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Conserved domains on  [gi|30686748|ref|NP_849438|]
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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
 1-312 0e+00

magnesium protoporphyrin IX methyltransferase


:

Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 572.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748    1 MPFAPSLLSSSSSVSQFLPRFPNATRFNVTPRSRAATVVAASVTDLAGVDSTTIAVLGGGSVAALAAMVSLTDPERRRKL 80
Cdd:PLN02585   1 MPFAPSALSASSSVAQFLPPFPNATLFAVPPRSRAATVAAASVADLAGVDSTTFAVGGGGAVAALAAALSLTDPERRRQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   81 QAEEVGGGDKEVVREYFNSTGFERWRKIYGETDEVNRVQKDIRLGHAKTVENTMLMLTEDRSLAGVTVCDAGCGTGLLSI 160
Cdd:PLN02585  81 QAEEVGGDDKEVVREYFNTTGFERWRKIYGETDEVNKVQLDIRLGHAQTVEKVLLWLAEDGSLAGVTVCDAGCGTGSLAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  161 PLAKEGAIVSASDISAAMVAEAEMKAKAQL---PSENLPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASL 237
Cdd:PLN02585 161 PLALEGAIVSASDISAAMVAEAERRAKEALaalPPEVLPKFEANDLESLSGKYDTVTCLDVLIHYPQDKADGMIAHLASL 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30686748  238 AEKRVILSFAPKTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEAVPM 312
Cdd:PLN02585 241 AEKRLIISFAPKTLYYDILKRIGELFPGPSKATRAYLHAEADVERALKKAGWKVARREMTATQFYFSRLLEAVPV 315
 
Name Accession Description Interval E-value
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 1-312 0e+00

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 572.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748    1 MPFAPSLLSSSSSVSQFLPRFPNATRFNVTPRSRAATVVAASVTDLAGVDSTTIAVLGGGSVAALAAMVSLTDPERRRKL 80
Cdd:PLN02585   1 MPFAPSALSASSSVAQFLPPFPNATLFAVPPRSRAATVAAASVADLAGVDSTTFAVGGGGAVAALAAALSLTDPERRRQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   81 QAEEVGGGDKEVVREYFNSTGFERWRKIYGETDEVNRVQKDIRLGHAKTVENTMLMLTEDRSLAGVTVCDAGCGTGLLSI 160
Cdd:PLN02585  81 QAEEVGGDDKEVVREYFNTTGFERWRKIYGETDEVNKVQLDIRLGHAQTVEKVLLWLAEDGSLAGVTVCDAGCGTGSLAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  161 PLAKEGAIVSASDISAAMVAEAEMKAKAQL---PSENLPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASL 237
Cdd:PLN02585 161 PLALEGAIVSASDISAAMVAEAERRAKEALaalPPEVLPKFEANDLESLSGKYDTVTCLDVLIHYPQDKADGMIAHLASL 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30686748  238 AEKRVILSFAPKTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEAVPM 312
Cdd:PLN02585 241 AEKRLIISFAPKTLYYDILKRIGELFPGPSKATRAYLHAEADVERALKKAGWKVARREMTATQFYFSRLLEAVPV 315
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 89-309 9.74e-124

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: 352.95  E-value: 9.74e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748    89 DKEVVREYFNSTGFERWRKIYGETDEVNRVQKDIRLGHAKTVENTMLMLTEDrSLAGVTVCDAGCGTGLLSIPLAKEGAI 168
Cdd:TIGR02021   1 QKEQVRHYFDGTAFQRWARIYGSGDPVSRVRQTVREGRAAMRRKLLDWLPKD-PLKGKRVLDAGCGTGLLSIELAKRGAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   169 VSASDISAAMVAEAEMKAKAQLPSENlPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASLAEKRVILSFAP 248
Cdd:TIGR02021  80 VKAVDISEQMVQMARNRAQGRDVAGN-VEFEVNDLLSLCGEFDIVVCMDVLIHYPASDMAKALGHLASLTKERVIFTFAP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30686748   249 KTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEA 309
Cdd:TIGR02021 159 KTAWLAFLKMIGELFPGSSRATSAYLHPMTDLERALGELGWKIVREGLVSTGFYNSMLLEI 219
Mg-por_mtran_C pfam07109
Magnesium-protoporphyrin IX methyltransferase C-terminus; This family represents the ...
 215-311 5.94e-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: 171.15  E-value: 5.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   215 CLDVLIHYPQNKADGMIAHLASLAEKRVILSFAPKTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKR 294
Cdd:pfam07109   1 CMDVLIHYPAEDAAQMLAHLASLTRGRLIFTFAPRTPLLALLKKIGELFPGPSRATRAYPHREADLRRALAAAGWKVGRT 80

                          90
                  ....*....|....*..
gi 30686748   295 GLTTTQFYFSRLIEAVP 311
Cdd:pfam07109  81 ERISTGFYFSRLLEAVR 97
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 139-246 6.71e-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: 83.53  E-value: 6.71e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 139 EDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAeaemKAKAQLPSENLpKFEVNDLESL---TGKYDTVVC 215
Cdd:COG2227  19 ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALE----IARERAAELNV-DFVQGDLEDLpleDGSFDLVIC 93

                        90       100       110
                ....*....|....*....|....*....|...
gi 30686748 216 LDVLIHYPQnkADGMIAHLASLAEK--RVILSF 246
Cdd:COG2227  94 SEVLEHLPD--PAALLRELARLLKPggLLLLST 124
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 147-244 3.67e-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: 50.51  E-value: 3.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 147 TVCDAGCGTGLLSIPLAK-EGAIVSASDISAAMVAEAEmKAKAQLPSENLpKFEVNDLESLT----GKYDTVVCLDVLIH 221
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELAR-KAAAALLADNV-EVLKGDAEELPpeadESFDVIISDPPLHH 78

                        90       100
                ....*....|....*....|...
gi 30686748 222 YPQNKADGMIAHLASLAEKRVIL 244
Cdd:cd02440  79 LVEDLARFLEEARRLLKPGGVLV 101
 
Name Accession Description Interval E-value
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 1-312 0e+00

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 572.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748    1 MPFAPSLLSSSSSVSQFLPRFPNATRFNVTPRSRAATVVAASVTDLAGVDSTTIAVLGGGSVAALAAMVSLTDPERRRKL 80
Cdd:PLN02585   1 MPFAPSALSASSSVAQFLPPFPNATLFAVPPRSRAATVAAASVADLAGVDSTTFAVGGGGAVAALAAALSLTDPERRRQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   81 QAEEVGGGDKEVVREYFNSTGFERWRKIYGETDEVNRVQKDIRLGHAKTVENTMLMLTEDRSLAGVTVCDAGCGTGLLSI 160
Cdd:PLN02585  81 QAEEVGGDDKEVVREYFNTTGFERWRKIYGETDEVNKVQLDIRLGHAQTVEKVLLWLAEDGSLAGVTVCDAGCGTGSLAI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  161 PLAKEGAIVSASDISAAMVAEAEMKAKAQL---PSENLPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASL 237
Cdd:PLN02585 161 PLALEGAIVSASDISAAMVAEAERRAKEALaalPPEVLPKFEANDLESLSGKYDTVTCLDVLIHYPQDKADGMIAHLASL 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30686748  238 AEKRVILSFAPKTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEAVPM 312
Cdd:PLN02585 241 AEKRLIISFAPKTLYYDILKRIGELFPGPSKATRAYLHAEADVERALKKAGWKVARREMTATQFYFSRLLEAVPV 315
BchM-ChlM TIGR02021
magnesium protoporphyrin O-methyltransferase; This model represents the ...
 89-309 9.74e-124

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: 352.95  E-value: 9.74e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748    89 DKEVVREYFNSTGFERWRKIYGETDEVNRVQKDIRLGHAKTVENTMLMLTEDrSLAGVTVCDAGCGTGLLSIPLAKEGAI 168
Cdd:TIGR02021   1 QKEQVRHYFDGTAFQRWARIYGSGDPVSRVRQTVREGRAAMRRKLLDWLPKD-PLKGKRVLDAGCGTGLLSIELAKRGAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   169 VSASDISAAMVAEAEMKAKAQLPSENlPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASLAEKRVILSFAP 248
Cdd:TIGR02021  80 VKAVDISEQMVQMARNRAQGRDVAGN-VEFEVNDLLSLCGEFDIVVCMDVLIHYPASDMAKALGHLASLTKERVIFTFAP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30686748   249 KTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEA 309
Cdd:TIGR02021 159 KTAWLAFLKMIGELFPGSSRATSAYLHPMTDLERALGELGWKIVREGLVSTGFYNSMLLEI 219
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 89-311 1.75e-116

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 334.88  E-value: 1.75e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   89 DKEVVREYFNSTGFERWRKIYGEtDEVNRVQKDIRLGHAKTVENTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAI 168
Cdd:PRK07580   9 HKSEVRTYFNRTGFDRWARIYSD-APVSKVRATVRAGHQRMRDTVLSWLPADGDLTGLRILDAGCGVGSLSIPLARRGAK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  169 VSASDISAAMVAEAEMKAKAQLPSENlPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKADGMIAHLASLAEKRVILSFAP 248
Cdd:PRK07580  88 VVASDISPQMVEEARERAPEAGLAGN-ITFEVGDLESLLGRFDTVVCLDVLIHYPQEDAARMLAHLASLTRGSLIFTFAP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30686748  249 KTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKRGLTTTQFYFSRLIEAVP 311
Cdd:PRK07580 167 YTPLLALLHWIGGLFPGPSRTTRIYPHREKGIRRALAAAGFKVVRTERISSGFYFSRLLEAVR 229
Mg-por_mtran_C pfam07109
Magnesium-protoporphyrin IX methyltransferase C-terminus; This family represents the ...
 215-311 5.94e-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: 171.15  E-value: 5.94e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   215 CLDVLIHYPQNKADGMIAHLASLAEKRVILSFAPKTFYYDILKRIGELFPGPSKATRAYLHSEADVERALGKVGWKISKR 294
Cdd:pfam07109   1 CMDVLIHYPAEDAAQMLAHLASLTRGRLIFTFAPRTPLLALLKKIGELFPGPSRATRAYPHREADLRRALAAAGWKVGRT 80

                          90
                  ....*....|....*..
gi 30686748   295 GLTTTQFYFSRLIEAVP 311
Cdd:pfam07109  81 ERISTGFYFSRLLEAVR 97
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 139-246 6.71e-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: 83.53  E-value: 6.71e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 139 EDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAeaemKAKAQLPSENLpKFEVNDLESL---TGKYDTVVC 215
Cdd:COG2227  19 ARLLPAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALE----IARERAAELNV-DFVQGDLEDLpleDGSFDLVIC 93

                        90       100       110
                ....*....|....*....|....*....|...
gi 30686748 216 LDVLIHYPQnkADGMIAHLASLAEK--RVILSF 246
Cdd:COG2227  94 SEVLEHLPD--PAALLRELARLLKPggLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 148-237 2.20e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 70.29  E-value: 2.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   148 VCDAGCGTGLLSIPLAKE-GAIVSASDISAAMVAEAEMKAKAQLPSenlPKFEVNDLESL---TGKYDTVVCLDVLIHYP 223
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRgGARVTGVDLSPEMLERARERAAEAGLN---VEFVQGDAEDLpfpDGSFDLVVSSGVLHHLP 77

                          90
                  ....*....|....
gi 30686748   224 QNKADGMIAHLASL 237
Cdd:pfam13649  78 DPDLEAALREIARV 91
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
102-291 3.54e-13

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 66.56  E-value: 3.54e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 102 FERWRKIYgETDEVNRVQKDirlGHAKTVENTMLMLTEDRSLagvTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAe 181
Cdd:COG4976  11 FDQYADSY-DAALVEDLGYE---APALLAEELLARLPPGPFG---RVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLA- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 182 aemKAKAQLPSENLPKFEVNDLESLTGKYDTVVCLDVLIHYPQNKAdgMIAHLASLAEK--RVILSFapktfyydilkri 259
Cdd:COG4976  83 ---KAREKGVYDRLLVADLADLAEPDGRFDLIVAADVLTYLGDLAA--VFAGVARALKPggLFIFSV------------- 144

                       170       180       190
                ....*....|....*....|....*....|..
gi 30686748 260 gelfpGPSKATRAYLHSEADVERALGKVGWKI 291
Cdd:COG4976 145 -----EDADGSGRYAHSLDYVRDLLAAAGFEV 171
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 144-261 5.94e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 63.78  E-value: 5.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 144 AGVTVCDAGCGTGLLSIPLAKE-GAIVSASDISAAMVAeaemKAKAQLPSENLPK--FEVNDLESL----TGKYDTVVCL 216
Cdd:COG0500  26 KGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIA----LARARAAKAGLGNveFLVADLAELdplpAESFDLVVAF 101

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 30686748 217 DVLIHYPQNKADGMIAHLASLAEK--RVILSFAPKTFYYDILKRIGE 261
Cdd:COG0500 102 GVLHHLPPEEREALLRELARALKPggVLLLSASDAAAALSLARLLLL 148
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 145-223 1.77e-11

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: 61.16  E-value: 1.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 145 GVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAemKAKAQLPSENLpKFEVNDLESL---TGKYDTVVCLDVLIH 221
Cdd:COG2226  23 GARVLDLGCGTGRLALALAERGARVTGVDISPEMLELA--RERAAEAGLNV-EFVVGDAEDLpfpDGSFDLVISSFVLHH 99


                ..
gi 30686748 222 YP 223
Cdd:COG2226 100 LP 101
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
144-237 5.12e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 55.60  E-value: 5.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 144 AGVTVCDAGCGTGLLSIPLAKE--GAIVSASDISAAMVAeaemKAKAQLPseNLpKFEVNDLESLT--GKYDTVVCLDVL 219
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLA----RARARLP--NV-RFVVADLRDLDppEPFDLVVSNAAL 73

                        90
                ....*....|....*...
gi 30686748 220 IHYPQNKAdgMIAHLASL 237
Cdd:COG4106  74 HWLPDHAA--LLARLAAA 89
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 150-223 1.33e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 54.21  E-value: 1.33e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30686748   150 DAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKaqlpsENLPKFEVNDLESLT---GKYDTVVCLDVLIHYP 223
Cdd:pfam08241   2 DVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAP-----REGLTFVVGDAEDLPfpdNSFDLVLSSEVLHHVE 73
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 144-237 1.38e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 56.09  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 144 AGVTVCDAGCGTGLLSIPLAKE-GAIVSASDISAAMVAEAEMKAKAQLPSENLpKFEVNDLESL--TGKYDTVVCLDVLI 220
Cdd:COG2230  51 PGMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAGLADRV-EVRLADYRDLpaDGQFDAIVSIGMFE 129

                        90
                ....*....|....*..
gi 30686748 221 HYPQNKADGMIAHLASL 237
Cdd:COG2230 130 HVGPENYPAYFAKVARL 146
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 147-291 2.85e-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: 2.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   147 TVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKAQLpsenlpkFEVNDLESLTGKYDTVVCLDVL--IHYPQ 224
Cdd:pfam13489  25 RVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQ-------FDEQEAAVPAGKFDVIVAREVLehVPDPP 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30686748   225 NKADGMIAHLAslAEKRVILSFAPKTFYYDIL-KRIGELFPgpsKATRAYLHSEADVERALGKVGWKI 291
Cdd:pfam13489  98 ALLRQIAALLK--PGGLLLLSTPLASDEADRLlLEWPYLRP---RNGHISLFSARSLKRLLEEAGFEV 160
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 147-244 3.67e-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: 50.51  E-value: 3.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 147 TVCDAGCGTGLLSIPLAK-EGAIVSASDISAAMVAEAEmKAKAQLPSENLpKFEVNDLESLT----GKYDTVVCLDVLIH 221
Cdd:cd02440   1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELAR-KAAAALLADNV-EVLKGDAEELPpeadESFDVIISDPPLHH 78

                        90       100
                ....*....|....*....|...
gi 30686748 222 YPQNKADGMIAHLASLAEKRVIL 244
Cdd:cd02440  79 LVEDLARFLEEARRLLKPGGVLV 101
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 150-237 3.99e-08

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 50.44  E-value: 3.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   150 DAGCGTGLLSIPLAKE--GAIVSASDISAAMV--AEAEMKAKAQLPSENLPKFEVNDLESLTGKYDTVVCLDVLiHYPQN 225
Cdd:pfam08242   2 EIGCGTGTLLRALLEAlpGLEYTGLDISPAALeaARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVL-HHLAD 80

                          90
                  ....*....|..
gi 30686748   226 KaDGMIAHLASL 237
Cdd:pfam08242  81 P-RAVLRNIRRL 91
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 144-223 4.51e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 51.65  E-value: 4.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   144 AGVTVCDAGCGTGLLSIPLAKE---GAIVSASDISAAMVAEAEMKAKaQLPSENLpKFEVNDLESLT-----GKYDTVVC 215
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQ-KLGFDNV-EFEQGDIEELPelledDKFDVVIS 80


                  ....*...
gi 30686748   216 LDVLIHYP 223
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 ...
 131-214 1.01e-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: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   131 ENTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAemKAKAQLPSENLPKFEVNDLESLTGKY 210
Cdd:TIGR00537   6 EDSLLLEANLRELKPDDVLEIGAGTGLVAIRLKGKGKCILTTDINPFAVKEL--RENAKLNNVGLDVVMTDLFKGVRGKF 83


                  ....
gi 30686748   211 DTVV 214
Cdd:TIGR00537  84 DVIL 87
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 102-252 2.31e-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: 2.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   102 FERWRKIYgetDEVNRVQKDIRLghaktveNTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVS--ASDISAAMV 179
Cdd:TIGR02072   2 FNKAAKTY---DRHAKIQREMAK-------RLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEfiALDISAGML 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   180 AEAEMKAKAQLpsenlpKFEVNDLESL---TGKYDTVVCLDVLihypQ--NKADGMIAHLASLAEKRVIL---SFAPKTF 251
Cdd:TIGR02072  72 AQAKTKLSENV------QFICGDAEKLpleDSSFDLIVSNLAL----QwcDDLSQALSELARVLKPGGLLafsTFGPGTL 141


                  .
gi 30686748   252 Y 252
Cdd:TIGR02072 142 H 142
PRK08317 PRK08317
hypothetical protein; Provisional
 144-221 2.90e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 47.62  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  144 AGVTVCDAGCGTGLLSIPLAKE---GAIVSASDISAAMVAEAEMKAKAQLPSEnlpKFEVNDLESL---TGKYDTVVCLD 217
Cdd:PRK08317  19 PGDRVLDVGCGPGNDARELARRvgpEGRVVGIDRSEAMLALAKERAAGLGPNV---EFVRGDADGLpfpDGSFDAVRSDR 95


                 ....
gi 30686748  218 VLIH 221
Cdd:PRK08317  96 VLQH 99
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
133-294 3.78e-06

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 47.48  E-value: 3.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 133 TMLMLT--EDRSLAGVTVCDAGCGTGLLSIPLAKEGAI-VSASDISAAMVAEAEmkakaqlpsENlpkFEVNDLESLTgk 209
Cdd:COG2264 135 TRLCLEalEKLLKPGKTVLDVGCGSGILAIAAAKLGAKrVLAVDIDPVAVEAAR---------EN---AELNGVEDRI-- 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 210 ydTVVCLDVLihyPQNKADGMIAHLasLAEkrVILSFAPKtfYYDILKrigelfPGpskatrAYL-------HSEADVER 282
Cdd:COG2264 201 --EVVLGDLL---EDGPYDLVVANI--LAN--PLIELAPD--LAALLK------PG------GYLilsgileEQADEVLA 257

                       170
                ....*....|..
gi 30686748 283 ALGKVGWKISKR 294
Cdd:COG2264 258 AYEAAGFELVER 269
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
 147-213 1.17e-05

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 45.90  E-value: 1.17e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  147 TVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKAQlpsenlpKFEVNDLESL---TGKYDTV 213
Cdd:PRK10258  45 HVLDAGCGPGWMSRYWRERGSQVTALDLSPPMLAQARQKDAAD-------HYLAGDIESLplaTATFDLA 107
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 148-215 2.81e-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: 43.73  E-value: 2.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30686748   148 VCDAGCGTGLLSIPLAKEG--AIVSASDISAAMVAEAEMKAKAQLPsENLPKFEVNDLESLT-GKYDTVVC 215
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESpdAELTMVDINARALESARENLAANGL-ENGEVVASDVYSGVEdGKFDLIIS 104
PLN02396 PLN02396
hexaprenyldihydroxybenzoate methyltransferase
 141-221 3.91e-05

hexaprenyldihydroxybenzoate methyltransferase


Pssm-ID: 178018 [Multi-domain]  Cd Length: 322  Bit Score: 44.72  E-value: 3.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  141 RSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKAQlPSENLPKFEVNDLESLTG---KYDTVVCLD 217
Cdd:PLN02396 128 KPFEGLKFIDIGCGGGLLSEPLARMGATVTGVDAVDKNVKIARLHADMD-PVTSTIEYLCTTAEKLADegrKFDAVLSLE 206


                 ....
gi 30686748  218 VLIH 221
Cdd:PLN02396 207 VIEH 210
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
133-245 4.53e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 43.99  E-value: 4.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  133 TMLMLT--EDRSLAGVTVCDAGCGTGLLSIPLAKEGAI-VSASDISAAMVAEAEmkakaqlpsENlpkFEVNDLESLT-- 207
Cdd:PRK00517 106 TRLCLEalEKLVLPGKTVLDVGCGSGILAIAAAKLGAKkVLAVDIDPQAVEAAR---------EN---AELNGVELNVyl 173

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 30686748  208 ----GKYDTVVC---LDVLIHypqnkadgMIAHLASLAEK--RVILS 245
Cdd:PRK00517 174 pqgdLKADVIVAnilANPLLE--------LAPDLARLLKPggRLILS 212
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 147-215 6.87e-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: 42.87  E-value: 6.87e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30686748 147 TVCDAGCGTGLLSIPLAKE--GAIVSASDISAAMVAEAEMKAKAQlpseNLPKFEV---NDLESL-TGKYDTVVC 215
Cdd:COG2813  52 RVLDLGCGYGVIGLALAKRnpEARVTLVDVNARAVELARANAAAN----GLENVEVlwsDGLSGVpDGSFDLILS 122
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 147-217 1.04e-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: 43.63  E-value: 1.04e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30686748 147 TVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKAQlpseNLP--KFEVNDLE------SLTGKYDTVVcLD 217
Cdd:COG2265 236 RVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVEDARENARLN----GLKnvEFVAGDLEevlpelLWGGRPDVVV-LD 309
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 139-245 1.55e-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: 42.64  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748   139 EDRSLAGVTVCDAGCGTGLLSIPLAKEGAI-VSASDISAAMVAEAEMKAKAQLPSENLPKFEVNDLesLTGKYDTVVC-- 215
Cdd:pfam06325 156 ERLVKPGESVLDVGCGSGILAIAALKLGAKkVVGVDIDPVAVRAAKENAELNGVEARLEVYLPGDL--PKEKADVVVAni 233

                          90       100       110
                  ....*....|....*....|....*....|...
gi 30686748   216 -LDVLIHypqnkadgMIAHLASL--AEKRVILS 245
Cdd:pfam06325 234 lADPLIE--------LAPDIYALvkPGGYLILS 258
PRK14968 PRK14968
putative methyltransferase; Provisional
 131-214 2.34e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 41.42  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  131 ENTMLMLTEDRSLAGVTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEMKAKAQLPSENLPKFEVNDL-ESLTG- 208
Cdd:PRK14968  10 EDSFLLAENAVDKKGDRVLEVGTGSGIVAIVAAKNGKKVVGVDINPYAVECAKCNAKLNNIRNNGVEVIRSDLfEPFRGd 89


                 ....*.
gi 30686748  209 KYDTVV 214
Cdd:PRK14968  90 KFDVIL 95
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
106-194 4.03e-04

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


Pssm-ID: 182918  Cd Length: 255  Bit Score: 41.10  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  106 RKIYGETDEVNR---VQKDIrlghaktveNTMLMLTEDRSLagvTVCDAGCGTGLLSIPLAKEGAIVSASDISAAMVAEA 182
Cdd:PRK11036  15 RNIYGTTKGQIRqaiLWQDL---------DRLLAELPPRPL---RVLDAGGGEGQTAIKLAELGHQVILCDLSAEMIQRA 82

                         90
                 ....*....|..
gi 30686748  183 EMKAKAQLPSEN 194
Cdd:PRK11036  83 KQAAEAKGVSDN 94
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
150-234 5.12e-04

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 40.49  E-value: 5.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748  150 DAGCGTGLLSIPLAKEGAIVSASDISAAMVAEAEmKAKAQLPSENLpKFEVNDLESLT--GKYDTVVCLDVLIHYPQNKA 227
Cdd:PRK11207  36 DLGCGNGRNSLYLAANGFDVTAWDKNPMSIANLE-RIKAAENLDNL-HTAVVDLNNLTfdGEYDFILSTVVLMFLEAKTI 113


                 ....*..
gi 30686748  228 DGMIAHL 234
Cdd:PRK11207 114 PGLIANM 120
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
143-214 5.67e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 40.27  E-value: 5.67e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30686748 143 LAGVTVCDAGCGTGLLSIPLAKEGA-IVSASDISAAMVAEAEMKAKAQLPSENLPKFEVNDLEsLTGKYDTVV 214
Cdd:COG2263  44 IEGKTVLDLGCGTGMLAIGAALLGAkKVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIP-LGGSVDTVV 115
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 141-249 7.77e-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: 7.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30686748 141 RSLAGVTVCDAGCGTGLLSIPLAKE--GAIVSASDISAAMVAEAEMKAkAQLPSENLPKFEVNDL-ESLT--GKYDTVVC 215
Cdd:COG2890 109 PAGAPPRVLDLGTGSGAIALALAKErpDARVTAVDISPDALAVARRNA-ERLGLEDRVRFLQGDLfEPLPgdGRFDLIVS 187

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 30686748 216 --------------LDVLIHYPQN----KADGMIAHlaslaekRVILSFAPK 249
Cdd:COG2890 188 nppyipedeiallpPEVRDHEPRLaldgGEDGLDFY-------RRIIAQAPR 232
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 137-183 4.02e-03

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 38.22  E-value: 4.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 30686748  137 LTEDRSLAGVTVCDAGCGTGLLSIPLAKE--GAIVSASDISAAMVAEAE 183
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSGAIALALAKErpDAEVTAVDISPEALAVAR 149
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 145-196 6.10e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 37.44  E-value: 6.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30686748  145 GVTVCDAGCGTGLLSIPLAKEG---AIVSASDISAAMVAEAEMKAKAQLPSENLP 196
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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