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Conserved domains on  [gi|30684743|ref|NP_188427|]
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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
17-491 0e+00

phosphoethanolamine N-methyltransferase


:

Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 1029.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   17 IEHSADLTVEAMMLDSRASDLDKEERPEVLSLLPPYEGKSVLELGAGIGRFTGELAQKAGELIALDFIDNVIKKNESING 96
Cdd:PLN02336   1 KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESING 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   97 HYKNVKFMCADVTSPDLKITDGSLDLIFSNWLLMYLSDKEVELLAERMVGWIKVGGYIFFRESCFHQSGDSKRKSNPTHY 176
Cdd:PLN02336  81 HYKNVKFMCADVTSPDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQSGDSKRKNNPTHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  177 REPRFYSKVFQECQTRDAAGNSFELSMIGCKCIGAYVKNKKNQNQICWIWQKVSSENDRGFQRFLDNVQYKSSGILRYER 256
Cdd:PLN02336 161 REPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTNDKGFQRFLDNVQYKSSGILRYER 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  257 VFGQGFVSTGGLETTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLSCSVEFEV 336
Cdd:PLN02336 241 VFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  337 ADCTTKHYPDNSFDVIYSRDTILHIQDKPALFRTFFKWLKPGGKVLISDYCRSPKTPSAEFSEYIKQRGYDLHDVQAYGQ 416
Cdd:PLN02336 321 ADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTPSPEFAEYIKQRGYDLHDVQAYGQ 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30684743  417 MLKDAGFTDVIAEDRTDQFMQVLKRELDRVEKEKEKFISDFSKEDYDDIVGGWKSKLERCASDEQKWGLFIANKN 491
Cdd:PLN02336 401 MLKDAGFDDVIAEDRTDQFLQVLQRELDAVEKEKDEFISDFSEEDYNDIVGGWKAKLVRSSSGEQKWGLFIAKKK 475
 
Name Accession Description Interval E-value
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
17-491 0e+00

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 1029.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   17 IEHSADLTVEAMMLDSRASDLDKEERPEVLSLLPPYEGKSVLELGAGIGRFTGELAQKAGELIALDFIDNVIKKNESING 96
Cdd:PLN02336   1 KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESING 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   97 HYKNVKFMCADVTSPDLKITDGSLDLIFSNWLLMYLSDKEVELLAERMVGWIKVGGYIFFRESCFHQSGDSKRKSNPTHY 176
Cdd:PLN02336  81 HYKNVKFMCADVTSPDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQSGDSKRKNNPTHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  177 REPRFYSKVFQECQTRDAAGNSFELSMIGCKCIGAYVKNKKNQNQICWIWQKVSSENDRGFQRFLDNVQYKSSGILRYER 256
Cdd:PLN02336 161 REPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTNDKGFQRFLDNVQYKSSGILRYER 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  257 VFGQGFVSTGGLETTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLSCSVEFEV 336
Cdd:PLN02336 241 VFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  337 ADCTTKHYPDNSFDVIYSRDTILHIQDKPALFRTFFKWLKPGGKVLISDYCRSPKTPSAEFSEYIKQRGYDLHDVQAYGQ 416
Cdd:PLN02336 321 ADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTPSPEFAEYIKQRGYDLHDVQAYGQ 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30684743  417 MLKDAGFTDVIAEDRTDQFMQVLKRELDRVEKEKEKFISDFSKEDYDDIVGGWKSKLERCASDEQKWGLFIANKN 491
Cdd:PLN02336 401 MLKDAGFDDVIAEDRTDQFLQVLQRELDAVEKEKDEFISDFSEEDYNDIVGGWKAKLVRSSSGEQKWGLFIAKKK 475
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
237-385 1.96e-32

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 121.19  E-value: 1.96e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 237 FQRFLDNVQYKSSGIlrYERvfGQGFVSTGGLETTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVN 316
Cdd:COG2230  10 YRLFLDPTMTYSCAY--FED--PDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPE 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30684743 317 MISFALERA--IGLSCSVEFEVADCtTKHYPDNSFDVIYSRDTILHIQDK--PALFRTFFKWLKPGGKVLISD 385
Cdd:COG2230  86 QLEYARERAaeAGLADRVEVRLADY-RDLPADGQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
286-379 1.24e-27

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 105.72  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   286 VLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLSCSVEFEVADCTTKHYPDNSFDVIYSRDTILHI--QD 363
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdPD 80
                          90
                  ....*....|....*.
gi 30684743   364 KPALFRTFFKWLKPGG 379
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
285-386 4.80e-16

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: 74.00  E-value: 4.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 285 KVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLSCS-VEFEVADCTT-KHYPDNSFDVIYSRDTILHI- 361
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEElPPEADESFDVIISDPPLHHLv 80
                        90       100
                ....*....|....*....|....*
gi 30684743 362 QDKPALFRTFFKWLKPGGKVLISDY 386
Cdd:cd02440  81 EDLARFLEEARRLLKPGGVLVLTLV 105
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
273-431 3.91e-13

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: 68.85  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   273 EFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKF-DVHVVGIDLSVNMISFALERaigLSCSVEFEVADCTTKHYPDNSFDV 351
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTK---LSENVQFICGDAEKLPLEDSSFDL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   352 IYSRDTILHIQDKPALFRTFFKWLKPGGKVLISDYCrsPKTpSAEFSEYIKQRGYDLHDVQAYGQMLKDAgFTDVIAEDR 431
Cdd:TIGR02072 102 IVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFG--PGT-LHELRQSFGQHGLRYLSLDELKALLKNS-FELLTLEEE 177
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
285-490 3.14e-08

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 54.34  E-value: 3.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743    285 KVLDVGCGIGGGDFYMAEKF-DVHVVGIDLSVNMISFALER--AIGLSCSVEFEVADCTTKHYPDNsFDVIYSRDTILHI 361
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHpHLQLHGYTISPEQAEVGRERirALGLQGRIRIFYRDSAKDPFPDT-YDLVFGFEVIHHI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743    362 QDKPALFRTFFKWLKPGGKVLISDYCRSPKTP-----SAEF----SEYIKQRGYDLHDV-------QAYGQMLKDAGFtd 425
Cdd:smart00828  81 KDKMDLFSNISRHLKDGGHLVLADFIANLLSAieheeTTSYlvtrEEWAELLARNNLRVvegvdasLEIANFLYDPGF-- 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30684743    426 viaedrTDQFMQVLKRELDRVEKEKEKFISDFSKEdyddIVGGWKSklercasdeqkWGLFIANK 490
Cdd:smart00828 159 ------EDNLERLYQDDLDEVTKRHFRGIANLGKL----LEKGLAS-----------YALLIVQK 202
 
Name Accession Description Interval E-value
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
17-491 0e+00

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 1029.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   17 IEHSADLTVEAMMLDSRASDLDKEERPEVLSLLPPYEGKSVLELGAGIGRFTGELAQKAGELIALDFIDNVIKKNESING 96
Cdd:PLN02336   1 KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESING 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   97 HYKNVKFMCADVTSPDLKITDGSLDLIFSNWLLMYLSDKEVELLAERMVGWIKVGGYIFFRESCFHQSGDSKRKSNPTHY 176
Cdd:PLN02336  81 HYKNVKFMCADVTSPDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQSGDSKRKNNPTHY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  177 REPRFYSKVFQECQTRDAAGNSFELSMIGCKCIGAYVKNKKNQNQICWIWQKVSSENDRGFQRFLDNVQYKSSGILRYER 256
Cdd:PLN02336 161 REPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQICWLWQKVSSTNDKGFQRFLDNVQYKSSGILRYER 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  257 VFGQGFVSTGGLETTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLSCSVEFEV 336
Cdd:PLN02336 241 VFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGRKCSVEFEV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  337 ADCTTKHYPDNSFDVIYSRDTILHIQDKPALFRTFFKWLKPGGKVLISDYCRSPKTPSAEFSEYIKQRGYDLHDVQAYGQ 416
Cdd:PLN02336 321 ADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRSPGTPSPEFAEYIKQRGYDLHDVQAYGQ 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30684743  417 MLKDAGFTDVIAEDRTDQFMQVLKRELDRVEKEKEKFISDFSKEDYDDIVGGWKSKLERCASDEQKWGLFIANKN 491
Cdd:PLN02336 401 MLKDAGFDDVIAEDRTDQFLQVLQRELDAVEKEKDEFISDFSEEDYNDIVGGWKAKLVRSSSGEQKWGLFIAKKK 475
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
239-491 5.53e-73

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 231.78  E-value: 5.53e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  239 RFLDNVQYKSSGILRYERVFGQGFVSTGGLETTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMI 318
Cdd:PTZ00098   9 TYLENNQYSDEGIKAYEFIFGEDYISSGGIEATTKILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  319 SFALERAIGLScSVEFEVADCTTKHYPDNSFDVIYSRDTILHI--QDKPALFRTFFKWLKPGGKVLISDYCRSPKTP-SA 395
Cdd:PTZ00098  89 NIAKLRNSDKN-KIEFEANDILKKDFPENTFDMIYSRDAILHLsyADKKKLFEKCYKWLKPNGILLITDYCADKIENwDE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  396 EFSEYIKQRGYDLHDVQAYGQMLKDAGFTDVIAEDRTDQFMQVLKRELDRVEKEKEKFISDFSKEDYDDIVGGWKSKLER 475
Cdd:PTZ00098 168 EFKAYIKKRKYTLIPIQEYGDLIKSCNFQNVVAKDISDYWLELLQVELKKLEEKKEEFLKLYSEKEYNSLKDGWTRKIKD 247
                        250
                 ....*....|....*.
gi 30684743  476 CASDEQKWGLFIANKN 491
Cdd:PTZ00098 248 TKRKLQKWGYFKAQKM 263
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
237-385 1.96e-32

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 121.19  E-value: 1.96e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 237 FQRFLDNVQYKSSGIlrYERvfGQGFVSTGGLETTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVN 316
Cdd:COG2230  10 YRLFLDPTMTYSCAY--FED--PDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPE 85
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30684743 317 MISFALERA--IGLSCSVEFEVADCtTKHYPDNSFDVIYSRDTILHIQDK--PALFRTFFKWLKPGGKVLISD 385
Cdd:COG2230  86 QLEYARERAaeAGLADRVEVRLADY-RDLPADGQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
269-424 9.47e-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: 118.94  E-value: 9.47e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 269 ETTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKfDVHVVGIDLSVNMISFALERAIGLSCSVEFEVADCTTKHYPDNS 348
Cdd:COG2226   9 DGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGS 87
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30684743 349 FDVIYSRDTILHIQDKPALFRTFFKWLKPGGKVLISDYCRspktpsaefseyikqrgydlHDVQAYGQMLKDAGFT 424
Cdd:COG2226  88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP--------------------PDLAELEELLAEAGFE 143
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
286-379 1.24e-27

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 105.72  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   286 VLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLSCSVEFEVADCTTKHYPDNSFDVIYSRDTILHI--QD 363
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdPD 80
                          90
                  ....*....|....*.
gi 30684743   364 KPALFRTFFKWLKPGG 379
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
273-386 7.65e-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: 102.02  E-value: 7.65e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 273 EFVEKMnLKPGQKVLDVGCGIGGGDFYMAEKFdVHVVGIDLSVNMISFALERAIGLScsVEFEVADCTTKHYPDNSFDVI 352
Cdd:COG2227  16 ALLARL-LPAGGRVLDVGCGTGRLALALARRG-ADVTGVDISPEALEIARERAAELN--VDFVQGDLEDLPLEDGSFDLV 91
                        90       100       110
                ....*....|....*....|....*....|....
gi 30684743 353 YSRDTILHIQDKPALFRTFFKWLKPGGKVLISDY 386
Cdd:COG2227  92 ICSEVLEHLPDPAALLRELARLLKPGGLLLLSTP 125
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
282-385 2.38e-22

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 91.42  E-value: 2.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 282 PGQKVLDVGCGIGGGDFYMAEKF-DVHVVGIDLSVNMISFALERAIGlscsVEFEVADCTTKHyPDNSFDVIYSRDTILH 360
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLPN----VRFVVADLRDLD-PPEPFDLVVSNAALHW 75
                        90       100
                ....*....|....*....|....*
gi 30684743 361 IQDKPALFRTFFKWLKPGGKVLISD 385
Cdd:COG4106  76 LPDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
287-383 3.48e-22

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 90.80  E-value: 3.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   287 LDVGCGIGGGDFYMAEKFdVHVVGIDLSVNMISFALERAIGLScsVEFEVADCTTKHYPDNSFDVIYSRDTILHIQDKPA 366
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG-ARVTGVDISPEMLELAREKAPREG--LTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPER 77
                          90
                  ....*....|....*..
gi 30684743   367 LFRTFFKWLKPGGKVLI 383
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
PRK08317 PRK08317
hypothetical protein; Provisional
276-385 6.06e-22

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 94.62  E-value: 6.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  276 EKMNLKPGQKVLDVGCGIGGGDFYMAEKF--DVHVVGIDLSVNMISFALERAIGLSCSVEFEVADCTTKHYPDNSFDVIY 353
Cdd:PRK08317  13 ELLAVQPGDRVLDVGCGPGNDARELARRVgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFPDGSFDAVR 92
                         90       100       110
                 ....*....|....*....|....*....|..
gi 30684743  354 SRDTILHIQDKPALFRTFFKWLKPGGKVLISD 385
Cdd:PRK08317  93 SDRVLQHLEDPARALAEIARVLRPGGRVVVLD 124
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
272-424 2.40e-21

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 91.21  E-value: 2.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 272 KEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKFDvHVVGIDLSVNMISFALERAIGlscsVEFEVADCTTKHYPDNSFDV 351
Cdd:COG4976  36 EELLARLPPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKGVY----DRLLVADLADLAEPDGRFDL 110
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30684743 352 IYSRDTILHIQDKPALFRTFFKWLKPGGKVLISdycrspktpsaefSEYIKQRGYDLHDVQAYGQMLKDAGFT 424
Cdd:COG4976 111 IVAADVLTYLGDLAAVFAGVARALKPGGLFIFS-------------VEDADGSGRYAHSLDYVRDLLAAAGFE 170
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
280-386 9.78e-21

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 89.98  E-value: 9.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 280 LKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLSCS-VEFEVADCT-TKHYPDNSFDVIYSRDT 357
Cdd:COG0500  24 LPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAeLDPLPAESFDLVVAFGV 103
                        90       100       110
                ....*....|....*....|....*....|.
gi 30684743 358 ILHIQDKP--ALFRTFFKWLKPGGKVLISDY 386
Cdd:COG0500 104 LHHLPPEEreALLRELARALKPGGVLLLSAS 134
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
280-422 2.47e-20

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 87.47  E-value: 2.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   280 LKPGQKVLDVGCGIGGGDFYMAEK--FDVHVVGIDLSVNMISFALERA--IGLScSVEFEVADCT--TKHYPDNSFDVIY 353
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEElgPNAEVVGIDISEEAIEKARENAqkLGFD-NVEFEQGDIEelPELLEDDKFDVVI 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30684743   354 SRDTILHIQDKPALFRTFFKWLKPGGKVLISDYCRSPKTPSA--EFSEYIKQRGYDLHDVQAYGQMLKDAG 422
Cdd:pfam13847  80 SNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHvkEDSTYYAGCVGGAILKKKLYELLEEAG 150
PLN02244 PLN02244
tocopherol O-methyltransferase
235-430 4.13e-20

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 91.34  E-value: 4.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  235 RGFQRFLDnvqyKSSGIlrYERVFGQ----GFVSTGG------------LETTKEF--VEKMNLKPGQKVLDVGCGIGGG 296
Cdd:PLN02244  59 EGIAEFYD----ESSGV--WEDVWGEhmhhGYYDPGAsrgdhrqaqirmIEESLAWagVPDDDEKRPKRIVDVGCGIGGS 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  297 DFYMAEKFDVHVVGIDLSVNMISFA--LERAIGLSCSVEFEVADCTTKHYPDNSFDVIYSRDTILHIQDKPALFRTFFKW 374
Cdd:PLN02244 133 SRYLARKYGANVKGITLSPVQAARAnaLAAAQGLSDKVSFQVADALNQPFEDGQFDLVWSMESGEHMPDKRKFVQELARV 212
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30684743  375 LKPGGKVLISDYCRSPKTPSAEFSEYIKQ-------RGYDLHD---VQAYGQMLKDAGFTDVIAED 430
Cdd:PLN02244 213 AAPGGRIIIVTWCHRDLEPGETSLKPDEQklldkicAAYYLPAwcsTSDYVKLAESLGLQDIKTED 278
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
279-426 1.23e-19

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 85.94  E-value: 1.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   279 NLKPGQKVLDVGCGIGggdfYMAEKFD---VHVVGIDLSVNMIsfalERAIGLSCSVEFEVADCTtkhYPDNSFDVIYSR 355
Cdd:pfam13489  19 KLPSPGRVLDFGCGTG----IFLRLLRaqgFSVTGVDPSPIAI----ERALLNVRFDQFDEQEAA---VPAGKFDVIVAR 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30684743   356 DTILHIQDKPALFRTFFKWLKPGGKVLISDYCRSPKTP-SAEFSEYIKQRG--YDLHDVQAYGQMLKDAGFTDV 426
Cdd:pfam13489  88 EVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADrLLLEWPYLRPRNghISLFSARSLKRLLEEAGFEVV 161
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
272-426 3.72e-18

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 83.66  E-value: 3.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  272 KEFVEKMNLKPGQKVLDVGCGIggGD--FYMAEKFDV--HVVGIDLSVNMISFALERAI--GLSCSVEFEVADCTTKHYP 345
Cdd:PRK00216  41 RKTIKWLGVRPGDKVLDLACGT--GDlaIALAKAVGKtgEVVGLDFSEGMLAVGREKLRdlGLSGNVEFVQGDAEALPFP 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  346 DNSFDVIysrdTI---L-HIQDKPALFRTFFKWLKPGGKVLIsdycrspktpsAEFSE---YIKQRGYDLH--------- 409
Cdd:PRK00216 119 DNSFDAV----TIafgLrNVPDIDKALREMYRVLKPGGRLVI-----------LEFSKptnPPLKKAYDFYlfkvlplig 183
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 30684743  410 -----DVQAY----------------GQMLKDAGFTDV 426
Cdd:PRK00216 184 kliskNAEAYsylaesirafpdqeelAAMLEEAGFERV 221
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
31-158 2.25e-17

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: 78.88  E-value: 2.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  31 DSRASDLDkeERPEVLSLLPPYEGKSVLELGAGIGRFTGELAQKAGELIALDFIDNVIKK-NESINGHYKNVKFMCADVT 109
Cdd:COG2226   2 DRVAARYD--GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELaRERAAEAGLNVEFVVGDAE 79
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 30684743 110 spDLKITDGSLDLIFSNWLLMYLSDKEvELLAErMVGWIKVGGYIFFRE 158
Cdd:COG2226  80 --DLPFPDGSFDLVISSFVLHHLPDPE-RALAE-IARVLKPGGRLVVVD 124
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
287-381 3.89e-17

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 76.64  E-value: 3.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   287 LDVGCGIGGGDFYMAEKF-DVHVVGIDLSVNMISFALER--AIGLSCSVEFEVADCTTKHYPDNSFDVIYSRDTILHIQD 363
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERlaALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80
                          90
                  ....*....|....*...
gi 30684743   364 KPALFRTFFKWLKPGGKV 381
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
arsM PRK11873
arsenite methyltransferase;
278-432 3.92e-16

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 78.45  E-value: 3.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  278 MNLKPGQKVLDVGCGiGGGDFYMAEKF---DVHVVGIDLSVNMISFALERA--IGLScSVEFEVADCTTKHYPDNSFDVI 352
Cdd:PRK11873  73 AELKPGETVLDLGSG-GGFDCFLAARRvgpTGKVIGVDMTPEMLAKARANArkAGYT-NVEFRLGEIEALPVADNSVDVI 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  353 YSRDTILHIQDKPALFRTFFKWLKPGGKVLISDYcrspkTPSAEFSEYIKQRGyDLH--------DVQAYGQMLKDAGFT 424
Cdd:PRK11873 151 ISNCVINLSPDKERVFKEAFRVLKPGGRFAISDV-----VLRGELPEEIRNDA-ELYagcvagalQEEEYLAMLAEAGFV 224

                 ....*....
gi 30684743  425 DV-IAEDRT 432
Cdd:PRK11873 225 DItIQPKRE 233
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
285-386 4.80e-16

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: 74.00  E-value: 4.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 285 KVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLSCS-VEFEVADCTT-KHYPDNSFDVIYSRDTILHI- 361
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEElPPEADESFDVIISDPPLHHLv 80
                        90       100
                ....*....|....*....|....*
gi 30684743 362 QDKPALFRTFFKWLKPGGKVLISDY 386
Cdd:cd02440  81 EDLARFLEEARRLLKPGGVLVLTLV 105
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
276-463 5.28e-16

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: 78.14  E-value: 5.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   276 EKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALER--AIGLSCSVEFEVADcttkhYPD--NSFDV 351
Cdd:pfam02353  55 DKLGLKPGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKNQYKLARKRvaAEGLARKVEVLLQD-----YRDfdEPFDR 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   352 IYSRDTILHIQDK--PALFRTFFKWLKPGGKVLI-SDYCRSPK------TPSAEFSEYIKQRGY--DLHDVQAYGQmlkD 420
Cdd:pfam02353 130 IVSVGMFEHVGHEnyDTFFKKLYNLLPPGGLMLLhTITGLHPDetsergLPLKFIDKYIFPGGElpSISMIVESSS---E 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 30684743   421 AGFTDVIAEDRTDQFMQVLKRELDRVEKEKEKFISDFSKEDYD 463
Cdd:pfam02353 207 AGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIALQSEEFYR 249
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
57-152 6.72e-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: 6.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743    57 VLELGAGIGRFTGELAQKAG-ELIALDFIDNVIKK-NESINGHYKNVKFMCADVTspDLKITDGSLDLIFSNWLLMYLSD 134
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERaRERAAEAGLNVEFVQGDAE--DLPFPDGSFDLVVSSGVLHHLPD 78
                          90
                  ....*....|....*...
gi 30684743   135 KEVELLAERMVGWIKVGG 152
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
276-383 4.39e-14

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 73.73  E-value: 4.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  276 EKMNLKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIGLscSVEFEVADcttkhYPD--NSFDVIY 353
Cdd:PRK11705 161 RKLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGL--PVEIRLQD-----YRDlnGQFDRIV 233
                         90       100       110
                 ....*....|....*....|....*....|....
gi 30684743  354 SRDTILHIQDKPalFRTFFK----WLKPGGKVLI 383
Cdd:PRK11705 234 SVGMFEHVGPKN--YRTYFEvvrrCLKPDGLFLL 265
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
58-156 1.28e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 66.53  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743    58 LELGAGIGRFTGELAQKAGELIALDFIDNVIKKNESiNGHYKNVKFMCADVTspDLKITDGSLDLIFSNWLLMYLSDKEv 137
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELARE-KAPREGLTFVVGDAE--DLPFPDNSFDLVLSSEVLHHVEDPE- 76
                          90
                  ....*....|....*....
gi 30684743   138 ELLAErMVGWIKVGGYIFF 156
Cdd:pfam08241  77 RALRE-IARVLKPGGILII 94
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
273-431 3.91e-13

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: 68.85  E-value: 3.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   273 EFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKF-DVHVVGIDLSVNMISFALERaigLSCSVEFEVADCTTKHYPDNSFDV 351
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTK---LSENVQFICGDAEKLPLEDSSFDL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   352 IYSRDTILHIQDKPALFRTFFKWLKPGGKVLISDYCrsPKTpSAEFSEYIKQRGYDLHDVQAYGQMLKDAgFTDVIAEDR 431
Cdd:TIGR02072 102 IVSNLALQWCDDLSQALSELARVLKPGGLLAFSTFG--PGT-LHELRQSFGQHGLRYLSLDELKALLKNS-FELLTLEEE 177
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
53-156 8.62e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 64.46  E-value: 8.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  53 EGKSVLELGAGIGRFTGELAQK--AGELIALDFIDNVIkknESINGHYKNVKFMCADVTSPDLkitDGSLDLIFSNWLLM 130
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEML---ARARARLPNVRFVVADLRDLDP---PEPFDLVVSNAALH 74
                        90       100
                ....*....|....*....|....*.
gi 30684743 131 YLSDKEvELLAeRMVGWIKVGGYIFF 156
Cdd:COG4106  75 WLPDHA-ALLA-RLAAALAPGGVLAV 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
28-156 1.25e-12

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: 64.65  E-value: 1.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  28 MMLDSRASDLDKEERPEVLSLLPPyeGKSVLELGAGIGRFTGELAQKAGELIALDFIDNVIKKNESiNGHYKNVKFMCAD 107
Cdd:COG2227   1 MSDPDARDFWDRRLAALLARLLPA--GGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARE-RAAELNVDFVQGD 77
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 30684743 108 VTspDLKITDGSLDLIFSNWLLMYLSDkeVELLAERMVGWIKVGGYIFF 156
Cdd:COG2227  78 LE--DLPLEDGSFDLVICSEVLEHLPD--PAALLRELARLLKPGGLLLL 122
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
272-426 1.36e-11

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 64.38  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   272 KEFVEK-MNLKPGQKVLDVGCGIGGGDFYMAEKFDV--HVVGIDLSVNMISFALERA--IGLScSVEFEVADCTTKHYPD 346
Cdd:pfam01209  31 KDFTMKcMGVKRGNKFLDVAGGTGDWTFGLSDSAGSsgKVVGLDINENMLKEGEKKAkeEGKY-NIEFLQGNAEELPFED 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   347 NSFDVIYSRDTILHIQDKPALFRTFFKWLKPGGKVLISDYCRsPKTP-----------------------SAEFSEYIKQ 403
Cdd:pfam01209 110 DSFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSK-PENPllsqayelyfkyvmpfmgkmfakSYKSYQYLQE 188
                         170       180
                  ....*....|....*....|...
gi 30684743   404 RGYDLHDVQAYGQMLKDAGFTDV 426
Cdd:pfam01209 189 SIRDFPDQKTLASMFEKAGFKSV 211
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
44-156 1.36e-10

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 60.40  E-value: 1.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  44 EVLSLLPPYEGKSVLELGAGIGRFTGELAQKAGELIALDFIDNVIKKNESiNGHYknVKFMCADVTspDLKITDGSLDLI 123
Cdd:COG4976  37 ELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKARE-KGVY--DRLLVADLA--DLAEPDGRFDLI 111
                        90       100       110
                ....*....|....*....|....*....|...
gi 30684743 124 FSNWLLMYLSDkeVELLAERMVGWIKVGGYIFF 156
Cdd:COG4976 112 VAADVLTYLGD--LAAVFAGVARALKPGGLFIF 142
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
53-178 5.18e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 57.81  E-value: 5.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743    53 EGKSVLELGAGIGRFTGELAQKAG---ELIALDFIDNVIK--KNESINGHYKNVKFMCADVTSPDLKITDGSLDLIFSNW 127
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEkaRENAQKLGFDNVEFEQGDIEELPELLEDDKFDVVISNC 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 30684743   128 LLMYLSDK-EVELLAERMVgwiKVGGYIFFRESCFHQSGDSKRKSNPTHYRE 178
Cdd:pfam13847  83 VLNHIPDPdKVLQEILRVL---KPGGRLIISDPDSLAELPAHVKEDSTYYAG 131
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
46-156 1.79e-09

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: 58.07  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743    46 LSLLP---PYEGKSVLELGAGIGRFTGELAQK--AGELIALDFIDNVIKKNESINGhyKNVKFMCADVTSpdLKITDGSL 120
Cdd:TIGR02072  24 LALLKekgIFIPASVLDIGCGTGYLTRALLKRfpQAEFIALDISAGMLAQAKTKLS--ENVQFICGDAEK--LPLEDSSF 99
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 30684743   121 DLIFSNWLLMYLSDKEvELLAErMVGWIKVGGYIFF 156
Cdd:TIGR02072 100 DLIVSNLALQWCDDLS-QALSE-LARVLKPGGLLAF 133
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
285-490 3.14e-08

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 54.34  E-value: 3.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743    285 KVLDVGCGIGGGDFYMAEKF-DVHVVGIDLSVNMISFALER--AIGLSCSVEFEVADCTTKHYPDNsFDVIYSRDTILHI 361
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHpHLQLHGYTISPEQAEVGRERirALGLQGRIRIFYRDSAKDPFPDT-YDLVFGFEVIHHI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743    362 QDKPALFRTFFKWLKPGGKVLISDYCRSPKTP-----SAEF----SEYIKQRGYDLHDV-------QAYGQMLKDAGFtd 425
Cdd:smart00828  81 KDKMDLFSNISRHLKDGGHLVLADFIANLLSAieheeTTSYlvtrEEWAELLARNNLRVvegvdasLEIANFLYDPGF-- 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30684743    426 viaedrTDQFMQVLKRELDRVEKEKEKFISDFSKEdyddIVGGWKSklercasdeqkWGLFIANK 490
Cdd:smart00828 159 ------EDNLERLYQDDLDEVTKRHFRGIANLGKL----LEKGLAS-----------YALLIVQK 202
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
57-156 3.19e-08

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 51.66  E-value: 3.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  57 VLELGAGIGRFTGELAQ-KAGELIALDFIDNVIKKNESI--NGHYKNVKFMCADVTSPDLKItDGSLDLIFSNWLLMYLS 133
Cdd:cd02440   2 VLDLGCGTGALALALASgPGARVTGVDISPVALELARKAaaALLADNVEVLKGDAEELPPEA-DESFDVIISDPPLHHLV 80
                        90       100
                ....*....|....*....|...
gi 30684743 134 DKEVELLaERMVGWIKVGGYIFF 156
Cdd:cd02440  81 EDLARFL-EEARRLLKPGGVLVL 102
PRK08317 PRK08317
hypothetical protein; Provisional
42-154 9.28e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 53.02  E-value: 9.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   42 RPEVLSLLPPYEGKSVLELGAGIGRFTGELAQ---KAGELIALDFIDNVIK-KNESINGHYKNVKFMCADVTSpdLKITD 117
Cdd:PRK08317   8 RARTFELLAVQPGDRVLDVGCGPGNDARELARrvgPEGRVVGIDRSEAMLAlAKERAAGLGPNVEFVRGDADG--LPFPD 85
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 30684743  118 GSLDLIFSNWLLMYLSDKEVeLLAErMVGWIKVGGYI 154
Cdd:PRK08317  86 GSFDAVRSDRVLQHLEDPAR-ALAE-IARVLRPGGRV 120
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
257-383 1.93e-07

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: 51.34  E-value: 1.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 257 VFGQGFVSTGgletTKEFVEKMNLKPGQKVLDVGCGIG--GGdfYMAEKF-DVHVVGIDLSvnmiSFALE------RAIG 327
Cdd:COG2813  28 VFSRDRLDIG----TRLLLEHLPEPLGGRVLDLGCGYGviGL--ALAKRNpEARVTLVDVN----ARAVElaranaAANG 97
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30684743 328 LScSVEFEVADCTTkHYPDNSFDVIYS----------RDTILHiqdkpALFRTFFKWLKPGGKVLI 383
Cdd:COG2813  98 LE-NVEVLWSDGLS-GVPDGSFDLILSnppfhagravDKEVAH-----ALIADAARHLRPGGELWL 156
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
35-156 7.14e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.91  E-value: 7.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  35 SDLDKEERPEVLSLLPPYE----GKSVLELGAGIGRFTGELAQKAGE-LIALDF----IDNVIKKNESINghYKNVKFMC 105
Cdd:COG0500   4 SYYSDELLPGLAALLALLErlpkGGRVLDLGCGTGRNLLALAARFGGrVIGIDLspeaIALARARAAKAG--LGNVEFLV 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 30684743 106 ADVTSPDlKITDGSLDLIFSNWLLMYLSDKEVELLAERMVGWIKVGGYIFF 156
Cdd:COG0500  82 ADLAELD-PLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
279-381 9.49e-07

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: 49.76  E-value: 9.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 279 NLKPGQKVLDVGCGIGGGDFYMAEKF-DVHVVGIDLSVNMISFALE--RAIGLSCSVEFEVADCTT--KHYPDNSFDVIY 353
Cdd:COG4123  34 PVKKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEAAELARRnvALNGLEDRITVIHGDLKEfaAELPPGSFDLVV 113
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 30684743 354 S-----------------RDTILHIQDKP--ALFRTFFKWLKPGGKV 381
Cdd:COG4123 114 SnppyfkagsgrkspdeaRAIARHEDALTleDLIRAAARLLKPGGRF 160
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
282-409 9.61e-07

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: 49.50  E-value: 9.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 282 PGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSvnmiSFALErAIGLSC-----SVEFEVADCTTKHyPDNSFDVI---- 352
Cdd:COG3897  70 AGKRVLELGCGLGLVGIAAAKAGAADVTATDYD----PEALA-ALRLNAalngvAITTRLGDWRDPP-AAGGFDLIlggd 143
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 353 --YSRDTILHIqdkPALFRTFfkwLKPGGKVLISDYCRSpktPSAEFSEY-IKQRGYDLH 409
Cdd:COG3897 144 vlYERDLAEPL---LPFLDRL---AAPGGEVLIGDPGRG---YLPAFRERlEALAGYEVV 194
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
281-414 2.13e-06

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 49.12  E-value: 2.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  281 KPGQKVLDVGCGIGGGDFYMAEKF--DVHVVGIDLSVNMISFALERAIGLSCS----VEFEVADCTTKHYPDNSFDVIYS 354
Cdd:PLN02233  72 KMGDRVLDLCCGSGDLAFLLSEKVgsDGKVMGLDFSSEQLAVAASRQELKAKScyknIEWIEGDATDLPFDDCYFDAITM 151
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30684743  355 RDTILHIQDKPALFRTFFKWLKPGGKVLISDYCRSPKTPSAEFSEYIKQR-------GYDLHDVQAY 414
Cdd:PLN02233 152 GYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEWMIDNvvvpvatGYGLAKEYEY 218
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
280-411 2.25e-06

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: 47.64  E-value: 2.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 280 LKPGQKVLDVGCGIGGgdfyM---AEKFDVHVVGIDLSVNMISFA---LERAigLSCSVEFEVADCTTKHYPDNSFDVI- 352
Cdd:COG1041  24 AKEGDTVLDPFCGTGT----IlieAGLLGRRVIGSDIDPKMVEGArenLEHY--GYEDADVIRGDARDLPLADESVDAIv 97
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30684743 353 ----------YSRDTILHIQDKpaLFRTFFKWLKPGGKVLISdycrspkTPsAEFSEYIKQRGYDLHDV 411
Cdd:COG1041  98 tdppygrsskISGEELLELYEK--ALEEAARVLKPGGRVVIV-------TP-RDIDELLEEAGFKVLER 156
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
283-391 4.65e-06

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: 47.67  E-value: 4.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   283 GQKVLDVGCGIGGGDFYMA-EKFDVhvVGIDLSVNMISFALERAIGLSCSVEFEvadCTT--KHYPDN--SFDVIYSRDT 357
Cdd:TIGR01983  47 GLRVLDVGCGGGLLSEPLArLGANV--TGIDASEENIEVAKLHAKKDPLQIDYR---CTTveDLAEKKagSFDVVTCMEV 121
                          90       100       110
                  ....*....|....*....|....*....|....
gi 30684743   358 ILHIQDKPALFRTFFKWLKPGGKVLISDYCRSPK 391
Cdd:TIGR01983 122 LEHVPDPQAFIRACAQLLKPGGILFFSTINRTPK 155
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
280-385 4.86e-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: 46.72  E-value: 4.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 280 LKPGQKVLDVGCGIGGGDFYMAE--KFDVHVVGIDLSVNMISFA---LERAiGLSCSVEFEVADCTT--KHYPDNSFDVI 352
Cdd:COG4122  14 LLGAKRILEIGTGTGYSTLWLARalPDDGRLTTIEIDPERAAIArenFARA-GLADRIRLILGDALEvlPRLADGPFDLV 92
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 30684743 353 YSrDTilhiqDK---PALFRTFFKWLKPGGkVLISD 385
Cdd:COG4122  93 FI-DA-----DKsnyPDYLELALPLLRPGG-LIVAD 121
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
280-358 1.03e-05

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: 46.29  E-value: 1.03e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30684743   280 LKPGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIglscSVEFEVADCTTKHYPDNSFDVIYSRDTI 358
Cdd:pfam07021  11 IPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAAGVAECVAKGL----YVIQGDLDEGLEHFPDKSFDYVILSQTL 85
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
280-382 1.05e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 46.86  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  280 LKPGQKVLDVGCGIGGGDFYMAEKF-DVHVVGIDLSVNMISFALERAIGlscsVEFEVADCTTKHyPDNSFDVIYSRDTI 358
Cdd:PRK01683  29 LENPRYVVDLGCGPGNSTELLVERWpAARITGIDSSPAMLAEARSRLPD----CQFVEADIASWQ-PPQALDLIFANASL 103
                         90       100
                 ....*....|....*....|....
gi 30684743  359 LHIQDKPALFRTFFKWLKPGGkVL 382
Cdd:PRK01683 104 QWLPDHLELFPRLVSLLAPGG-VL 126
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
344-397 1.05e-05

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 45.63  E-value: 1.05e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30684743 344 YPDNSFDVIYSRDTILHIQDK--PALFRTFFKWLKPGGKVLISdycrspkTPSAEF 397
Cdd:COG4627  42 FPDNSVDAIYSSHVLEHLDYEeaPLALKECYRVLKPGGILRIV-------VPDLEH 90
PRK06202 PRK06202
hypothetical protein; Provisional
286-390 1.47e-05

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 46.15  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  286 VLDVGCGigGGDF-----YMAEK--FDVHVVGIDLSVNMISFALERAIGLSCSVEFEVADCTTKHypDNSFDVIYSrDTI 358
Cdd:PRK06202  64 LLDIGCG--GGDLaidlaRWARRdgLRLEVTAIDPDPRAVAFARANPRRPGVTFRQAVSDELVAE--GERFDVVTS-NHF 138
                         90       100       110
                 ....*....|....*....|....*....|....
gi 30684743  359 LHIQDkPALFRTFFK--WLKPGGKVLISDYCRSP 390
Cdd:PRK06202 139 LHHLD-DAEVVRLLAdsAALARRLVLHNDLIRSR 171
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
53-126 4.53e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.51  E-value: 4.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  53 EGKSVLELGAGIGRFtGELAQKAG--ELIALDfID----NVIKKNESINGHykNVKFMCADVTSPDLkitDGSLDLIFSN 126
Cdd:COG2263  45 EGKTVLDLGCGTGML-AIGAALLGakKVVGVD-IDpealEIARENAERLGV--RVDFIRADVTRIPL---GGSVDTVVMN 117
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
58-154 8.07e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 41.58  E-value: 8.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743    58 LELGAGIGRFTGELAQKA--GELIALDFIDNVIKKNESINGHYKNVKFMCADVTSPDLKITDG-SLDLIFSNWLLMYLSD 134
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpgLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPgSFDVVVASNVLHHLAD 80
                          90       100
                  ....*....|....*....|
gi 30684743   135 KEvELLaERMVGWIKVGGYI 154
Cdd:pfam08242  81 PR-AVL-RNIRRLLKPGGVL 98
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
44-156 1.02e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.61  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  44 EVLSLLPPYEGKSVLELGAGIGRFTGELAQKAG-ELIALDF----IDNVIKKNESINGHYKnVKFMCADVTSPDLkitDG 118
Cdd:COG2230  42 LILRKLGLKPGMRVLDIGCGWGGLALYLARRYGvRVTGVTLspeqLEYARERAAEAGLADR-VEVRLADYRDLPA---DG 117
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 30684743 119 SLDLIFSNWLLMYLSDKEVELLAERMVGWIKVGGYIFF 156
Cdd:COG2230 118 QFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
257-383 1.46e-04

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 42.58  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   257 VFGQGFVSTGgletTKEFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKF-DVHVVGIDLSVNMISFALE--RAIGLScSVE 333
Cdd:pfam05175  10 VFSHGRLDIG----SRLLLEHLPKDLSGKVLDLGCGAGVLGAALAKESpDAELTMVDINARALESAREnlAANGLE-NGE 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 30684743   334 FEVADCTTKhYPDNSFDVIYS-------RDTILHIQDkpALFRTFFKWLKPGGKVLI 383
Cdd:pfam05175  85 VVASDVYSG-VEDGKFDLIISnppfhagLATTYNVAQ--RFIADAKRHLRPGGELWI 138
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
47-146 1.92e-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: 43.19  E-value: 1.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  47 SLLPPYEGKSVLELGAGIGRFTGELAQKAGELIALDfIDNV-IKKNESINGHYKNVKFMCADVTSPDL-KITDGSLDLIF 124
Cdd:COG0030  31 DAAGITPGDTVLEIGPGLGALTRALLERAARVTAVE-IDRRlAAILRETFAAYPNLTVIEGDALKVDLpALAAGEPLKVV 109
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 30684743 125 SN-----------WLLMYLSD---------KEVellAERMVG 146
Cdd:COG0030 110 GNlpynistpilfKLLEARPPiedavlmvqKEV---AERLVA 148
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
286-387 2.55e-04

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 42.82  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  286 VLDVGCGIGGGDFYMAEKfDVHVVGIDLSVNMISFALERaiglSCSVEFEVADCTTKHYPDNSFDVIYSRDTILHIQDKP 365
Cdd:PRK10258  46 VLDAGCGPGWMSRYWRER-GSQVTALDLSPPMLAQARQK----DAADHYLAGDIESLPLATATFDLAWSNLAVQWCGNLS 120
                         90       100
                 ....*....|....*....|..
gi 30684743  366 ALFRTFFKWLKPGGKVLISDYC 387
Cdd:PRK10258 121 TALRELYRVVRPGGVVAFTTLV 142
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
258-384 3.27e-04

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 42.47  E-value: 3.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 258 FGqgfvsTGGLETTK---EFVEKMnLKPGQKVLDVGCG-----IGggdfymAEKF-DVHVVGIDLSvnmiSFALERAI-- 326
Cdd:COG2264 127 FG-----TGTHPTTRlclEALEKL-LKPGKTVLDVGCGsgilaIA------AAKLgAKRVLAVDID----PVAVEAARen 190
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30684743 327 ----GLSCSVEFEVADcttkHYPDNSFDVIYS---RDTILhiqdkpALFRTFFKWLKPGGKVLIS 384
Cdd:COG2264 191 aelnGVEDRIEVVLGD----LLEDGPYDLVVAnilANPLI------ELAPDLAALLKPGGYLILS 245
capping_2-OMTase_Flaviviridae cd20761
Cap-0 specific (nucleoside-2'-O-)-methyltransferase of flaviviridae; Cap-0 specific ...
245-301 7.06e-04

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: 41.05  E-value: 7.06e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30684743 245 QYKSSGILRYERVFGqgFVSTGgleTTK--EFVEKMNLKPGQKVLDVGCGIGGGDFYMA 301
Cdd:cd20761  20 AYKKRGVVEVATKGH--AVSRG---YAKlrWLVERGYVKPSGKVVDLGCGRGGWSQYAA 73
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
275-352 7.86e-04

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


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 41.70  E-value: 7.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743 275 VEKMNLKPGQKVLDVGCGIGGgdF--YMAEKFDvHVVGIDLSVNMISFALE--RAIGLScSVEFEVADCT---TKHYPDN 347
Cdd:COG2265 226 LEWLDLTGGERVLDLYCGVGT--FalPLARRAK-KVIGVEIVPEAVEDAREnaRLNGLK-NVEFVAGDLEevlPELLWGG 301

                ....*
gi 30684743 348 SFDVI 352
Cdd:COG2265 302 RPDVV 306
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
43-153 9.62e-04

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 40.49  E-value: 9.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   43 PEVLSLLPPYEGKSVLELGAGIGRFTGELAQKAGELIALD----FIDNV--IKKNESINGHYKNVKfmcaDVTSPDLkit 116
Cdd:PRK11207  20 SEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDknpmSIANLerIKAAENLDNLHTAVV----DLNNLTF--- 92
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 30684743  117 DGSLDLIFSNWLLMYLSDKEVELLAERMVGWIKVGGY 153
Cdd:PRK11207  93 DGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGY 129
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
282-358 1.02e-03

methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273958  Cd Length: 194  Bit Score: 40.43  E-value: 1.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30684743   282 PGQKVLDVGCGIGGGDFYMAEKFDVHVVGIDLSVNMISFALERAIglscSVEFEVADCTTKHYPDNSFDVIYSRDTI 358
Cdd:TIGR02081  13 PGSRVLDLGCGDGELLALLRDEKQVRGYGIEIDQDGVLACVARGV----NVIQGDLDEGLEAFPDKSFDYVILSQTL 85
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
282-338 1.41e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 40.21  E-value: 1.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30684743  282 PGQKVLDVGCGIGGGDFYMAEKfDVHVVGIDLSVNMISFALERA--IGLSCSVEFEVAD 338
Cdd:PRK07580  63 TGLRILDAGCGVGSLSIPLARR-GAKVVASDISPQMVEEARERApeAGLAGNITFEVGD 120
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
274-383 1.66e-03

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 39.66  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743   274 FVEKMNLKPGQKVLDVGCGIGggdfYMAEKFDVHV--VGIDLSVNMISFALERAI------GLScSVEFEVADcTTKHYP 345
Cdd:pfam01135  65 MLELLELKPGMRVLEIGSGSG----YLTACFARMVgeVGRVVSIEHIPELVEIARrnleklGLE-NVIVVVGD-GRQGWP 138
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 30684743   346 DNS-FDVIYSRDTIlhiqdkPALFRTFFKWLKPGGKVLI 383
Cdd:pfam01135 139 EFApYDAIHVGAAA------PEIPEALIDQLKEGGRLVI 171
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
282-352 1.79e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 39.50  E-value: 1.79e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30684743 282 PGQKVLDVGCGIG----GGDFYMAEKfdvhVVGIDLSVNMISFALERAIGLSCSVEFEVADCtTKHYPDNSFDVI 352
Cdd:COG2263  45 EGKTVLDLGCGTGmlaiGAALLGAKK----VVGVDIDPEALEIARENAERLGVRVDFIRADV-TRIPLGGSVDTV 114
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
41-124 2.45e-03

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: 39.48  E-value: 2.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  41 ERPEVlsllppyEGKSVLELGAGIGrFTGELAQKAG--ELIALDFIDNV---IKKNESINGhyKNVKFMCADVTSPDLki 115
Cdd:COG3897  65 DHPEV-------AGKRVLELGCGLG-LVGIAAAKAGaaDVTATDYDPEAlaaLRLNAALNG--VAITTRLGDWRDPPA-- 132

                ....*....
gi 30684743 116 tDGSLDLIF 124
Cdd:COG3897 133 -AGGFDLIL 140
rADc smart00650
Ribosomal RNA adenine dimethylases;
44-153 3.14e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 38.65  E-value: 3.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743     44 EVLSLLPPYEGKSVLELGAGIGRFTGELAQKAGELIAL----DFIDNVIKKNEsingHYKNVKFMCADVTSPDLkiTDGS 119
Cdd:smart00650   4 KIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIeidpRLAPRLREKFA----AADNLTVIHGDALKFDL--PKLQ 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 30684743    120 LDLIFSN-----------WLL--------MYL-SDKEVellAERMVGWIKVGGY 153
Cdd:smart00650  78 PYKVVGNlpynistpilfKLLeeppafrdAVLmVQKEV---ARRLAAKPGSKDY 128
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
273-379 3.17e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 39.29  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  273 EFVEKMNLKPGQKVLDVGCGIGGGDFYMAEKF-DVHVVGIDLSVNMISFALERAiglscsVEFEVADCTTkHYPDNSFDV 351
Cdd:PRK14103  20 DLLARVGAERARRVVDLGCGPGNLTRYLARRWpGAVIEALDSSPEMVAAARERG------VDARTGDVRD-WKPKPDTDV 92
                         90       100
                 ....*....|....*....|....*...
gi 30684743  352 IYSRDTILHIQDKPALFRTFFKWLKPGG 379
Cdd:PRK14103  93 VVSNAALQWVPEHADLLVRWVDELAPGS 120
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
46-126 5.90e-03

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 37.57  E-value: 5.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743    46 LSLLPPYEGKSVLELGAGIGRFTGELAQKAGElIALDFID------NVIKKNESINGHyKNVKFMCADVTSPdlkITDGS 119
Cdd:pfam05175  24 LEHLPKDLSGKVLDLGCGAGVLGAALAKESPD-AELTMVDinaralESARENLAANGL-ENGEVVASDVYSG---VEDGK 98

                  ....*..
gi 30684743   120 LDLIFSN 126
Cdd:pfam05175  99 FDLIISN 105
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
276-383 6.04e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 38.07  E-value: 6.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  276 EKMNLKPGQKVLDVGCGIGGGDFYMAEKF--DVHVVGIDLSVNMISFALE--RAIGLScSVEFEVADcTTKHYPDNS-FD 350
Cdd:PRK13942  70 ELLDLKEGMKVLEIGTGSGYHAAVVAEIVgkSGKVVTIERIPELAEKAKKtlKKLGYD-NVEVIVGD-GTLGYEENApYD 147
                         90       100       110
                 ....*....|....*....|....*....|...
gi 30684743  351 VIYSRDTilhiqdKPALFRTFFKWLKPGGKVLI 383
Cdd:PRK13942 148 RIYVTAA------GPDIPKPLIEQLKDGGIMVI 174
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
54-126 6.33e-03

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 38.20  E-value: 6.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  54 GKSVLELGAGigrfTGE----LAQK--AGELIALDfIDNV----IKKNESINGHYKNVKFMCADVTSPDLKITDGSLDLI 123
Cdd:COG4123  38 GGRVLDLGTG----TGVialmLAQRspGARITGVE-IQPEaaelARRNVALNGLEDRITVIHGDLKEFAAELPPGSFDLV 112

                ...
gi 30684743 124 FSN 126
Cdd:COG4123 113 VSN 115
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
53-145 7.24e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 38.09  E-value: 7.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30684743  53 EGKSVLELGAGIGRFTGELAQK-AGELIALD---FIDNVIKKNESINGHYKNVKFMCADVTSPDLKitdGSLDLIFSNWL 128
Cdd:COG4076  35 PGDVVLDIGTGSGLLSMLAARAgAKKVYAVEvnpDIAAVARRIIAANGLSDRITVINADATDLDLP---EKADVIISEML 111
                        90
                ....*....|....*..
gi 30684743 129 lmylsdkEVELLAERMV 145
Cdd:COG4076 112 -------DTALLDEGQV 121
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
258-313 9.31e-03

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 37.82  E-value: 9.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30684743  258 FGqgfvsTGGLETTK---EFVEKMnLKPGQKVLDVGCG-----IGggdfymAEKFDV-HVVGIDL 313
Cdd:PRK00517  98 FG-----TGTHPTTRlclEALEKL-VLPGKTVLDVGCGsgilaIA------AAKLGAkKVLAVDI 150
 
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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