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Conserved domains on  [gi|487749098|ref|WP_001831089|]
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MULTISPECIES: demethylmenaquinone methyltransferase [Staphylococcus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 106779)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 5-233 5.68e-144

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.).


The actual alignment was detected with superfamily member TIGR02752:

Pssm-ID: 473071  Cd Length: 231  Bit Score: 401.87  E-value: 5.68e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098    5 QAKKEQVHTVFQNISQKYDRLNNIISFEQHKVWRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSE 84
Cdd:TIGR02752   1 ESKEERVHKVFEKIYKKYDRMNSVISFQRHKKWRKDTMKRMNVQAGTSALDVCCGTADWSIALAEAVGPEGHVIGLDFSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   85 NMLEVGKQKTAS--LENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQPTLPLF 162
Cdd:TIGR02752  81 NMLSVGRQKVKDagLHNVELVHGNAMELPFDDNSFDYVTIGFGLRNVPDYMQVLREMYRVVKPGGKVVCLETSQPTIPGF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487749098  163 KQIYSLYFKFVMPIFGKMFAKSKEEYEWLQQSTFNFPDKQTLKGLFFEAGFNDIIVRSFTGGVAAMHLGYK 233
Cdd:TIGR02752 161 KQLYFFYFKYIMPLFGKLFAKSYKEYSWLQESTRDFPGMDELAEMFQEAGFKDVEVKSYTGGVAAMHMGFK 231
 
Name Accession Description Interval E-value
MenG_heptapren TIGR02752
demethylmenaquinone methyltransferase; MenG is a generic term for a methyltransferase that ...
 5-233 5.68e-144

demethylmenaquinone methyltransferase; MenG is a generic term for a methyltransferase that catalyzes the last step in menaquinone biosynthesis; the exact enzymatic activity differs for different MenG because the menaquinone differ in their prenoid side chains in different species. Members of this MenG protein family are 2-heptaprenyl-1,4-naphthoquinone methyltransferase, and are found together in operons with the two subunits of the heptaprenyl diphosphate synthase in Bacillus subtilis and related species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131799  Cd Length: 231  Bit Score: 401.87  E-value: 5.68e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098    5 QAKKEQVHTVFQNISQKYDRLNNIISFEQHKVWRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSE 84
Cdd:TIGR02752   1 ESKEERVHKVFEKIYKKYDRMNSVISFQRHKKWRKDTMKRMNVQAGTSALDVCCGTADWSIALAEAVGPEGHVIGLDFSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   85 NMLEVGKQKTAS--LENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQPTLPLF 162
Cdd:TIGR02752  81 NMLSVGRQKVKDagLHNVELVHGNAMELPFDDNSFDYVTIGFGLRNVPDYMQVLREMYRVVKPGGKVVCLETSQPTIPGF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487749098  163 KQIYSLYFKFVMPIFGKMFAKSKEEYEWLQQSTFNFPDKQTLKGLFFEAGFNDIIVRSFTGGVAAMHLGYK 233
Cdd:TIGR02752 161 KQLYFFYFKYIMPLFGKLFAKSYKEYSWLQESTRDFPGMDELAEMFQEAGFKDVEVKSYTGGVAAMHMGFK 231
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 1-234 9.79e-142

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 396.45  E-value: 9.79e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   1 MAENQAKKEQVHTVFQNISQKYDRLNNIISFEQHKVWRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGL 80
Cdd:PRK00216   3 TVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  81 DFSENMLEVGKQKTASL---ENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQP 157
Cdd:PRK00216  83 DFSEGMLAVGREKLRDLglsGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFSKP 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487749098 158 TLPLFKQIYSLYFKFVMPIFGKMFAKSKEEYEWLQQSTFNFPDKQTLKGLFFEAGFNDIIVRSFTGGVAAMHLGYKE 234
Cdd:PRK00216 163 TNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
9-233 3.81e-110

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 315.92  E-value: 3.81e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098    9 EQVHTVFQNISQKYDRLNNIISFEQHKVWRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSENMLE 88
Cdd:pfam01209   2 QRVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   89 VGKQKT--ASLENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQPTLPLFKQIY 166
Cdd:pfam01209  82 EGEKKAkeEGKYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAY 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487749098  167 SLYFKFVMPIFGKMFAKSKEEYEWLQQSTFNFPDKQTLKGLFFEAGFNDIIVRSFTGGVAAMHLGYK 233
Cdd:pfam01209 162 ELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 15-165 8.19e-46

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: 149.37  E-value: 8.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  15 FQNISQKYDRlnniisfeqhkvwRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGskgQVTGLDFSENMLEVGKQKT 94
Cdd:COG2226    1 FDRVAARYDG-------------REALLAALGLRPGARVLDLGCGTGRLALALAERGA---RVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487749098  95 ASLE-NIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQPTLPLFKQI 165
Cdd:COG2226   65 AEAGlNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 52-151 6.30e-18

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: 76.31  E-value: 6.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  52 KALDVCCGTADWTIALseAVGSKGQVTGLDFSENMLEVGKQKTASL--ENIQLVHGDAMNLPFD-DNSFDYV-TIGFGLR 127
Cdd:cd02440    1 RVLDLGCGTGALALAL--ASGPGARVTGVDISPVALELARKAAAALlaDNVEVLKGDAEELPPEaDESFDVIiSDPPLHH 78

                         90       100
                 ....*....|....*....|....
gi 487749098 128 NVPDYLSALKEMHRVLKPGGMVVC 151
Cdd:cd02440   79 LVEDLARFLEEARRLLKPGGVLVL 102
rADc smart00650
Ribosomal RNA adenine dimethylases;
37-135 3.83e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.88  E-value: 3.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098    37 WRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGskgQVTGLDFSENMLEVGKQKTASLENIQLVHGDAMNLPFDDNS 116
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAK---RVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQ 77

                           90
                   ....*....|....*....
gi 487749098   117 FDYVtigFGlrNVPDYLSA 135
Cdd:smart00650  78 PYKV---VG--NLPYNIST 91
 
Name Accession Description Interval E-value
MenG_heptapren TIGR02752
demethylmenaquinone methyltransferase; MenG is a generic term for a methyltransferase that ...
 5-233 5.68e-144

demethylmenaquinone methyltransferase; MenG is a generic term for a methyltransferase that catalyzes the last step in menaquinone biosynthesis; the exact enzymatic activity differs for different MenG because the menaquinone differ in their prenoid side chains in different species. Members of this MenG protein family are 2-heptaprenyl-1,4-naphthoquinone methyltransferase, and are found together in operons with the two subunits of the heptaprenyl diphosphate synthase in Bacillus subtilis and related species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131799  Cd Length: 231  Bit Score: 401.87  E-value: 5.68e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098    5 QAKKEQVHTVFQNISQKYDRLNNIISFEQHKVWRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSE 84
Cdd:TIGR02752   1 ESKEERVHKVFEKIYKKYDRMNSVISFQRHKKWRKDTMKRMNVQAGTSALDVCCGTADWSIALAEAVGPEGHVIGLDFSE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   85 NMLEVGKQKTAS--LENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQPTLPLF 162
Cdd:TIGR02752  81 NMLSVGRQKVKDagLHNVELVHGNAMELPFDDNSFDYVTIGFGLRNVPDYMQVLREMYRVVKPGGKVVCLETSQPTIPGF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487749098  163 KQIYSLYFKFVMPIFGKMFAKSKEEYEWLQQSTFNFPDKQTLKGLFFEAGFNDIIVRSFTGGVAAMHLGYK 233
Cdd:TIGR02752 161 KQLYFFYFKYIMPLFGKLFAKSYKEYSWLQESTRDFPGMDELAEMFQEAGFKDVEVKSYTGGVAAMHMGFK 231
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 1-234 9.79e-142

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 396.45  E-value: 9.79e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   1 MAENQAKKEQVHTVFQNISQKYDRLNNIISFEQHKVWRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGL 80
Cdd:PRK00216   3 TVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVVGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  81 DFSENMLEVGKQKTASL---ENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQP 157
Cdd:PRK00216  83 DFSEGMLAVGREKLRDLglsGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFSKP 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487749098 158 TLPLFKQIYSLYFKFVMPIFGKMFAKSKEEYEWLQQSTFNFPDKQTLKGLFFEAGFNDIIVRSFTGGVAAMHLGYKE 234
Cdd:PRK00216 163 TNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 11-233 4.97e-117

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 333.08  E-value: 4.97e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   11 VHTVFQNISQKYDRLNNIISFEQHKVWRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSENMLEVG 90
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   91 KQKTASLENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQPTLPLFKQIYSLYF 170
Cdd:TIGR01934  81 KKKSELPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYKFYL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487749098  171 KFVMPIFGKMFAKSKEEYEWLQQSTFNFPDKQTLKGLFFEAGFNDIIVRSFTGGVAAMHLGYK 233
Cdd:TIGR01934 161 KNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
9-233 3.81e-110

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 315.92  E-value: 3.81e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098    9 EQVHTVFQNISQKYDRLNNIISFEQHKVWRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSENMLE 88
Cdd:pfam01209   2 QRVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   89 VGKQKT--ASLENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQPTLPLFKQIY 166
Cdd:pfam01209  82 EGEKKAkeEGKYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQAY 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487749098  167 SLYFKFVMPIFGKMFAKSKEEYEWLQQSTFNFPDKQTLKGLFFEAGFNDIIVRSFTGGVAAMHLGYK 233
Cdd:pfam01209 162 ELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 14-225 5.77e-47

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 156.59  E-value: 5.77e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  14 VFQNISQKYDRLNNIISFEQHKVWRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSENMLEVGKQK 93
Cdd:PLN02233  38 LFNRIAPVYDNLNDLLSLGQHRIWKRMAVSWSGAKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAASR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  94 -----TASLENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQPTLPLFKQIYSL 168
Cdd:PLN02233 118 qelkaKSCYKNIEWIEGDATDLPFDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEW 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 487749098 169 YFKFVMPIFGKMFAKSKeEYEWLQQSTFNFPDKQTLKGLFFEAGFNDIIVRSFTGGV 225
Cdd:PLN02233 198 MIDNVVVPVATGYGLAK-EYEYLKSSINEYLTGEELEKLALEAGFSSAKHYEISGGL 253
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 15-165 8.19e-46

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: 149.37  E-value: 8.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  15 FQNISQKYDRlnniisfeqhkvwRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGskgQVTGLDFSENMLEVGKQKT 94
Cdd:COG2226    1 FDRVAARYDG-------------REALLAALGLRPGARVLDLGCGTGRLALALAERGA---RVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487749098  95 ASLE-NIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQPTLPLFKQI 165
Cdd:COG2226   65 AEAGlNVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 54-147 8.99e-35

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 119.59  E-value: 8.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   54 LDVCCGTADWTIALSEAVGskGQVTGLDFSENMLEVGKQKTASLE-NIQLVHGDAMNLPFDDNSFDYVTIGFGL--RNVP 130
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGlNVEFVQGDAEDLPFPDGSFDLVVSSGVLhhLPDP 79

                          90
                  ....*....|....*..
gi 487749098  131 DYLSALKEMHRVLKPGG 147
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 38-154 1.46e-30

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 113.11  E-value: 1.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  38 RKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSENMLEVGKQKTASLE-NIQLVHGDAMNLPFDDNS 116
Cdd:PRK08317   8 RARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGpNVEFVRGDADGLPFPDGS 87

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 487749098 117 FDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLET 154
Cdd:PRK08317  88 FDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDT 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 54-151 6.21e-27

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 99.28  E-value: 6.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   54 LDVCCGTADWTIALSEAVGskgQVTGLDFSENMLEVGKQKtASLENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYL 133
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA---RVTGVDISPEMLELAREK-APREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPE 76

                          90
                  ....*....|....*...
gi 487749098  134 SALKEMHRVLKPGGMVVC 151
Cdd:pfam08241  77 RALREIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 37-150 2.66e-25

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: 96.24  E-value: 2.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  37 WRKHVMSTMN--VQKGSKALDVCCGTADWTIALSEAvgskG-QVTGLDFSENMLEVGKQKTASLeNIQLVHGDAMNLPFD 113
Cdd:COG2227   10 WDRRLAALLArlLPAGGRVLDVGCGTGRLALALARR----GaDVTGVDISPEALEIARERAAEL-NVDFVQGDLEDLPLE 84

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 487749098 114 DNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVV 150
Cdd:COG2227   85 DGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLL 121
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 79-228 4.70e-23

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 91.67  E-value: 4.70e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  79 GLDFSENMLEVGKQKTA-----SLENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLE 153
Cdd:PLN02232   2 GLDFSSEQLAVAATRQSlkarsCYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098 154 --TSQPTLPLFKQIYsLYFKFVMPIfGKMFAKSKeEYEWLQQSTFNFPDKQTLKGLFFEAGFNDI----IVRSFTGGVAA 227
Cdd:PLN02232  82 fnKSNQSVTTFMQGW-MIDNVVVPV-ATVYDLAK-EYEYLKYSINGYLTGEELETLALEAGFSSAchyeISGGFMGNLVA 158


                 .
gi 487749098 228 M 228
Cdd:PLN02232 159 M 159
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
6-159 7.19e-20

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 83.51  E-value: 7.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   6 AKKEQVHTVFQNISQKYD-RLNNIISFEQHKVWRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSkgqVTGLDFSE 84
Cdd:COG4976    2 ALDAYVEALFDQYADSYDaALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR---LTGVDLSE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487749098  85 NMLEVGKQKTASlenIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVV-CLETSQPTL 159
Cdd:COG4976   79 EMLAKAREKGVY---DRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIfSVEDADGSG 151
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 49-153 4.32e-19

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 80.54  E-value: 4.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   49 KGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSENMLEVGKQKTASL--ENIQLVHGDAMNLP--FDDNSFDYVTIGF 124
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLgfDNVEFEQGDIEELPelLEDDKFDVVISNC 82

                          90       100
                  ....*....|....*....|....*....
gi 487749098  125 GLRNVPDYLSALKEMHRVLKPGGMVVCLE 153
Cdd:pfam13847  83 VLNHIPDPDKVLQEILRVLKPGGRLIISD 111
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 48-150 3.06e-18

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 79.58  E-value: 3.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  48 QKGSKALDVCCGTADWTIALSEAVGskGQVTGLDFSENMLEVGKQKTAS--LENIQLVHGD-AMNLPFDDNSFDYVTigf 124
Cdd:COG0500   25 PKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKagLGNVEFLVADlAELDPLPAESFDLVV--- 99

                         90       100       110
                 ....*....|....*....|....*....|..
gi 487749098 125 gLRNV-----PDYL-SALKEMHRVLKPGGMVV 150
Cdd:COG0500  100 -AFGVlhhlpPEEReALLRELARALKPGGVLL 130
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 52-151 6.30e-18

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: 76.31  E-value: 6.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  52 KALDVCCGTADWTIALseAVGSKGQVTGLDFSENMLEVGKQKTASL--ENIQLVHGDAMNLPFD-DNSFDYV-TIGFGLR 127
Cdd:cd02440    1 RVLDLGCGTGALALAL--ASGPGARVTGVDISPVALELARKAAAALlaDNVEVLKGDAEELPPEaDESFDVIiSDPPLHH 78

                         90       100
                 ....*....|....*....|....
gi 487749098 128 NVPDYLSALKEMHRVLKPGGMVVC 151
Cdd:cd02440   79 LVEDLARFLEEARRLLKPGGVLVL 102
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-150 1.88e-17

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 76.51  E-value: 1.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  40 HVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSkgQVTGLDFSENMLEVGKQKTASL---ENIQLVHGDAMNLPFDdNS 116
Cdd:COG2230   42 LILRKLGLKPGMRVLDIGCGWGGLALYLARRYGV--RVTGVTLSPEQLEYARERAAEAglaDRVEVRLADYRDLPAD-GQ 118

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 487749098 117 FDYVT-IG----FGLRNVPDYLsalKEMHRVLKPGGMVV 150
Cdd:COG2230  119 FDAIVsIGmfehVGPENYPAYF---AKVARLLKPGGRLL 154
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
49-150 3.11e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 74.47  E-value: 3.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  49 KGSKALDVCCGTADWTIALSEAVgSKGQVTGLDFSENMLEVGKQKtasLENIQLVHGDAMNLPFDDnSFDYVTIGFGLRN 128
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERF-PGARVTGVDLSPEMLARARAR---LPNVRFVVADLRDLDPPE-PFDLVVSNAALHW 75

                         90       100
                 ....*....|....*....|..
gi 487749098 129 VPDYLSALKEMHRVLKPGGMVV 150
Cdd:COG4106   76 LPDHAALLARLAAALAPGGVLA 97
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 54-149 1.53e-15

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 69.70  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   54 LDVCCGTADWTIALSEAVGSkGQVTGLDFSENMLEVGKQKTASLE--NIQLVHGDAMNLPFDD-NSFDYVTIGFGLRNVP 130
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPG-LEYTGLDISPAALEAARERLAALGllNAVRVELFQLDLGELDpGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 487749098  131 DYLSALKEMHRVLKPGGMV 149
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
PRK05785 PRK05785
hypothetical protein; Provisional
 6-188 2.89e-15

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 72.41  E-value: 2.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   6 AKKEQVHTVFQNISQKYDRLNNIISFEQHKVWRKHVMSTMNVQKGS--KALDVCCGTADWTIALSEAVgsKGQVTGLDFS 83
Cdd:PRK05785   6 ATWEELQEAYNKIPKAYDRANRFISFNQDVRWRAELVKTILKYCGRpkKVLDVAAGKGELSYHFKKVF--KYYVVALDYA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  84 ENMLEVgkqktaSLENIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLetSQPTLPLFK 163
Cdd:PRK05785  84 ENMLKM------NLVADDKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAEFTRVSRKQVGFIAM--GKPDNVIKR 155

                        170       180
                 ....*....|....*....|....*
gi 487749098 164 QIYSLYFKFVMPIFGKMFAKSKEEY 188
Cdd:PRK05785 156 KYLSFYLRYIMPYIACLAGAKCRDY 180
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 22-169 1.98e-14

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: 70.01  E-value: 1.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   22 YDRLNNIisfeQHKVwRKHVMS---TMNVQKGSKALDVCCGTADWTIALSEAvGSKGQVTGLDFSENMLEVGKQKTAslE 98
Cdd:TIGR02072   9 YDRHAKI----QREM-AKRLLAllkEKGIFIPASVLDIGCGTGYLTRALLKR-FPQAEFIALDISAGMLAQAKTKLS--E 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487749098   99 NIQLVHGDAMNLPFDDNSFDYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVVCLETSQPTLPLFKQIYSLY 169
Cdd:TIGR02072  81 NVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQH 151
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 52-196 1.21e-13

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 69.15  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  52 KALDVCCGTADWTIALSEAVGSKgQVTGLDFSENMLEVGKQKTAsLENIQLVHGDAMNLPFDDNSFD-YVTIGfGLRNVP 130
Cdd:PLN02490 116 KVVDVGGGTGFTTLGIVKHVDAK-NVTILDQSPHQLAKAKQKEP-LKECKIIEGDAEDLPFPTDYADrYVSAG-SIEYWP 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487749098 131 DYLSALKEMHRVLKPGGMVVCLETSQPTLPLfkqiySLYFKFVMPIFGKmfaksKEEY-EWLQQSTF 196
Cdd:PLN02490 193 DPQRGIKEAYRVLKIGGKACLIGPVHPTFWL-----SRFFADVWMLFPK-----EEEYiEWFTKAGF 249
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 47-150 3.68e-13

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: 65.36  E-value: 3.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  47 VQKGSKALDVCCGTAdwTIALsEAVGSKGQVTGLDFSENMLEVGKQ--KTASLENIQLVHGDAMNLPFDDNSFD------ 118
Cdd:COG1041   24 AKEGDTVLDPFCGTG--TILI-EAGLLGRRVIGSDIDPKMVEGAREnlEHYGYEDADVIRGDARDLPLADESVDaivtdp 100

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 487749098 119 ----YVTIGFG-LRNVpdYLSALKEMHRVLKPGGMVV 150
Cdd:COG1041  101 pygrSSKISGEeLLEL--YEKALEEAARVLKPGGRVV 135
arsM PRK11873
arsenite methyltransferase;
70-147 4.12e-13

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 66.90  E-value: 4.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  70 AVGSKGQVTGLDFSENMLEVGK--QKTASLENIQLVHGDAMNLPFDDNSFDyVTIGFGLRN-VPDYLSALKEMHRVLKPG 146
Cdd:PRK11873  98 RVGPTGKVIGVDMTPEMLAKARanARKAGYTNVEFRLGEIEALPVADNSVD-VIISNCVINlSPDKERVFKEAFRVLKPG 176


                 .
gi 487749098 147 G 147
Cdd:PRK11873 177 G 177
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 38-150 8.89e-11

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 59.43  E-value: 8.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  38 RKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSENMLEVGK---QKTASLENIQLVHGDAMN-LPFD 113
Cdd:PRK00377  29 RALALSKLRLRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRrnaEKFGVLNNIVLIKGEAPEiLFTI 108

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 487749098 114 DNSFDYVTIGFGLRNVPDYLSALKEmhrVLKPGGMVV 150
Cdd:PRK00377 109 NEKFDRIFIGGGSEKLKEIISASWE---IIKKGGRIV 142
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 46-152 3.17e-10

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: 58.63  E-value: 3.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  46 NVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSENMLEVGKQ---KTASLENIQLVHGDAMNlPFDDNSFDYVTI 122
Cdd:COG2519   88 DIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKnleRFGLPDNVELKLGDIRE-GIDEGDVDAVFL 166

                         90       100       110
                 ....*....|....*....|....*....|
gi 487749098 123 gfglrNVPDYLSALKEMHRVLKPGGMVVCL 152
Cdd:COG2519  167 -----DMPDPWEALEAVAKALKPGGVLVAY 191
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 49-216 6.73e-10

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 56.28  E-value: 6.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   49 KGSKALDVCCGTADWTIALSEaVGSkgQVTGLDFSENMLEVGKQKtasleNIQLVHgDAMNLPFDDNSFDYVTIGFGLRN 128
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRA-QGF--SVTGVDPSPIAIERALLN-----VRFDQF-DEQEAAVPAGKFDVIVAREVLEH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  129 VPDYLSALKEMHRVLKPGGMVVCLE--TSQPTLPLFKQIYSLyfkfvMPIFGKMfakskeeyewlqqstfNFPDKQTLKG 206
Cdd:pfam13489  93 VPDPPALLRQIAALLKPGGLLLLSTplASDEADRLLLEWPYL-----RPRNGHI----------------SLFSARSLKR 151

                         170
                  ....*....|
gi 487749098  207 LFFEAGFNDI 216
Cdd:pfam13489 152 LLEEAGFEVV 161
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 54-164 1.43e-09

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 56.69  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  54 LDVCCGTA----DWtialsEAVGSkgQVTGLDFSENMLEVGKQKTASLENIQlvhGDAMNLPFDDNSFDYVTIGFGLRNV 129
Cdd:PRK10258  47 LDAGCGPGwmsrYW-----RERGS--QVTALDLSPPMLAQARQKDAADHYLA---GDIESLPLATATFDLAWSNLAVQWC 116

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 487749098 130 PDYLSALKEMHRVLKPGGMVVCLETSQPTLPLFKQ 164
Cdd:PRK10258 117 GNLSTALRELYRVVRPGGVVAFTTLVQGSLPELHQ 151
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 64-151 5.07e-08

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: 50.95  E-value: 5.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  64 TIALSEAVGSKGQVTGLDFSENMLEVGKQ--KTASLEN-IQLVHGDAMN-LP-FDDNSFDYVTIGFGLRNVPDYLSALKE 138
Cdd:COG4122   31 TLWLARALPDDGRLTTIEIDPERAAIAREnfARAGLADrIRLILGDALEvLPrLADGPFDLVFIDADKSNYPDYLELALP 110

                         90
                 ....*....|...
gi 487749098 139 MhrvLKPGGMVVC 151
Cdd:COG4122  111 L---LRPGGLIVA 120
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
40-150 8.40e-08

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 50.83  E-value: 8.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   40 HVMSTM----NVQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSENMLEVGKQ--KTASLENIQLVHGDAmNLPFD 113
Cdd:pfam01135  60 HMHAMMlellELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRnlEKLGLENVIVVVGDG-RQGWP 138

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 487749098  114 DNS-FDYVTIGFGLRNVPdylsalKEMHRVLKPGGMVV 150
Cdd:pfam01135 139 EFApYDAIHVGAAAPEIP------EALIDQLKEGGRLV 170
PLN02244 PLN02244
tocopherol O-methyltransferase
 52-170 1.34e-07

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 51.28  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  52 KALDVCCGTADWTIALSEAVGSkgQVTGLDFSENMLEVGKQ--KTASLEN-IQLVHGDAMNLPFDDNSFDYVTIGFGLRN 128
Cdd:PLN02244 121 RIVDVGCGIGGSSRYLARKYGA--NVKGITLSPVQAARANAlaAAQGLSDkVSFQVADALNQPFEDGQFDLVWSMESGEH 198

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 487749098 129 VPDYLSALKEMHRVLKPGGMVV----C---LETSQPTLP-----LFKQIYSLYF 170
Cdd:PLN02244 199 MPDKRKFVQELARVAAPGGRIIivtwChrdLEPGETSLKpdeqkLLDKICAAYY 252
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
98-151 9.81e-07

Predicted SAM-depedendent methyltransferase [General function prediction only];


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 47.17  E-value: 9.81e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  98 ENIQLVHGDAMNLPFDDNSFDYVtigFGlRNV------PDYLSALKEMHRVLKPGGMVVC 151
Cdd:COG4627   28 PGVDIVGDLTDPLPFPDNSVDAI---YS-SHVlehldyEEAPLALKECYRVLKPGGILRI 83
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 38-149 2.55e-06

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 47.32  E-value: 2.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   38 RKHVMSTMNVQKGSKALDVCCGtadWTIALSEAVGSKG-QVTGLDFSENMLEVGKQKTASLEN-----IQLVHGDAMNLP 111
Cdd:pfam02353  50 LDLILDKLGLKPGMTLLDIGCG---WGGLMRRAAERYDvNVVGLTLSKNQYKLARKRVAAEGLarkveVLLQDYRDFDEP 126

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 487749098  112 FDdnsfDYVTIG----FGLRNVPDYLSALkemHRVLKPGGMV 149
Cdd:pfam02353 127 FD----RIVSVGmfehVGHENYDTFFKKL---YNLLPPGGLM 161
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
47-150 2.38e-05

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 44.52  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  47 VQKGSKALDVCCGTADWTIALSEAVGSKGQVTGLDFSENML--EVGKQKTASLE-----------NIQLVHGDAMNLPF- 112
Cdd:COG4798   64 VKPGMTVVEIWPGGGWYTEILAPYLGPKGKVYAANFDPDSEppEYAKRSREAFSaklaadpalygNVRVTAFAPPDDPIa 143

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 487749098 113 DDNSFDYVTIGfglRNVPDYL------SALKEMHRVLKPGGMVV 150
Cdd:COG4798  144 PPGSADLVLTF---RNYHNWYragdaaAMFAAFFKALKPGGVLG 184
rADc smart00650
Ribosomal RNA adenine dimethylases;
37-135 3.83e-05

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 42.88  E-value: 3.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098    37 WRKHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGskgQVTGLDFSENMLEVGKQKTASLENIQLVHGDAMNLPFDDNS 116
Cdd:smart00650   1 VIDKIVRAANLRPGDTVLEIGPGKGALTEELLERAK---RVTAIEIDPRLAPRLREKFAAADNLTVIHGDALKFDLPKLQ 77

                           90
                   ....*....|....*....
gi 487749098   117 FDYVtigFGlrNVPDYLSA 135
Cdd:smart00650  78 PYKV---VG--NLPYNIST 91
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 47-188 1.28e-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: 41.42  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   47 VQKGSKALDVCCGTADWTIALSEAvgSKGQVTGLDfsenMLEVGKQKTASLENIQLVHGDAMNLPFDDNSFDYVTIGF-- 124
Cdd:pfam01728  19 LKPGKTVLDLGAAPGGWSQVALQR--GAGKVVGVD----LGPMQLWKPRNDPGVTFIQGDIRDPETLDLLEELLGRKVdl 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  125 ----------GLRNVPDYLS------ALKEMHRVLKPGGMVVCLETSQPTLPLFKQIYSLYFKFVM----PIFGKmfaKS 184
Cdd:pfam01728  93 vlsdgspfisGNKVLDHLRSldlvkaALEVALELLRKGGNFVCKVFQGEDFSELLYLLKLGFEKVGvfkpPASRP---ES 169


                  ....
gi 487749098  185 KEEY 188
Cdd:pfam01728 170 SEEY 173
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
22-150 2.11e-04

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 42.16  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  22 YDRLNNiisfeqHKVWRKHVMSTMNVQK-------GSKALDVCCGTADWTIALSEAVGSKgQVTGLDFSENMLE-VGKQK 93
Cdd:PRK06922 390 YDRFHN------EEVYLEHMNSSADDKRiildyikGDTIVDVGAGGGVMLDMIEEETEDK-RIYGIDISENVIDtLKKKK 462

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487749098  94 TASLENIQLVHGDAMNLP--FDDNSFDYVTIGFGLRNVPDYL-------------SALKEMHRVLKPGGMVV 150
Cdd:PRK06922 463 QNEGRSWNVIKGDAINLSssFEKESVDTIVYSSILHELFSYIeyegkkfnhevikKGLQSAYEVLKPGGRII 534
TrmB COG0220
tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 ...
 54-151 3.97e-04

tRNA G46 N7-methylase TrmB [Translation, ribosomal structure and biogenesis]; tRNA G46 N7-methylase TrmB is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439990  Cd Length: 204  Bit Score: 40.12  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  54 LDVCCGTADWTIALSEAVGSKGqVTGLDFSENMLEVGKQK--TASLENIQLVHGDAMNLP--FDDNSFDYVTIGFglrnv 129
Cdd:COG0220   37 LEIGFGKGEFLVELAAANPDIN-FIGIEVHEPGVAKALKKaeEEGLTNVRLLRGDAVELLelFPDGSLDRIYLNF----- 110

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 487749098 130 PD-------------YLSALKEMHRVLKPGGMVVC 151
Cdd:COG0220  111 PDpwpkkrhhkrrlvQPEFLALLARVLKPGGELHL 145
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 47-142 6.07e-04

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 39.75  E-value: 6.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   47 VQKGSKALDVCCGTADWTIALSEAVGSKGQvtGLDFSENMLEVGKQKtasleNIQLVHGDA-MNLP-FDDNSFDYVTIGF 124
Cdd:pfam07021  11 IPPGSRVLDLGCGDGTLLYLLKEEKGVDGY--GIELDAAGVAECVAK-----GLYVIQGDLdEGLEhFPDKSFDYVILSQ 83

                          90
                  ....*....|....*...
gi 487749098  125 GLRNVPDYLSALKEMHRV 142
Cdd:pfam07021  84 TLQATRNPREVLDEMLRI 101
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 39-217 1.33e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 39.35  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  39 KHVMSTMNVQKGSKALDVCCGTADWTIALSEAVGSkgQVTGLDFSENMLEVGKQKTASLE-NIQLVHGDAMNLPFDDNSF 117
Cdd:PLN02336 256 KEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDV--HVVGIDLSVNMISFALERAIGRKcSVEFEVADCTKKTYPDNSF 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098 118 DYVTIGFGLRNVPDYLSALKEMHRVLKPGGMVV----CLETSQPtlplfkqiyslyfkfvmpifgkmfakSKEEYEWLQQ 193
Cdd:PLN02336 334 DVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLisdyCRSPGTP--------------------------SPEFAEYIKQ 387

                        170       180
                 ....*....|....*....|....
gi 487749098 194 STFNFPDKQTLKGLFFEAGFNDII 217
Cdd:PLN02336 388 RGYDLHDVQAYGQMLKDAGFDDVI 411
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 46-121 2.82e-03

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: 37.82  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  46 NVQKGSKALDVCCGTAdwtiALSEAVGSK---GQVTGLDFSENMLEVGkQKTASL----ENIQLVHGDAMNLP--FDDNS 116
Cdd:COG4123   34 PVKKGGRVLDLGTGTG----VIALMLAQRspgARITGVEIQPEAAELA-RRNVALngleDRITVIHGDLKEFAaeLPPGS 108


                 ....*
gi 487749098 117 FDYVT 121
Cdd:COG4123  109 FDLVV 113
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 54-149 3.23e-03

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 37.27  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   54 LDVCCGTADWTIALSEAVGSKgQVTGLDFSENMLEVGKQKTASLE--NIQLVHGDAMN-LP--FDDNSFDYVTIGFglrn 128
Cdd:pfam02390   6 LEIGCGMGGFLVAMAKANPDK-NFIGIEIRVPGVAKALKKIDALGlqNLRILCGNALDvLPnyFPPGSLQKIFINF---- 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 487749098  129 vPD-------------YLSALKEMHRVLKPGGMV 149
Cdd:pfam02390  81 -PDpwpkkrhhkrrllQPEFLKEYARVLKPGGVL 113
Methyltransf_24 pfam13578
Methyltransferase domain; This family appears to be a methyltransferase domain.
 56-151 5.46e-03

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


Pssm-ID: 433324 [Multi-domain]  Cd Length: 106  Bit Score: 35.36  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098   56 VCCGTadWTIALSEAV--GSKGQVTGLDFSENMLEVGK--QKTASLENIQLVHGDAMNL--PFDDNSFDYVTIGfGLRNV 129
Cdd:pfam13578   5 TYSGV--STLWLAAALrdNGLGRLTAVDPDPGAEEAGAllRKAGLDDRVRLIVGDSREAlpSLADGPIDLLFID-GDHTY 81

                          90       100
                  ....*....|....*....|..
gi 487749098  130 PDYLSALKEMHRVLKPGGMVVC 151
Cdd:pfam13578  82 EAVLNDLELWLPRLAPGGVILF 103
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 42-150 7.92e-03

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: 36.32  E-value: 7.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487749098  42 MSTMNVQKGSKALDVCCGtadW---TIALSEAvGSKGQVTGLDFSENMLEVGKQ--KTASLENIQLVHGDAMNlPFDDNS 116
Cdd:COG2813   42 LEHLPEPLGGRVLDLGCG---YgviGLALAKR-NPEARVTLVDVNARAVELARAnaAANGLENVEVLWSDGLS-GVPDGS 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 487749098 117 FDYVtigfgLRNVP------DYLSALKEM----HRVLKPGG---MVV 150
Cdd:COG2813  117 FDLI-----LSNPPfhagraVDKEVAHALiadaARHLRPGGelwLVA 158
 
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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