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Conserved domains on  [gi|648231086|ref|WP_026012235|]
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MULTISPECIES: bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE [Vibrionaceae]

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 ...
 21-259 9.05e-153

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


:

Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 424.95  E-value: 9.05e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  21 FETVAKDEKVAKVAEVFHSVAAKYDIMNDLMSGGVHRLWKRFTIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVV 100
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 101 LADINNSMLNVGRDKLRDSGIVGNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFS 180
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648231086 181 KPVLEPLSKVYDAYSFHLLPKMGELIANDADSYRYLAESIRMHPNQETLEGMMQEAGFENTKYFNLTGGIVALHRGYKF 259
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 21-259 9.05e-153

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 424.95  E-value: 9.05e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  21 FETVAKDEKVAKVAEVFHSVAAKYDIMNDLMSGGVHRLWKRFTIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVV 100
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 101 LADINNSMLNVGRDKLRDSGIVGNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFS 180
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648231086 181 KPVLEPLSKVYDAYSFHLLPKMGELIANDADSYRYLAESIRMHPNQETLEGMMQEAGFENTKYFNLTGGIVALHRGYKF 259
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
31-258 2.81e-122

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 347.50  E-value: 2.81e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   31 AKVAEVFHSVAAKYDIMNDLMSGGVHRLWKRFTIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLN 110
Cdd:pfam01209   2 QRVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  111 VGRDKLRDSGiVGNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLEPLSKV 190
Cdd:pfam01209  82 EGEKKAKEEG-KYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648231086  191 YDAYSFHLLPKMGELIANDADSYRYLAESIRMHPNQETLEGMMQEAGFENTKYFNLTGGIVALHRGYK 258
Cdd:pfam01209 161 YELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 33-258 1.21e-114

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: 328.07  E-value: 1.21e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   33 VAEVFHSVAAKYDIMNDLMSGGVHRLWKRFTIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVG 112
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  113 RDKlrdSGIVGNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLEPLSKVYD 192
Cdd:TIGR01934  81 KKK---SELPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648231086  193 AYSFHLLPKMGELIANDADSYRYLAESIRMHPNQETLEGMMQEAGFENTKYFNLTGGIVALHRGYK 258
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 37-187 2.88e-44

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: 146.29  E-value: 2.88e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  37 FHSVAAKYDIMNDLMSggvhRLwkrftidcsGVRPGQRILDLGGGTGDLTAKFSRIVGekgHVVLADINNSMLNVGRDKL 116
Cdd:COG2226    1 FDRVAARYDGREALLA----AL---------GLRPGARVLDLGCGTGRLALALAERGA---RVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648231086 117 RDSGIvgNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLEPL 187
Cdd:COG2226   65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAEL 133
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-176 4.10e-15

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: 69.38  E-value: 4.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  74 RILDLGGGTGDLTAKFSRivGEKGHVVLADINNSMLNVGRDKLRDSGIVgNVHYVQANAEELPF-PDNYFD-CITISFCL 151
Cdd:cd02440    1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLAD-NVEVLKGDAEELPPeADESFDvIISDPPLH 77

                         90       100
                 ....*....|....*....|....*
gi 648231086 152 RNVTDKDQALRSMYRVLKPGGRLLV 176
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVLVL 102
rADc smart00650
Ribosomal RNA adenine dimethylases;
64-145 3.56e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.11  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086    64 IDCSGVRPGQRILDLGGGTGDLTakfsRIVGEKGHVVLA-DINNSMLNVGRDKLRDSgivGNVHYVQANAEELPFPDNYF 142
Cdd:smart00650   6 VRAANLRPGDTVLEIGPGKGALT----EELLERAKRVTAiEIDPRLAPRLREKFAAA---DNLTVIHGDALKFDLPKLQP 78


                   ...
gi 648231086   143 DCI 145
Cdd:smart00650  79 YKV 81
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 21-259 9.05e-153

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 424.95  E-value: 9.05e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  21 FETVAKDEKVAKVAEVFHSVAAKYDIMNDLMSGGVHRLWKRFTIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVV 100
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 101 LADINNSMLNVGRDKLRDSGIVGNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFS 180
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 648231086 181 KPVLEPLSKVYDAYSFHLLPKMGELIANDADSYRYLAESIRMHPNQETLEGMMQEAGFENTKYFNLTGGIVALHRGYKF 259
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
31-258 2.81e-122

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 347.50  E-value: 2.81e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   31 AKVAEVFHSVAAKYDIMNDLMSGGVHRLWKRFTIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLN 110
Cdd:pfam01209   2 QRVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  111 VGRDKLRDSGiVGNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLEPLSKV 190
Cdd:pfam01209  82 EGEKKAKEEG-KYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648231086  191 YDAYSFHLLPKMGELIANDADSYRYLAESIRMHPNQETLEGMMQEAGFENTKYFNLTGGIVALHRGYK 258
Cdd:pfam01209 161 YELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 33-258 1.21e-114

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: 328.07  E-value: 1.21e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   33 VAEVFHSVAAKYDIMNDLMSGGVHRLWKRFTIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVG 112
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  113 RDKlrdSGIVGNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLEPLSKVYD 192
Cdd:TIGR01934  81 KKK---SELPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648231086  193 AYSFHLLPKMGELIANDADSYRYLAESIRMHPNQETLEGMMQEAGFENTKYFNLTGGIVALHRGYK 258
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 36-251 1.09e-46

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 156.20  E-value: 1.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  36 VFHSVAAKYDIMNDLMSGGVHRLWKRFTIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVG--R 113
Cdd:PLN02233  38 LFNRIAPVYDNLNDLLSLGQHRIWKRMAVSWSGAKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAasR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 114 DKLRDSGIVGNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKP----------- 182
Cdd:PLN02233 118 QELKAKSCYKNIEWIEGDATDLPFDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKStqpfttsmqew 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 648231086 183 ----VLEPLSKVYDAysfhllpkmgeliandADSYRYLAESIRMHPNQETLEGMMQEAGFENTKYFNLTGGIV 251
Cdd:PLN02233 198 midnVVVPVATGYGL----------------AKEYEYLKSSINEYLTGEELEKLALEAGFSSAKHYEISGGLM 254
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 37-187 2.88e-44

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: 146.29  E-value: 2.88e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  37 FHSVAAKYDIMNDLMSggvhRLwkrftidcsGVRPGQRILDLGGGTGDLTAKFSRIVGekgHVVLADINNSMLNVGRDKL 116
Cdd:COG2226    1 FDRVAARYDGREALLA----AL---------GLRPGARVLDLGCGTGRLALALAERGA---RVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 648231086 117 RDSGIvgNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLEPL 187
Cdd:COG2226   65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAEL 133
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 75-172 2.38e-30

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 108.81  E-value: 2.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   75 ILDLGGGTGDLTAKFSRIVGekGHVVLADINNSMLNVGRDKLRDSGIvgNVHYVQANAEELPFPDNYFDCITISFCLRNV 154
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 648231086  155 TDKD--QALRSMYRVLKPGG 172
Cdd:pfam13649  77 PDPDleAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 60-242 5.22e-29

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 109.64  E-value: 5.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  60 KRFTIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVGRDKLRDSGivGNVHYVQANAEELPFPD 139
Cdd:PRK08317   8 RARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLG--PNVEFVRGDADGLPFPD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 140 NYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLE--FSKPVLEP-----LSKVYDAYSFHLL-PKMGeliandad 211
Cdd:PRK08317  86 GSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDtdWDTLVWHSgdralMRKILNFWSDHFAdPWLG-------- 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 648231086 212 syRYLAesirmhpnqetleGMMQEAGFENTK 242
Cdd:PRK08317 158 --RRLP-------------GLFREAGLTDIE 173
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 76-176 6.53e-25

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 94.65  E-value: 6.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   76 LDLGGGTGdltaKFSRIVGEKGHVVLA-DINNSMLNVGRDKLRDSGivgnVHYVQANAEELPFPDNYFDCITISFCLRNV 154
Cdd:pfam08241   1 LDVGCGTG----LLTELLARLGARVTGvDISPEMLELAREKAPREG----LTFVVGDAEDLPFPDNSFDLVLSSEVLHHV 72

                          90       100
                  ....*....|....*....|..
gi 648231086  155 TDKDQALRSMYRVLKPGGRLLV 176
Cdd:pfam08241  73 EDPERALREIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 69-176 9.50e-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: 95.47  E-value: 9.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  69 VRPGQRILDLGGGTGDLTAKFSRivgeKGHVVLA-DINNSMLNVGRDKLRDSgivgNVHYVQANAEELPFPDNYFDCITI 147
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALAR----RGADVTGvDISPEALEIARERAAEL----NVDFVQGDLEDLPLEDGSFDLVIC 93

                         90       100
                 ....*....|....*....|....*....
gi 648231086 148 SFCLRNVTDKDQALRSMYRVLKPGGRLLV 176
Cdd:COG2227   94 SEVLEHLPDPAALLRELARLLKPGGLLLL 122
arsM PRK11873
arsenite methyltransferase;
70-240 7.09e-22

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 91.55  E-value: 7.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  70 RPGQRILDLGGGTG-D--LTAkfsRIVGEKGHVVLADINNSMLNVGRDKLRDSGIvGNVHYVQANAEELPFPDNYFDCIt 146
Cdd:PRK11873  76 KPGETVLDLGSGGGfDcfLAA---RRVGPTGKVIGVDMTPEMLAKARANARKAGY-TNVEFRLGEIEALPVADNSVDVI- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 147 ISFCLRN-VTDKDQALRSMYRVLKPGGRLLVlefSKPVLEplskvydaysfhllpkmGEL---IANDADSYrylAESIRM 222
Cdd:PRK11873 151 ISNCVINlSPDKERVFKEAFRVLKPGGRFAI---SDVVLR-----------------GELpeeIRNDAELY---AGCVAG 207

                        170
                 ....*....|....*...
gi 648231086 223 HPNQETLEGMMQEAGFEN 240
Cdd:PRK11873 208 ALQEEEYLAMLAEAGFVD 225
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 37-200 5.18e-21

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: 88.50  E-value: 5.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   37 FHSVAAKYDIMNDLMSGGVHRLWKRftIDCSGVRPGQRILDLGGGTGDLTAKFSRiVGEKGHVVLADINNSMLNVGRDKL 116
Cdd:TIGR02072   2 FNKAAKTYDRHAKIQREMAKRLLAL--LKEKGIFIPASVLDIGCGTGYLTRALLK-RFPQAEFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  117 RdsgivGNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGrllVLEFSKPVLEPLSKVYDAYSF 196
Cdd:TIGR02072  79 S-----ENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGG---LLAFSTFGPGTLHELRQSFGQ 150


                  ....
gi 648231086  197 HLLP 200
Cdd:TIGR02072 151 HGLR 154
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 70-180 2.22e-20

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 84.39  E-value: 2.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   70 RPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVGRDKLRDSGIvGNVHYVQANAEELP--FPDNYFDCItI 147
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPelLEDDKFDVV-I 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 648231086  148 SFCLRN-VTDKDQALRSMYRVLKPGGRLLVLEFS 180
Cdd:pfam13847  80 SNCVLNhIPDPDKVLQEILRVLKPGGRLIISDPD 113
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
71-176 7.21e-20

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 81.79  E-value: 7.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  71 PGQRILDLGGGTGDLTAKFSRIVGEkGHVVLADINNSMLNVGRDKLrdsgivGNVHYVQANAEELPFPDNyFDCITISFC 150
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPG-ARVTGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEP-FDLVVSNAA 72

                         90       100
                 ....*....|....*....|....*.
gi 648231086 151 LRNVTDKDQALRSMYRVLKPGGRLLV 176
Cdd:COG4106   73 LHWLPDHAALLARLAAALAPGGVLAV 98
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 103-252 1.06e-19

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 83.20  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 103 DINNSMLNVG--RDKLRDSGIVGNVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFS 180
Cdd:PLN02232   4 DFSSEQLAVAatRQSLKARSCYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDFN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 181 KP---------------VLEPLSKVYDAysfhllpkmgeliandADSYRYLAESIRMHPNQETLEGMMQEAGFENTKYFN 245
Cdd:PLN02232  84 KSnqsvttfmqgwmidnVVVPVATVYDL----------------AKEYEYLKYSINGYLTGEELETLALEAGFSSACHYE 147


                 ....*..
gi 648231086 246 LTGGIVA 252
Cdd:PLN02232 148 ISGGFMG 154
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 58-176 3.39e-17

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 77.26  E-value: 3.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  58 LWKRFTIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGekGHVVLADINNSMLNVGRDKLRDSGIvGNVHYVQANAEEL-P 136
Cdd:COG0500   13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELdP 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 648231086 137 FPDNYFDCITISFCLR--NVTDKDQALRSMYRVLKPGGRLLV 176
Cdd:COG0500   90 LPAESFDLVVAFGVLHhlPPEEREALLRELARALKPGGVLLL 131
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 67-193 3.41e-15

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: 72.88  E-value: 3.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  67 SGVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVGRDKLRDSGIVGNVHYVQANAEElPFPDNYFDCIT 146
Cdd:COG2519   87 LDIFPGARVLEAGTGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIRE-GIDEGDVDAVF 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 648231086 147 IsfclrNVTDKDQALRSMYRVLKPGGRLLVLefsKPVLEPLSKVYDA 193
Cdd:COG2519  166 L-----DMPDPWEALEAVAKALKPGGVLVAY---VPTVNQVSKLVEA 204
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 76-174 4.10e-15

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 68.93  E-value: 4.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   76 LDLGGGTGDLTAKFSRIVGEkGHVVLADINNSMLNVGRDKLRDSGI--VGNVHYVQANAEELPFPDnyFDCITISFCLRN 153
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPG-LEYTGLDISPAALEAARERLAALGLlnAVRVELFQLDLGELDPGS--FDVVVASNVLHH 77

                          90       100
                  ....*....|....*....|.
gi 648231086  154 VTDKDQALRSMYRVLKPGGRL 174
Cdd:pfam08242  78 LADPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-176 4.10e-15

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: 69.38  E-value: 4.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  74 RILDLGGGTGDLTAKFSRivGEKGHVVLADINNSMLNVGRDKLRDSGIVgNVHYVQANAEELPF-PDNYFD-CITISFCL 151
Cdd:cd02440    1 RVLDLGCGTGALALALAS--GPGARVTGVDISPVALELARKAAAALLAD-NVEVLKGDAEELPPeADESFDvIISDPPLH 77

                         90       100
                 ....*....|....*....|....*
gi 648231086 152 RNVTDKDQALRSMYRVLKPGGRLLV 176
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVLVL 102
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
31-175 1.29e-14

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 70.03  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  31 AKVAEVFHSVAAKYDimNDLMSGGVHRLWKRF---TIDCSGVRPGQRILDLGGGTGDLTAKFSRIVGekgHVVLADINNS 107
Cdd:COG4976    5 AYVEALFDQYADSYD--AALVEDLGYEAPALLaeeLLARLPPGPFGRVLDLGCGTGLLGEALRPRGY---RLTGVDLSEE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648231086 108 MLNVGRDKLRDsgivgnVHYVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLL 175
Cdd:COG4976   80 MLAKAREKGVY------DRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 68-176 3.12e-14

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 68.42  E-value: 3.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  68 GVRPGQRILDLGGGTGDLTAkfsRIVGEKGHVVLA-DINNSMLNVGRDKLRDSGIVGNVHYVQANAEELPfPDNYFDCIT 146
Cdd:COG2230   48 GLKPGMRVLDIGCGWGGLAL---YLARRYGVRVTGvTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADGQFDAIV 123

                         90       100       110
                 ....*....|....*....|....*....|..
gi 648231086 147 I--SFCLRNVTDKDQALRSMYRVLKPGGRLLV 176
Cdd:COG2230  124 SigMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 55-241 5.41e-14

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 67.84  E-value: 5.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   55 VHRLWKRFTIDCSGVRP-GQRILDLGGGTGdltaKFSRIVGEKG-HVVLADINNSMLNVGRDklrdsgivgNVHYVQANA 132
Cdd:pfam13489   5 RERLLADLLLRLLPKLPsPGRVLDFGCGTG----IFLRLLRAQGfSVTGVDPSPIAIERALL---------NVRFDQFDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  133 EELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLEPLSKVYDAYSFHllpkMGELIAndads 212
Cdd:pfam13489  72 QEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRP----RNGHIS----- 142

                         170       180
                  ....*....|....*....|....*....
gi 648231086  213 yrylaesirmHPNQETLEGMMQEAGFENT 241
Cdd:pfam13489 143 ----------LFSARSLKRLLEEAGFEVV 161
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
68-239 2.85e-11

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 61.86  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  68 GVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLA-----DINNSMLNVGRDKLR-----DSGIVGNVHYVQANAEELPF 137
Cdd:COG4798   63 GVKPGMTVVEIWPGGGWYTEILAPYLGPKGKVYAAnfdpdSEPPEYAKRSREAFSaklaaDPALYGNVRVTAFAPPDDPI 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 138 -PDNYFDCITISfclRNV------TDKDQALRSMYRVLKPGGRLLVLEfskpvleplskvydaysfHLLPKMGELiaNDA 210
Cdd:COG4798  143 aPPGSADLVLTF---RNYhnwyraGDAAAMFAAFFKALKPGGVLGVVD------------------HRAPPGTGL--EAV 199

                        170       180       190
                 ....*....|....*....|....*....|.
gi 648231086 211 DSYRYLAES--IRmhpnqetlegMMQEAGFE 239
Cdd:COG4798  200 ATLGYIDEAyvIA----------LAEAAGFE 220
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 71-174 4.09e-10

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 58.62  E-value: 4.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  71 PGQR---ILDLGGGTGDLtakfSRIVGEKGHVVLA-DINNSMLNVGRDKLRDSgivgnvHYVQANAEELPFPDNYFDCIT 146
Cdd:PRK10258  39 PQRKfthVLDAGCGPGWM----SRYWRERGSQVTAlDLSPPMLAQARQKDAAD------HYLAGDIESLPLATATFDLAW 108

                         90       100
                 ....*....|....*....|....*...
gi 648231086 147 ISFCLRNVTDKDQALRSMYRVLKPGGRL 174
Cdd:PRK10258 109 SNLAVQWCGNLSTALRELYRVVRPGGVV 136
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
68-176 6.86e-10

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 57.38  E-value: 6.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   68 GVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVGRDKLRDSGIvGNVHYVQAN-----AEELPfpdnyF 142
Cdd:pfam01135  70 ELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGL-ENVIVVVGDgrqgwPEFAP-----Y 143

                          90       100       110
                  ....*....|....*....|....*....|....
gi 648231086  143 DCITISFCLRNVTdkdQALrsmYRVLKPGGRLLV 176
Cdd:pfam01135 144 DAIHVGAAAPEIP---EAL---IDQLKEGGRLVI 171
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 67-177 1.05e-08

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: 53.41  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  67 SGVRPGQRILD--LGGGTgdlTAKFSRIVGekGHVVLADINNSMLNVGRDKLRDSGIvGNVHYVQANAEELPFPDNYFDC 144
Cdd:COG1041   22 AGAKEGDTVLDpfCGTGT---ILIEAGLLG--RRVIGSDIDPKMVEGARENLEHYGY-EDADVIRGDARDLPLADESVDA 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 648231086 145 ItisfclrnVTD--------------KD---QALRSMYRVLKPGGRLLVL 177
Cdd:COG1041   96 I--------VTDppygrsskisgeelLElyeKALEEAARVLKPGGRVVIV 137
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
74-174 1.15e-08

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 54.20  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  74 RILDLGGGTGdltaKFSRIVGEKGH-VVLADINNSMLNVGRDKLRDSGIVGNVHYVQANAEEL-PFPDNYFDCITISFCL 151
Cdd:PRK11036  47 RVLDAGGGEG----QTAIKLAELGHqVILCDLSAEMIQRAKQAAEAKGVSDNMQFIHCAAQDIaQHLETPVDLILFHAVL 122

                         90       100
                 ....*....|....*....|...
gi 648231086 152 RNVTDKDQALRSMYRVLKPGGRL 174
Cdd:PRK11036 123 EWVADPKSVLQTLWSVLRPGGAL 145
PRK05785 PRK05785
hypothetical protein; Provisional
 33-216 4.13e-08

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 52.38  E-value: 4.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  33 VAEVFHSVAAKYDIMNDLMS-GGVHRlWKRFTID-----CSgvRPGqRILDLGGGTGDLTAKFSRIVgeKGHVVLADINN 106
Cdd:PRK05785  11 LQEAYNKIPKAYDRANRFISfNQDVR-WRAELVKtilkyCG--RPK-KVLDVAAGKGELSYHFKKVF--KYYVVALDYAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 107 SML---NVGRDKlrdsgivgnvhyVQANAEELPFPDNYFDCITISFCLRNVTDKDQALRSMYRVLKpgGRLLVLEFSKPV 183
Cdd:PRK05785  85 NMLkmnLVADDK------------VVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAEFTRVSR--KQVGFIAMGKPD 150

                        170       180       190
                 ....*....|....*....|....*....|...
gi 648231086 184 LEPLSKVYDAYSFHLLPKMGELIANDADSYRYL 216
Cdd:PRK05785 151 NVIKRKYLSFYLRYIMPYIACLAGAKCRDYKYI 183
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 71-206 5.26e-08

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 52.97  E-value: 5.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  71 PGQRILDLGGGTGDLTAKFSRIVGEKgHVVLADINNSMLNVGRDK--LRDSGIVgnvhyvQANAEELPFPDNYFDCITIS 148
Cdd:PLN02490 113 RNLKVVDVGGGTGFTTLGIVKHVDAK-NVTILDQSPHQLAKAKQKepLKECKII------EGDAEDLPFPTDYADRYVSA 185

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 648231086 149 FCLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLePLSKVYdAYSFHLLPKMGELI 206
Cdd:PLN02490 186 GSIEYWPDPQRGIKEAYRVLKIGGKACLIGPVHPTF-WLSRFF-ADVWMLFPKEEEYI 241
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 67-185 7.67e-08

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 51.20  E-value: 7.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   67 SGVRPGQRILDLGGGTGDL-----TAKFSRIVGEKGHVVLA-----DINNSMLNVGRDKLRDSGIVGNVHYVQANAEELP 136
Cdd:pfam01170  24 AGWKPGDPLLDPMCGSGTIlieaaLMGANIAPGKFDARVRAplygsDIDRRMVQGARLNAENAGVGDLIEFVQADAADLP 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648231086  137 FPDNYFDCItisfclrnVTDK----------------DQALRSMYRVLKPGGRLLVLEFSKPVLE 185
Cdd:pfam01170 104 LLEGSVDVI--------VTNPpygirlgskgalealyPEFLREAKRVLRGGGWLVLLTAENKDFE 160
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 69-194 1.50e-07

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 51.68  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  69 VRPGQRILDLGGGTGDltAKFSRIVGEKGHVVLADINNSMLNVGRDklRDSGIVGNVHYVQANAEELPFPDNYFDCITIS 148
Cdd:PLN02336 264 LKPGQKVLDVGCGIGG--GDFYMAENFDVHVVGIDLSVNMISFALE--RAIGRKCSVEFEVADCTKKTYPDNSFDVIYSR 339

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 648231086 149 FCLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLEPlSKVYDAY 194
Cdd:PLN02336 340 DTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTP-SPEFAEY 384
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
69-175 3.49e-07

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 49.65  E-value: 3.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  69 VRPGQRILDLGGGTGDLTAKFSRIvgEKGHVVLADINNSMLNVGRDKLRDSGIVGNVHYVQANAEELPFPdNYFDcITIS 148
Cdd:COG4076   33 VKPGDVVLDIGTGSGLLSMLAARA--GAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLP-EKAD-VIIS 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 648231086 149 FCLRNVTDKDQALR----SMYRVLKPGGRLL 175
Cdd:COG4076  109 EMLDTALLDEGQVPilnhARKRLLKPGGRII 139
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 69-176 4.72e-07

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 48.93  E-value: 4.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  69 VRPGQRILDLGGGTGDLTAKFSRIVGekgHVVLADINNSMLNVGRDKLRDSGIvGNVHYVQAN-----AEELPFpdnyfD 143
Cdd:COG2518   64 LKPGDRVLEIGTGSGYQAAVLARLAG---RVYSVERDPELAERARERLAALGY-DNVTVRVGDgalgwPEHAPF-----D 134

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 648231086 144 CITISFCLRNVTD--KDQalrsmyrvLKPGGRLLV 176
Cdd:COG2518  135 RIIVTAAAPEVPEalLEQ--------LAPGGRLVA 161
PLN02244 PLN02244
tocopherol O-methyltransferase
 74-194 7.78e-07

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 49.36  E-value: 7.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  74 RILDLGGGTGD----LTAKFSRIVgeKGhVVLADINnsmLNVGRDKLRDSGIVGNVHYVQANAEELPFPDNYFDCITISF 149
Cdd:PLN02244 121 RIVDVGCGIGGssryLARKYGANV--KG-ITLSPVQ---AARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSME 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 648231086 150 CLRNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLEP------------LSKVYDAY 194
Cdd:PLN02244 195 SGEHMPDKRKFVQELARVAAPGGRIIIVTWCHRDLEPgetslkpdeqklLDKICAAY 251
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 72-176 1.34e-06

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 48.69  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  72 GQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVGRDKLRDSGIvGNVHYVQANAEELPFPDNYFDCITISFCL 151
Cdd:PRK13943  81 GMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRRLGI-ENVIFVCGDGYYGVPEFAPYDVIFVTVGV 159

                         90       100
                 ....*....|....*....|....*
gi 648231086 152 RNVTDkdqalrSMYRVLKPGGRLLV 176
Cdd:PRK13943 160 DEVPE------TWFTQLKEGGRVIV 178
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
62-141 1.41e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.51  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  62 FTIDCSGVRPGQRILDLGGGTGDLtAKFSRIVGEKgHVVLADINNSMLNVGRDKLRDSGivGNVHYVQANAEELPFPDNY 141
Cdd:COG2263   36 HLAYLRGDIEGKTVLDLGCGTGML-AIGAALLGAK-KVVGVDIDPEALEIARENAERLG--VRVDFIRADVTRIPLGGSV 111
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
135-240 2.59e-05

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 43.32  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086 135 LPFPDNYFDCITISFCLRNVTDKD--QALRSMYRVLKPGGRLLV----LEFskpVLEPLSKVYDAYSFHLLPKMGELIAN 208
Cdd:COG4627   40 LPFPDNSVDAIYSSHVLEHLDYEEapLALKECYRVLKPGGILRIvvpdLEH---VARLYLAEYDAALDVAELRLAGPIDP 116

                         90       100       110
                 ....*....|....*....|....*....|..
gi 648231086 209 DADSYRYLAESIRMHPNQETLEGMMQEAGFEN 240
Cdd:COG4627  117 LGIILGERLAGLAARHSVLFRTGFTRLALTAR 148
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 69-179 2.68e-05

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: 43.60  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   69 VRPGQRILDLGGGTGDLTakfsRIVGEKGHVVLADINNSMLNVGRdklrdsGIVGNVHYVQANAEE--LPFPDNYFDCIT 146
Cdd:pfam07021  11 IPPGSRVLDLGCGDGTLL----YLLKEEKGVDGYGIELDAAGVAE------CVAKGLYVIQGDLDEglEHFPDKSFDYVI 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 648231086  147 ISFCLRNVTDKDQALRSMYRVlkpgGRLLVLEF 179
Cdd:pfam07021  81 LSQTLQATRNPREVLDEMLRI----GRRCIVSF 109
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 69-176 3.18e-05

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: 43.64  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  69 VRPGQRILDLGGGTGDLTAKFSRIVGEkGHVVLADINNSMLNVGRDKLRDSGiVGNVHYVQANAEElPFPDNYFDCItIS 148
Cdd:COG2813   47 EPLGGRVLDLGCGYGVIGLALAKRNPE-ARVTLVDVNARAVELARANAAANG-LENVEVLWSDGLS-GVPDGSFDLI-LS 122

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 648231086 149 fclrN------VTDKDQALRSM----YRVLKPGGRLLV 176
Cdd:COG2813  123 ----NppfhagRAVDKEVAHALiadaARHLRPGGELWL 156
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 56-126 3.24e-05

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 44.02  E-value: 3.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648231086   56 HRLWKRFTIDCS------GVRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVGRDKLRDSGIVGNVH 126
Cdd:pfam08704  19 HRTQILYTPDISlitmmlELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRADKAREEFREHGIDQLVT 95
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 73-178 1.07e-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: 42.64  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  73 QRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVGRDKLRDSGIVG--NVHYVQANAEElPFPDNYFDCITISFC 150
Cdd:COG5459   82 LTVLDVGAGPGTAAWAAADAWPSLLDATLLERSAAALALGRRLARAAANPAleTAEWRLADLAA-ALPAPPADLVVASYV 160

                         90       100       110
                 ....*....|....*....|....*....|
gi 648231086 151 LRNVTDKDQA--LRSMYrvLKPGGRLLVLE 178
Cdd:COG5459  161 LNELADAARAalVDRLW--LAPDGALLIVE 188
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 69-190 2.55e-04

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 40.94  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  69 VRPGQRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVGRDKLRDSGIVGNVHYVQANAEE-LPFPDNYFDCITI 147
Cdd:PRK00377  38 LRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEAPEiLFTINEKFDRIFI 117

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 648231086 148 SFCLRNVtdkDQALRSMYRVLKPGGRLLV----LEFSKPVLEPLSKV 190
Cdd:PRK00377 118 GGGSEKL---KEIISASWEIIKKGGRIVIdailLETVNNALSALENI 161
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 71-194 8.04e-04

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 39.95  E-value: 8.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  71 PGQRILDLGGGTGDltakFSRIVGEK--GHVVLADINNSMLNVGRDKLRDSGivgNVHYVQANAEELPFPDNYFDCITIS 148
Cdd:PTZ00098  52 ENSKVLDIGSGLGG----GCKYINEKygAHVHGVDICEKMVNIAKLRNSDKN---KIEFEANDILKKDFPENTFDMIYSR 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 648231086 149 FCLRNVT--DKDQALRSMYRVLKPGGRLLVLEFSKPVLEPLSKVYDAY 194
Cdd:PTZ00098 125 DAILHLSyaDKKKLFEKCYKWLKPNGILLITDYCADKIENWDEEFKAY 172
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 69-176 1.23e-03

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: 38.73  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   69 VRPGQRILDLGGGTGDLTAKFSRIVGEkGHVVLADINNSMLNVGRDKLRDSGiVGNVHYVQANAEElPFPDNYFDCItIS 148
Cdd:pfam05175  29 KDLSGKVLDLGCGAGVLGAALAKESPD-AELTMVDINARALESARENLAANG-LENGEVVASDVYS-GVEDGKFDLI-IS 104

                          90       100       110
                  ....*....|....*....|....*....|....
gi 648231086  149 ---FCLRNVTDKDQA---LRSMYRVLKPGGRLLV 176
Cdd:pfam05175 105 nppFHAGLATTYNVAqrfIADAKRHLRPGGELWI 138
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 73-172 1.34e-03

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 38.63  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  73 QRILDLGGGTGDLTAKFSRIVGEKGHVVLADINNSMLNVGRDKLRDSGIVGNVHYVQANAEE-LP-FPDNYFDCItisFC 150
Cdd:COG4122   18 KRILEIGTGTGYSTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEvLPrLADGPFDLV---FI 94

                         90       100
                 ....*....|....*....|....*
gi 648231086 151 lrnVTDKDQ---ALRSMYRVLKPGG 172
Cdd:COG4122   95 ---DADKSNypdYLELALPLLRPGG 116
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 69-185 1.63e-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: 38.34  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086   69 VRPGQRILDLGGGTGdltaKFSRIVGEKG--HVVLADINNSMLNVGRDKLRDSGIVGNVHYVQANAEELPFPDNYFDCIT 146
Cdd:pfam01728  19 LKPGKTVLDLGAAPG----GWSQVALQRGagKVVGVDLGPMQLWKPRNDPGVTFIQGDIRDPETLDLLEELLGRKVDLVL 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 648231086  147 ----ISFCLRNVTDkdqALRSMY----------RVLKPGGRLLVLEFSKPVLE 185
Cdd:pfam01728  95 sdgsPFISGNKVLD---HLRSLDlvkaalevalELLRKGGNFVCKVFQGEDFS 144
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 68-181 3.02e-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: 38.32  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  68 GVRPGQRILDLG-GGTGDLTAKFSRIVGekGHVVLADINNSMLNVGRDKLRDSGIVGNVHYVQANAEEL---PFPDNYFD 143
Cdd:cd08261  156 GVTAGDTVLVVGaGPIGLGVIQVAKARG--ARVIVVDIDDERLEFARELGADDTINVGDEDVAARLRELtdgEGADVVID 233

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 648231086 144 CITISfclrnvtdkdQALRSMYRVLKPGGRLLVLEFSK 181
Cdd:cd08261  234 ATGNP----------ASMEEAVELVAHGGRVVLVGLSK 261
rADc smart00650
Ribosomal RNA adenine dimethylases;
64-145 3.56e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.11  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086    64 IDCSGVRPGQRILDLGGGTGDLTakfsRIVGEKGHVVLA-DINNSMLNVGRDKLRDSgivGNVHYVQANAEELPFPDNYF 142
Cdd:smart00650   6 VRAANLRPGDTVLEIGPGKGALT----EELLERAKRVTAiEIDPRLAPRLREKFAAA---DNLTVIHGDALKFDLPKLQP 78


                   ...
gi 648231086   143 DCI 145
Cdd:smart00650  79 YKV 81
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 69-177 3.87e-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: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  69 VRPGQRILDLGGGTGD----LTAKFSrivgeKGHVVLADINNSMLNVGRDKLRDSGIVGNVHYVQANAEELP--FPDNYF 142
Cdd:COG4123   35 VKKGGRVLDLGTGTGVialmLAQRSP-----GARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAaeLPPGSF 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 648231086 143 DCIT--------ISFCLRNVTDKDQA-----------LRSMYRVLKPGGRL-LVL 177
Cdd:COG4123  110 DLVVsnppyfkaGSGRKSPDEARAIArhedaltledlIRAAARLLKPGGRFaLIH 164
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 67-222 5.17e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (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 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, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 37.30  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086  67 SGVRPGQRILDLG-GGTGDLTAKFSRIVGekGHVVLADINNSMLNVGRDKLRDSGIvgNVHYVQANAEELPFPDNYFDCI 145
Cdd:cd05188  130 GVLKPGDTVLVLGaGGVGLLAAQLAKAAG--ARVIVTDRSDEKLELAKELGADHVI--DYKEEDLEEELRLTGGGGADVV 205

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648231086 146 TisfclrNVTDKDQALRSMYRVLKPGGRLLVLEFSKPVLEPlskvydAYSFHLLPKMGELIANDADSYRYLAESIRM 222
Cdd:cd05188  206 I------DAVGGPETLAQALRLLRPGGRIVVVGGTSGGPPL------DDLRRLLFKELTIIGSTGGTREDFEEALDL 270
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
74-207 5.64e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.01  E-value: 5.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648231086    74 RILDLGGGTG-DLTAKFSRivgeKGHVVLADINNS--MLNVGRDKLRDSGIVGNVHYVQANAEELPFPDNYfDCITISFC 150
Cdd:smart00828   2 RVLDFGCGYGsDLIDLAER----HPHLQLHGYTISpeQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTY-DLVFGFEV 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 648231086   151 LRNVTDKDQALRSMYRVLKPGGRLLVLEFskpVLEPLSKVYDAYSFHLLPKMGELIA 207
Cdd:smart00828  77 IHHIKDKMDLFSNISRHLKDGGHLVLADF---IANLLSAIEHEETTSYLVTREEWAE 130
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 71-135 8.39e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 36.74  E-value: 8.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648231086  71 PGQRILDLGGGTGDLTAkfsRIVGEKGHVVLADINNSMLNVGRDKLRDSGIVGNVHYVQANAEEL 135
Cdd:PRK07580  63 TGLRILDAGCGVGSLSI---PLARRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGDLESL 124
 
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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