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Conserved domains on  [gi|743523842|ref|WP_039041078|]
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MULTISPECIES: bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE [Aeromonas]

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 ...
 12-250 2.30e-148

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


:

Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 413.39  E-value: 2.30e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  12 YKTVAATEKETLVAGVFHSVAAKYDLMNDLMSFGIHRLWKRFTIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVV 91
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  92 LADINDSMLKVGRDKLRNLGVANNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFS 171
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743523842 172 KPVSEVIAKLYDLYSFKLLPKMGEIVANDSESYKYLAESIRMHPDQQTLAGMMENVGFEQVEFYNLTQGVVALHRGYKF 250
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 12-250 2.30e-148

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 413.39  E-value: 2.30e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  12 YKTVAATEKETLVAGVFHSVAAKYDLMNDLMSFGIHRLWKRFTIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVV 91
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  92 LADINDSMLKVGRDKLRNLGVANNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFS 171
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743523842 172 KPVSEVIAKLYDLYSFKLLPKMGEIVANDSESYKYLAESIRMHPDQQTLAGMMENVGFEQVEFYNLTQGVVALHRGYKF 250
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
21-249 5.95e-120

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 341.34  E-value: 5.95e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   21 ETLVAGVFHSVAAKYDLMNDLMSFGIHRLWKRFTIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSML 100
Cdd:pfam01209   1 EQRVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  101 KVGRDKLRNLGVANnVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFSKPVSEVIAK 180
Cdd:pfam01209  81 KEGEKKAKEEGKYN-IEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743523842  181 LYDLYSFKLLPKMGEIVANDSESYKYLAESIRMHPDQQTLAGMMENVGFEQVEFYNLTQGVVALHRGYK 249
Cdd:pfam01209 160 AYELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 24-249 6.63e-115

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: 6.63e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   24 VAGVFHSVAAKYDLMNDLMSFGIHRLWKRFTIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSMLKVG 103
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  104 RDKLRnlgVANNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFSKPVSEVIAKLYD 183
Cdd:TIGR01934  81 KKKSE---LPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743523842  184 LYSFKLLPKMGEIVANDSESYKYLAESIRMHPDQQTLAGMMENVGFEQVEFYNLTQGVVALHRGYK 249
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 28-181 7.71e-43

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: 142.44  E-value: 7.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  28 FHSVAAKYDLMNDLmsfgIHRLwkrftidcsGVRKGQKVLDLAGGTGDLTAKFSRivgETGQVVLADINDSMLKVGRDKL 107
Cdd:COG2226    1 FDRVAARYDGREAL----LAAL---------GLRPGARVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743523842 108 RNLGVanNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFSKPVSEVIAKL 181
Cdd:COG2226   65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 65-167 2.67e-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: 69.77  E-value: 2.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  65 KVLDLAGGTGDLTAKFSRIVGetGQVVLADINDSMLKVGRDKLRNLGvANNVSYVQANAEALPF-PDNHFD-VITIGFGL 142
Cdd:cd02440    1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKAAAALL-ADNVEVLKGDAEELPPeADESFDvIISDPPLH 77

                         90       100
                 ....*....|....*....|....*
gi 743523842 143 RNVTDKDKALASMFRVLKPGGRLLV 167
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVLVL 102
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
65-177 3.20e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.78  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842    65 KVLDLAGGTG----DLTAKFS--RIVGETgqvvladINDSMLKVGRDKLRNLGVANNVSYVQANAEALPFPDNhFDVItI 138
Cdd:smart00828   2 RVLDFGCGYGsdliDLAERHPhlQLHGYT-------ISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDT-YDLV-F 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 743523842   139 GFG-LRNVTDKDKALASMFRVLKPGGRLLVLEF-SKPVSEV 177
Cdd:smart00828  73 GFEvIHHIKDKMDLFSNISRHLKDGGHLVLADFiANLLSAI 113
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 12-250 2.30e-148

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 413.39  E-value: 2.30e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  12 YKTVAATEKETLVAGVFHSVAAKYDLMNDLMSFGIHRLWKRFTIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVV 91
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  92 LADINDSMLKVGRDKLRNLGVANNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFS 171
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743523842 172 KPVSEVIAKLYDLYSFKLLPKMGEIVANDSESYKYLAESIRMHPDQQTLAGMMENVGFEQVEFYNLTQGVVALHRGYKF 250
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
21-249 5.95e-120

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 341.34  E-value: 5.95e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   21 ETLVAGVFHSVAAKYDLMNDLMSFGIHRLWKRFTIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSML 100
Cdd:pfam01209   1 EQRVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  101 KVGRDKLRNLGVANnVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFSKPVSEVIAK 180
Cdd:pfam01209  81 KEGEKKAKEEGKYN-IEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQ 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743523842  181 LYDLYSFKLLPKMGEIVANDSESYKYLAESIRMHPDQQTLAGMMENVGFEQVEFYNLTQGVVALHRGYK 249
Cdd:pfam01209 160 AYELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 24-249 6.63e-115

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: 6.63e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   24 VAGVFHSVAAKYDLMNDLMSFGIHRLWKRFTIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSMLKVG 103
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  104 RDKLRnlgVANNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFSKPVSEVIAKLYD 183
Cdd:TIGR01934  81 KKKSE---LPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743523842  184 LYSFKLLPKMGEIVANDSESYKYLAESIRMHPDQQTLAGMMENVGFEQVEFYNLTQGVVALHRGYK 249
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 27-242 5.87e-45

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 151.58  E-value: 5.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  27 VFHSVAAKYDLMNDLMSFGIHRLWKRFTIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSMLKVG--R 104
Cdd:PLN02233  38 LFNRIAPVYDNLNDLLSLGQHRIWKRMAVSWSGAKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAasR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842 105 DKLRNLGVANNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFSKPVSEVIAKLYDL 184
Cdd:PLN02233 118 QELKAKSCYKNIEWIEGDATDLPFDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEW 197

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 743523842 185 YSFKLLPKMGEiVANDSESYKYLAESIRMHPDQQTLAGMMENVGFEQVEFYNLTQGVV 242
Cdd:PLN02233 198 MIDNVVVPVAT-GYGLAKEYEYLKSSINEYLTGEELEKLALEAGFSSAKHYEISGGLM 254
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 28-181 7.71e-43

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: 142.44  E-value: 7.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  28 FHSVAAKYDLMNDLmsfgIHRLwkrftidcsGVRKGQKVLDLAGGTGDLTAKFSRivgETGQVVLADINDSMLKVGRDKL 107
Cdd:COG2226    1 FDRVAARYDGREAL----LAAL---------GLRPGARVLDLGCGTGRLALALAE---RGARVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743523842 108 RNLGVanNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFSKPVSEVIAKL 181
Cdd:COG2226   65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEEL 136
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 66-163 6.12e-29

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 104.95  E-value: 6.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   66 VLDLAGGTGDLTAKFSRIVGetGQVVLADINDSMLKVGRDKLRNLGVanNVSYVQANAEALPFPDNHFDVITIGFGLRNV 145
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 743523842  146 TDKD--KALASMFRVLKPGG 163
Cdd:pfam13649  77 PDPDleAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 51-170 5.00e-27

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 104.25  E-value: 5.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  51 KRFTIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSMLKVGRDKLRNLGVanNVSYVQANAEALPFPD 130
Cdd:PRK08317   8 RARTFELLAVQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLGP--NVEFVRGDADGLPFPD 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 743523842 131 NHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEF 170
Cdd:PRK08317  86 GSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDT 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 67-167 1.11e-22

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 88.49  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   67 LDLAGGTGDLTAKFSRIVGetgQVVLADINDSMLKVGRDKLRNLGVannvSYVQANAEALPFPDNHFDVITIGFGLRNVT 146
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA---RVTGVDISPEMLELAREKAPREGL----TFVVGDAEDLPFPDNSFDLVLSSEVLHHVE 73

                          90       100
                  ....*....|....*....|.
gi 743523842  147 DKDKALASMFRVLKPGGRLLV 167
Cdd:pfam08241  74 DPERALREIARVLKPGGILII 94
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 61-184 1.93e-21

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 87.09  E-value: 1.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   61 RKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSMLKVGRDKLRNLGVAnNVSYVQANAEALP--FPDNHFDVITI 138
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGFD-NVEFEQGDIEELPelLEDDKFDVVIS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 743523842  139 GFGLRNVTDKDKALASMFRVLKPGGRLLVLEFSkPVSEVIAKLYDL 184
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPD-SLAELPAHVKED 125
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 60-167 5.09e-21

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: 5.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  60 VRKGQKVLDLAGGTGDLTAKFSRivgeTG-QVVLADINDSMLKVGRDKLRNLgvanNVSYVQANAEALPFPDNHFDVITI 138
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALAR----RGaDVTGVDISPEALEIARERAAEL----NVDFVQGDLEDLPLEDGSFDLVIC 93

                         90       100
                 ....*....|....*....|....*....
gi 743523842 139 GFGLRNVTDKDKALASMFRVLKPGGRLLV 167
Cdd:COG2227   94 SEVLEHLPDPAALLRELARLLKPGGLLLL 122
arsM PRK11873
arsenite methyltransferase;
61-167 9.67e-19

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 82.69  E-value: 9.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  61 RKGQKVLDLAGGTG-D--LTAkfsRIVGETGQVVLADINDSMLKVGRDKLRNLGVaNNVSYVQANAEALPFPDNHFDVIt 137
Cdd:PRK11873  76 KPGETVLDLGSGGGfDcfLAA---RRVGPTGKVIGVDMTPEMLAKARANARKAGY-TNVEFRLGEIEALPVADNSVDVI- 150

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 743523842 138 igfgLRN-----VTDKDKALASMFRVLKPGGRLLV 167
Cdd:PRK11873 151 ----ISNcvinlSPDKERVFKEAFRVLKPGGRFAI 181
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 28-214 2.00e-17

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: 78.48  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   28 FHSVAAKYDLMNDLMSFGIHRLWKRftIDCSGVRKGQKVLDLAGGTGDLTAKFSRiVGETGQVVLADINDSMLKVGRDKL 107
Cdd:TIGR02072   2 FNKAAKTYDRHAKIQREMAKRLLAL--LKEKGIFIPASVLDIGCGTGYLTRALLK-RFPQAEFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  108 RnlgvaNNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGrllVLEFSKPVSEVIAKLYDLYSF 187
Cdd:TIGR02072  79 S-----ENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGG---LLAFSTFGPGTLHELRQSFGQ 150

                         170       180       190
                  ....*....|....*....|....*....|..
gi 743523842  188 KLLP-----KMGEIVANDSESYKYLAESIRMH 214
Cdd:TIGR02072 151 HGLRylsldELKALLKNSFELLTLEEELITLS 182
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
62-167 3.46e-16

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 71.78  E-value: 3.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  62 KGQKVLDLAGGTGDLTAKFSRIVGEtGQVVLADINDSMLKVGRDKLrnlgvaNNVSYVQANAEALPfPDNHFDVITIGFG 141
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPG-ARVTGVDLSPEMLARARARL------PNVRFVVADLRDLD-PPEPFDLVVSNAA 72

                         90       100
                 ....*....|....*....|....*.
gi 743523842 142 LRNVTDKDKALASMFRVLKPGGRLLV 167
Cdd:COG4106   73 LHWLPDHAALLARLAAALAPGGVLAV 98
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 94-243 4.00e-16

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 73.18  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  94 DINDSMLKVG--RDKLRNLGVANNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFS 171
Cdd:PLN02232   4 DFSSEQLAVAatRQSLKARSCYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDFN 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743523842 172 KPVSEVIAKLYDLYSFKLLPKMGeIVANDSESYKYLAESIRMHPDQQTLAGMMENVGFEQVEFYNLTQGVVA 243
Cdd:PLN02232  84 KSNQSVTTFMQGWMIDNVVVPVA-TVYDLAKEYEYLKYSINGYLTGEELETLALEAGFSSACHYEISGGFMG 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 65-167 2.67e-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: 69.77  E-value: 2.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  65 KVLDLAGGTGDLTAKFSRIVGetGQVVLADINDSMLKVGRDKLRNLGvANNVSYVQANAEALPF-PDNHFD-VITIGFGL 142
Cdd:cd02440    1 RVLDLGCGTGALALALASGPG--ARVTGVDISPVALELARKAAAALL-ADNVEVLKGDAEELPPeADESFDvIISDPPLH 77

                         90       100
                 ....*....|....*....|....*
gi 743523842 143 RNVTDKDKALASMFRVLKPGGRLLV 167
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVLVL 102
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 49-185 1.48e-14

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 69.95  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  49 LWKRFTIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGetGQVVLADINDSMLKVGRDKLRNLGVANnVSYVQAN-AEALP 127
Cdd:COG0500   13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFG--GRVIGIDLSPEAIALARARAAKAGLGN-VEFLVADlAELDP 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743523842 128 FPDNHFDVITigfgLRNV------TDKDKALASMFRVLKPGGRLLVLEFSKPVSEVIAKLYDLY 185
Cdd:COG0500   90 LPAESFDLVV----AFGVlhhlppEEREALLRELARALKPGGVLLLSASDAAAALSLARLLLLA 149
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 59-167 6.16e-14

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 67.26  E-value: 6.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  59 GVRKGQKVLDLAGGTGDLTAkfsRIVGETG-QVVLADINDSMLKVGRDKLRNLGVANNVSYVQANAEALPfPDNHFDVIT 137
Cdd:COG2230   48 GLKPGMRVLDIGCGWGGLAL---YLARRYGvRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADGQFDAIV 123

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 743523842 138 -IG----FGLRNVtdkDKALASMFRVLKPGGRLLV 167
Cdd:COG2230  124 sIGmfehVGPENY---PAYFAKVARLLKPGGRLLL 155
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 67-165 4.53e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 60.84  E-value: 4.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   67 LDLAGGTGDLTAKFSRiVGETGQVVLADINDSMLKVGRDKLRNLGVANNVSYVQANAEALPFPDNHFDVITIGFGLRNVT 146
Cdd:pfam08242   1 LEIGCGTGTLLRALLE-ALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLA 79

                          90
                  ....*....|....*....
gi 743523842  147 DKDKALASMFRVLKPGGRL 165
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
19-166 5.24e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 62.71  E-value: 5.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  19 EKETLVAGVFHSVAAKYD--LMNDLMSFGIHRLWKRFtIDCSGVRKGQKVLDLAGGTGDLTAKFSRIVGE-TGqvvlADI 95
Cdd:COG4976    2 ALDAYVEALFDQYADSYDaaLVEDLGYEAPALLAEEL-LARLPPGPFGRVLDLGCGTGLLGEALRPRGYRlTG----VDL 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743523842  96 NDSMLKVGRDKlrnlgvANNVSYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLL 166
Cdd:COG4976   77 SEEMLAKAREK------GVYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
59-169 8.28e-12

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 63.40  E-value: 8.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  59 GVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLA-----DINDSMLKVGRDKLR-----NLGVANNVSYVQANAEALPF 128
Cdd:COG4798   63 GVKPGMTVVEIWPGGGWYTEILAPYLGPKGKVYAAnfdpdSEPPEYAKRSREAFSaklaaDPALYGNVRVTAFAPPDDPI 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 743523842 129 -PDNHFDVITIGfglRNV------TDKDKALASMFRVLKPGGRLLVLE 169
Cdd:COG4798  143 aPPGSADLVLTF---RNYhnwyraGDAAAMFAAFFKALKPGGVLGVVD 187
PRK05785 PRK05785
hypothetical protein; Provisional
 27-207 8.56e-12

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 62.78  E-value: 8.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  27 VFHSVAAKYDLMNDLMSFGIHRLWKRFTIDCSGVRKGQ--KVLDLAGGTGDLTAKFSRIVGEtgQVVLADINDSMLK--- 101
Cdd:PRK05785  14 AYNKIPKAYDRANRFISFNQDVRWRAELVKTILKYCGRpkKVLDVAAGKGELSYHFKKVFKY--YVVALDYAENMLKmnl 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842 102 VGRDKlrnlgvannvsyVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKpgGRLLVLEFSKPVSEVIAKL 181
Cdd:PRK05785  92 VADDK------------VVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAEFTRVSR--KQVGFIAMGKPDNVIKRKY 157

                        170       180
                 ....*....|....*....|....*.
gi 743523842 182 YDLYSFKLLPKMGEIVANDSESYKYL 207
Cdd:PRK05785 158 LSFYLRYIMPYIACLAGAKCRDYKYI 183
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 58-168 7.32e-11

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: 60.56  E-value: 7.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  58 SGVRKGQKVLDlAG-GTGDLTAKFSRIVGETGQVVLADINDSMLKVGRDKLRNLGVANNVSYVQANAEAlPFPDNHFDVI 136
Cdd:COG2519   87 LDIFPGARVLE-AGtGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIRE-GIDEGDVDAV 164

                         90       100       110
                 ....*....|....*....|....*....|..
gi 743523842 137 TIgfglrNVTDKDKALASMFRVLKPGGRLLVL 168
Cdd:COG2519  165 FL-----DMPDPWEALEAVAKALKPGGVLVAY 191
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 59-167 1.44e-09

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 57.16  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  59 GVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSMLKVGRDKLRNLGVaNNVSYVQANAEALPFPDNHFDVITI 138
Cdd:PRK13943  77 GLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRRLGI-ENVIFVCGDGYYGVPEFAPYDVIFV 155

                         90       100
                 ....*....|....*....|....*....
gi 743523842 139 GFGLRNVTDkdkalaSMFRVLKPGGRLLV 167
Cdd:PRK13943 156 TVGVDEVPE------TWFTQLKEGGRVIV 178
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
59-167 1.49e-09

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 56.22  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   59 GVRKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSMLKVGRDKLRNLGvANNVSYVQAN-----AEALPfpdnhF 133
Cdd:pfam01135  70 ELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLG-LENVIVVVGDgrqgwPEFAP-----Y 143

                          90       100       110
                  ....*....|....*....|....*....|....
gi 743523842  134 DVITIGFGLRNVTdkdKALasmFRVLKPGGRLLV 167
Cdd:pfam01135 144 DAIHVGAAAPEIP---EAL---IDQLKEGGRLVI 171
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-233 4.72e-09

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 53.97  E-value: 4.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   46 IHRLWKRFTIDCSGV-RKGQKVLDLAGGTGdltaKFSRIVGETG-QVVLADINDSMLKvgrdklrnlGVANNVSYVQANA 123
Cdd:pfam13489   5 RERLLADLLLRLLPKlPSPGRVLDFGCGTG----IFLRLLRAQGfSVTGVDPSPIAIE---------RALLNVRFDQFDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  124 EALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRLLVLEFSKPVSEVIAKLYDLYSFkllpKMGEIVANDSEs 203
Cdd:pfam13489  72 QEAAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLR----PRNGHISLFSA- 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 743523842  204 ykylaesirmhpdqQTLAGMMENVGFEQVE 233
Cdd:pfam13489 147 --------------RSLKRLLEEAGFEVVS 162
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 60-167 1.47e-08

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 53.26  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  60 VRKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSMLKVGRDKLRNLGVANNVSYVQANA-EALPFPDNHFDVITI 138
Cdd:PRK00377  38 LRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEApEILFTINEKFDRIFI 117

                         90       100
                 ....*....|....*....|....*....
gi 743523842 139 GFGLRNVtdkDKALASMFRVLKPGGRLLV 167
Cdd:PRK00377 118 GGGSEKL---KEIISASWEIIKKGGRIVI 143
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 24-165 2.55e-08

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 53.22  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  24 VAGVFHSVAAKYDLMNDLMSFGIHRLWKRFtidcsGVRKGQKVLDLAGGTGDLtakfSRIVGETGQVVLA-DINDSMLKV 102
Cdd:PRK10258   9 IAAAFGRAAAHYEQHAELQRQSADALLAML-----PQRKFTHVLDAGCGPGWM----SRYWRERGSQVTAlDLSPPMLAQ 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743523842 103 GRDKlrnlGVANNvsYVQANAEALPFPDNHFDVITIGFGLRNVTDKDKALASMFRVLKPGGRL 165
Cdd:PRK10258  80 ARQK----DAADH--YLAGDIESLPLATATFDLAWSNLAVQWCGNLSTALRELYRVVRPGGVV 136
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 60-167 9.82e-08

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 50.86  E-value: 9.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  60 VRKGQKVLDLAGGTGDLTAKFSRIVGEtgqVVLADINDSMLKVGRDKLRNLGVaNNVSYVQANAeALPFPDNH-FDVITI 138
Cdd:COG2518   64 LKPGDRVLEIGTGSGYQAAVLARLAGR---VYSVERDPELAERARERLAALGY-DNVTVRVGDG-ALGWPEHApFDRIIV 138

                         90       100
                 ....*....|....*....|....*....
gi 743523842 139 GFGLRNVTDkdkALASMfrvLKPGGRLLV 167
Cdd:COG2518  139 TAAAPEVPE---ALLEQ---LAPGGRLVA 161
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 58-192 1.05e-07

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: 50.33  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  58 SGVRKGQKVLDLAGGTGdLTAKFSRIVGetGQVVLADINDSMLKVGRDKLRNLGVANnVSYVQANAEALPFPDNHFDVIt 137
Cdd:COG1041   22 AGAKEGDTVLDPFCGTG-TILIEAGLLG--RRVIGSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLADESVDAI- 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743523842 138 igfglrnVTD--------------KD---KALASMFRVLKPGGRlLVLEFSKPVSEVIAKLYdlysFKLLPK 192
Cdd:COG1041   97 -------VTDppygrsskisgeelLElyeKALEEAARVLKPGGR-VVIVTPRDIDELLEEAG----FKVLER 156
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 63-200 4.04e-07

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 50.13  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  63 GQKVLDLAGGTGDltAKFSRIVGETGQVVLADINDSMLKVGRDklRNLGVANNVSYVQANAEALPFPDNHFDVITIGFGL 142
Cdd:PLN02336 267 GQKVLDVGCGIGG--GDFYMAENFDVHVVGIDLSVNMISFALE--RAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTI 342

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743523842 143 RNVTDKDKALASMFRVLKPGGRLLVLEFSK----PVSEVIAKL----YDLYSFKLLPKM------GEIVAND 200
Cdd:PLN02336 343 LHIQDKPALFRSFFKWLKPGGKVLISDYCRspgtPSPEFAEYIkqrgYDLHDVQAYGQMlkdagfDDVIAED 414
PLN02244 PLN02244
tocopherol O-methyltransferase
 111-167 3.04e-06

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 47.43  E-value: 3.04e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 743523842 111 GVANNVSYVQANAEALPFPDNHFD-VITIGFGlRNVTDKDKALASMFRVLKPGGRLLV 167
Cdd:PLN02244 165 GLSDKVSFQVADALNQPFEDGQFDlVWSMESG-EHMPDKRKFVQELARVAAPGGRIII 221
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
53-136 3.13e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 46.44  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  53 FTIDCSGVRKGQKVLDLAGGTGDLtAKFSRIVGeTGQVVLADINDSMLKVGRDKLRNLGVanNVSYVQANAEALPfPDNH 132
Cdd:COG2263   36 HLAYLRGDIEGKTVLDLGCGTGML-AIGAALLG-AKKVVGVDIDPEALEIARENAERLGV--RVDFIRADVTRIP-LGGS 110


                 ....
gi 743523842 133 FDVI 136
Cdd:COG2263  111 VDTV 114
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
60-166 3.44e-06

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 46.57  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  60 VRKGQKVLDLAGGTGDLTAKFSRIvgETGQVVLADINDSMLKVGRDKLRNLGVANNVSYVQANAEALPFPdNHFDVI--- 136
Cdd:COG4076   33 VKPGDVVLDIGTGSGLLSMLAARA--GAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLDLP-EKADVIise 109

                         90       100       110
                 ....*....|....*....|....*....|....
gi 743523842 137 TIGFGLRnvtdKDKALASMF----RVLKPGGRLL 166
Cdd:COG4076  110 MLDTALL----DEGQVPILNharkRLLKPGGRII 139
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 63-167 2.14e-04

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 40.94  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  63 GQKVLDLAGGTGDLTAKFSRIVGETgQVVLADINDSMLKVGRDKLRNLGVANnVSYVQANAeALPFPDNHFDVItigfgL 142
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKRNPEA-RVTLVDVNARAVELARANAAANGLEN-VEVLWSDG-LSGVPDGSFDLI-----L 121

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 743523842 143 RN------VTDKDKALASMF----RVLKPGGRLLV 167
Cdd:COG2813  122 SNppfhagRAVDKEVAHALIadaaRHLRPGGELWL 156
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
126-240 2.48e-04

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 40.62  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842 126 LPFPDNHFDVI---------TIGFGLRnvtdkdkALASMFRVLKPGGRLLV----LEFskpVSEVIAKLYDLYSFKLLPK 192
Cdd:COG4627   40 LPFPDNSVDAIysshvlehlDYEEAPL-------ALKECYRVLKPGGILRIvvpdLEH---VARLYLAEYDAALDVAELR 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 743523842 193 MGEIVANDSESYKYLAESIRMHPDQQTLAGMMENVGFEQVEFYNLTQG 240
Cdd:COG4627  110 LAGPIDPLGIILGERLAGLAARHSVLFRTGFTRLALTARRSAAGARAA 157
PRK14968 PRK14968
putative methyltransferase; Provisional
 60-168 9.01e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 9.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  60 VRKGQKVLDLAGGTGDLTAKFSRivgETGQVVLADINDSMLKVGRDKLRNLGVANN-VSYVQANaeaL--PFPDNHFDVI 136
Cdd:PRK14968  21 DKKGDRVLEVGTGSGIVAIVAAK---NGKKVVGVDINPYAVECAKCNAKLNNIRNNgVEVIRSD---LfePFRGDKFDVI 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 743523842 137 T-----------------IGFGL------RNVTdkDKALASMFRVLKPGGRLLVL 168
Cdd:PRK14968  95 LfnppylpteeeeewddwLNYALsggkdgREVI--DRFLDEVGRYLKPGGRILLL 147
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 60-191 1.05e-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: 39.36  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  60 VRKGQKVLDLAGGTGD----LTAKFSRIvgetgQVVLADINDSMLKVGRDKLRNLGVANNVSYVQANAEALP--FPDNHF 133
Cdd:COG4123   35 VKKGGRVLDLGTGTGVialmLAQRSPGA-----RITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAaeLPPGSF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842 134 DVIT-------IGFGLRNvTDKDKALA-------------SMFRVLKPGGRL-LVLefskPV---SEVIAKL--YDLYSF 187
Cdd:COG4123  110 DLVVsnppyfkAGSGRKS-PDEARAIArhedaltledlirAAARLLKPGGRFaLIH----PAerlAEILAALrkYGLGPK 184


                 ....
gi 743523842 188 KLLP 191
Cdd:COG4123  185 RLRP 188
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 58-213 1.07e-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: 39.61  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  58 SGVRKGQKVLDL-AGGTGDLTAKFSRIVGetGQVVLADINDSMLkvgrDKLRNLGVAN--NVSYVQANAEALPFPDNHFD 134
Cdd:cd05188  130 GVLKPGDTVLVLgAGGVGLLAAQLAKAAG--ARVIVTDRSDEKL----ELAKELGADHviDYKEEDLEEELRLTGGGGAD 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743523842 135 VITigfglrNVTDKDKALASMFRVLKPGGRLLVLEFSKPVSEVIAklydlySFKLLPKMGEIVANDSESYKYLAESIRM 213
Cdd:cd05188  204 VVI------DAVGGPETLAQALRLLRPGGRIVVVGGTSGGPPLDD------LRRLLFKELTIIGSTGGTREDFEEALDL 270
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 61-182 1.10e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 39.23  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  61 RKGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSMLKVGRDKLRNLGVaNNVSYVQANAEALPFPDNHFDVITigf 140
Cdd:PRK13942  75 KEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERIPELAEKAKKTLKKLGY-DNVEVIVGDGTLGYEENAPYDRIY--- 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 743523842 141 glrnVT----DKDKALasmFRVLKPGGRLLVlefskPVSEVIAKLY 182
Cdd:PRK13942 151 ----VTaagpDIPKPL---IEQLKDGGIMVI-----PVGSYSQELI 184
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 65-164 2.67e-03

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 38.33  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  65 KVLDLAGGTGDLTAKFSRIVgETGQVVLADINDSMLKVGRDKlrnlGVANNVSYVQANAEALPFPDNHFDVITIGFGLRN 144
Cdd:PLN02490 116 KVVDVGGGTGFTTLGIVKHV-DAKNVTILDQSPHQLAKAKQK----EPLKECKIIEGDAEDLPFPTDYADRYVSAGSIEY 190

                         90       100
                 ....*....|....*....|
gi 743523842 145 VTDKDKALASMFRVLKPGGR 164
Cdd:PLN02490 191 WPDPQRGIKEAYRVLKIGGK 210
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
65-177 3.20e-03

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 37.78  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842    65 KVLDLAGGTG----DLTAKFS--RIVGETgqvvladINDSMLKVGRDKLRNLGVANNVSYVQANAEALPFPDNhFDVItI 138
Cdd:smart00828   2 RVLDFGCGYGsdliDLAERHPhlQLHGYT-------ISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDT-YDLV-F 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 743523842   139 GFG-LRNVTDKDKALASMFRVLKPGGRLLVLEF-SKPVSEV 177
Cdd:smart00828  73 GFEvIHHIKDKMDLFSNISRHLKDGGHLVLADFiANLLSAI 113
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 60-167 4.40e-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: 36.80  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842   60 VRKGQKVLDLAGGTGDLTAKFSRIVGETgQVVLADINDSMLKVGRDKLRNLGVaNNVSYVQANAEAlPFPDNHFDVItig 139
Cdd:pfam05175  29 KDLSGKVLDLGCGAGVLGAALAKESPDA-ELTMVDINARALESARENLAANGL-ENGEVVASDVYS-GVEDGKFDLI--- 102

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 743523842  140 fgLRN-------VTDKDKALAsMF----RVLKPGGRLLV 167
Cdd:pfam05175 103 --ISNppfhaglATTYNVAQR-FIadakRHLRPGGELWI 138
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
60-166 5.75e-03

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 37.07  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  60 VRKGQKVLDLagGTGdltakfsrivgeTGqvVLA--------------DINDSMLKVGRDKL-RNlGVANNVSYVQANAe 124
Cdd:COG2264  146 LKPGKTVLDV--GCG------------SG--ILAiaaaklgakrvlavDIDPVAVEAARENAeLN-GVEDRIEVVLGDL- 207

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 743523842 125 alpFPDNHFDVIT--IgfgLRNVTdkdKALASMF-RVLKPGGRLL 166
Cdd:COG2264  208 ---LEDGPYDLVVanI---LANPL---IELAPDLaALLKPGGYLI 243
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 62-169 6.73e-03

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: 37.24  E-value: 6.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  62 KGQKVLDLAGGTGDLTAKFSRIVGETGQVVLADINDSMLKVGRDKLRNLGVAN--NVSYVQANAEAlPFPDNHFDVITIG 139
Cdd:COG5459   80 APLTVLDVGAGPGTAAWAAADAWPSLLDATLLERSAAALALGRRLARAAANPAleTAEWRLADLAA-ALPAPPADLVVAS 158

                         90       100       110
                 ....*....|....*....|....*....|..
gi 743523842 140 FGLRNVTDKDKA--LASMFrvLKPGGRLLVLE 169
Cdd:COG5459  159 YVLNELADAARAalVDRLW--LAPDGALLIVE 188
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 59-175 9.70e-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: 36.78  E-value: 9.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743523842  59 GVRKGQKVLDL-AGGTGDLTAKFSRIVGetGQVVLADINDSML----KVGRDKLRNLGVANNVSYVQANAEAlPFPDNHF 133
Cdd:cd08261  156 GVTAGDTVLVVgAGPIGLGVIQVAKARG--ARVIVVDIDDERLefarELGADDTINVGDEDVAARLRELTDG-EGADVVI 232

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 743523842 134 DVitigfglrnvTDKDKALASMFRVLKPGGRLLVLEFSK-PVS 175
Cdd:cd08261  233 DA----------TGNPASMEEAVELVAHGGRVVLVGLSKgPVT 265
 
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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