E-value: 4.00e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  44 REALQNVHEEVALRYYGCGLVIPEHLENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLDYHMEKYG 123
Cdd:NF040538  35 AQLLKNIPKRIIDADFGCGNPTKYVREGDVVLDLGSGSGKICYILAQIVGPQGAVIGVDINPSMLQLARSEQKAFQEATG 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364 124 FqaSNVTFIHGYI-----------EKLGEAGIKN-----------------------ESHDIVVSNCVINLV--PDKQQV 167
Cdd:NF040538 115 S--ANLRFFRASIsdlktdlelaeERLSGESCENlaswknfeqflsdsrqsnpliadNSIDLVVSNCVINLVgtTEKQNV 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364 168 LQEAYRVLKHGGELYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKELAVLAQKIGFcpprlvTANLITIQNKELERVI 247
Cdd:NF040538 193 FAEIFRVLRPGGRIAISDNVSNIAVPEELKNDTELWSACYSGVLQEQEFYRQLQDVGF------TGLTIEARNDAPTKRI 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364 248 GDCRFVSATFRLFK--HSKTGPTKRCQVIYNGGITghekELMFDANFTFKEGEIVEVDEETAAILKNSRFAQDFLIRPIG 325
Cdd:NF040538 267 GSVEFYSVTVTATKplEAVVGSGDMTTVIYRGPWT----EVTDDSGNQYKRGKITLVPTELAAQDRYLSFQEHLFVLDGQ 342

                        330
                 ....*....|
gi 109389364 326 EKLPTSGGCS 335
Cdd:NF040538 343 PGSNGKSCCG 352
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 70-216 1.47e-32

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 119.44  E-value: 1.47e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   70 ENCWILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKyldyHMEKYGFqaSNVTFIHGYIEKLGEAgIKNESH 149
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARE----NAQKLGF--DNVEFEQGDIEELPEL-LEDDKF 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 109389364  150 DIVVSNCVINLVPDKQQVLQEAYRVLKHGGELYFSDVYTSLELPEEIRTHKVLWGECLGGALYWKEL 216
Cdd:pfam13847  76 DVVISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAGCVGGAILKKKL 142
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 74-185 1.83e-23

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: 94.68  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGekgHVTGIDMTKGQVEVAEkyldyhmEKYGFQASNVTFIHGYIEKLGeagIKNESHDIVV 153
Cdd:COG2226   26 VLDLGCGTGRLALALAERGA---RVTGVDISPEMLELAR-------ERAAEAGLNVEFVVGDAEDLP---FPDGSFDLVI 92

                         90       100       110
                 ....*....|....*....|....*....|..
gi 109389364 154 SNCVINLVPDKQQVLQEAYRVLKHGGELYFSD 185
Cdd:COG2226   93 SSFVLHHLPDPERALAEIARVLKPGGRLVVVD 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-179 7.95e-22

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 88.77  E-value: 7.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   74 ILDLGSGSGRDCYVLSQLVGekGHVTGIDMTKGQVEVAEkyldyhmEKYGFQASNVTFIHGYIEKLGEAgikNESHDIVV 153
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERAR-------ERAAEAGLNVEFVQGDAEDLPFP---DGSFDLVV 68

                          90       100
                  ....*....|....*....|....*...
gi 109389364  154 SNCVINLV--PDKQQVLQEAYRVLKHGG 179
Cdd:pfam13649  69 SSGVLHHLpdPDLEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 74-185 5.91e-19

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: 81.99  E-value: 5.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLvgekGH-VTGIDMTKGQVEVAEKYLDyhmekygfqASNVTFIHGYIEKLGEAGiknESHDIV 152
Cdd:COG2227   28 VLDVGCGTGRLALALARR----GAdVTGVDISPEALEIARERAA---------ELNVDFVQGDLEDLPLED---GSFDLV 91

                         90       100       110
                 ....*....|....*....|....*....|...
gi 109389364 153 VSNCVINLVPDKQQVLQEAYRVLKHGGELYFSD 185
Cdd:COG2227   92 ICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-183 1.66e-17

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 76.93  E-value: 1.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   75 LDLGSGSGRDCYVLSQLVGekgHVTGIDMTKGQVEVAEKYLdyhmekygfQASNVTFIHGYIEKLGeagIKNESHDIVVS 154
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA---RVTGVDISPEMLELAREKA---------PREGLTFVVGDAEDLP---FPDNSFDLVLS 65

                          90       100
                  ....*....|....*....|....*....
gi 109389364  155 NCVINLVPDKQQVLQEAYRVLKHGGELYF 183
Cdd:pfam08241  66 SEVLHHVEDPERALREIARVLKPGGILII 94
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 74-181 2.07e-16

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 77.89  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVA-EKYLDYHmekygfQASNVTFIHGYIEKLGeagIKNESHDIV 152
Cdd:PRK00216  55 VLDLACGTGDLAIALAKAVGKTGEVVGLDFSEGMLAVGrEKLRDLG------LSGNVEFVQGDAEALP---FPDNSFDAV 125

                         90       100       110
                 ....*....|....*....|....*....|
gi 109389364 153 -VSNCVINlVPDKQQVLQEAYRVLKHGGEL 181
Cdd:PRK00216 126 tIAFGLRN-VPDIDKALREMYRVLKPGGRL 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-187 7.36e-16

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: 72.85  E-value: 7.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQlvGEKGHVTGIDMTKGQVEVAEKYLDYHmekygfQASNVTFIHGYIEKLGEagIKNESHDIVV 153
Cdd:cd02440    2 VLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAAL------LADNVEVLKGDAEELPP--EADESFDVII 71

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 109389364 154 SNCVIN-LVPDKQQVLQEAYRVLKHGGELYFSDVY 187
Cdd:cd02440   72 SDPPLHhLVEDLARFLEEARRLLKPGGVLVLTLVL 106
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 74-221 5.91e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 66.86  E-value: 5.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGekGHVTGIDMTKGQVEVAEKYLDyhmekyGFQASNVTFIHGYIEKLGEagIKNESHDIVV 153
Cdd:COG0500   30 VLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAA------KAGLGNVEFLVADLAELDP--LPAESFDLVV 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 109389364 154 SNCVINLVP--DKQQVLQEAYRVLKHGGELYFSDVYTSLELPEEIRTHKV---LWGECLGGALYWKELAVLAQ 221
Cdd:COG0500  100 AFGVLHHLPpeEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLAtasLLELLLLLRLLALELYLRAL 172
PRK08317 PRK08317
hypothetical protein; Provisional
 74-179 7.35e-13

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 67.65  E-value: 7.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEkyldyhmEKYGFQASNVTFIHGYIEKLGEAGiknESHDIVV 153
Cdd:PRK08317  23 VLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAK-------ERAAGLGPNVEFVRGDADGLPFPD---GSFDAVR 92

                         90       100
                 ....*....|....*....|....*.
gi 109389364 154 SNCVINLVPDKQQVLQEAYRVLKHGG 179
Cdd:PRK08317  93 SDRVLQHLEDPARALAEIARVLRPGG 118
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
74-182 2.50e-11

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 62.84  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   74 ILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLdyhmEKYGFqaSNVTFIHGYIEKLGEagiKNESHDIVV 153
Cdd:pfam01209  46 FLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLKEGEKKA----KEEGK--YNIEFLQGNAEELPF---EDDSFDIVT 116

                          90       100
                  ....*....|....*....|....*....
gi 109389364  154 SNCVINLVPDKQQVLQEAYRVLKHGGELY 182
Cdd:pfam01209 117 ISFGLRNFPDYLKVLKEAFRVLKPGGRVV 145
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
74-185 4.36e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 59.07  E-value: 4.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGEkGHVTGIDMTKGQVEVAEKYLdyhmekygfqaSNVTFIHGYIEKLGeagiKNESHDIVV 153
Cdd:COG4106    5 VLDLGCGTGRLTALLAERFPG-ARVTGVDLSPEMLARARARL-----------PNVRFVVADLRDLD----PPEPFDLVV 68

                         90       100       110
                 ....*....|....*....|....*....|..
gi 109389364 154 SNCVINLVPDKQQVLQEAYRVLKHGGELYFSD 185
Cdd:COG4106   69 SNAALHWLPDHAALLARLAAALAPGGVLAVQV 100
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
74-184 7.65e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 60.40  E-value: 7.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGekgHVTGIDMTKGQVEVAEKYLDYhmekygfqasnVTFIHGYIEKLGEAGiknESHDIVV 153
Cdd:COG4976   50 VLDLGCGTGLLGEALRPRGY---RLTGVDLSEEMLAKAREKGVY-----------DRLLVADLADLAEPD---GRFDLIV 112

                         90       100       110
                 ....*....|....*....|....*....|.
gi 109389364 154 SNCVINLVPDKQQVLQEAYRVLKHGGELYFS 184
Cdd:COG4976  113 AADVLTYLGDLAAVFAGVARALKPGGLFIFS 143
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-181 1.65e-10

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 57.38  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   75 LDLGSGSGRDC-YVLSQLVGekGHVTGIDMTKGQVEVAEKYLDyhmEKYGFQASNVTFIHGYIEKLGEAGIkneshDIVV 153
Cdd:pfam08242   1 LEIGCGTGTLLrALLEALPG--LEYTGLDISPAALEAARERLA---ALGLLNAVRVELFQLDLGELDPGSF-----DVVV 70

                          90       100
                  ....*....|....*....|....*...
gi 109389364  154 SNCVINLVPDKQQVLQEAYRVLKHGGEL 181
Cdd:pfam08242  71 ASNVLHHLADPRAVLRNIRRLLKPGGVL 98
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 74-185 1.41e-09

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 58.07  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   74 ILDLGSGSGrdcYVLSQLV--GEKGHVTGIDMTKGQVEVAEKYLdyhmekygfqASNVTFIHGYIEKLGEAGiknESHDI 151
Cdd:TIGR02072  38 VLDIGCGTG---YLTRALLkrFPQAEFIALDISAGMLAQAKTKL----------SENVQFICGDAEKLPLED---SSFDL 101

                          90       100       110
                  ....*....|....*....|....*....|....
gi 109389364  152 VVSNCVINLVPDKQQVLQEAYRVLKHGGELYFSD 185
Cdd:TIGR02072 102 IVSNLALQWCDDLSQALSELARVLKPGGLLAFST 135
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 74-185 1.04e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 51.08  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGekGHVTGIDMTKGQVEVAEKyldyHMEKYGFqASNVTFIHGYIEKLGEagikNESHDIVV 153
Cdd:COG2230   55 VLDIGCGWGGLALYLARRYG--VRVTGVTLSPEQLEYARE----RAAEAGL-ADRVEVRLADYRDLPA----DGQFDAIV 123

                         90       100       110
                 ....*....|....*....|....*....|....
gi 109389364 154 SNCVINLVPDKQ--QVLQEAYRVLKHGGELYFSD 185
Cdd:COG2230  124 SIGMFEHVGPENypAYFAKVARLLKPGGRLLLHT 157
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 74-179 1.34e-06

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: 49.00  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLdyhmEKYGFQAsNVTFIHGYIEKlgeaGIKNESHDIVV 153
Cdd:COG2519   95 VLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNL----ERFGLPD-NVELKLGDIRE----GIDEGDVDAVF 165

                         90       100
                 ....*....|....*....|....*..
gi 109389364 154 sncvinL-VPDKQQVLQEAYRVLKHGG 179
Cdd:COG2519  166 ------LdMPDPWEALEAVAKALKPGG 186
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
74-134 2.38e-06

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 47.75  E-value: 2.38e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109389364   74 ILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLdyhmEKYGfqASNVTFIHG 134
Cdd:pfam01135  77 VLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNL----EKLG--LENVIVVVG 131
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 74-226 8.54e-05

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 43.73  E-value: 8.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEkylDYHMEKYGFQASNVTFIHGYIEKLgeaGIKNESHDIVV 153
Cdd:PLN02233  77 VLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAA---SRQELKAKSCYKNIEWIEGDATDL---PFDDCYFDAIT 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364 154 SNCVINLVPDKQQVLQEAYRVLKHGGELYFSD-----------------------VYTSLELPEEIRTHKVLWGECLGGa 210
Cdd:PLN02233 151 MGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDfnkstqpfttsmqewmidnvvvpVATGYGLAKEYEYLKSSINEYLTG- 229

                        170
                 ....*....|....*.
gi 109389364 211 lywKELAVLAQKIGFC 226
Cdd:PLN02233 230 ---EELEKLALEAGFS 242
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
 74-183 9.75e-05

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 43.23  E-value: 9.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   74 ILDLGSGSGrdCYVLSqLVGE--KGHVTGIDMTKGQVEVAEKYLDYHmekygfQASNVTFIHGyieKLGEAgIKNESHDI 151
Cdd:TIGR03534  90 VLDLGTGSG--AIALA-LAKErpDARVTAVDISPEALAVARKNARRL------GLENVEFLQG---DWFEP-LPSGKFDL 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 109389364  152 VVSN------CVINLVPDK--------------------QQVLQEAYRVLKHGGELYF 183
Cdd:TIGR03534 157 IVSNppyipeADIHLLDPEvrdfeprlalfggedgldfyRRIIAQAPRLLKPGGWLLL 214
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 74-183 2.93e-04

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: 41.33  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364  74 ILDLGSGSGrdcyVLS---QLVGEKGHVTGIDMTKGQVEVAEKYLDYHmekygfQASNVTFIHGYieklGEAGIKNESHD 150
Cdd:COG2813   53 VLDLGCGYG----VIGlalAKRNPEARVTLVDVNARAVELARANAAAN------GLENVEVLWSD----GLSGVPDGSFD 118

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 109389364 151 IVVSNCVI--NLVPDK---QQVLQEAYRVLKHGGELYF 183
Cdd:COG2813  119 LILSNPPFhaGRAVDKevaHALIADAARHLRPGGELWL 156
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-225 2.86e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 38.18  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109389364   74 ILDLGSGSGRDCyvlsQLVGEKG-HVTGIDMTKGQVEVAEKYLDYHmekyGFQASNVTFIHGYIeklgeagikneshDIV 152
Cdd:pfam13489  26 VLDFGCGTGIFL----RLLRAQGfSVTGVDPSPIAIERALLNVRFD----QFDEQEAAVPAGKF-------------DVI 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 109389364  153 VSNCVINLVPDKQQVLQEAYRVLKHGGELYFSDVYTSLELPEEIRtHKVLWGECLGGALYW--KELAVLAQKIGF 225
Cdd:pfam13489  85 VAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLL-EWPYLRPRNGHISLFsaRSLKRLLEEAGF 158
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 74-134 3.48e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 38.46  E-value: 3.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKYLdyhmEKYGFQasNVTFIHG 134
Cdd:PRK13942  80 VLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTL----KKLGYD--NVEVIVG 134
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 74-134 4.47e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 38.67  E-value: 4.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 109389364  74 ILDLGSGSGRDCYVLSQLVGEKGHVTGIDMTKGQVEVAEKyldyHMEKYGFQasNVTFIHG 134
Cdd:PRK13943  84 VLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKR----NVRRLGIE--NVIFVCG 138
 
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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