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Conserved domains on  [gi|1063724804|ref|NP_001328344|]
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magnesium-protoporphyrin IX methyltransferase [Arabidopsis thaliana]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11476976)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 35-326 0e+00

magnesium protoporphyrin IX methyltransferase


:

Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 566.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804  35 FPNATRFNVTPRSRAATVVAASVTDLAGVDSTTIAVLGGGSVAALAAMVSLTDPERRRKLQAEEVGGGDKEVVREYFNST 114
Cdd:PLN02585   21 FPNATLFAVPPRSRAATVAAASVADLAGVDSTTFAVGGGGAVAALAAALSLTDPERRRQLQAEEVGGDDKEVVREYFNTT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 115 GFERWRKIYGETDEVNRVQKDIRLGHAKTVENTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVA 194
Cdd:PLN02585  101 GFERWRKIYGETDEVNKVQLDIRLGHAQTVEKVLLWLAEDGSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 195 EAEMKAKAQL---PSENLPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASLAEKRVILSFAPKTFYYDILK 271
Cdd:PLN02585  181 EAERRAKEALaalPPEVLPKFEANDLESLSGKYDTVTCLDVLIHYPQDKADGMIAHLASLAEKRLIISFAPKTLYYDILK 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063724804 272 RIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEAVPM 326
Cdd:PLN02585  261 RIGELFPGPSKATRAYLHAEADVERALKKAGWKVARREMTATQFYFSRLLEAVPV 315
 
Name Accession Description Interval E-value
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 35-326 0e+00

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 566.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804  35 FPNATRFNVTPRSRAATVVAASVTDLAGVDSTTIAVLGGGSVAALAAMVSLTDPERRRKLQAEEVGGGDKEVVREYFNST 114
Cdd:PLN02585   21 FPNATLFAVPPRSRAATVAAASVADLAGVDSTTFAVGGGGAVAALAAALSLTDPERRRQLQAEEVGGDDKEVVREYFNTT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 115 GFERWRKIYGETDEVNRVQKDIRLGHAKTVENTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVA 194
Cdd:PLN02585  101 GFERWRKIYGETDEVNKVQLDIRLGHAQTVEKVLLWLAEDGSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 195 EAEMKAKAQL---PSENLPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASLAEKRVILSFAPKTFYYDILK 271
Cdd:PLN02585  181 EAERRAKEALaalPPEVLPKFEANDLESLSGKYDTVTCLDVLIHYPQDKADGMIAHLASLAEKRLIISFAPKTLYYDILK 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063724804 272 RIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEAVPM 326
Cdd:PLN02585  261 RIGELFPGPSKATRAYLHAEADVERALKKAGWKVARREMTATQFYFSRLLEAVPV 315
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 103-323 3.13e-123

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 352.56  E-value: 3.13e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 103 DKEVVREYFNSTGFERWRKIYGETDEVNRVQKDIRLGHAKTVENTMLMLTEDrSLAGVTVCDAGCGTGLLSIPLAKEGAI 182
Cdd:TIGR02021   1 QKEQVRHYFDGTAFQRWARIYGSGDPVSRVRQTVREGRAAMRRKLLDWLPKD-PLKGKRVLDAGCGTGLLSIELAKRGAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 183 VSASDISAAMVAEAEMKAKAQLPSENlPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASLAEKRVILSFAP 262
Cdd:TIGR02021  80 VKAVDISEQMVQMARNRAQGRDVAGN-VEFEVNDLLSLCGEFDIVVCMDVLIHYPASDMAKALGHLASLTKERVIFTFAP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063724804 263 KTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEA 323
Cdd:TIGR02021 159 KTAWLAFLKMIGELFPGSSRATSAYLHPMTDLERALGELGWKIVREGLVSTGFYNSMLLEI 219
Mg-por_mtran_C pfam07109
Magnesium-protoporphyrin IX methyltransferase C-terminus; This family represents the ...
 229-325 5.56e-54

Magnesium-protoporphyrin IX methyltransferase C-terminus; This family represents the C-terminus (approximately 100 residues) of bacterial and eukaryotic Magnesium-protoporphyrin IX methyltransferase (EC:2.1.1.11). This converts magnesium-protoporphyrin IX to magnesium-protoporphyrin IX methylester using S-adenosyl-L-methionine as a cofactor.


Pssm-ID: 462091  Cd Length: 97  Bit Score: 171.53  E-value: 5.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 229 CLDVLIHYPQNKADGMIAHLASLAEKRVILSFAPKTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKR 308
Cdd:pfam07109   1 CMDVLIHYPAEDAAQMLAHLASLTRGRLIFTFAPRTPLLALLKKIGELFPGPSRATRAYPHREADLRRALAAAGWKVGRT 80

                          90
                  ....*....|....*..
gi 1063724804 309 GLTTTQFYFSRLIEAVP 325
Cdd:pfam07109  81 ERISTGFYFSRLLEAVR 97
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 153-260 5.52e-20

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 83.91  E-value: 5.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 153 EDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAeaemKAKAQLPSENLpKFEVNDLESL---TGKYDTVVC 229
Cdd:COG2227    19 ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALE----IARERAAELNV-DFVQGDLEDLpleDGSFDLVIC 93

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063724804 230 LDVLIHYPQnkADGMIAHLASLAEK--RVILSF 260
Cdd:COG2227    94 SEVLEHLPD--PAALLRELARLLKPggLLLLST 124
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 161-258 2.72e-08

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: 51.28  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 161 TVCDAGCGTGLLSIPLAK-EGAIVSASDISAAMVAEAEmKAKAQLPSENLpKFEVNDLESLT----GKYDTVVCLDVLIH 235
Cdd:cd02440     1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELAR-KAAAALLADNV-EVLKGDAEELPpeadESFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|...
gi 1063724804 236 YPQNKADGMIAHLASLAEKRVIL 258
Cdd:cd02440    79 LVEDLARFLEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 35-326 0e+00

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 566.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804  35 FPNATRFNVTPRSRAATVVAASVTDLAGVDSTTIAVLGGGSVAALAAMVSLTDPERRRKLQAEEVGGGDKEVVREYFNST 114
Cdd:PLN02585   21 FPNATLFAVPPRSRAATVAAASVADLAGVDSTTFAVGGGGAVAALAAALSLTDPERRRQLQAEEVGGDDKEVVREYFNTT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 115 GFERWRKIYGETDEVNRVQKDIRLGHAKTVENTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVA 194
Cdd:PLN02585  101 GFERWRKIYGETDEVNKVQLDIRLGHAQTVEKVLLWLAEDGSLAGVTVCDAGCGTGSLAIPLALEGAIVSASDISAAMVA 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 195 EAEMKAKAQL---PSENLPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASLAEKRVILSFAPKTFYYDILK 271
Cdd:PLN02585  181 EAERRAKEALaalPPEVLPKFEANDLESLSGKYDTVTCLDVLIHYPQDKADGMIAHLASLAEKRLIISFAPKTLYYDILK 260

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063724804 272 RIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEAVPM 326
Cdd:PLN02585  261 RIGELFPGPSKATRAYLHAEADVERALKKAGWKVARREMTATQFYFSRLLEAVPV 315
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 103-323 3.13e-123

magnesium protoporphyrin O-methyltransferase; This model represents the S-adenosylmethionine-dependent O-methyltransferase responsible for methylation of magnesium protoporphyrin IX. This step is essentiasl for the biosynthesis of both chlorophyll and bacteriochlorophyll. This model encompasses two closely related clades, from cyanobacteria (and plants) where it is called ChlM and other photosynthetic bacteria where it is known as BchM. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273930 [Multi-domain]  Cd Length: 219  Bit Score: 352.56  E-value: 3.13e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 103 DKEVVREYFNSTGFERWRKIYGETDEVNRVQKDIRLGHAKTVENTMLMLTEDrSLAGVTVCDAGCGTGLLSIPLAKEGAI 182
Cdd:TIGR02021   1 QKEQVRHYFDGTAFQRWARIYGSGDPVSRVRQTVREGRAAMRRKLLDWLPKD-PLKGKRVLDAGCGTGLLSIELAKRGAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 183 VSASDISAAMVAEAEMKAKAQLPSENlPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASLAEKRVILSFAP 262
Cdd:TIGR02021  80 VKAVDISEQMVQMARNRAQGRDVAGN-VEFEVNDLLSLCGEFDIVVCMDVLIHYPASDMAKALGHLASLTKERVIFTFAP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063724804 263 KTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEA 323
Cdd:TIGR02021 159 KTAWLAFLKMIGELFPGSSRATSAYLHPMTDLERALGELGWKIVREGLVSTGFYNSMLLEI 219
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 103-325 1.40e-116

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 336.04  E-value: 1.40e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 103 DKEVVREYFNSTGFERWRKIYGEtDEVNRVQKDIRLGHAKTVENTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAI 182
Cdd:PRK07580    9 HKSEVRTYFNRTGFDRWARIYSD-APVSKVRATVRAGHQRMRDTVLSWLPADGDLTGLRILDAGCGVGSLSIPLARRGAK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 183 VSASDISAAMVAEAEMKAKAQLPSENlPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASLAEKRVILSFAP 262
Cdd:PRK07580   88 VVASDISPQMVEEARERAPEAGLAGN-ITFEVGDLESLLGRFDTVVCLDVLIHYPQEDAARMLAHLASLTRGSLIFTFAP 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063724804 263 KTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEAVP 325
Cdd:PRK07580  167 YTPLLALLHWIGGLFPGPSRTTRIYPHREKGIRRALAAAGFKVVRTERISSGFYFSRLLEAVR 229
Mg-por_mtran_C pfam07109
Magnesium-protoporphyrin IX methyltransferase C-terminus; This family represents the ...
 229-325 5.56e-54

Magnesium-protoporphyrin IX methyltransferase C-terminus; This family represents the C-terminus (approximately 100 residues) of bacterial and eukaryotic Magnesium-protoporphyrin IX methyltransferase (EC:2.1.1.11). This converts magnesium-protoporphyrin IX to magnesium-protoporphyrin IX methylester using S-adenosyl-L-methionine as a cofactor.


Pssm-ID: 462091  Cd Length: 97  Bit Score: 171.53  E-value: 5.56e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 229 CLDVLIHYPQNKADGMIAHLASLAEKRVILSFAPKTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKR 308
Cdd:pfam07109   1 CMDVLIHYPAEDAAQMLAHLASLTRGRLIFTFAPRTPLLALLKKIGELFPGPSRATRAYPHREADLRRALAAAGWKVGRT 80

                          90
                  ....*....|....*..
gi 1063724804 309 GLTTTQFYFSRLIEAVP 325
Cdd:pfam07109  81 ERISTGFYFSRLLEAVR 97
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 153-260 5.52e-20

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 83.91  E-value: 5.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 153 EDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAeaemKAKAQLPSENLpKFEVNDLESL---TGKYDTVVC 229
Cdd:COG2227    19 ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALE----IARERAAELNV-DFVQGDLEDLpleDGSFDLVIC 93

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063724804 230 LDVLIHYPQnkADGMIAHLASLAEK--RVILSF 260
Cdd:COG2227    94 SEVLEHLPD--PAALLRELARLLKPggLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 162-251 1.53e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 71.06  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 162 VCDAGCGTGLLSIPLAKE-GAIVSASDISAAMVAEAEMKAKAQLPSenlPKFEVNDLESL---TGKYDTVVCLDVLIHYP 237
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLN---VEFVQGDAEDLpfpDGSFDLVVSSGVLHHLP 77

                          90
                  ....*....|....
gi 1063724804 238 QNKADGMIAHLASL 251
Cdd:pfam13649  78 DPDLEAALREIARV 91
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
116-305 1.47e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 67.72  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 116 FERWRKIYgETDEVNRVQKDirlGHAKTVENTMLMLTEDRSLagvTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAe 195
Cdd:COG4976    11 FDQYADSY-DAALVEDLGYE---APALLAEELLARLPPGPFG---RVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLA- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 196 aemKAKAQLPSENLPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKAdgMIAHLASLAEK--RVILSFapktfyydilkri 273
Cdd:COG4976    83 ---KAREKGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAA--VFAGVARALKPggLFIFSV------------- 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063724804 274 gelfpGPSKATRAYLHSEADVERALGKVGWKI 305
Cdd:COG4976   145 -----EDADGSGRYAHSLDYVRDLLAAAGFEV 171
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 158-275 2.57e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 64.94  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 158 AGVTVCDAGCGTGLLSIPLAKE-GAIVSASDISAAMVAeaemKAKAQLPSENLPK--FEVNDLESL----TGKYDTVVCL 230
Cdd:COG0500    26 KGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIA----LARARAAKAGLGNveFLVADLAELdplpAESFDLVVAF 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063724804 231 DVLIHYPQNKADGMIAHLASLAEK--RVILSFAPKTFYYDILKRIGE 275
Cdd:COG0500   102 GVLHHLPPEEREALLRELARALKPggVLLLSASDAAAALSLARLLLL 148
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 159-237 9.53e-12

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: 61.93  E-value: 9.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 159 GVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAemKAKAQLPSENLpKFEVNDLESL---TGKYDTVVCLDVLIH 235
Cdd:COG2226    23 GARVLDLGCGTGRLALALAERGARVTGVDISPEMLELA--RERAAEAGLNV-EFVVGDAEDLpfpDGSFDLVISSFVLHH 99


                  ..
gi 1063724804 236 YP 237
Cdd:COG2226   100 LP 101
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
158-251 2.88e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 56.37  E-value: 2.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 158 AGVTVCDAGCGTGLLSIPLAKE--GAIVSASDISAAMVAeaemKAKAQLPseNLpKFEVNDLESLT--GKYDTVVCLDVL 233
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLA----RARARLP--NV-RFVVADLRDLDppEPFDLVVSNAAL 73

                          90
                  ....*....|....*...
gi 1063724804 234 IHYPQNKAdgMIAHLASL 251
Cdd:COG4106    74 HWLPDHAA--LLARLAAA 89
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 158-251 9.25e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 56.48  E-value: 9.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 158 AGVTVCDAGCGTGLLSIPLAKE-GAIVSASDISAAMVAEAEMKAKAQLPSENLpKFEVNDLESL--TGKYDTVVCLDVLI 234
Cdd:COG2230    51 PGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLADRV-EVRLADYRDLpaDGQFDAIVSIGMFE 129

                          90
                  ....*....|....*..
gi 1063724804 235 HYPQNKADGMIAHLASL 251
Cdd:COG2230   130 HVGPENYPAYFAKVARL 146
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 164-237 9.55e-10

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 54.98  E-value: 9.55e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063724804 164 DAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKaqlpsENLPKFEVNDLESLT---GKYDTVVCLDVLIHYP 237
Cdd:pfam08241   2 DVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAP-----REGLTFVVGDAEDLPfpdNSFDLVLSSEVLHHVE 73
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 161-258 2.72e-08

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: 51.28  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 161 TVCDAGCGTGLLSIPLAK-EGAIVSASDISAAMVAEAEmKAKAQLPSENLpKFEVNDLESLT----GKYDTVVCLDVLIH 235
Cdd:cd02440     1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELAR-KAAAALLADNV-EVLKGDAEELPpeadESFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|...
gi 1063724804 236 YPQNKADGMIAHLASLAEKRVIL 258
Cdd:cd02440    79 LVEDLARFLEEARRLLKPGGVLV 101
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 164-251 2.89e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 50.83  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 164 DAGCGTGLLSIPLAKE--GAIVSASDISAAMV--AEAEMKAKAQLPSENLPKFEVNDLESLTGKYDTVVCLDVLiHYPQN 239
Cdd:pfam08242   2 EIGCGTGTLLRALLEAlpGLEYTGLDISPAALeaARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVL-HHLAD 80

                          90
                  ....*....|..
gi 1063724804 240 KaDGMIAHLASL 251
Cdd:pfam08242  81 P-RAVLRNIRRL 91
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 161-305 3.07e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 52.43  E-value: 3.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 161 TVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKAQLpsenlpkFEVNDLESLTGKYDTVVCLDVL--IHYPQ 238
Cdd:pfam13489  25 RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQ-------FDEQEAAVPAGKFDVIVAREVLehVPDPP 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063724804 239 NKADGMIAHLAslAEKRVILSFAPKTFYYDIL-KRIGELFPgpsKATRAYLHSEADVERALGKVGWKI 305
Cdd:pfam13489  98 ALLRQIAALLK--PGGLLLLSTPLASDEADRLlLEWPYLRP---RNGHISLFSARSLKRLLEEAGFEV 160
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 158-237 5.69e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 51.26  E-value: 5.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 158 AGVTVCDAGCGTGLLSIPLAKE---GAIVSASDISAAMVAEAEMKAKaQLPSENLpKFEVNDLESLT-----GKYDTVVC 229
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQ-KLGFDNV-EFEQGDIEELPelledDKFDVVIS 80


                  ....*...
gi 1063724804 230 LDVLIHYP 237
Cdd:pfam13847  81 NCVLNHIP 88
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 145-228 1.17e-07

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 51.01  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 145 ENTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAemKAKAQLPSENLPKFEVNDLESLTGKY 224
Cdd:TIGR00537   6 EDSLLLEANLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKEL--RENAKLNNVGLDVVMTDLFKGVRGKF 83


                  ....
gi 1063724804 225 DTVV 228
Cdd:TIGR00537  84 DVIL 87
PRK08317 PRK08317
hypothetical protein; Provisional
 158-235 2.13e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 48.01  E-value: 2.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 158 AGVTVCDAGCGTGLLSIPLAKE---GAIVSASDISAAMVAEAEMKAKAQLPSEnlpKFEVNDLESL---TGKYDTVVCLD 231
Cdd:PRK08317   19 PGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNV---EFVRGDADGLpfpDGSFDAVRSDR 95


                  ....
gi 1063724804 232 VLIH 235
Cdd:PRK08317   96 VLQH 99
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 116-266 2.49e-06

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: 48.05  E-value: 2.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 116 FERWRKIYgetDEVNRVQKDIRLghaktveNTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVS--ASDISAAMV 193
Cdd:TIGR02072   2 FNKAAKTY---DRHAKIQREMAK-------RLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEfiALDISAGML 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 194 AEAEMKAKAQLpsenlpKFEVNDLESL---TGKYDTVVCLDVLihypQ--NKADGMIAHLASLAEKRVIL---SFAPKTF 265
Cdd:TIGR02072  72 AQAKTKLSENV------QFICGDAEKLpleDSSFDLIVSNLAL----QwcDDLSQALSELARVLKPGGLLafsTFGPGTL 141


                  .
gi 1063724804 266 Y 266
Cdd:TIGR02072 142 H 142
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
147-308 8.27e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 46.70  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 147 TMLMLT--EDRSLAGVTVCDAGCGTGLLSIPLAKEGAI-VSASDISAAMVAEAEmkakaqlpsENlpkFEVNDLESLTgk 223
Cdd:COG2264   135 TRLCLEalEKLLKPGKTVLDVGCGSGILAIAAAKLGAKrVLAVDIDPVAVEAAR---------EN---AELNGVEDRI-- 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 224 ydTVVCLDVLihyPQNKADGMIAHLasLAEkrVILSFAPKtfYYDILKrigelfPGpskatrAYL-------HSEADVER 296
Cdd:COG2264   201 --EVVLGDLL---EDGPYDLVVANI--LAN--PLIELAPD--LAALLK------PG------GYLilsgileEQADEVLA 257

                         170
                  ....*....|..
gi 1063724804 297 ALGKVGWKISKR 308
Cdd:COG2264   258 AYEAAGFELVER 269
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 161-227 9.17e-06

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 46.29  E-value: 9.17e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 161 TVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKAQlpsenlpKFEVNDLESL---TGKYDTV 227
Cdd:PRK10258   45 HVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAAD-------HYLAGDIESLplaTATFDLA 107
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 162-229 2.11e-05

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: 44.12  E-value: 2.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063724804 162 VCDAGCGTGLLSIPLAKEG--AIVSASDISAAMVAEAEMKAKAQLPsENLPKFEVNDLESLT-GKYDTVVC 229
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGL-ENGEVVASDVYSGVEdGKFDLIIS 104
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 155-235 4.25e-05

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 44.72  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 155 RSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKAQlPSENLPKFEVNDLESLTG---KYDTVVCLD 231
Cdd:PLN02396  128 KPFEGLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHADMD-PVTSTIEYLCTTAEKLADegrKFDAVLSLE 206


                  ....
gi 1063724804 232 VLIH 235
Cdd:PLN02396  207 VIEH 210
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 161-229 4.47e-05

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 43.64  E-value: 4.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063724804 161 TVCDAGCGTGLLSIPLAKE--GAIVSASDISAAMVAEAEMKAKAQlpseNLPKFEV---NDLESL-TGKYDTVVC 229
Cdd:COG2813    52 RVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVELARANAAAN----GLENVEVlwsDGLSGVpDGSFDLILS 122
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 161-231 7.84e-05

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: 44.01  E-value: 7.84e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063724804 161 TVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKAQlpseNLP--KFEVNDLE------SLTGKYDTVVcLD 231
Cdd:COG2265   236 RVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLN----GLKnvEFVAGDLEevlpelLWGGRPDVVV-LD 309
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
147-259 9.25e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 43.22  E-value: 9.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 147 TMLMLT--EDRSLAGVTVCDAGCGTGLLSIPLAKEGAI-VSASDISAAMVAEAEmkakaqlpsENlpkFEVNDLESLT-- 221
Cdd:PRK00517  106 TRLCLEalEKLVLPGKTVLDVGCGSGILAIAAAKLGAKkVLAVDIDPQAVEAAR---------EN---AELNGVELNVyl 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1063724804 222 ----GKYDTVVC---LDVLIHypqnkadgMIAHLASLAEK--RVILS 259
Cdd:PRK00517  174 pqgdLKADVIVAnilANPLLE--------LAPDLARLLKPggRLILS 212
PRK14968 PRK14968
putative methyltransferase; Provisional
 145-228 2.76e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.04  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 145 ENTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKAQLPSENLPKFEVNDL-ESLTG- 222
Cdd:PRK14968   10 EDSFLLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEVIRSDLfEPFRGd 89


                  ....*.
gi 1063724804 223 KYDTVV 228
Cdd:PRK14968   90 KFDVIL 95
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 153-259 2.90e-04

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 41.87  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 153 EDRSLAGVTVCDAGCGTGLLSIPLAKEGAI-VSASDISAAMVAEAEMKAKAQLPSENLPKFEVNDLesLTGKYDTVVC-- 229
Cdd:pfam06325 156 ERLVKPGESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDL--PKEKADVVVAni 233

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063724804 230 -LDVLIHypqnkadgMIAHLASL--AEKRVILS 259
Cdd:pfam06325 234 lADPLIE--------LAPDIYALvkPGGYLILS 258
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
120-208 4.33e-04

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 41.10  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 120 RKIYGETDEVNR---VQKDIrlghaktveNTMLMLTEDRSLagvTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEA 196
Cdd:PRK11036   15 RNIYGTTKGQIRqaiLWQDL---------DRLLAELPPRPL---RVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRA 82

                          90
                  ....*....|..
gi 1063724804 197 EMKAKAQLPSEN 208
Cdd:PRK11036   83 KQAAEAKGVSDN 94
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
157-228 4.85e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 40.66  E-value: 4.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063724804 157 LAGVTVCDAGCGTGLLSIPLAKEGA-IVSASDISAAMVAEAEMKAKAQLPSENLPKFEVNDLEsLTGKYDTVV 228
Cdd:COG2263    44 IEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIP-LGGSVDTVV 115
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
164-248 5.47e-04

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 40.49  E-value: 5.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 164 DAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEmKAKAQLPSENLpKFEVNDLESLT--GKYDTVVCLDVLIHYPQNKA 241
Cdd:PRK11207   36 DLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLE-RIKAAENLDNL-HTAVVDLNNLTfdGEYDFILSTVVLMFLEAKTI 113


                  ....*..
gi 1063724804 242 DGMIAHL 248
Cdd:PRK11207  114 PGLIANM 120
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 155-263 7.24e-04

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.52  E-value: 7.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063724804 155 RSLAGVTVCDAGCGTGLLSIPLAKE--GAIVSASDISAAMVAEAEMKAkAQLPSENLPKFEVNDL-ESLT--GKYDTVVC 229
Cdd:COG2890   109 PAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVARRNA-ERLGLEDRVRFLQGDLfEPLPgdGRFDLIVS 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063724804 230 --------------LDVLIHYPQN----KADGMIAHlaslaekRVILSFAPK 263
Cdd:COG2890   188 nppyipedeiallpPEVRDHEPRLaldgGEDGLDFY-------RRIIAQAPR 232
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 151-197 4.32e-03

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 38.22  E-value: 4.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1063724804 151 LTEDRSLAGVTVCDAGCGTGLLSIPLAKE--GAIVSASDISAAMVAEAE 197
Cdd:PRK09328  101 LEALLLKEPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVAR 149
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 159-210 5.64e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 37.83  E-value: 5.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063724804 159 GVTVCDAGCGTGLLSIPLAKEG---AIVSASDISAAMVAEAEMKAKAQLPSENLP 210
Cdd:PRK00216   52 GDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGMLAVGREKLRDLGLSGNVE 106
 
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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