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Conserved domains on  [gi|516061977|ref|WP_017492560|]
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bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE [Rouxiella badensis]

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 ...
 19-257 1.90e-152

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


:

Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 424.18  E-value: 1.90e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  19 FRTVAKNNKAEMVAEVFHSVAAKYDLMNDLMSFGIHRIWKRYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVV 98
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  99 LADINDSMLKMGREKLRNNGIVGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFS 178
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516061977 179 KPLLAPLSKAYDTYSFHILPRIGELVAQDAESYRYLAESIRMHPDQETLKDMMSDAGFENVTYNNLTGGIVALHRGFKF 257
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 19-257 1.90e-152

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 424.18  E-value: 1.90e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  19 FRTVAKNNKAEMVAEVFHSVAAKYDLMNDLMSFGIHRIWKRYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVV 98
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  99 LADINDSMLKMGREKLRNNGIVGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFS 178
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516061977 179 KPLLAPLSKAYDTYSFHILPRIGELVAQDAESYRYLAESIRMHPDQETLKDMMSDAGFENVTYNNLTGGIVALHRGFKF 257
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
29-256 2.40e-125

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 355.21  E-value: 2.40e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   29 EMVAEVFHSVAAKYDLMNDLMSFGIHRIWKRYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVVLADINDSMLK 108
Cdd:pfam01209   2 QRVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  109 MGREKLRNNGiVGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPLLAPLSKA 188
Cdd:pfam01209  82 EGEKKAKEEG-KYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516061977  189 YDTYSFHILPRIGELVAQDAESYRYLAESIRMHPDQETLKDMMSDAGFENVTYNNLTGGIVALHRGFK 256
Cdd:pfam01209 161 YELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 31-256 3.69e-118

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: 336.93  E-value: 3.69e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   31 VAEVFHSVAAKYDLMNDLMSFGIHRIWKRYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVVLADINDSMLKMG 110
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  111 REKLRnngIVGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPLLAPLSKAYD 190
Cdd:TIGR01934  81 KKKSE---LPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516061977  191 TYSFHILPRIGELVAQDAESYRYLAESIRMHPDQETLKDMMSDAGFENVTYNNLTGGIVALHRGFK 256
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 35-185 1.39e-42

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 141.67  E-value: 1.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  35 FHSVAAKYDLmndlmsfgihriwKRYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLvgeQGEVVLADINDSMLKMGREKL 114
Cdd:COG2226    1 FDRVAARYDG-------------REALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516061977 115 RNNGIvgNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPLLAPL 185
Cdd:COG2226   65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAEL 133
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 72-174 2.08e-13

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: 64.76  E-value: 2.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  72 RVLDLAGGTGDLTAKFSRLVGEQgeVVLADINDSMLKMGREKLRNNGIVgNVSYVQANAEALPF-PDNYFD-CITISFGL 149
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGAR--VTGVDISPVALELARKAAAALLAD-NVEVLKGDAEELPPeADESFDvIISDPPLH 77

                         90       100
                 ....*....|....*....|....*
gi 516061977 150 RNVTEKEKALRSMFRVLKPGGRLLV 174
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVLVL 102
 
Name Accession Description Interval E-value
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 19-257 1.90e-152

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 424.18  E-value: 1.90e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  19 FRTVAKNNKAEMVAEVFHSVAAKYDLMNDLMSFGIHRIWKRYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVV 98
Cdd:PRK00216   1 FMTVAEEEKQEKVAEMFDSIAPKYDLMNDLLSFGLHRVWRRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKTGEVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  99 LADINDSMLKMGREKLRNNGIVGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFS 178
Cdd:PRK00216  81 GLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALPFPDNSFDAVTIAFGLRNVPDIDKALREMYRVLKPGGRLVILEFS 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516061977 179 KPLLAPLSKAYDTYSFHILPRIGELVAQDAESYRYLAESIRMHPDQETLKDMMSDAGFENVTYNNLTGGIVALHRGFKF 257
Cdd:PRK00216 161 KPTNPPLKKAYDFYLFKVLPLIGKLISKNAEAYSYLAESIRAFPDQEELAAMLEEAGFERVRYRNLTGGIVALHVGYKP 239
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
29-256 2.40e-125

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 355.21  E-value: 2.40e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   29 EMVAEVFHSVAAKYDLMNDLMSFGIHRIWKRYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVVLADINDSMLK 108
Cdd:pfam01209   2 QRVGDVFSSVASKYDLMNDVISFGIHRLWKDFTMKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSSGKVVGLDINENMLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  109 MGREKLRNNGiVGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPLLAPLSKA 188
Cdd:pfam01209  82 EGEKKAKEEG-KYNIEFLQGNAEELPFEDDSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLLSQA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516061977  189 YDTYSFHILPRIGELVAQDAESYRYLAESIRMHPDQETLKDMMSDAGFENVTYNNLTGGIVALHRGFK 256
Cdd:pfam01209 161 YELYFKYVMPFMGKMFAKSYKSYQYLQESIRDFPDQKTLASMFEKAGFKSVGYESLTGGIAAIHWGIK 228
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 31-256 3.69e-118

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: 336.93  E-value: 3.69e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   31 VAEVFHSVAAKYDLMNDLMSFGIHRIWKRYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVVLADINDSMLKMG 110
Cdd:TIGR01934   1 VQEMFDRIAPKYDLLNDLLSFGLHRLWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRGKVTGVDFSSEMLEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  111 REKLRnngIVGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPLLAPLSKAYD 190
Cdd:TIGR01934  81 KKKSE---LPLNIEFIQADAEALPFEDNSFDAVTIAFGLRNVTDIQKALREMYRVLKPGGRLVILEFSKPANALLKKFYK 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516061977  191 TYSFHILPRIGELVAQDAESYRYLAESIRMHPDQETLKDMMSDAGFENVTYNNLTGGIVALHRGFK 256
Cdd:TIGR01934 158 FYLKNVLPSIGGLISKNAEAYTYLPESIRAFPSQEELAAMLKEAGFEEVRYRSLTFGVAAIHVGKK 223
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 34-249 7.42e-48

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 159.29  E-value: 7.42e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  34 VFHSVAAKYDLMNDLMSFGIHRIWKRYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVVLADINDSMLKMG--R 111
Cdd:PLN02233  38 LFNRIAPVYDNLNDLLSLGQHRIWKRMAVSWSGAKMGDRVLDLCCGSGDLAFLLSEKVGSDGKVMGLDFSSEQLAVAasR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977 112 EKLRNNGIVGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKP----------- 180
Cdd:PLN02233 118 QELKAKSCYKNIEWIEGDATDLPFDDCYFDAITMGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKStqpfttsmqew 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516061977 181 ----LLAPLSKAYDTysfhilprigelvaqdAESYRYLAESIRMHPDQETLKDMMSDAGFENVTYNNLTGGIV 249
Cdd:PLN02233 198 midnVVVPVATGYGL----------------AKEYEYLKSSINEYLTGEELEKLALEAGFSSAKHYEISGGLM 254
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 35-185 1.39e-42

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 141.67  E-value: 1.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  35 FHSVAAKYDLmndlmsfgihriwKRYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLvgeQGEVVLADINDSMLKMGREKL 114
Cdd:COG2226    1 FDRVAARYDG-------------REALLAALGLRPGARVLDLGCGTGRLALALAER---GARVTGVDISPEMLELARERA 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516061977 115 RNNGIvgNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPLLAPL 185
Cdd:COG2226   65 AEAGL--NVEFVVGDAEDLPFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAEL 133
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 73-170 1.79e-29

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 106.49  E-value: 1.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   73 VLDLAGGTGDLTAKFSRLVGeqGEVVLADINDSMLKMGREKLRNNGIvgNVSYVQANAEALPFPDNYFDCITISFGLRNV 152
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGG--ARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLHHL 76

                          90       100
                  ....*....|....*....|
gi 516061977  153 T--EKEKALRSMFRVLKPGG 170
Cdd:pfam13649  77 PdpDLEAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 48-177 8.67e-29

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 109.26  E-value: 8.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  48 LMSFGIHRIWKRYAIDcsgVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVVLADINDSMLKMGREKLRNNGivGNVSYVQ 127
Cdd:PRK08317   1 LPDFRRYRARTFELLA---VQPGDRVLDVGCGPGNDARELARRVGPEGRVVGIDRSEAMLALAKERAAGLG--PNVEFVR 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 516061977 128 ANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEF 177
Cdd:PRK08317  76 GDADGLPFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDT 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 74-174 9.91e-24

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 91.57  E-value: 9.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   74 LDLAGGTGDLTAKFSRLVGEqgeVVLADINDSMLKMGREKLRNNGivgnVSYVQANAEALPFPDNYFDCITISFGLRNVT 153
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR---VTGVDISPEMLELAREKAPREG----LTFVVGDAEDLPFPDNSFDLVLSSEVLHHVE 73

                          90       100
                  ....*....|....*....|.
gi 516061977  154 EKEKALRSMFRVLKPGGRLLV 174
Cdd:pfam08241  74 DPERALREIARVLKPGGILII 94
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 67-174 4.15e-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: 85.84  E-value: 4.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  67 VRRGQRVLDLAGGTGDLTAKFSRLvgeqG-EVVLADINDSMLKMGREKLRNNgivgNVSYVQANAEALPFPDNYFDCITI 145
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARR----GaDVTGVDISPEALEIARERAAEL----NVDFVQGDLEDLPLEDGSFDLVIC 93

                         90       100
                 ....*....|....*....|....*....
gi 516061977 146 SFGLRNVTEKEKALRSMFRVLKPGGRLLV 174
Cdd:COG2227   94 SEVLEHLPDPAALLRELARLLKPGGLLLL 122
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 68-178 2.20e-20

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 84.39  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   68 RRGQRVLDLAGGTGDLTAKFSRLVGEQGEVVLADINDSMLKMGREKLRNNGIvGNVSYVQANAEALP--FPDNYFDCItI 145
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDISEEAIEKARENAQKLGF-DNVEFEQGDIEELPelLEDDKFDVV-I 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 516061977  146 SFGLRN-VTEKEKALRSMFRVLKPGGRLLVLEFS 178
Cdd:pfam13847  80 SNCVLNhIPDPDKVLQEILRVLKPGGRLIISDPD 113
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 35-221 7.45e-19

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: 82.72  E-value: 7.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   35 FHSVAAKYDLMNDLMSFGIHRIWKRyaIDCSGVRRGQRVLDLAGGTGDLTAKFSRLvGEQGEVVLADINDSMLKMGREKL 114
Cdd:TIGR02072   2 FNKAAKTYDRHAKIQREMAKRLLAL--LKEKGIFIPASVLDIGCGTGYLTRALLKR-FPQAEFIALDISAGMLAQAKTKL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  115 RnngivGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPLLAPLSKAYDTYSF 194
Cdd:TIGR02072  79 S-----ENVQFICGDAEKLPLEDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGPGTLHELRQSFGQHGL 153

                         170       180
                  ....*....|....*....|....*....
gi 516061977  195 HILPR--IGELVAQDAESYRYLAESIRMH 221
Cdd:TIGR02072 154 RYLSLdeLKALLKNSFELLTLEEELITLS 182
arsM PRK11873
arsenite methyltransferase;
70-240 2.48e-18

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 81.92  E-value: 2.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  70 GQRVLDLAGGTG-D--LTAkfsRLVGEQGEVVLADINDSMLKMGREKLRNNGIvGNVSYVQANAEALPFPDNYFDCItIS 146
Cdd:PRK11873  78 GETVLDLGSGGGfDcfLAA---RRVGPTGKVIGVDMTPEMLAKARANARKAGY-TNVEFRLGEIEALPVADNSVDVI-IS 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977 147 FGLRN-VTEKEKALRSMFRVLKPGGRLLVLEFSkpLLAPlskaydtysfhiLPrigELVAQDAESYrylAESIRMHPDQE 225
Cdd:PRK11873 153 NCVINlSPDKERVFKEAFRVLKPGGRFAISDVV--LRGE------------LP---EEIRNDAELY---AGCVAGALQEE 212

                        170
                 ....*....|....*
gi 516061977 226 TLKDMMSDAGFENVT 240
Cdd:PRK11873 213 EYLAMLAEAGFVDIT 227
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
69-174 1.02e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 76.02  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  69 RGQRVLDLAGGTGDLTAKFSRLVGeQGEVVLADINDSMLKMGREKLrnngivGNVSYVQANAEALPFPDNyFDCITISFG 148
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFP-GARVTGVDLSPEMLARARARL------PNVRFVVADLRDLDPPEP-FDLVVSNAA 72

                         90       100
                 ....*....|....*....|....*.
gi 516061977 149 LRNVTEKEKALRSMFRVLKPGGRLLV 174
Cdd:COG4106   73 LHWLPDHAALLARLAAALAPGGVLAV 98
PLN02232 PLN02232
ubiquinone biosynthesis methyltransferase
 111-250 1.15e-17

ubiquinone biosynthesis methyltransferase


Pssm-ID: 165876  Cd Length: 160  Bit Score: 77.81  E-value: 1.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977 111 REKLRNNGIVGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKP---------- 180
Cdd:PLN02232  16 RQSLKARSCYKCIEWIEGDAIDLPFDDCEFDAVTMGYGLRNVVDRLRAMKEMYRVLKPGSRVSILDFNKSnqsvttfmqg 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516061977 181 -----LLAPLSKAYDTysfhilprigelvaqdAESYRYLAESIRMHPDQETLKDMMSDAGFENVTYNNLTGGIVA 250
Cdd:PLN02232  96 wmidnVVVPVATVYDL----------------AKEYEYLKYSINGYLTGEELETLALEAGFSSACHYEISGGFMG 154
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 59-174 7.37e-16

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 73.80  E-value: 7.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  59 RYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEQgeVVLADINDSMLKMGREKLRNNGIvGNVSYVQAN-AEALPFPD 137
Cdd:COG0500   16 ALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGR--VIGIDLSPEAIALARARAAKAGL-GNVEFLVADlAELDPLPA 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 516061977 138 NYFDCItISFGLRNVTEKE---KALRSMFRVLKPGGRLLV 174
Cdd:COG0500   93 ESFDLV-VAFGVLHHLPPEereALLRELARALKPGGVLLL 131
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 72-174 2.08e-13

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: 64.76  E-value: 2.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  72 RVLDLAGGTGDLTAKFSRLVGEQgeVVLADINDSMLKMGREKLRNNGIVgNVSYVQANAEALPF-PDNYFD-CITISFGL 149
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGAR--VTGVDISPVALELARKAAAALLAD-NVEVLKGDAEELPPeADESFDvIISDPPLH 77

                         90       100
                 ....*....|....*....|....*
gi 516061977 150 RNVTEKEKALRSMFRVLKPGGRLLV 174
Cdd:cd02440   78 HLVEDLARFLEEARRLLKPGGVLVL 102
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
28-173 1.11e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 64.63  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  28 AEMVAEVFHSVAAKYD--LMNDLMSFGIHRIWKRyAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEqgeVVLADINDS 105
Cdd:COG4976    4 DAYVEALFDQYADSYDaaLVEDLGYEAPALLAEE-LLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR---LTGVDLSEE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516061977 106 MLKMGREKLrnngivGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGRLL 173
Cdd:COG4976   80 MLAKAREKG------VYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFI 141
PRK05785 PRK05785
hypothetical protein; Provisional
 29-232 1.27e-12

hypothetical protein; Provisional


Pssm-ID: 235607 [Multi-domain]  Cd Length: 226  Bit Score: 65.09  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  29 EMVAEVFHSVAAKYDLMNDLMSFGIHRIWKRYAIDCSGVRRGQ--RVLDLAGGTGDLTAKFSRLVgeQGEVVLADINDSM 106
Cdd:PRK05785   9 EELQEAYNKIPKAYDRANRFISFNQDVRWRAELVKTILKYCGRpkKVLDVAAGKGELSYHFKKVF--KYYVVALDYAENM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977 107 LKMGREKlrnngivgnVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKpgGRLLVLEFSKPLLAPLS 186
Cdd:PRK05785  87 LKMNLVA---------DDKVVGSFEALPFRDKSFDVVMSSFALHASDNIEKVIAEFTRVSR--KQVGFIAMGKPDNVIKR 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 516061977 187 KAYDTYSFHILPRIGELVAQDAESYRYLAESIRMHPDQETLKDMMS 232
Cdd:PRK05785 156 KYLSFYLRYIMPYIACLAGAKCRDYKYIYYIYERLPTNSFHREIFE 201
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 74-172 3.52e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 61.23  E-value: 3.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   74 LDLAGGTGDLTAKFSRLVgEQGEVVLADINDSMLKMGREKLRNNGIvGNVSYVQANAEALPFPD-NYFDCITISFGLRNV 152
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAL-PGLEYTGLDISPAALEAARERLAALGL-LNAVRVELFQLDLGELDpGSFDVVVASNVLHHL 78

                          90       100
                  ....*....|....*....|
gi 516061977  153 TEKEKALRSMFRVLKPGGRL 172
Cdd:pfam08242  79 ADPRAVLRNIRRLLKPGGVL 98
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 68-240 1.13e-11

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 61.29  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   68 RRGQRVLDLAGGTGdltaKFSRLVGEQG-EVVLADINDSMlkmgreklrNNGIVGNVSYVQANAEALPFPDNYFDCITIS 146
Cdd:pfam13489  21 PSPGRVLDFGCGTG----IFLRLLRAQGfSVTGVDPSPIA---------IERALLNVRFDQFDEQEAAVPAGKFDVIVAR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  147 FGLRNVTEKEKALRSMFRVLKPGGRLLVLEFSKPLLAPLSKAYDTYSFHILPRIgelvaqdaeSYrylaesirmhPDQET 226
Cdd:pfam13489  88 EVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLLEWPYLRPRNGHI---------SL----------FSARS 148

                         170
                  ....*....|....
gi 516061977  227 LKDMMSDAGFENVT 240
Cdd:pfam13489 149 LKRLLEEAGFEVVS 162
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 66-174 2.34e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 60.33  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  66 GVRRGQRVLDLAGGTGDLTAkfsRLVGEQG-EVVLADINDSMLKMGREKLRNNGIVGNVSYVQANAEALPfPDNYFDCIt 144
Cdd:COG2230   48 GLKPGMRVLDIGCGWGGLAL---YLARRYGvRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADGQFDAI- 122

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 516061977 145 ISFGlrnVTE------KEKALRSMFRVLKPGGRLLV 174
Cdd:COG2230  123 VSIG---MFEhvgpenYPAYFAKVARLLKPGGRLLL 155
COG4798 COG4798
Predicted methyltransferase [General function prediction only];
66-237 4.32e-11

Predicted methyltransferase [General function prediction only];


Pssm-ID: 443826  Cd Length: 274  Bit Score: 61.47  E-value: 4.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  66 GVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVVLA-----DINDSMLKMGREKLR-----NNGIVGNVSYVQANAEALPF 135
Cdd:COG4798   63 GVKPGMTVVEIWPGGGWYTEILAPYLGPKGKVYAAnfdpdSEPPEYAKRSREAFSaklaaDPALYGNVRVTAFAPPDDPI 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977 136 -PDNYFDCITISfglRNV------TEKEKALRSMFRVLKPGGRLLVLEfskpllaplskaydtysfHILPRiGELVAQDA 208
Cdd:COG4798  143 aPPGSADLVLTF---RNYhnwyraGDAAAMFAAFFKALKPGGVLGVVD------------------HRAPP-GTGLEAVA 200

                        170       180
                 ....*....|....*....|....*....
gi 516061977 209 ESyRYLaesirmhpDQETLKDMMSDAGFE 237
Cdd:COG4798  201 TL-GYI--------DEAYVIALAEAAGFE 220
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 59-175 1.01e-10

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: 58.81  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  59 RYAIDCSGVRRGQRVLDLAGGTGdLTAKFSRLVGeqGEVVLADINDSMLKMGREKLRNNGIvGNVSYVQANAEALPFPDN 138
Cdd:COG1041   16 RALVNLAGAKEGDTVLDPFCGTG-TILIEAGLLG--RRVIGSDIDPKMVEGARENLEHYGY-EDADVIRGDARDLPLADE 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 516061977 139 YFDCI--------TISFGLRNVTEK-EKALRSMFRVLKPGGRLLVL 175
Cdd:COG1041   92 SVDAIvtdppygrSSKISGEELLELyEKALEEAARVLKPGGRVVIV 137
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 65-175 2.79e-10

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 59.02  E-value: 2.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  65 SGVRRGQRVLDlAG-GTGDLTAKFSRLVGEQGEVVLADINDSMLKMGREKLRNNGIVGNVSYVQANAEAlPFPDNYFDCI 143
Cdd:COG2519   87 LDIFPGARVLE-AGtGSGALTLALARAVGPEGKVYSYERREDFAEIARKNLERFGLPDNVELKLGDIRE-GIDEGDVDAV 164

                         90       100       110
                 ....*....|....*....|....*....|..
gi 516061977 144 TIsfglrNVTEKEKALRSMFRVLKPGGRLLVL 175
Cdd:COG2519  165 FL-----DMPDPWEALEAVAKALKPGGVLVAY 191
PRK13943 PRK13943
protein-L-isoaspartate O-methyltransferase; Provisional
 60-174 1.53e-08

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 237568 [Multi-domain]  Cd Length: 322  Bit Score: 54.47  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  60 YAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVVLADINDSMLKMGREKLRNNGIvGNVSYVQANAEALPFPDNY 139
Cdd:PRK13943  71 LFMEWVGLDKGMRVLEIGGGTGYNAAVMSRVVGEKGLVVSVEYSRKICEIAKRNVRRLGI-ENVIFVCGDGYYGVPEFAP 149

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 516061977 140 FDCITISFGLRNVTEkekalrSMFRVLKPGGRLLV 174
Cdd:PRK13943 150 YDVIFVTVGVDEVPE------TWFTQLKEGGRVIV 178
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
70-213 3.53e-08

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 52.37  E-value: 3.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   70 GQRVLDLAGGTGDLTAKFSRLVGEQGEVVLADINDSMLKMGREKLRNNGIvGNVSYVQAN-----AEALPfpdnyFDCIT 144
Cdd:pfam01135  74 GMRVLEIGSGSGYLTACFARMVGEVGRVVSIEHIPELVEIARRNLEKLGL-ENVIVVVGDgrqgwPEFAP-----YDAIH 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  145 ISFGLRNVTEkekalrSMFRVLKPGGRLLVlefskpllaPLSKAYDTYSFHILPR-IGELVAQDAESYRY 213
Cdd:pfam01135 148 VGAAAPEIPE------ALIDQLKEGGRLVI---------PVGPNGNQVLQQFDKRnDGSVVIKDLEGVRF 202
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 66-172 4.75e-08

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 52.45  E-value: 4.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  66 GVRRGQRVLDLAGGTGDLtakfSRLVGEQGEVVLA-DINDSMLKMGREKLRNNgivgnvSYVQANAEALPFPDNYFDCIT 144
Cdd:PRK10258  39 PQRKFTHVLDAGCGPGWM----SRYWRERGSQVTAlDLSPPMLAQARQKDAAD------HYLAGDIESLPLATATFDLAW 108

                         90       100
                 ....*....|....*....|....*...
gi 516061977 145 ISFGLRNVTEKEKALRSMFRVLKPGGRL 172
Cdd:PRK10258 109 SNLAVQWCGNLSTALRELYRVVRPGGVV 136
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
55-173 7.53e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 51.58  E-value: 7.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  55 RIWKRyAIDcSGVRRGQRVLDLAGGTGDLTAKFSRLvgEQGEVVLADINDSMLKMGREKLRNNGIVGNVSYVQANAEALP 134
Cdd:COG4076   23 DAFKA-AIE-RVVKPGDVVLDIGTGSGLLSMLAARA--GAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDLD 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 516061977 135 FPdNYFDcITISFGLRNVTEKEKALRSMF----RVLKPGGRLL 173
Cdd:COG4076   99 LP-EKAD-VIISEMLDTALLDEGQVPILNharkRLLKPGGRII 139
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 67-174 3.11e-07

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 49.32  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  67 VRRGQRVLDLAGGTGDLTAKFSRLVgeqGEVVLADINDSMLKMGREKLRNNGIvGNVSYVQANAeALPFPDN-YFDCITI 145
Cdd:COG2518   64 LKPGDRVLEIGTGSGYQAAVLARLA---GRVYSVERDPELAERARERLAALGY-DNVTVRVGDG-ALGWPEHaPFDRIIV 138

                         90       100
                 ....*....|....*....|....*....
gi 516061977 146 SFGLRNVTEkekALRSMfrvLKPGGRLLV 174
Cdd:COG2518  139 TAAAPEVPE---ALLEQ---LAPGGRLVA 161
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 70-174 1.50e-06

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: 47.49  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  70 GQRVLDLAGGTGDLTAKFSRLvGEQGEVVLADINDSMLKMGREKLRNNGiVGNVSYVQANAeALPFPDNYFDCItIS--- 146
Cdd:COG2813   50 GGRVLDLGCGYGVIGLALAKR-NPEARVTLVDVNARAVELARANAAANG-LENVEVLWSDG-LSGVPDGSFDLI-LSnpp 125

                         90       100       110
                 ....*....|....*....|....*....|..
gi 516061977 147 FGLRNVTEKEkALRSMF----RVLKPGGRLLV 174
Cdd:COG2813  126 FHAGRAVDKE-VAHALIadaaRHLRPGGELWL 156
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
72-172 5.13e-06

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 46.50  E-value: 5.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  72 RVLDLAGGTGDLTAKFSRLvGEQgeVVLADINDSMLKMGREKLRNNGIVGNVSYVQANAEAL-PFPDNYFDCITISFGLR 150
Cdd:PRK11036  47 RVLDAGGGEGQTAIKLAEL-GHQ--VILCDLSAEMIQRAKQAAEAKGVSDNMQFIHCAAQDIaQHLETPVDLILFHAVLE 123

                         90       100
                 ....*....|....*....|..
gi 516061977 151 NVTEKEKALRSMFRVLKPGGRL 172
Cdd:PRK11036 124 WVADPKSVLQTLWSVLRPGGAL 145
PLN02490 PLN02490
MPBQ/MSBQ methyltransferase
 69-239 1.78e-05

MPBQ/MSBQ methyltransferase


Pssm-ID: 215270 [Multi-domain]  Cd Length: 340  Bit Score: 45.27  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  69 RGQRVLDLAGGTGDLTAKFSRLVgEQGEVVLADINDSMLKMGREKlrnnGIVGNVSYVQANAEALPFPDNYFDCITISFG 148
Cdd:PLN02490 113 RNLKVVDVGGGTGFTTLGIVKHV-DAKNVTILDQSPHQLAKAKQK----EPLKECKIIEGDAEDLPFPTDYADRYVSAGS 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977 149 LRNVTEKEKALRSMFRVLKPGGRLLvlefskpLLAPLskaYDTYSFHilprigelvaqdaesyRYLAESIRMHPDQETLK 228
Cdd:PLN02490 188 IEYWPDPQRGIKEAYRVLKIGGKAC-------LIGPV---HPTFWLS----------------RFFADVWMLFPKEEEYI 241

                        170
                 ....*....|.
gi 516061977 229 DMMSDAGFENV 239
Cdd:PLN02490 242 EWFTKAGFKDV 252
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 70-239 4.24e-05

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 44.36  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  70 GQRVLDLAGGTGDltAKFSRLVGEQGEVVLADINDSMLKMGREklRNNGIVGNVSYVQANAEALPFPDNYFDCITISFGL 149
Cdd:PLN02336 267 GQKVLDVGCGIGG--GDFYMAENFDVHVVGIDLSVNMISFALE--RAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTI 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977 150 RNVTEKEKALRSMFRVLKPGGRLLVLEFSKPLLAPLSKaydtYSFHILPRIGELvaQDAESYrylaesirmhpdqetlKD 229
Cdd:PLN02336 343 LHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTPSPE----FAEYIKQRGYDL--HDVQAY----------------GQ 400

                        170
                 ....*....|
gi 516061977 230 MMSDAGFENV 239
Cdd:PLN02336 401 MLKDAGFDDV 410
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
66-172 5.09e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 43.74  E-value: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  66 GVRRGQRVLDLAGGTGdLTAKFSRlvgEQG--EVVLADINDSMLKMGR-----EKLRNNGI---VGNVSyvqanaEALP- 134
Cdd:COG2521  129 GVRRGDRVLDTCTGLG-YTAIEAL---KRGarEVITVEKDPNVLELAElnpwsRELANERIkiiLGDAS------EVIKt 198

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 516061977 135 FPDNYFDCItI----SFGLRNVTEKEKALRSMFRVLKPGGRL 172
Cdd:COG2521  199 FPDESFDAI-IhdppRFSLAGELYSLEFYRELYRVLKPGGRL 239
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 67-174 5.11e-05

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 42.86  E-value: 5.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  67 VRRGQRVLDLAGGTGDLTAKFSRLVGEQGEVVLADINDSMLKMGREKLRNNGIVGNVSYVQANA-EALPFPDNYFDCITI 145
Cdd:PRK00377  38 LRKGDMILDIGCGTGSVTVEASLLVGETGKVYAVDKDEKAINLTRRNAEKFGVLNNIVLIKGEApEILFTINEKFDRIFI 117

                         90       100
                 ....*....|....*....|....*....
gi 516061977 146 SFGLRnvtEKEKALRSMFRVLKPGGRLLV 174
Cdd:PRK00377 118 GGGSE---KLKEIISASWEIIKKGGRIVI 143
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
60-139 1.12e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 41.81  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  60 YAIDCSGVRRGQRVLDLAGGTGDLtAKFSRLVGEQgEVVLADINDSMLKMGREKLRNNGivGNVSYVQANAEALPFPDNY 139
Cdd:COG2263   36 HLAYLRGDIEGKTVLDLGCGTGML-AIGAALLGAK-KVVGVDIDPEALEIARENAERLG--VRVDFIRADVTRIPLGGSV 111
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 67-172 1.66e-04

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: 41.67  E-value: 1.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  67 VRRGQRVLDLAGGTGD----LTAKFSRLvgeqgEVVLADINDSMLKMGREKLRNNGIVGNVSYVQANAEALP--FPDNYF 140
Cdd:COG4123   35 VKKGGRVLDLGTGTGVialmLAQRSPGA-----RITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAaeLPPGSF 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516061977 141 DCIT-------ISFGLRNVTEKEKA------------LRSMFRVLKPGGRL 172
Cdd:COG4123  110 DLVVsnppyfkAGSGRKSPDEARAIarhedaltledlIRAAARLLKPGGRF 160
PLN02244 PLN02244
tocopherol O-methyltransferase
 13-174 1.93e-04

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 42.04  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  13 ETTHFGFRTVAKNNKAEMVAEVfhsvaakyDLMNDLMSFGihriwkryAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVG 92
Cdd:PLN02244  78 EHMHHGYYDPGASRGDHRQAQI--------RMIEESLAWA--------GVPDDDEKRPKRIVDVGCGIGGSSRYLARKYG 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  93 EQGE-VVLADINdsmLKMGREKLRNNGIVGNVSYVQANAEALPFPDNYFDCITISFGLRNVTEKEKALRSMFRVLKPGGR 171
Cdd:PLN02244 142 ANVKgITLSPVQ---AARANALAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPDKRKFVQELARVAAPGGR 218


                 ...
gi 516061977 172 LLV 174
Cdd:PLN02244 219 III 221
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 59-132 3.82e-04

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 41.32  E-value: 3.82e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516061977  59 RYAIDCSGVRRGQRVLDLAGGTGDLTAKFSRLVgeqGEVVLADINDSMLKMGREKLRNNGIvGNVSYVQANAEA 132
Cdd:COG2265  223 AAALEWLDLTGGERVLDLYCGVGTFALPLARRA---KKVIGVEIVPEAVEDARENARLNGL-KNVEFVAGDLEE 292
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 67-174 6.46e-04

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: 39.50  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977   67 VRRGQRVLDLAGGTGDLTAKFSRLVGEQgEVVLADINDSMLKMGREKLRNNGiVGNVSYVQANAEAlPFPDNYFDCItIS 146
Cdd:pfam05175  29 KDLSGKVLDLGCGAGVLGAALAKESPDA-ELTMVDINARALESARENLAANG-LENGEVVASDVYS-GVEDGKFDLI-IS 104

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 516061977  147 ---FGLRNVTEKEKALRsMF----RVLKPGGRLLV 174
Cdd:pfam05175 105 nppFHAGLATTYNVAQR-FIadakRHLRPGGELWI 138
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 60-179 1.04e-03

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


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 39.86  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  60 YAIDCSGVRRGQ-----RVLDL-AGGTGDLTAKFSRLVGeqGEVVLADINDSML----KMGREKLRNNGIVGNVSYVQAN 129
Cdd:cd08261  145 LAIGAHAVRRAGvtagdTVLVVgAGPIGLGVIQVAKARG--ARVIVVDIDDERLefarELGADDTINVGDEDVAARLREL 222

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 516061977 130 AEAlPFPDNYFDCITISfglrnvtekeKALRSMFRVLKPGGRLLVLEFSK 179
Cdd:cd08261  223 TDG-EGADVVIDATGNP----------ASMEEAVELVAHGGRVVLVGLSK 261
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 65-175 1.47e-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: 39.23  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516061977  65 SGVRRGQRVLDL-AGGTGDLTAKFSRLVGeqGEVVLADINDSMLKMGREKLRNNGIvgNVSYVQANAEALPFPDNYFDCI 143
Cdd:cd05188  130 GVLKPGDTVLVLgAGGVGLLAAQLAKAAG--ARVIVTDRSDEKLELAKELGADHVI--DYKEEDLEEELRLTGGGGADVV 205

                         90       100       110
                 ....*....|....*....|....*....|..
gi 516061977 144 TisfglrNVTEKEKALRSMFRVLKPGGRLLVL 175
Cdd:cd05188  206 I------DAVGGPETLAQALRLLRPGGRIVVV 231
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
133-174 2.15e-03

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 37.92  E-value: 2.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 516061977 133 LPFPDNYFDCITIS-----FGLRNVtekEKALRSMFRVLKPGGRLLV 174
Cdd:COG4627   40 LPFPDNSVDAIYSShvlehLDYEEA---PLALKECYRVLKPGGILRI 83
 
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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