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Conserved domains on  [gi|491220997|ref|WP_005079312|]
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MULTISPECIES: bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE [Acinetobacter]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10011316)

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 ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0032259|GO:1904047
PubMed:  9045837|12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 77-315 2.31e-145

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


:

Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 408.77  E-value: 2.31e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  77 YSTVRTEDKAQKVAEVFHSVASKYDLMNDLMSFGIHRLWKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVV 156
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 157 LSDINESMLNVGRDRLIDAG-CTNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEF 235
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGlSGNVEFVQGDAEAL-PFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 236 SKPVFEPFSKLYDLYSFTALPIMGKLVANDSESYKYLAESIRMHPDQRTLKGMMENAGFQNCDYHNLTAGIVAVHRGFKL 315
Cdd:PRK00216 160 SKPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 77-315 2.31e-145

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 408.77  E-value: 2.31e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  77 YSTVRTEDKAQKVAEVFHSVASKYDLMNDLMSFGIHRLWKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVV 156
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 157 LSDINESMLNVGRDRLIDAG-CTNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEF 235
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGlSGNVEFVQGDAEAL-PFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 236 SKPVFEPFSKLYDLYSFTALPIMGKLVANDSESYKYLAESIRMHPDQRTLKGMMENAGFQNCDYHNLTAGIVAVHRGFKL 315
Cdd:PRK00216 160 SKPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
87-314 1.10e-116

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 335.56  E-value: 1.10e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997   87 QKVAEVFHSVASKYDLMNDLMSFGIHRLWKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLN 166
Cdd:pfam01209   2 QRVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  167 VGRDRLIDAGCTNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEFSKPVFEPFSKL 246
Cdd:pfam01209  82 EGEKKAKEEGKYNIEFLQGNAEEL-PFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491220997  247 YDLYSFTALPIMGKLVANDSESYKYLAESIRMHPDQRTLKGMMENAGFQNCDYHNLTAGIVAVHRGFK 314
Cdd:pfam01209 161 YELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 89-314 7.91e-112

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: 323.06  E-value: 7.91e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997   89 VAEVFHSVASKYDLMNDLMSFGIHRLWKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVG 168
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  169 RDRLIDAGctNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEFSKPVFEPFSKLYD 248
Cdd:TIGR01934  81 KKKSELPL--NIEFIQADAEAL-PFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491220997  249 LYSFTALPIMGKLVANDSESYKYLAESIRMHPDQRTLKGMMENAGFQNCDYHNLTAGIVAVHRGFK 314
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 93-246 2.48e-42

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: 143.21  E-value: 2.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  93 FHSVASKYDLmndlmsfgihrlwKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREvgpQGHVVLSDINESMLNVGRDRL 172
Cdd:COG2226    1 FDRVAARYDG-------------REALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491220997 173 IDAGCtNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEFSKPVFEPFSKL 246
Cdd:COG2226   65 AEAGL-NVEFVVGDAEDL-PFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 131-232 6.46e-17

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: 75.16  E-value: 6.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 131 VLDIAGGTGDLAKVFSRevGPQGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANAETLEPFADNSFDLV-TISFGLRN 209
Cdd:cd02440    2 VLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIiSDPPLHHL 79

                         90       100
                 ....*....|....*....|...
gi 491220997 210 VTDKDAALASMFRVLKPGGRLLI 232
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 77-315 2.31e-145

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 408.77  E-value: 2.31e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  77 YSTVRTEDKAQKVAEVFHSVASKYDLMNDLMSFGIHRLWKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVV 156
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 157 LSDINESMLNVGRDRLIDAG-CTNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEF 235
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGlSGNVEFVQGDAEAL-PFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 236 SKPVFEPFSKLYDLYSFTALPIMGKLVANDSESYKYLAESIRMHPDQRTLKGMMENAGFQNCDYHNLTAGIVAVHRGFKL 315
Cdd:PRK00216 160 SKPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
87-314 1.10e-116

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 335.56  E-value: 1.10e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997   87 QKVAEVFHSVASKYDLMNDLMSFGIHRLWKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLN 166
Cdd:pfam01209   2 QRVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  167 VGRDRLIDAGCTNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEFSKPVFEPFSKL 246
Cdd:pfam01209  82 EGEKKAKEEGKYNIEFLQGNAEEL-PFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491220997  247 YDLYSFTALPIMGKLVANDSESYKYLAESIRMHPDQRTLKGMMENAGFQNCDYHNLTAGIVAVHRGFK 314
Cdd:pfam01209 161 YELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 89-314 7.91e-112

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: 323.06  E-value: 7.91e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997   89 VAEVFHSVASKYDLMNDLMSFGIHRLWKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVG 168
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  169 RDRLIDAGctNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEFSKPVFEPFSKLYD 248
Cdd:TIGR01934  81 KKKSELPL--NIEFIQADAEAL-PFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491220997  249 LYSFTALPIMGKLVANDSESYKYLAESIRMHPDQRTLKGMMENAGFQNCDYHNLTAGIVAVHRGFK 314
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 93-246 2.48e-42

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: 143.21  E-value: 2.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  93 FHSVASKYDLmndlmsfgihrlwKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREvgpQGHVVLSDINESMLNVGRDRL 172
Cdd:COG2226    1 FDRVAARYDG-------------REALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491220997 173 IDAGCtNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEFSKPVFEPFSKL 246
Cdd:COG2226   65 AEAGL-NVEFVVGDAEDL-PFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 92-307 2.68e-41

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 144.26  E-value: 2.68e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  92 VFHSVASKYDLMNDLMSFGIHRLWKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVGRDR 171
Cdd:PLN02233  38 LFNRIAPVYDNLNDLLSLGQHRIWKRMAVSWSGAKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAASR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 172 --LIDAGC-TNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEFSKPVfEPFSKLYD 248
Cdd:PLN02233 118 qeLKAKSCyKNIEWIEGDATDL-PFDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKST-QPFTTSMQ 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491220997 249 LYSFTALPIMGKLVANDSESYKYLAESIRMHPDQRTLKGMMENAGFQNCDYHNLTAGIV 307
Cdd:PLN02233 196 EWMIDNVVVPVATGYGLAKEYEYLKSSINEYLTGEELEKLALEAGFSSAKHYEISGGLM 254
PRK08317 PRK08317
hypothetical protein; Provisional
 116-304 1.45e-28

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 110.03  E-value: 1.45e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 116 KRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVGRDRlIDAGCTNVDFVLANAETLePFAD 195
Cdd:PRK08317   8 RARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKER-AAGLGPNVEFVRGDADGL-PFPD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 196 NSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILE--FSKPVFEPF-----SKLYDLYS-FTALPIMGklvandse 267
Cdd:PRK08317  86 GSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDtdWDTLVWHSGdralmRKILNFWSdHFADPWLG-------- 157

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491220997 268 sykylaesirmhpdqRTLKGMMENAGFQN--CDYHNLTA 304
Cdd:PRK08317 158 ---------------RRLPGLFREAGLTDieVEPYTLIE 181
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 131-228 1.70e-28

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 105.34  E-value: 1.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  131 VLDIAGGTGDLAKVFSREVGpqGHVVLSDINESMLNVGRDRLIDAGCtNVDFVLANAETLePFADNSFDLVTISFGLRNV 210
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDL-PFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 491220997  211 TDKD--AALASMFRVLKPGG 228
Cdd:pfam13649  77 PDPDleAALREIARVLKPGG 96
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 126-236 1.57e-22

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 91.32  E-value: 1.57e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  126 RRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANAETLE-PFADNSFDLVtIS 204
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEELPeLLEDDKFDVV-IS 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 491220997  205 FGLRN-VTDKDAALASMFRVLKPGGRLLILEFS 236
Cdd:pfam13847  81 NCVLNhIPDPDKVLQEILRVLKPGGRLIISDPD 113
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 132-232 9.07e-22

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 87.72  E-value: 9.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  132 LDIAGGTGDLAKVFSReVGPQghVVLSDINESMLNVGRDRLIDAGctnVDFVLANAETLePFADNSFDLVTISFGLRNVT 211
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGAR--VTGVDISPEMLELAREKAPREG---LTFVVGDAEDL-PFPDNSFDLVLSSEVLHHVE 73

                          90       100
                  ....*....|....*....|.
gi 491220997  212 DKDAALASMFRVLKPGGRLLI 232
Cdd:pfam08241  74 DPERALREIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 125-232 1.30e-20

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: 85.45  E-value: 1.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 125 VRRGQHVLDIAGGTGDLAKVFSRevgpQGH-VVLSDINESMLNVGRDRLIDAgctNVDFVLANAETLePFADNSFDLVTI 203
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALAR----RGAdVTGVDISPEALEIARERAAEL---NVDFVQGDLEDL-PLEDGSFDLVIC 93

                         90       100
                 ....*....|....*....|....*....
gi 491220997 204 SFGLRNVTDKDAALASMFRVLKPGGRLLI 232
Cdd:COG2227   94 SEVLEHLPDPAALLRELARLLKPGGLLLL 122
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
127-232 3.58e-19

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 81.02  E-value: 3.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 127 RGQHVLDIAGGTGDLAKVFSREVgPQGHVVLSDINESMLNVGRDRLidagcTNVDFVLANAETLEPfaDNSFDLVTISFG 206
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERF-PGARVTGVDLSPEMLARARARL-----PNVRFVVADLRDLDP--PEPFDLVVSNAA 72

                         90       100
                 ....*....|....*....|....*.
gi 491220997 207 LRNVTDKDAALASMFRVLKPGGRLLI 232
Cdd:COG4106   73 LHWLPDHAALLARLAAALAPGGVLAV 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 114-232 3.72e-18

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 81.12  E-value: 3.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 114 LWKRFAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGpqGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANAETLEPF 193
Cdd:COG0500   13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLAELDPL 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491220997 194 ADNSFDLVtISFGLRNVTDKD---AALASMFRVLKPGGRLLI 232
Cdd:COG0500   91 PAESFDLV-VAFGVLHHLPPEereALLRELARALKPGGVLLL 131
arsM PRK11873
arsenite methyltransferase;
128-232 5.94e-18

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 81.92  E-value: 5.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 128 GQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANAETLePFADNSFDlVTISFGL 207
Cdd:PRK11873  78 GETVLDLGSGGGFDCFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTNVEFRLGEIEAL-PVADNSVD-VIISNCV 155

                         90       100
                 ....*....|....*....|....*.
gi 491220997 208 RN-VTDKDAALASMFRVLKPGGRLLI 232
Cdd:PRK11873 156 INlSPDKERVFKEAFRVLKPGGRFAI 181
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 131-232 6.46e-17

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: 75.16  E-value: 6.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 131 VLDIAGGTGDLAKVFSRevGPQGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANAETLEPFADNSFDLV-TISFGLRN 209
Cdd:cd02440    2 VLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPPEADESFDVIiSDPPLHHL 79

                         90       100
                 ....*....|....*....|...
gi 491220997 210 VTDKDAALASMFRVLKPGGRLLI 232
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVL 102
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 93-256 7.41e-16

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: 75.40  E-value: 7.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997   93 FHSVASKYDLMNDLMSFGIHRLWKRfaINMSGVRRGQHVLDIAGGTGDLAKVFSREvGPQGHVVLSDINESMLNVGRDRL 172
Cdd:TIGR02072   2 FNKAAKTYDRHAKIQREMAKRLLAL--LKEKGIFIPASVLDIGCGTGYLTRALLKR-FPQAEFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  173 idagCTNVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGrllILEFSKPVFEPFSKLYDLYSF 252
Cdd:TIGR02072  79 ----SENVQFICGDAEKL-PLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGG---LLAFSTFGPGTLHELRQSFGQ 150


                  ....
gi 491220997  253 TALP 256
Cdd:TIGR02072 151 HGLR 154
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 132-230 7.58e-16

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 71.63  E-value: 7.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  132 LDIAGGTGDLAKVFsREVGPQGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANAETLEPFADNSFDLVTISFGLRNVT 211
Cdd:pfam08242   1 LEIGCGTGTLLRAL-LEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 491220997  212 DKDAALASMFRVLKPGGRL 230
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 124-232 1.96e-14

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 69.57  E-value: 1.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 124 GVRRGQHVLDIAGGTGDLAKVFSREVGpqGHVVLSDINESMLNVGRDRLIDAGCTN-VDFVLANAETLEPfaDNSFDLVt 202
Cdd:COG2230   48 GLKPGMRVLDIGCGWGGLALYLARRYG--VRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDLPA--DGQFDAI- 122

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491220997 203 ISFG-LRNVTDKD--AALASMFRVLKPGGRLLI 232
Cdd:COG2230  123 VSIGmFEHVGPENypAYFAKVARLLKPGGRLLL 155
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
89-232 3.27e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 66.95  E-value: 3.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  89 VAEVFHSVASKYD--LMNDLMSFGIHRLWKRfAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGpqgHVVLSDINESMLN 166
Cdd:COG4976    7 VEALFDQYADSYDaaLVEDLGYEAPALLAEE-LLARLPPGPFGRVLDLGCGTGLLGEALRPRGY---RLTGVDLSEEMLA 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491220997 167 VGRDRLIDagctnVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLI 232
Cdd:COG4976   83 KAREKGVY-----DRLLVADLADL-AEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIF 142
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 192-308 3.89e-13

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 66.25  E-value: 3.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 192 PFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRLLILEFSKP---------------VFEPFSKLYDLysftalp 256
Cdd:PLN02232  39 PFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDFNKSnqsvttfmqgwmidnVVVPVATVYDL------- 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491220997 257 imgklvandSESYKYLAESIRMHPDQRTLKGMMENAGFQNCDYHNLTAGIVA 308
Cdd:PLN02232 112 ---------AKEYEYLKYSINGYLTGEELETLALEAGFSSACHYEISGGFMG 154
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 117-233 5.63e-12

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: 63.04  E-value: 5.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 117 RFAINMSGVRRGQHVLDIAGGTGDLAkVFSREVGPqgHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANAETLePFADN 196
Cdd:COG1041   16 RALVNLAGAKEGDTVLDPFCGTGTIL-IEAGLLGR--RVIGSDIDPKMVEGARENLEHYGYEDADVIRGDARDL-PLADE 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491220997 197 SFDLVtisfglrnVTD-------KDA----------ALASMFRVLKPGGRLLIL 233
Cdd:COG1041   92 SVDAI--------VTDppygrssKISgeellelyekALEEAARVLKPGGRVVIV 137
PRK05785 PRK05785
hypothetical protein; Provisional
 89-272 1.98e-11

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 62.78  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  89 VAEVFHSVASKYDLMNDLMSFGIHRLWKRFAINMSGVRRGQ--HVLDIAGGTGDLAKVFSREVgpQGHVVLSDINESML- 165
Cdd:PRK05785  11 LQEAYNKIPKAYDRANRFISFNQDVRWRAELVKTILKYCGRpkKVLDVAAGKGELSYHFKKVF--KYYVVALDYAENMLk 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 166 --NVGRDRlidagctnvdfVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKpgGRLLILEFSKPVFEPF 243
Cdd:PRK05785  89 mnLVADDK-----------VVGSFEAL-PFRDKSFDVVMSSFALHASDNIEKVIAEFTRVSR--KQVGFIAMGKPDNVIK 154

                        170       180
                 ....*....|....*....|....*....
gi 491220997 244 SKLYDLYSFTALPIMGKLVANDSESYKYL 272
Cdd:PRK05785 155 RKYLSFYLRYIMPYIACLAGAKCRDYKYI 183
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
124-234 4.90e-11

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 62.24  E-value: 4.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 124 GVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVV-----LSDINESMLNVGRDRLI------DAGCTNVDFVLANAETLEP 192
Cdd:COG4798   63 GVKPGMTVVEIWPGGGWYTEILAPYLGPKGKVYaanfdPDSEPPEYAKRSREAFSaklaadPALYGNVRVTAFAPPDDPI 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 491220997 193 FADNSFDLVTISfglRNV------TDKDAALASMFRVLKPGGRLLILE 234
Cdd:COG4798  143 APPGSADLVLTF---RNYhnwyraGDAAAMFAAFFKALKPGGVLGVVD 187
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 87-230 5.76e-11

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 61.70  E-value: 5.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  87 QKVAEVFHSVASKYDLMNDLMSFGIHRLwkrfaINMSGVRRGQHVLDIAGGTGDLAKVFsREVGpqGHVVLSDINESMLN 166
Cdd:PRK10258   7 QAIAAAFGRAAAHYEQHAELQRQSADAL-----LAMLPQRKFTHVLDAGCGPGWMSRYW-RERG--SQVTALDLSPPMLA 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491220997 167 VGRDRliDAGctnVDFVLANAETLePFADNSFDLVTISFGLRNVTDKDAALASMFRVLKPGGRL 230
Cdd:PRK10258  79 QARQK--DAA---DHYLAGDIESL-PLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVV 136
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 128-232 1.04e-10

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 59.82  E-value: 1.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 128 GQHVLDIAGGTGDLAKVFSREvGPQGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANAetLEPFADNSFDLVtIS--- 204
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKR-NPEARVTLVDVNARAVELARANAAANGLENVEVLWSDG--LSGVPDGSFDLI-LSnpp 125

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491220997 205 FGLRNVTDKDAALAsMF----RVLKPGGRLLI 232
Cdd:COG2813  126 FHAGRAVDKEVAHA-LIadaaRHLRPGGELWL 156
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 131-296 7.79e-10

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 56.67  E-value: 7.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  131 VLDIAGGTGDLAKVFsREVGPqgHVVLSDINESMLNVGRDrlidagctNVDFVLANAEtLEPFADNSFDLVTISFGLRNV 210
Cdd:pfam13489  26 VLDFGCGTGIFLRLL-RAQGF--SVTGVDPSPIAIERALL--------NVRFDQFDEQ-EAAVPAGKFDVIVAREVLEHV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  211 TDKDAALASMFRVLKPGGRLLILEFSKPVFEPFSKLYDLYSFtalpIMGKLVANDSEsykylaesirmhpdqRTLKGMME 290
Cdd:pfam13489  94 PDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLR----PRNGHISLFSA---------------RSLKRLLE 154


                  ....*.
gi 491220997  291 NAGFQN 296
Cdd:pfam13489 155 EAGFEV 160
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 122-233 8.76e-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: 58.25  E-value: 8.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 122 MSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVGRDRLIDAGCT-NVDFVLANAEtlEPFADNSFDL 200
Cdd:COG2519   86 RLDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPdNVELKLGDIR--EGIDEGDVDA 163

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491220997 201 VtisfglrnVTD-KD--AALASMFRVLKPGGRLLIL 233
Cdd:COG2519  164 V--------FLDmPDpwEALEAVAKALKPGGVLVAY 191
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 128-254 8.21e-09

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 56.30  E-value: 8.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 128 GQHVLD----IAGGTGDLAKVFSRevgpqgHVVLSDINESMLNVGRDRLIDAGCTnVDFVLANAeTLEPFADNSFDLVTI 203
Cdd:PLN02336 267 GQKVLDvgcgIGGGDFYMAENFDV------HVVGIDLSVNMISFALERAIGRKCS-VEFEVADC-TKKTYPDNSFDVIYS 338

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491220997 204 SFGLRNVTDKDAALASMFRVLKPGGRLLILEFSK------PVFEPFSKL--YDLYSFTA 254
Cdd:PLN02336 339 RDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRspgtpsPEFAEYIKQrgYDLHDVQA 397
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 124-240 7.92e-08

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 52.93  E-value: 7.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 124 GVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLAN-AETLEPFAdnSFDLVT 202
Cdd:PRK13943  77 GLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRRLGIENVIFVCGDgYYGVPEFA--PYDVIF 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 491220997 203 ISFGLRNVTDkdaalaSMFRVLKPGGRLLI-----LEFSKPVF 240
Cdd:PRK13943 155 VTVGVDEVPE------TWFTQLKEGGRVIVpinlkLSRRQPAF 191
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
165-291 2.22e-07

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 49.86  E-value: 2.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 165 LNVGRDRLIDAGCTNVDFV-------LANAETLEPFADNSFDLVTIS-----FGLRNVtdkDAALASMFRVLKPGGRLLI 232
Cdd:COG4627    7 LNIGCGPKRLPGWLNVDIVpapgvdiVGDLTDPLPFPDNSVDAIYSShvlehLDYEEA---PLALKECYRVLKPGGILRI 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491220997 233 ----LEFskpVFEPFSKLYDLYSFTALPIMGKLVANDS-ESYKYLAESIRMHPDQRTLKGMMEN 291
Cdd:COG4627   84 vvpdLEH---VARLYLAEYDAALDVAELRLAGPIDPLGiILGERLAGLAARHSVLFRTGFTRLA 144
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
128-232 4.71e-06

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 46.59  E-value: 4.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  128 GQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANA-ETLEPFAdnSFDLVTISFG 206
Cdd:pfam01135  74 GMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGLENVIVVVGDGrQGWPEFA--PYDAIHVGAA 151

                          90       100
                  ....*....|....*....|....*.
gi 491220997  207 LRNVTDkdaalaSMFRVLKPGGRLLI 232
Cdd:pfam01135 152 APEIPE------ALIDQLKEGGRLVI 171
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 125-232 5.77e-06

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 46.23  E-value: 5.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 125 VRRGQHVLDIAGGTGDLAKVFSREVgpqGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLAN-AETLEPFAdnSFDLVTI 203
Cdd:COG2518   64 LKPGDRVLEIGTGSGYQAAVLARLA---GRVYSVERDPELAERARERLAALGYDNVTVRVGDgALGWPEHA--PFDRIIV 138

                         90       100
                 ....*....|....*....|....*....
gi 491220997 204 SFGLRNVTDkdaALASMfrvLKPGGRLLI 232
Cdd:COG2518  139 TAAAPEVPE---ALLEQ---LAPGGRLVA 161
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 125-232 6.99e-06

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 45.66  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  125 VRRGQHVLDIAGGTGDLAKVFSREvGPQGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANAetLEPFADNSFDLVtIS 204
Cdd:pfam05175  29 KDLSGKVLDLGCGAGVLGAALAKE-SPDAELTMVDINARALESARENLAANGLENGEVVASDV--YSGVEDGKFDLI-IS 104

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 491220997  205 ---FGLRNVTDKDAALAsMF----RVLKPGGRLLI 232
Cdd:pfam05175 105 nppFHAGLATTYNVAQR-FIadakRHLRPGGELWI 138
PRK14968 PRK14968
putative methyltransferase; Provisional
 125-233 8.90e-06

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 45.66  E-value: 8.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 125 VRRGQHVLDIAGGTGDLAKVFSRevgpQGH-VVLSDINESMLNVGRDRLIDAGCTNVDFVLANAETLEPFADNSFDLVT- 202
Cdd:PRK14968  21 DKKGDRVLEVGTGSGIVAIVAAK----NGKkVVGVDINPYAVECAKCNAKLNNIRNNGVEVIRSDLFEPFRGDKFDVILf 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491220997 203 ----------------ISFGL------RNVTDKdaALASMFRVLKPGGRLLIL 233
Cdd:PRK14968  97 nppylpteeeeewddwLNYALsggkdgREVIDR--FLDEVGRYLKPGGRILLL 147
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 117-228 1.54e-05

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: 44.40  E-value: 1.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 117 RFAINMSGVRRgqhVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVGRDRLIDAGCTN-VDFVLANA-ETLEPFA 194
Cdd:COG4122    9 YLLARLLGAKR---ILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADrIRLILGDAlEVLPRLA 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491220997 195 DNSFDLVTIsfglrnvtdkDAA-------LASMFRVLKPGG 228
Cdd:COG4122   86 DGPFDLVFI----------DADksnypdyLELALPLLRPGG 116
PLN02244 PLN02244
tocopherol O-methyltransferase
 70-242 2.07e-05

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 45.51  E-value: 2.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  70 GETTHFGYSTVRTEDKAQKVAEVfhsvaskyDLMNDLMSFGihrlwkrfAINMSGVRRGQHVLDIAGGTGDLAKVFSREV 149
Cdd:PLN02244  77 GEHMHHGYYDPGASRGDHRQAQI--------RMIEESLAWA--------GVPDDDEKRPKRIVDVGCGIGGSSRYLARKY 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 150 GPQGH-VVLSDINesmLNVGRDRLIDAGCTN-VDFVLANAetLE-PFADNSFDLVTISFGLRNVTDKDAALASMFRVLKP 226
Cdd:PLN02244 141 GANVKgITLSPVQ---AARANALAAAQGLSDkVSFQVADA--LNqPFEDGQFDLVWSMESGEHMPDKRKFVQELARVAAP 215

                        170
                 ....*....|....*.
gi 491220997 227 GGRLLILEFSKPVFEP 242
Cdd:PLN02244 216 GGRIIIVTWCHRDLEP 231
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
122-201 2.61e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.12  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 122 MSGVRRGQHVLDIAGGTGDLAkVFSREVGPQgHVVLSDINESMLNVGRDRLIDAGCtNVDFVLANAETLEPfaDNSFDLV 201
Cdd:COG2263   40 LRGDIEGKTVLDLGCGTGMLA-IGAALLGAK-KVVGVDIDPEALEIARENAERLGV-RVDFIRADVTRIPL--GGSVDTV 114
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
130-230 3.28e-05

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 44.57  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 130 HVLDIAGGTGDLakvfSREVGPQGH-VVLSDINESMLNVGRDRLIDAGCT-NVDFVLANAETLEPFADNSFDLVTISFGL 207
Cdd:PRK11036  47 RVLDAGGGEGQT----AIKLAELGHqVILCDLSAEMIQRAKQAAEAKGVSdNMQFIHCAAQDIAQHLETPVDLILFHAVL 122

                         90       100
                 ....*....|....*....|...
gi 491220997 208 RNVTDKDAALASMFRVLKPGGRL 230
Cdd:PRK11036 123 EWVADPKSVLQTLWSVLRPGGAL 145
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 119-247 1.14e-04

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 42.70  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 119 AINMSGV-------RRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDINESMLNVGRDRLIDAGCTNVDFVLANAeTL- 190
Cdd:PRK13942  61 AIHMVAImcelldlKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKKLGYDNVEVIVGDG-TLg 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491220997 191 -EPFAdnSFDLVTISFGLRNVTDkdaalaSMFRVLKPGGRLLIlefskPVFEPFSKLY 247
Cdd:PRK13942 140 yEENA--PYDRIYVTAAGPDIPK------PLIEQLKDGGIMVI-----PVGSYSQELI 184
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 127-234 2.94e-04

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 41.86  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 127 RGQHVLDIAGGTGD----LAKVFSREVgpqgHVVLSDINESMLNVGRdRLIDAGC----TNVDFVLANAETLEPFAdnSF 198
Cdd:COG5459   80 APLTVLDVGAGPGTaawaAADAWPSLL----DATLLERSAAALALGR-RLARAAAnpalETAEWRLADLAAALPAP--PA 152

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491220997 199 DLVTISFGLRNVTD--KDAALASMFrvLKPGGRLLILE 234
Cdd:COG5459  153 DLVVASYVLNELADaaRAALVDRLW--LAPDGALLIVE 188
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
117-233 3.87e-04

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 41.33  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 117 RFAINMSGVRRGQHVLDIAGGTGDL---AKVFSREVGPQGHVVLS----DINESMLNVGRDRLIDAGCTNVDFVLANAET 189
Cdd:COG0286   33 RLMVELLDPKPGETVYDPACGSGGFlveAAEYLKEHGGDERKKLSlygqEINPTTYRLAKMNLLLHGIGDPNIELGDTLS 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491220997 190 LEPFADNSFDLV---------------------TISFGLRNVTDKDAA-LASMFRVLKPGGRLLIL 233
Cdd:COG0286  113 NDGDELEKFDVVlanppfggkwkkeelkddllgRFGYGLPPKSNADLLfLQHILSLLKPGGRAAVV 178
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 131-257 5.41e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 40.72  E-value: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 131 VLDIAGGTGDLAKVFSREVGPQGHVVlsDINESMLNVGRDRliDAGCTNVDFVlANAETLEPFADNSFDLVTISFGLRNV 210
Cdd:PTZ00098  56 VLDIGSGLGGGCKYINEKYGAHVHGV--DICEKMVNIAKLR--NSDKNKIEFE-ANDILKKDFPENTFDMIYSRDAILHL 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491220997 211 T--DKDAALASMFRVLKPGGRLLILEFSKPVFEPFSKLYDLY----SFTALPI 257
Cdd:PTZ00098 131 SyaDKKKLFEKCYKWLKPNGILLITDYCADKIENWDEEFKAYikkrKYTLIPI 183
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
125-231 1.53e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 39.25  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 125 VRRGQHVLDIAGGTGDLAKVFSREvgPQGHVVLSDINESMLNVGRDRLIDAGCT-NVDFVLANAETLEPfaDNSFDlVTI 203
Cdd:COG4076   33 VKPGDVVLDIGTGSGLLSMLAARA--GAKKVYAVEVNPDIAAVARRIIAANGLSdRITVINADATDLDL--PEKAD-VII 107

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491220997 204 SFGLRNVTDKDAALASMF----RVLKPGGRLL 231
Cdd:COG4076  108 SEMLDTALLDEGQVPILNharkRLLKPGGRII 139
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 118-237 1.87e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 39.48  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 118 FAINMSGVRRGQ-----HVLDI-AGGTGDLAKVFSREVGpqGHVVLSDINESML----NVGRDRLIDAGCTNVDFVLAnA 187
Cdd:cd08261  145 LAIGAHAVRRAGvtagdTVLVVgAGPIGLGVIQVAKARG--ARVIVVDIDDERLefarELGADDTINVGDEDVAARLR-E 221

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 491220997 188 ETLEPFADNSFDLVTISfglrnvtdkdAALASMFRVLKPGGRLLILEFSK 237
Cdd:cd08261  222 LTDGEGADVVIDATGNP----------ASMEEAVELVAHGGRVVLVGLSK 261
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 116-243 2.98e-03

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: 37.95  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  116 KRFAInmsgVRRGQHVLDIAGGTG---------DLAKVFSREVGPQGHvvlsdinESMLNVGRDRLIdagCTNVdFVLAN 186
Cdd:pfam01728  14 EKFGL----LKPGKTVLDLGAAPGgwsqvalqrGAGKVVGVDLGPMQL-------WKPRNDPGVTFI---QGDI-RDPET 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491220997  187 AETLEPFADNSFDLVT----ISFGLRNVTDK-------DAALASMFRVLKPGGRLLILEFSKPVFEPF 243
Cdd:pfam01728  79 LDLLEELLGRKVDLVLsdgsPFISGNKVLDHlrsldlvKAALEVALELLRKGGNFVCKVFQGEDFSEL 146
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 119-233 3.61e-03

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 38.76  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997 119 AINMSGVRRGQHVLDIAGGT-GDLAKVFSREVGpQGHVVLSDINESMLNVGR----DRLIDAGctnvdfvlanAETLEPF 193
Cdd:cd08232  157 AVNRAGDLAGKRVLVTGAGPiGALVVAAARRAG-AAEIVATDLADAPLAVARamgaDETVNLA----------RDPLAAY 225

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 491220997 194 ADNS--FDLVtisFglrNVTDKDAALASMFRVLKPGGRLLIL 233
Cdd:cd08232  226 AADKgdFDVV---F---EASGAPAALASALRVVRPGGTVVQV 261
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 118-235 4.53e-03

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: 37.43  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491220997  118 FAINMSGVRRGQHVLDIAGGTGDLAKVFSREVGPQGHVVLSDinesmlnvgRDRLIDAGCTNVDFVLANAET-LEPFADN 196
Cdd:pfam07021   4 FRYILEWIPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELD---------AAGVAECVAKGLYVIQGDLDEgLEHFPDK 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 491220997  197 SFDLVTISFGLRNVTDKDAALASMFRVlkpgGRLLILEF 235
Cdd:pfam07021  75 SFDYVILSQTLQATRNPREVLDEMLRI----GRRCIVSF 109
 
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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