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Conserved domains on  [gi|145362386|ref|NP_974139|]
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S-adenosyl-L-methionine-dependent methyltransferases superfamily protein [Arabidopsis thaliana]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 11476664)

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
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
30-504 0e+00

phosphoethanolamine N-methyltransferase


:

Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 1015.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  30 KEHSVGLSVEAMMLDSKASDLDKEERPEILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKKNENING 109
Cdd:PLN02336   1 KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESING 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 110 HYKNVKFLCADVTSPNMNFPNESMDLIFSNWLLMYLSDQEVEDLAKKMLQWTKVGGYIFFRESCFHQSGDNKRKYNPTHY 189
Cdd:PLN02336  81 HYKNVKFMCADVTSPDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQSGDSKRKNNPTHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 190 REPKFYTKLFKECHMNDEDGNSYELSLVSCKCIGAYVRNKKNQNQICWLWQKVSSDNDRGFQRFLDNVQYKSSGILRYER 269
Cdd:PLN02336 161 REPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTNDKGFQRFLDNVQYKSSGILRYER 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 270 VFGEGFVSTGGLETTKEFVDMLDLKPGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLKCSVEFEV 349
Cdd:PLN02336 241 VFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 350 ADCTKKEYPDNTFDVIYSRDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRSPKTPSPDFAIYIKKRGYDLHDVQAYGQ 429
Cdd:PLN02336 321 ADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTPSPEFAEYIKQRGYDLHDVQAYGQ 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145362386 430 MLRDAGFEEVIAEDRTDQFMKVLKRELDAVEKEKEEFISDFSKEDYEDIIGGWKSKLLRSSSGEQKWGLFIAKRN 504
Cdd:PLN02336 401 MLKDAGFDDVIAEDRTDQFLQVLQRELDAVEKEKDEFISDFSEEDYNDIVGGWKAKLVRSSSGEQKWGLFIAKKK 475
 
Name Accession Description Interval E-value
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
30-504 0e+00

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 1015.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  30 KEHSVGLSVEAMMLDSKASDLDKEERPEILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKKNENING 109
Cdd:PLN02336   1 KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESING 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 110 HYKNVKFLCADVTSPNMNFPNESMDLIFSNWLLMYLSDQEVEDLAKKMLQWTKVGGYIFFRESCFHQSGDNKRKYNPTHY 189
Cdd:PLN02336  81 HYKNVKFMCADVTSPDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQSGDSKRKNNPTHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 190 REPKFYTKLFKECHMNDEDGNSYELSLVSCKCIGAYVRNKKNQNQICWLWQKVSSDNDRGFQRFLDNVQYKSSGILRYER 269
Cdd:PLN02336 161 REPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTNDKGFQRFLDNVQYKSSGILRYER 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 270 VFGEGFVSTGGLETTKEFVDMLDLKPGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLKCSVEFEV 349
Cdd:PLN02336 241 VFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 350 ADCTKKEYPDNTFDVIYSRDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRSPKTPSPDFAIYIKKRGYDLHDVQAYGQ 429
Cdd:PLN02336 321 ADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTPSPEFAEYIKQRGYDLHDVQAYGQ 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145362386 430 MLRDAGFEEVIAEDRTDQFMKVLKRELDAVEKEKEEFISDFSKEDYEDIIGGWKSKLLRSSSGEQKWGLFIAKRN 504
Cdd:PLN02336 401 MLKDAGFDDVIAEDRTDQFLQVLQRELDAVEKEKDEFISDFSEEDYNDIVGGWKAKLVRSSSGEQKWGLFIAKKK 475
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
282-437 2.96e-32

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: 120.48  E-value: 2.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 282 ETTKEFVDMLDLKPGQKVLDVGCGIGGGDFYMAENfDVDVVGIDLSVNMISFALEHAIGLKCSVEFEVADCTKKEYPDNT 361
Cdd:COG2226    9 DGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGS 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145362386 362 FDVIYSRDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRspktpspdfaiyikkrgydlHDVQAYGQMLRDAGFE 437
Cdd:COG2226   88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP--------------------PDLAELEELLAEAGFE 143
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
299-392 1.03e-27

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 106.11  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  299 VLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLKCSVEFEVADCTKKEYPDNTFDVIYSRDTILHI--QD 376
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdPD 80
                          90
                  ....*....|....*.
gi 145362386  377 KPALFRRFYKWLKPGG 392
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
298-399 3.44e-17

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: 77.09  E-value: 3.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 298 KVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLKCS-VEFEVADCTK-KEYPDNTFDVIYSRDTILHI- 374
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEElPPEADESFDVIISDPPLHHLv 80
                         90       100
                 ....*....|....*....|....*
gi 145362386 375 QDKPALFRRFYKWLKPGGKVLITDY 399
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTLV 105
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
282-444 7.52e-11

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: 62.30  E-value: 7.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  282 ETTKEFVDMLDLKPG---QKVLDVGCGIGGGDFYMAENF-DVDVVGIDLSVNMISFALEHaigLKCSVEFEVADCTKKEY 357
Cdd:TIGR02072  18 EMAKRLLALLKEKGIfipASVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTK---LSENVQFICGDAEKLPL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  358 PDNTFDVIYSRDTILHIQDKPALFRRFYKWLKPGGKVLITDYC--------RSPKTPSPDFaiyikkrgYDLHDVQaygQ 429
Cdd:TIGR02072  95 EDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGpgtlhelrQSFGQHGLRY--------LSLDELK---A 163
                         170
                  ....*....|....*
gi 145362386  430 MLrDAGFEEVIAEDR 444
Cdd:TIGR02072 164 LL-KNSFELLTLEEE 177
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
298-488 4.85e-09

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 56.66  E-value: 4.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   298 KVLDVGCGIGGGDFYMAENF-DVDVVGIDLSVNMISFALE--HAIGLKCSVEFEVADCTKKEYPDnTFDVIYSRDTILHI 374
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHpHLQLHGYTISPEQAEVGREriRALGLQGRIRIFYRDSAKDPFPD-TYDLVFGFEVIHHI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   375 QDKPALFRRFYKWLKPGGKVLITDYCRSPKTP--SPDFAIYI----------KKRGYDLHDV----QAYGQMLRDAGFEe 438
Cdd:smart00828  81 KDKMDLFSNISRHLKDGGHLVLADFIANLLSAieHEETTSYLvtreewaellARNNLRVVEGvdasLEIANFLYDPGFE- 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 145362386   439 viaedrtDQFMKVLKRELDAVEKEKEEFISDFSKEdyedIIGGWKSKLLR 488
Cdd:smart00828 160 -------DNLERLYQDDLDEVTKRHFRGIANLGKL----LEKGLASYALL 198
 
Name Accession Description Interval E-value
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
30-504 0e+00

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 1015.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  30 KEHSVGLSVEAMMLDSKASDLDKEERPEILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKKNENING 109
Cdd:PLN02336   1 KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESING 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 110 HYKNVKFLCADVTSPNMNFPNESMDLIFSNWLLMYLSDQEVEDLAKKMLQWTKVGGYIFFRESCFHQSGDNKRKYNPTHY 189
Cdd:PLN02336  81 HYKNVKFMCADVTSPDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQSGDSKRKNNPTHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 190 REPKFYTKLFKECHMNDEDGNSYELSLVSCKCIGAYVRNKKNQNQICWLWQKVSSDNDRGFQRFLDNVQYKSSGILRYER 269
Cdd:PLN02336 161 REPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTNDKGFQRFLDNVQYKSSGILRYER 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 270 VFGEGFVSTGGLETTKEFVDMLDLKPGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLKCSVEFEV 349
Cdd:PLN02336 241 VFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 350 ADCTKKEYPDNTFDVIYSRDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRSPKTPSPDFAIYIKKRGYDLHDVQAYGQ 429
Cdd:PLN02336 321 ADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTPSPEFAEYIKQRGYDLHDVQAYGQ 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145362386 430 MLRDAGFEEVIAEDRTDQFMKVLKRELDAVEKEKEEFISDFSKEDYEDIIGGWKSKLLRSSSGEQKWGLFIAKRN 504
Cdd:PLN02336 401 MLKDAGFDDVIAEDRTDQFLQVLQRELDAVEKEKDEFISDFSEEDYNDIVGGWKAKLVRSSSGEQKWGLFIAKKK 475
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
252-504 8.76e-70

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 223.69  E-value: 8.76e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 252 RFLDNVQYKSSGILRYERVFGEGFVSTGGLETTKEFVDMLDLKPGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMI 331
Cdd:PTZ00098   9 TYLENNQYSDEGIKAYEFIFGEDYISSGGIEATTKILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 332 SFALEHAIGlKCSVEFEVADCTKKEYPDNTFDVIYSRDTILHI--QDKPALFRRFYKWLKPGGKVLITDYCRSPKTPSPD 409
Cdd:PTZ00098  89 NIAKLRNSD-KNKIEFEANDILKKDFPENTFDMIYSRDAILHLsyADKKKLFEKCYKWLKPNGILLITDYCADKIENWDE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 410 -FAIYIKKRGYDLHDVQAYGQMLRDAGFEEVIAEDRTDQFMKVLKRELDAVEKEKEEFISDFSKEDYEDIIGGWKSKLLR 488
Cdd:PTZ00098 168 eFKAYIKKRKYTLIPIQEYGDLIKSCNFQNVVAKDISDYWLELLQVELKKLEEKKEEFLKLYSEKEYNSLKDGWTRKIKD 247
                        250
                 ....*....|....*.
gi 145362386 489 SSSGEQKWGLFIAKRN 504
Cdd:PTZ00098 248 TKRKLQKWGYFKAQKM 263
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
282-437 2.96e-32

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: 120.48  E-value: 2.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 282 ETTKEFVDMLDLKPGQKVLDVGCGIGGGDFYMAENfDVDVVGIDLSVNMISFALEHAIGLKCSVEFEVADCTKKEYPDNT 361
Cdd:COG2226    9 DGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGS 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145362386 362 FDVIYSRDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRspktpspdfaiyikkrgydlHDVQAYGQMLRDAGFE 437
Cdd:COG2226   88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP--------------------PDLAELEELLAEAGFE 143
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
250-398 1.11e-30

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 116.57  E-value: 1.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 250 FQRFLDNVQYKSSGIlrYERvfGEGFVSTGGLETTKEFVDMLDLKPGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVN 329
Cdd:COG2230   10 YRLFLDPTMTYSCAY--FED--PDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPE 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145362386 330 MISFALE--HAIGLKCSVEFEVADCTkKEYPDNTFDVIYSRDTILHIQDK--PALFRRFYKWLKPGGKVLITD 398
Cdd:COG2230   86 QLEYAREraAEAGLADRVEVRLADYR-DLPADGQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
299-392 1.03e-27

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 106.11  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  299 VLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLKCSVEFEVADCTKKEYPDNTFDVIYSRDTILHI--QD 376
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdPD 80
                          90
                  ....*....|....*.
gi 145362386  377 KPALFRRFYKWLKPGG 392
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
293-399 3.23e-26

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: 103.17  E-value: 3.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 293 LKPGQKVLDVGCGIGGGDFYMAENFdVDVVGIDLSVNMISFALEHAIGLKcsVEFEVADCTKKEYPDNTFDVIYSRDTIL 372
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARRG-ADVTGVDISPEALEIARERAAELN--VDFVQGDLEDLPLEDGSFDLVICSEVLE 98
                         90       100
                 ....*....|....*....|....*..
gi 145362386 373 HIQDKPALFRRFYKWLKPGGKVLITDY 399
Cdd:COG2227   99 HLPDPAALLRELARLLKPGGLLLLSTP 125
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
300-396 5.21e-23

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 93.11  E-value: 5.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  300 LDVGCGIGGGDFYMAENFdVDVVGIDLSVNMISFALEHAIGLKcsVEFEVADCTKKEYPDNTFDVIYSRDTILHIQDKPA 379
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG-ARVTGVDISPEMLELAREKAPREG--LTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPER 77
                          90
                  ....*....|....*..
gi 145362386  380 LFRRFYKWLKPGGKVLI 396
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
295-398 1.54e-22

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 91.81  E-value: 1.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 295 PGQKVLDVGCGIGGGDFYMAENF-DVDVVGIDLSVNMISFALEHAIGlkcsVEFEVADCTKKEyPDNTFDVIYSRDTILH 373
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLPN----VRFVVADLRDLD-PPEPFDLVVSNAALHW 75
                         90       100
                 ....*....|....*....|....*
gi 145362386 374 IQDKPALFRRFYKWLKPGGKVLITD 398
Cdd:COG4106   76 LPDHAALLARLAAALAPGGVLAVQV 100
PRK08317 PRK08317
hypothetical protein; Provisional
290-398 2.91e-21

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 92.69  E-value: 2.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 290 MLDLKPGQKVLDVGCGIGGGDFYMAENFDVD--VVGIDLSVNMISFALEHAIGLKCSVEFEVADCTKKEYPDNTFDVIYS 367
Cdd:PRK08317  14 LLAVQPGDRVLDVGCGPGNDARELARRVGPEgrVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDAVRS 93
                         90       100       110
                 ....*....|....*....|....*....|.
gi 145362386 368 RDTILHIQDKPALFRRFYKWLKPGGKVLITD 398
Cdd:PRK08317  94 DRVLQHLEDPARALAEIARVLRPGGRVVVLD 124
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
286-399 7.59e-21

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 90.36  E-value: 7.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 286 EFVDMLDLKPGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLKCS-VEFEVADCTK-KEYPDNTFD 363
Cdd:COG0500   17 LLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAElDPLPAESFD 96
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145362386 364 VIYSRDTILHIQDKP--ALFRRFYKWLKPGGKVLITDY 399
Cdd:COG0500   97 LVVAFGVLHHLPPEEreALLRELARALKPGGVLLLSAS 134
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
290-437 3.72e-20

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 87.48  E-value: 3.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  290 MLDLKPGQKVLDVGCGIGggdfYMAENFD---VDVVGIDLSVNMISFALEHAIglkcsveFEVADCTKKEYPDNTFDVIY 366
Cdd:pfam13489  17 LPKLPSPGRVLDFGCGTG----IFLRLLRaqgFSVTGVDPSPIAIERALLNVR-------FDQFDEQEAAVPAGKFDVIV 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145362386  367 SRDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRSPKTPS-----PDFAIYikKRGYDLHDVQAYGQMLRDAGFE 437
Cdd:pfam13489  86 AREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRlllewPYLRPR--NGHISLFSARSLKRLLEEAGFE 159
PLN02244 PLN02244
tocopherol O-methyltransferase
248-443 7.92e-20

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 90.57  E-value: 7.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 248 RGFQRFLDnvqyKSSGIlrYERVFGE----GFVSTGG------------LETTKEF--VDMLDLKPGQKVLDVGCGIGGG 309
Cdd:PLN02244  59 EGIAEFYD----ESSGV--WEDVWGEhmhhGYYDPGAsrgdhrqaqirmIEESLAWagVPDDDEKRPKRIVDVGCGIGGS 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 310 DFYMAENFDVDVVGIDLSVNMISFA--LEHAIGLKCSVEFEVADCTKKEYPDNTFDVIYSRDTILHIQDKpalfRRFYKW 387
Cdd:PLN02244 133 SRYLARKYGANVKGITLSPVQAARAnaLAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPDK----RKFVQE 208
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 388 L----KPGGKVLITDYCRSPKTPS-----PDFAIYIKK--RGYDLHD---VQAYGQMLRDAGFEEVIAED 443
Cdd:PLN02244 209 LarvaAPGGRIIIVTWCHRDLEPGetslkPDEQKLLDKicAAYYLPAwcsTSDYVKLAESLGLQDIKTED 278
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
285-438 9.06e-20

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 86.98  E-value: 9.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 285 KEFVDMLDLKPGQKVLDVGCGIGGGDFYMAENFDvDVVGIDLSVNMISFALEHAIGlkcsVEFEVADCTKKEYPDNTFDV 364
Cdd:COG4976   36 EELLARLPPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKGVY----DRLLVADLADLAEPDGRFDL 110
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145362386 365 IYSRDTILHIQDKPALFRRFYKWLKPGGKVLITdycrspkTPSPDfaiyikKRGYDLHDVQAYGQMLRDAGFEE 438
Cdd:COG4976  111 IVAADVLTYLGDLAAVFAGVARALKPGGLFIFS-------VEDAD------GSGRYAHSLDYVRDLLAAAGFEV 171
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
44-171 2.26e-19

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: 84.66  E-value: 2.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  44 DSKASDLDkeERPEILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKK-NENINGHYKNVKFLCADVT 122
Cdd:COG2226    2 DRVAARYD--GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELaRERAAEAGLNVEFVVGDAE 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 145362386 123 spNMNFPNESMDLIFSNWLLMYLSDQevEDLAKKMLQWTKVGGYIFFRE 171
Cdd:COG2226   80 --DLPFPDGSFDLVISSFVLHHLPDP--ERALAEIARVLKPGGRLVVVD 124
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
293-435 3.34e-19

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 84.39  E-value: 3.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  293 LKPGQKVLDVGCGIGGGDFYMAE--NFDVDVVGIDLSVNMISFALEHAIGLKCS-VEFEVADCTKKE--YPDNTFDVIYS 367
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEELPelLEDDKFDVVIS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  368 RDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRSPKTPSP--DFAIYIKKRGYDLHDVQAYGQMLRDAG 435
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHvkEDSTYYAGCVGGAILKKKLYELLEEAG 150
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
70-165 6.91e-19

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 81.46  E-value: 6.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   70 VLEFGAGIGRFTTELAQKAG-QVIAVDFIESVIKK-NENINGHYKNVKFLCADVTspNMNFPNESMDLIFSNWLLMYLSD 147
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERaRERAAEAGLNVEFVQGDAE--DLPFPDGSFDLVVSSGVLHHLPD 78
                          90
                  ....*....|....*...
gi 145362386  148 QEVEDLAKKMLQWTKVGG 165
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
300-394 7.89e-18

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 78.56  E-value: 7.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  300 LDVGCGIGGGDFYMAENF-DVDVVGIDLSVNMISFALEH--AIGLKCSVEFEVADCTKKEYPDNTFDVIYSRDTILHIQD 376
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERlaALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80
                          90
                  ....*....|....*...
gi 145362386  377 KPALFRRFYKWLKPGGKV 394
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
298-399 3.44e-17

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: 77.09  E-value: 3.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 298 KVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLKCS-VEFEVADCTK-KEYPDNTFDVIYSRDTILHI- 374
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEElPPEADESFDVIISDPPLHHLv 80
                         90       100
                 ....*....|....*....|....*
gi 145362386 375 QDKPALFRRFYKWLKPGGKVLITDY 399
Cdd:cd02440   81 EDLARFLEEARRLLKPGGVLVLTLV 105
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
285-439 8.33e-17

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 79.81  E-value: 8.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 285 KEFVDMLDLKPGQKVLDVGCGIggGD--FYMAENFDV--DVVGIDLSVNMISFALEHAI--GLKCSVEFEVADCTKKEYP 358
Cdd:PRK00216  41 RKTIKWLGVRPGDKVLDLACGT--GDlaIALAKAVGKtgEVVGLDFSEGMLAVGREKLRdlGLSGNVEFVQGDAEALPFP 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 359 DNTFDVIysrdTI---L-HIQDKPALFRRFYKWLKPGGKVLITDYCRsPKTPspdfaiyIKKRGYDLH------------ 422
Cdd:PRK00216 119 DNSFDAV----TIafgLrNVPDIDKALREMYRVLKPGGRLVILEFSK-PTNP-------PLKKAYDFYlfkvlpligkli 186
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 145362386 423 --DVQAY----------------GQMLRDAGFEEV 439
Cdd:PRK00216 187 skNAEAYsylaesirafpdqeelAAMLEEAGFERV 221
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
71-169 8.79e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 72.70  E-value: 8.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   71 LEFGAGIGRFTTELAQKAGQVIAVDFIESVIKKNENiNGHYKNVKFLCADVTspNMNFPNESMDLIFSNWLLMYLSDqeV 150
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELARE-KAPREGLTFVVGDAE--DLPFPDNSFDLVLSSEVLHHVED--P 75
                          90
                  ....*....|....*....
gi 145362386  151 EDLAKKMLQWTKVGGYIFF 169
Cdd:pfam08241  76 ERALREIARVLKPGGILII 94
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
289-476 7.64e-15

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 74.67  E-value: 7.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  289 DMLDLKPGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALE--HAIGLKCSVEFEVADctKKEYPDNtFDVIY 366
Cdd:pfam02353  55 DKLGLKPGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKNQYKLARKrvAAEGLARKVEVLLQD--YRDFDEP-FDRIV 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  367 SRDTILHIQDK--PALFRRFYKWLKPGGKVLI-TDYCRSPK------TPSPDFAIYIKKRGYdLHDVQAYGQMLRDAGFE 437
Cdd:pfam02353 132 SVGMFEHVGHEnyDTFFKKLYNLLPPGGLMLLhTITGLHPDetsergLPLKFIDKYIFPGGE-LPSISMIVESSSEAGFT 210
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 145362386  438 EVIAEDRTDQFMKVLKRELDAVEKEKEEFISDFSKEDYE 476
Cdd:pfam02353 211 VEDVESLRPHYAKTLDLWAENLQANKDEAIALQSEEFYR 249
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
41-169 2.36e-14

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: 69.66  E-value: 2.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  41 MMLDSKASDLDKEERPEILAFLPPieGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKKNENiNGHYKNVKFLCAD 120
Cdd:COG2227    1 MSDPDARDFWDRRLAALLARLLPA--GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARE-RAAELNVDFVQGD 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 145362386 121 VTspNMNFPNESMDLIFSNWLLMYLSDqeVEDLAKKMLQWTKVGGYIFF 169
Cdd:COG2227   78 LE--DLPLEDGSFDLVICSEVLEHLPD--PAALLRELARLLKPGGLLLL 122
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
69-169 3.64e-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: 65.53  E-value: 3.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  69 TVLEFGAGIGRFTTELAQ-KAGQVIAVDFIESVIKKNE--NINGHYKNVKFLCADVTSPNMnFPNESMDLIFSNWLLMYL 145
Cdd:cd02440    1 RVLDLGCGTGALALALASgPGARVTGVDISPVALELARkaAAALLADNVEVLKGDAEELPP-EADESFDVIISDPPLHHL 79
                         90       100
                 ....*....|....*....|....
gi 145362386 146 sDQEVEDLAKKMLQWTKVGGYIFF 169
Cdd:cd02440   80 -VEDLARFLEEARRLLKPGGVLVL 102
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
291-367 7.36e-13

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 69.88  E-value: 7.36e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145362386 291 LDLKPGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLkcSVEFEVADctkkeYPD--NTFDVIYS 367
Cdd:PRK11705 163 LQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGL--PVEIRLQD-----YRDlnGQFDRIVS 234
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
66-169 1.67e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 63.69  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  66 EGTTVLEFGAGIGRFTTELAQK--AGQVIAVDFIESVIkknENINGHYKNVKFLCADVTSPNmnfPNESMDLIFSNWLLM 143
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEML---ARARARLPNVRFVVADLRDLD---PPEPFDLVVSNAALH 74
                         90       100
                 ....*....|....*....|....*.
gi 145362386 144 YLSDQevEDLAKKMLQWTKVGGYIFF 169
Cdd:COG4106   75 WLPDH--AALLARLAAALAPGGVLAV 98
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
48-169 2.42e-12

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 65.71  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  48 SDLDKEERPEILAFLPPIE----GTTVLEFGAGIGRFTTELAQKAG-QVIAVDFIESVIKKNENINGHYK--NVKFLCAD 120
Cdd:COG0500    4 SYYSDELLPGLAALLALLErlpkGGRVLDLGCGTGRNLLALAARFGgRVIGIDLSPEAIALARARAAKAGlgNVEFLVAD 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 145362386 121 VTSPNmNFPNESMDLIFSNWLLMYLSDQEVEDLAKKMLQWTKVGGYIFF 169
Cdd:COG0500   84 LAELD-PLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
285-439 6.80e-12

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 65.15  E-value: 6.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  285 KEFV-DMLDLKPGQKVLDVGCGIGGGDFYMAENFDV--DVVGIDLSVNMISFALEHAI-GLKCSVEFEVADCTKKEYPDN 360
Cdd:pfam01209  31 KDFTmKCMGVKRGNKFLDVAGGTGDWTFGLSDSAGSsgKVVGLDINENMLKEGEKKAKeEGKYNIEFLQGNAEELPFEDD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  361 TFDVIYSRDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRsPKTPSPDFAI-----------------------YIKKR 417
Cdd:pfam01209 111 SFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSK-PENPLLSQAYelyfkyvmpfmgkmfaksyksyqYLQES 189
                         170       180
                  ....*....|....*....|..
gi 145362386  418 GYDLHDVQAYGQMLRDAGFEEV 439
Cdd:pfam01209 190 IRDFPDQKTLASMFEKAGFKSV 211
arsM PRK11873
arsenite methyltransferase;
293-445 1.44e-11

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 64.97  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 293 LKPGQKVLDVGCGIGggdfymaenFDV-----------DVVGIDLSVNMISFALEHAIGLKCS-VEFEVADCTKKEYPDN 360
Cdd:PRK11873  75 LKPGETVLDLGSGGG---------FDCflaarrvgptgKVIGVDMTPEMLAKARANARKAGYTnVEFRLGEIEALPVADN 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 361 TFDVIYSRDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRspKTPSPDfAIyikKRGYDLH--------DVQAYGQMLR 432
Cdd:PRK11873 146 SVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFAISDVVL--RGELPE-EI---RNDAELYagcvagalQEEEYLAMLA 219
                        170
                 ....*....|....
gi 145362386 433 DAGFEEV-IAEDRT 445
Cdd:PRK11873 220 EAGFVDItIQPKRE 233
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
57-169 1.60e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 63.09  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  57 EILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKKNENiNGHYknVKFLCADVTspNMNFPNESMDLI 136
Cdd:COG4976   37 ELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKARE-KGVY--DRLLVADLA--DLAEPDGRFDLI 111
                         90       100       110
                 ....*....|....*....|....*....|...
gi 145362386 137 FSNWLLMYLSDQevEDLAKKMLQWTKVGGYIFF 169
Cdd:COG4976  112 VAADVLTYLGDL--AAVFAGVARALKPGGLFIF 142
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
66-191 4.68e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 60.89  E-value: 4.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   66 EGTTVLEFGAGIGRFTTELAQKAG---QVIAVDFIESVIKKNENI--NGHYKNVKFLCADVTSPNMNFPNESMDLIFSNW 140
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENaqKLGFDNVEFEQGDIEELPELLEDDKFDVVISNC 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145362386  141 LLMYLSDQevEDLAKKMLQWTKVGGYIFFRESCFHQSGDNKRKYNPTHYRE 191
Cdd:pfam13847  83 VLNHIPDP--DKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDSTYYAG 131
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
282-444 7.52e-11

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: 62.30  E-value: 7.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  282 ETTKEFVDMLDLKPG---QKVLDVGCGIGGGDFYMAENF-DVDVVGIDLSVNMISFALEHaigLKCSVEFEVADCTKKEY 357
Cdd:TIGR02072  18 EMAKRLLALLKEKGIfipASVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTK---LSENVQFICGDAEKLPL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  358 PDNTFDVIYSRDTILHIQDKPALFRRFYKWLKPGGKVLITDYC--------RSPKTPSPDFaiyikkrgYDLHDVQaygQ 429
Cdd:TIGR02072  95 EDSSFDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFGpgtlhelrQSFGQHGLRY--------LSLDELK---A 163
                         170
                  ....*....|....*
gi 145362386  430 MLrDAGFEEVIAEDR 444
Cdd:TIGR02072 164 LL-KNSFELLTLEEE 177
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
298-488 4.85e-09

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 56.66  E-value: 4.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   298 KVLDVGCGIGGGDFYMAENF-DVDVVGIDLSVNMISFALE--HAIGLKCSVEFEVADCTKKEYPDnTFDVIYSRDTILHI 374
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHpHLQLHGYTISPEQAEVGREriRALGLQGRIRIFYRDSAKDPFPD-TYDLVFGFEVIHHI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   375 QDKPALFRRFYKWLKPGGKVLITDYCRSPKTP--SPDFAIYI----------KKRGYDLHDV----QAYGQMLRDAGFEe 438
Cdd:smart00828  81 KDKMDLFSNISRHLKDGGHLVLADFIANLLSAieHEETTSYLvtreewaellARNNLRVVEGvdasLEIANFLYDPGFE- 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 145362386   439 viaedrtDQFMKVLKRELDAVEKEKEEFISDFSKEdyedIIGGWKSKLLR 488
Cdd:smart00828 160 -------DNLERLYQDDLDEVTKRHFRGIANLGKL----LEKGLASYALL 198
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
296-404 2.86e-08

ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase believed to act at two points in the ubiquinone biosynthetic pathway in bacteria (UbiG) and fungi (COQ3). A separate methylase (MenG/UbiE) catalyzes the single C-methylation step. The most commonly used names for genes in this family do not indicate whether this gene is an O-methyl, or C-methyl transferase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273910  Cd Length: 224  Bit Score: 54.22  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  296 GQKVLDVGCGIGGGDFYMAENfDVDVVGIDLSVNMISFALEHAIGLKCSVEFEVadCTKKEYPDN---TFDVIYSRDTIL 372
Cdd:TIGR01983  47 GLRVLDVGCGGGLLSEPLARL-GANVTGIDASEENIEVAKLHAKKDPLQIDYRC--TTVEDLAEKkagSFDVVTCMEVLE 123
                          90       100       110
                  ....*....|....*....|....*....|..
gi 145362386  373 HIQDKPALFRRFYKWLKPGGKVLITDYCRSPK 404
Cdd:TIGR01983 124 HVPDPQAFIRACAQLLKPGGILFFSTINRTPK 155
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
290-422 3.16e-08

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 54.12  E-value: 3.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 290 MLDLK--PGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIGLKCSVEFEVADCTKKEyPDNTFDVI-- 365
Cdd:COG3897   63 LLDHPevAGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPP-AAGGFDLIlg 141
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145362386 366 ----YSRDTILHIqdkPALFRRFykwLKPGGKVLITDYCRSPKTPSPDFAiyIKKRGYDLH 422
Cdd:COG3897  142 gdvlYERDLAEPL---LPFLDRL---AAPGGEVLIGDPGRGYLPAFRERL--EALAGYEVV 194
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
293-424 3.42e-08

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 53.03  E-value: 3.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 293 LKPGQKVLDVGCGIGGgdfyM---AENFDVDVVGIDLSVNMISFA---LEHAigLKCSVEFEVADCTKKEYPDNTFDVI- 365
Cdd:COG1041   24 AKEGDTVLDPFCGTGT----IlieAGLLGRRVIGSDIDPKMVEGArenLEHY--GYEDADVIRGDARDLPLADESVDAIv 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145362386 366 ----------YSRDTILHIQDKpaLFRRFYKWLKPGGKVLITdycrspkTPSpDFAIYIKKRGYDLHDV 424
Cdd:COG1041   98 tdppygrsskISGEELLELYEK--ALEEAARVLKPGGRVVIV-------TPR-DIDELLEEAGFKVLER 156
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
57-169 3.81e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 52.62  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  57 EILAFLPPIEGTTVLEFGAGIGRFTTELAQKAG-QVIAVDF----IESVIKKNENINGHYKnVKFLCADVTSPnmnFPNE 131
Cdd:COG2230   42 LILRKLGLKPGMRVLDIGCGWGGLALYLARRYGvRVTGVTLspeqLEYARERAAEAGLADR-VEVRLADYRDL---PADG 117
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145362386 132 SMDLIFSNWLLMYLSDQEVEDLAKKMLQWTKVGGYIFF 169
Cdd:COG2230  118 QFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
rADc smart00650
Ribosomal RNA adenine dimethylases;
57-139 6.42e-08

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 52.13  E-value: 6.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386    57 EILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAV----DFIESVIKKNEningHYKNVKFLCADVTspNMNFPNES 132
Cdd:smart00650   4 KIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIeidpRLAPRLREKFA----AADNLTVIHGDAL--KFDLPKLQ 77

                   ....*..
gi 145362386   133 MDLIFSN 139
Cdd:smart00650  78 PYKVVGN 84
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
57-169 9.26e-08

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: 53.06  E-value: 9.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   57 EILAFLPPIEGTTVLEFGAGIGRFTTELAQK--AGQVIAVDFIESVIKKNENINGhyKNVKFLCADVTspNMNFPNESMD 134
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRALLKRfpQAEFIALDISAGMLAQAKTKLS--ENVQFICGDAE--KLPLEDSSFD 100
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 145362386  135 LIFSNwllmyLSDQEVEDLA---KKMLQWTKVGGYIFF 169
Cdd:TIGR02072 101 LIVSN-----LALQWCDDLSqalSELARVLKPGGLLAF 133
PRK12335 PRK12335
tellurite resistance protein TehB; Provisional
57-166 3.38e-07

tellurite resistance protein TehB; Provisional


Pssm-ID: 183450 [Multi-domain]  Cd Length: 287  Bit Score: 51.87  E-value: 3.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  57 EILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVD-------FIESVIKKnENINghyknVKFLCADVTSPNMNfp 129
Cdd:PRK12335 111 EVLEAVQTVKPGKALDLGCGQGRNSLYLALLGFDVTAVDinqqsleNLQEIAEK-ENLN-----IRTGLYDINSASIQ-- 182
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 145362386 130 nESMDLIFSNWLLMYLSDQEVEDLAKKMLQWTKVGGY 166
Cdd:PRK12335 183 -EEYDFILSTVVLMFLNRERIPAIIKNMQEHTNPGGY 218
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
57-122 1.22e-06

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: 50.56  E-value: 1.22e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145362386  57 EILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVI---KKNENINGhYKNVKFLCADVT 122
Cdd:COG2265  224 AALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIGVEIVPEAVedaRENARLNG-LKNVEFVAGDLE 291
PRK06202 PRK06202
hypothetical protein; Provisional
299-403 1.60e-06

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 49.23  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 299 VLDVGCGigGGDF-----YMAE--NFDVDVVGIDLSVNMISFALEHAIGLKCSVEFEVADCTKKEypDNTFDVIYSrDTI 371
Cdd:PRK06202  64 LLDIGCG--GGDLaidlaRWARrdGLRLEVTAIDPDPRAVAFARANPRRPGVTFRQAVSDELVAE--GERFDVVTS-NHF 138
                         90       100       110
                 ....*....|....*....|....*....|....
gi 145362386 372 LHIQDkPALFRRFYK--WLKPGGKVLITDYCRSP 403
Cdd:PRK06202 139 LHHLD-DAEVVRLLAdsAALARRLVLHNDLIRSR 171
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
284-396 2.01e-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: 48.26  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 284 TKEFVDMLDLKPGQKVLDVGCGIGG-GDFYMAENFDVDVVGIDLSVNMISFALEHAI--GLKcSVEFEVADCTKKeYPDN 360
Cdd:COG2813   38 TRLLLEHLPEPLGGRVLDLGCGYGViGLALAKRNPEARVTLVDVNARAVELARANAAanGLE-NVEVLWSDGLSG-VPDG 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 145362386 361 TFDVIYS----------RDTILHiqdkpALFRRFYKWLKPGGKVLI 396
Cdd:COG2813  116 SFDLILSnppfhagravDKEVAH-----ALIADAARHLRPGGELWL 156
PRK08317 PRK08317
hypothetical protein; Provisional
55-167 2.41e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 48.78  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  55 RPEILAFLPPIEGTTVLEFGAGIGRFTTELAQ---KAGQVIAVDFIESVIK-KNENINGHYKNVKFLCADVTSpnMNFPN 130
Cdd:PRK08317   8 RARTFELLAVQPGDRVLDVGCGPGNDARELARrvgPEGRVVGIDRSEAMLAlAKERAAGLGPNVEFVRGDADG--LPFPD 85
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 145362386 131 ESMDLIFSNWLLMYLSDqeVEDLAKKMLQWTKVGGYI 167
Cdd:PRK08317  86 GSFDAVRSDRVLQHLED--PARALAEIARVLRPGGRV 120
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
293-440 4.24e-06

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


Pssm-ID: 443298  Cd Length: 173  Bit Score: 47.10  E-value: 4.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 293 LKPGQKVLDVGCGIGGGDFYMAENFDVD--VVGIDLSVNMISFALEH--AIGLKCSVEFEVADCTK--KEYPDNTFDVIY 366
Cdd:COG4122   14 LLGAKRILEIGTGTGYSTLWLARALPDDgrLTTIEIDPERAAIARENfaRAGLADRIRLILGDALEvlPRLADGPFDLVF 93
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145362386 367 SrDTilhiqDK---PALFRRFYKWLKPGGKVLITDYCRSPKTPSPdfaiyiKKRGYDLHDVQAYGQMLR-DAGFEEVI 440
Cdd:COG4122   94 I-DA-----DKsnyPDYLELALPLLRPGGLIVADNVLWHGRVADP------ARRDPSTRAIREFNEYLReDPRLESVL 159
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
56-166 5.41e-06

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 47.04  E-value: 5.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  56 PEILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVD-------FIESvIKKNENINGHYKNVKFLcadvtsPNMNF 128
Cdd:PRK11207  20 SEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDknpmsiaNLER-IKAAENLDNLHTAVVDL------NNLTF 92
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145362386 129 pNESMDLIFSNWLLMYLSDQEVEDLAKKMLQWTKVGGY 166
Cdd:PRK11207  93 -DGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGY 129
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
349-397 7.81e-06

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 46.01  E-value: 7.81e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145362386 349 VADCTKKE-YPDNTFDVIYSRDTILHIQDK--PALFRRFYKWLKPGGKVLIT 397
Cdd:COG4627   33 VGDLTDPLpFPDNSVDAIYSSHVLEHLDYEeaPLALKECYRVLKPGGILRIV 84
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
294-404 2.19e-05

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 46.04  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 294 KPGQKVLDVGCGIGGGDFYMAENFDVD--VVGIDLSVNMISFA-----LEHAIGLKCsVEFEVADCTKKEYPDNTFDVIY 366
Cdd:PLN02233  72 KMGDRVLDLCCGSGDLAFLLSEKVGSDgkVMGLDFSSEQLAVAasrqeLKAKSCYKN-IEWIEGDATDLPFDDCYFDAIT 150
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145362386 367 SRDTILHIQDKPALFRRFYKWLKPGGKVLITDYCRSPK 404
Cdd:PLN02233 151 MGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQ 188
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
65-139 2.86e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.89  E-value: 2.86e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145362386  65 IEGTTVLEFGAGIGRFT--TELAQkAGQVIAVDFIESVIK-KNENINGHYKNVKFLCADVTSPNmnfPNESMDLIFSN 139
Cdd:COG2263   44 IEGKTVLDLGCGTGMLAigAALLG-AKKVVGVDIDPEALEiARENAERLGVRVDFIRADVTRIP---LGGSVDTVVMN 117
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
290-400 3.04e-05

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 45.52  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 290 MLDLKPGQK---VLDVGCGIGGGDFYMAENfDVDVVGIDLSVNMISFALEHaiglKCSVEFEVADCTKKEYPDNTFDVIY 366
Cdd:PRK10258  34 LLAMLPQRKfthVLDAGCGPGWMSRYWRER-GSQVTALDLSPPMLAQARQK----DAADHYLAGDIESLPLATATFDLAW 108
                         90       100       110
                 ....*....|....*....|....*....|....
gi 145362386 367 SRDTILHIQDKPALFRRFYKWLKPGGKVLITDYC 400
Cdd:PRK10258 109 SNLAVQWCGNLSTALRELYRVVRPGGVVAFTTLV 142
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
71-167 3.04e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 42.74  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   71 LEFGAGIGRFTTELAQKA--GQVIAVDFIESVIKKNENINGHYKNVKFLCADVTSPNM-NFPNESMDLIFSNWLLMYLSD 147
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpgLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLgELDPGSFDVVVASNVLHHLAD 80
                          90       100
                  ....*....|....*....|
gi 145362386  148 qeVEDLAKKMLQWTKVGGYI 167
Cdd:pfam08242  81 --PRAVLRNIRRLLKPGGVL 98
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
282-395 5.15e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 44.93  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 282 ETTKEFVDML---DLKPGQKVLDVGCGIGGGDFYMAENF-DVDVVGIDLSVNMISFALEHAIGlkcsVEFEVADCTKKEY 357
Cdd:PRK01683  15 ERTRPARDLLarvPLENPRYVVDLGCGPGNSTELLVERWpAARITGIDSSPAMLAEARSRLPD----CQFVEADIASWQP 90
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145362386 358 PDNTfDVIYSRDTILHIQDKPALFRRFYKWLKPGGkVL 395
Cdd:PRK01683  91 PQAL-DLIFANASLQWLPDHLELFPRLVSLLAPGG-VL 126
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
341-396 6.59e-05

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 44.58  E-value: 6.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 145362386   341 LKCSVEFEVADCTKKEYPDNTFDVIYSRDTILHI--QDKPALFRRFYKWLKPGGKVLI 396
Cdd:smart00138 183 LKERVRFAKHNLLAESPPLGDFDLIFCRNVLIYFdePTQRKLLNRFAEALKPGGYLFL 240
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
287-365 6.79e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 43.74  E-value: 6.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 287 FVDMLDLKPGQKVLDVGCGIG----GGDFYMAEnfdvDVVGIDLSVNMISFALEHAIGLKCSVEFEVADCTKKEyPDNTF 362
Cdd:COG2263   37 LAYLRGDIEGKTVLDLGCGTGmlaiGAALLGAK----KVVGVDIDPEALEIARENAERLGVRVDFIRADVTRIP-LGGSV 111

                 ...
gi 145362386 363 DVI 365
Cdd:COG2263  112 DTV 114
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
288-365 7.32e-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: 45.17  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 288 VDMLDLKPGQKVLDVGCGIGGgdF--YMAENFDvDVVGIDLSVNMISFALEHAI--GLKcSVEFEVADCTK---KEYPDN 360
Cdd:COG2265  226 LEWLDLTGGERVLDLYCGVGT--FalPLARRAK-KVIGVEIVPEAVEDARENARlnGLK-NVEFVAGDLEEvlpELLWGG 301

                 ....*
gi 145362386 361 TFDVI 365
Cdd:COG2265  302 RPDVV 306
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
58-167 8.30e-05

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: 43.99  E-value: 8.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  58 ILAFLPPIEGTTVLEFGAGIGRFTTELAQ---KAGQVIAV----DFIEsVIKKNENINGHYKNVKFLCADVTSpnmNFPN 130
Cdd:COG2519   83 IIARLDIFPGARVLEAGTGSGALTLALARavgPEGKVYSYerreDFAE-IARKNLERFGLPDNVELKLGDIRE---GIDE 158
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 145362386 131 ESMDLIFsnwLLMyLSDQEVEDLAKKMLqwtKVGGYI 167
Cdd:COG2519  159 GDVDAVF---LDM-PDPWEALEAVAKAL---KPGGVL 188
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
58-121 1.25e-04

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 43.96  E-value: 1.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145362386  58 ILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKKNENINGHYKNVKFLCADV 121
Cdd:COG0030   29 IVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNLTVIEGDA 92
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
66-141 1.60e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 43.10  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  66 EGTTVLEFGAGIGRFTTELAQK-AGQVIAVD---FIESVIKKNENINGHYKNVKFLCADVTSpnMNFPnESMDLIFSNWL 141
Cdd:COG4076   35 PGDVVLDIGTGSGLLSMLAARAgAKKVYAVEvnpDIAAVARRIIAANGLSDRITVINADATD--LDLP-EKADVIISEML 111
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
311-396 1.71e-04

CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.


Pssm-ID: 426403  Cd Length: 190  Bit Score: 42.65  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  311 FYMAENFDVDVVGIDLSVNMISFA-----------------LEHAIG------------LKCSVEFEVADCTKKEYPDNT 361
Cdd:pfam01739  56 FPNAARWDFKILATDIDLSVLEKAragvypereleglpeelLRRYFEktagggytvkpeIKSMVLFEYLNLLDEYPPLGD 135
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 145362386  362 FDVIYSRDTILHI--QDKPALFRRFYKWLKPGGKVLI 396
Cdd:pfam01739 136 FDVIFCRNVLIYFdeETQRKILNRFAEKLKPGGYLFL 172
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
51-108 2.53e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 42.97  E-value: 2.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145362386  51 DKEERPEILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAV-------DFIESVIKKNENIN 108
Cdd:PRK14896  14 DDRVVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKRAKKVYAIeldprlaEFLRDDEIAAGNVE 78
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
57-171 3.84e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.26  E-value: 3.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   57 EILAFLPPIEGT--TVLEFGAGIGRFTTELAQKAGQVIAVDFiesvikKNENINGHYKNVKFLCADVTSPnmNFPNESMD 134
Cdd:pfam13489  11 DLLLRLLPKLPSpgRVLDFGCGTGIFLRLLRAQGFSVTGVDP------SPIAIERALLNVRFDQFDEQEA--AVPAGKFD 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 145362386  135 LIFSNWLLMYLSDQEVedLAKKMLQWTKVGGYIFFRE 171
Cdd:pfam13489  83 VIVAREVLEHVPDPPA--LLRQIAALLKPGGLLLLST 117
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
60-139 4.22e-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: 42.05  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  60 AFLPPIEGTTVLEFGAGIGRFTTELAQK--AGQVIAVDFIESVI---KKNENINGHYKNVKFLCADVTSPNMNFPNESMD 134
Cdd:COG4123   31 AFAPVKKGGRVLDLGTGTGVIALMLAQRspGARITGVEIQPEAAelaRRNVALNGLEDRITVIHGDLKEFAAELPPGSFD 110

                 ....*
gi 145362386 135 LIFSN 139
Cdd:COG4123  111 LVVSN 115
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
292-367 5.54e-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: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 292 DLKPGQKVLDVGCGIGGGDFYMAENF-DVDVVGIDLSVNMISFALE--HAIGLKCSVEFEVADCT--KKEYPDNTFDVIY 366
Cdd:COG4123   34 PVKKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEAAELARRnvALNGLEDRITVIHGDLKefAAELPPGSFDLVV 113

                 .
gi 145362386 367 S 367
Cdd:COG4123  114 S 114
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
293-371 6.85e-04

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 40.90  E-value: 6.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145362386  293 LKPGQKVLDVGCGIGGGDFYMAENFDVDVVGIDLSVNMISFALEHAIglkcSVEFEVADCTKKEYPDNTFDVIYSRDTI 371
Cdd:pfam07021  11 IPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAAGVAECVAKGL----YVIQGDLDEGLEHFPDKSFDYVILSQTL 85
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
63-137 9.10e-04

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 40.64  E-value: 9.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  63 PPIEGTTVLEFGAGIGrFTTELAQKAG--QVIAVD---FIESVIKKNENINGhyKNVKFLCADVTSPNmnfPNESMDLIF 137
Cdd:COG3897   67 PEVAGKRVLELGCGLG-LVGIAAAKAGaaDVTATDydpEALAALRLNAALNG--VAITTRLGDWRDPP---AAGGFDLIL 140
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
66-217 1.12e-03

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 40.72  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  66 EGTTVLEFGAGIGRFTTELAQKAG-QVIAVDFIESVIKKNENINGHYKNVKFLCADVTSPNmnFPNESMDLIFSNWLLMY 144
Cdd:PTZ00098  52 ENSKVLDIGSGLGGGCKYINEKYGaHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKD--FPENTFDMIYSRDAILH 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 145 LSDQEVEDLAKKMLQWTKVGGYIFFRESCFHQSGD---------NKRKYNPTHYREpkfYTKLFKECHMND---EDGNSY 212
Cdd:PTZ00098 130 LSYADKKKLFEKCYKWLKPNGILLITDYCADKIENwdeefkayiKKRKYTLIPIQE---YGDLIKSCNFQNvvaKDISDY 206

                 ....*
gi 145362386 213 ELSLV 217
Cdd:PTZ00098 207 WLELL 211
PRK14968 PRK14968
putative methyltransferase; Provisional
289-365 1.74e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 39.50  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 289 DMLDLKPGQKVLDVGCGIGGGDFYMAENfDVDVVGIDLSVNMISFALEHAIGLKCS---VEFEVADCTKKeYPDNTFDVI 365
Cdd:PRK14968  17 ENAVDKKGDRVLEVGTGSGIVAIVAAKN-GKKVVGVDINPYAVECAKCNAKLNNIRnngVEVIRSDLFEP-FRGDKFDVI 94
capping_2-OMTase_Flaviviridae cd20761
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific ...
258-322 1.94e-03

Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific (nucleoside-2'-O-)-methyltransferase (2'OMTase) catalyzes the methylation of Cap-0 (m7GpppNp) at the 2'-hydroxyl of the ribose of the first nucleotide, using S-adenosyl-L-methionine (AdoMet) as the methyl donor. This reaction is the fourth and last step in mRNA capping, the creation of the stabilizing five-prime cap (5' cap) on mRNA. Flaviviridae viruses, comprise a family of ss(+)RNA viruses, cap their mRNAs. The 2'OMTase activity is located in the non-structural protein 5 (NS5).


Pssm-ID: 467736  Cd Length: 225  Bit Score: 39.90  E-value: 1.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145362386 258 QYKSSGILRYERVFGegFVSTGgleTTK--EFVDMLDLKPGQKVLDVGCGIGGGDFYMAENFDVDVV 322
Cdd:cd20761   20 AYKKRGVVEVATKGH--AVSRG---YAKlrWLVERGYVKPSGKVVDLGCGRGGWSQYAAGLPKVTEV 81
arsM PRK11873
arsenite methyltransferase;
55-139 1.95e-03

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 40.32  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  55 RPEILAFLPPieGTTVLEFGAGIGrFTTELAQKA----GQVIAVDFIESVI---KKNENINGhYKNVKFLCADVTspNMN 127
Cdd:PRK11873  68 NPTALAELKP--GETVLDLGSGGG-FDCFLAARRvgptGKVIGVDMTPEMLakaRANARKAG-YTNVEFRLGEIE--ALP 141
                         90
                 ....*....|..
gi 145362386 128 FPNESMDLIFSN 139
Cdd:PRK11873 142 VADNSVDVIISN 153
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
62-136 2.02e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 39.75  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386  62 LPPIEGTTVLEFGAGIGRFTTELAQKAG---QVIAVDFIES---VIKKNENINGHYKNVKFLCADVTspNMNFPNESMDL 135
Cdd:PRK00216  47 LGVRPGDKVLDLACGTGDLAIALAKAVGktgEVVGLDFSEGmlaVGREKLRDLGLSGNVEFVQGDAE--ALPFPDNSFDA 124

                 .
gi 145362386 136 I 136
Cdd:PRK00216 125 V 125
PRK14903 PRK14903
16S rRNA methyltransferase B; Provisional
269-366 2.36e-03

16S rRNA methyltransferase B; Provisional


Pssm-ID: 184896 [Multi-domain]  Cd Length: 431  Bit Score: 40.24  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 269 RVFGEGFVSTGGlETTKEFVDMLDLKPGQKVLDVGCGIGGGDFYMAE--NFDVDVVGIDLSVNMISFALEHAIGLKCS-V 345
Cdd:PRK14903 212 RVIKDGLATVQG-ESSQIVPLLMELEPGLRVLDTCAAPGGKTTAIAElmKDQGKILAVDISREKIQLVEKHAKRLKLSsI 290
                         90       100
                 ....*....|....*....|..
gi 145362386 346 EFEVADCTK-KEYPDNTFDVIY 366
Cdd:PRK14903 291 EIKIADAERlTEYVQDTFDRIL 312
TehB pfam03848
Tellurite resistance protein TehB;
70-166 3.35e-03

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 38.68  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   70 VLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKKNENINgHYKNVKFLCADVTSPNMNFPNESMDLIFSNWLLMYLSDQE 149
Cdd:pfam03848  34 VLDLGCGQGRNSLYLSLLGYDVTAWDKNENSIANLQRIK-EKENLDNIHTALYDINNATIDENYDFILSTVVLMFLEPER 112
                          90
                  ....*....|....*..
gi 145362386  150 VEDLAKKMLQWTKVGGY 166
Cdd:pfam03848 113 IPGIIANMQECTNPGGY 129
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
290-398 3.65e-03

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 39.85  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386 290 MLDLKPGQKVLDVGCGigGG---DFYMAENFDVDVVGIDLSVNMISF-----ALEH---------AIGLKCSVEFEVADC 352
Cdd:PRK06922 413 ILDYIKGDTIVDVGAG--GGvmlDMIEEETEDKRIYGIDISENVIDTlkkkkQNEGrswnvikgdAINLSSSFEKESVDT 490
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145362386 353 tkkeypdntfdVIYSrdTILHiqdkpALF-------RRF------------YKWLKPGGKVLITD 398
Cdd:PRK06922 491 -----------IVYS--SILH-----ELFsyieyegKKFnhevikkglqsaYEVLKPGGRIIIRD 537
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
58-139 6.54e-03

ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 38.37  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   58 ILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKKNENINGHYKNVKFLCADVTSPNMNFPNESMDLIF 137
Cdd:TIGR00755  21 IVEAANIQEGDRVLEIGPGLGALTEPLLKRAKKVTAIEIDPRLAERLRKLLSLYNNLEIIEGDALKFDLNELAKDLTKVV 100

                  ..
gi 145362386  138 SN 139
Cdd:TIGR00755 101 GN 102
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
57-161 8.02e-03

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 38.12  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362386   57 EILAFLPPIEGTTVLEFGAGIGRFTTELAQKAGQVIAVDFIESVIKK-NENINGHyKNVKFLCAD---------VTSPNM 126
Cdd:pfam00398  21 EIVDKANLRESDTVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLlQKKLSLD-ENLTVIHQDflkfefpslVTHIHQ 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 145362386  127 NF------PNESMDLIFSNWLLMYLsdqeveDLAKKMLQWT 161
Cdd:pfam00398 100 EFlvvgnlPYNISTPIVKQLLFESR------FGIVDMLLML 134
 
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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