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Conserved domains on  [gi|1280981287|ref|XP_023003731|]
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phosphomethylethanolamine N-methyltransferase-like isoform X1 [Cucurbita maxima]

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
19-522 0e+00

phosphoethanolamine N-methyltransferase


:

Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 971.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  19 MEHSAGLTLEGMLLDSNASDLDKEERPEVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAGQVIALDFIEGVIKKNESING 98
Cdd:PLN02336    1 KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESING 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  99 HHKNVKFMCADVTSPELKVSENSVDLIFSNWLLMYLSDKEVKNLAERMVKWLKVGGYIFFRESCFHQSGDCKRKYNPTHY 178
Cdd:PLN02336   81 HYKNVKFMCADVTSPDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQSGDSKRKNNPTHY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 179 REPRFYTKVFKECHMQDEGGDCYELSLVGYKCIGAYARNKKNQNQvlnhlyfvssfansqalnqknqiclwvfqICWIWQ 258
Cdd:PLN02336  161 REPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQ-----------------------------ICWLWQ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 259 KQkSSNDDRGFQRFLDTVQYKCSGILRYERVFGPGFVSTGGIETTKEFVGKLDLKPGQRVLDVGCGIGGGDFYMAENFDV 338
Cdd:PLN02336  212 KV-SSTNDKGFQRFLDNVQYKSSGILRYERVFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDV 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 339 EVVGIDLSINMISLALERAIGLKCAVEFEVADCTKKVYPDNAFDVIYSRDTILHIQDKPALFRSFYKWVKPGGKILITDY 418
Cdd:PLN02336  291 HVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDY 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 419 CKSSGAPSPAFAEYIKQRGYDLHDVKSYGQMLEEAGFKDVVAEDRTDQFMSVLQRELDAVEKEKDAFIHDFSEEDYNDIV 498
Cdd:PLN02336  371 CRSPGTPSPEFAEYIKQRGYDLHDVQAYGQMLKDAGFDDVIAEDRTDQFLQVLQRELDAVEKEKDEFISDFSEEDYNDIV 450
                         490       500
                  ....*....|....*....|....
gi 1280981287 499 GGWKAKLERCWCGEQKWGLFIAHK 522
Cdd:PLN02336  451 GGWKAKLVRSSSGEQKWGLFIAKK 474
 
Name Accession Description Interval E-value
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
19-522 0e+00

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 971.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  19 MEHSAGLTLEGMLLDSNASDLDKEERPEVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAGQVIALDFIEGVIKKNESING 98
Cdd:PLN02336    1 KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESING 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  99 HHKNVKFMCADVTSPELKVSENSVDLIFSNWLLMYLSDKEVKNLAERMVKWLKVGGYIFFRESCFHQSGDCKRKYNPTHY 178
Cdd:PLN02336   81 HYKNVKFMCADVTSPDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQSGDSKRKNNPTHY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 179 REPRFYTKVFKECHMQDEGGDCYELSLVGYKCIGAYARNKKNQNQvlnhlyfvssfansqalnqknqiclwvfqICWIWQ 258
Cdd:PLN02336  161 REPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQ-----------------------------ICWLWQ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 259 KQkSSNDDRGFQRFLDTVQYKCSGILRYERVFGPGFVSTGGIETTKEFVGKLDLKPGQRVLDVGCGIGGGDFYMAENFDV 338
Cdd:PLN02336  212 KV-SSTNDKGFQRFLDNVQYKSSGILRYERVFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDV 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 339 EVVGIDLSINMISLALERAIGLKCAVEFEVADCTKKVYPDNAFDVIYSRDTILHIQDKPALFRSFYKWVKPGGKILITDY 418
Cdd:PLN02336  291 HVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDY 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 419 CKSSGAPSPAFAEYIKQRGYDLHDVKSYGQMLEEAGFKDVVAEDRTDQFMSVLQRELDAVEKEKDAFIHDFSEEDYNDIV 498
Cdd:PLN02336  371 CRSPGTPSPEFAEYIKQRGYDLHDVQAYGQMLKDAGFDDVIAEDRTDQFLQVLQRELDAVEKEKDEFISDFSEEDYNDIV 450
                         490       500
                  ....*....|....*....|....
gi 1280981287 499 GGWKAKLERCWCGEQKWGLFIAHK 522
Cdd:PLN02336  451 GGWKAKLVRSSSGEQKWGLFIAKK 474
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
301-456 1.45e-30

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: 115.86  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 301 ETTKEFVGKLDLKPGQRVLDVGCGIGGGDFYMAENfDVEVVGIDLSINMISLALERAIGLKCAVEFEVADCTKKVYPDNA 380
Cdd:COG2226     9 DGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGS 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1280981287 381 FDVIYSRDTILHIQDKPALFRSFYKWVKPGGKILITDyckssgapspafaeyikqrgYDLHDVKSYGQMLEEAGFK 456
Cdd:COG2226    88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVD--------------------FSPPDLAELEELLAEAGFE 143
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
318-411 2.29e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 99.95  E-value: 2.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 318 VLDVGCGIGGGDFYMAENFDVEVVGIDLSINMISLALERAIGLKCAVEFEVADCTKKVYPDNAFDVIYSRDTILHI--QD 395
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdPD 80
                          90
                  ....*....|....*.
gi 1280981287 396 KPALFRSFYKWVKPGG 411
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
317-418 2.11e-15

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: 72.08  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 317 RVLDVGCGIGGGDFYMAENFDVEVVGIDLSINMISLALERAIGLKCA-VEFEVADCTK-KVYPDNAFDVIYSRDTILHI- 393
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEElPPEADESFDVIISDPPLHHLv 80
                          90       100
                  ....*....|....*....|....*
gi 1280981287 394 QDKPALFRSFYKWVKPGGKILITDY 418
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLTLV 105
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
316-478 2.79e-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: 63.46  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 316 QRVLDVGCGIGGGDFYMAENF-DVEVVGIDLSINMISLALERaigLKCAVEFEVADCTKKVYPDNAFDVIYSRDTILHIQ 394
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTK---LSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 395 DKPALFRSFYKWVKPGGKILITDYCKSSgapspaFAEY---IKQRGYDLHDVKSYGQMLEEAgFKDVVAEDR--TDQFMS 469
Cdd:TIGR02072 113 DLSQALSELARVLKPGGLLAFSTFGPGT------LHELrqsFGQHGLRYLSLDELKALLKNS-FELLTLEEEliTLSFDD 185
                         170
                  ....*....|.
gi 1280981287 470 VLQ--RELDAV 478
Cdd:TIGR02072 186 PLDvlRHLKKT 196
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
317-491 2.00e-08

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 54.73  E-value: 2.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  317 RVLDVGCGIGGGDFYMAENF-DVEVVGIDLSINMISLALER--AIGLKCAVEFEVADCTKKVYPDNaFDVIYSRDTILHI 393
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHpHLQLHGYTISPEQAEVGRERirALGLQGRIRIFYRDSAKDPFPDT-YDLVFGFEVIHHI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  394 QDKPALFRSFYKWVKPGGKILITDYCKSSGAP---------SPAFAEYIKQ---RGYDLHDVKSYGQ----MLEEAGFkd 457
Cdd:smart00828  81 KDKMDLFSNISRHLKDGGHLVLADFIANLLSAieheettsyLVTREEWAELlarNNLRVVEGVDASLeianFLYDPGF-- 158
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1280981287  458 vvaedrTDQFMSVLQRELDAVEKEKDAFIHDFSE 491
Cdd:smart00828 159 ------EDNLERLYQDDLDEVTKRHFRGIANLGK 186
 
Name Accession Description Interval E-value
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
19-522 0e+00

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 971.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  19 MEHSAGLTLEGMLLDSNASDLDKEERPEVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAGQVIALDFIEGVIKKNESING 98
Cdd:PLN02336    1 KEHSVDLTVEAMMLDSKASDLDKEERPEILSLLPPYEGKSVLELGAGIGRFTGELAKKAGQVIALDFIESVIKKNESING 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  99 HHKNVKFMCADVTSPELKVSENSVDLIFSNWLLMYLSDKEVKNLAERMVKWLKVGGYIFFRESCFHQSGDCKRKYNPTHY 178
Cdd:PLN02336   81 HYKNVKFMCADVTSPDLNISDGSVDLIFSNWLLMYLSDKEVENLAERMVKWLKVGGYIFFRESCFHQSGDSKRKNNPTHY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 179 REPRFYTKVFKECHMQDEGGDCYELSLVGYKCIGAYARNKKNQNQvlnhlyfvssfansqalnqknqiclwvfqICWIWQ 258
Cdd:PLN02336  161 REPRFYTKVFKECHTRDEDGNSFELSLVGCKCIGAYVKNKKNQNQ-----------------------------ICWLWQ 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 259 KQkSSNDDRGFQRFLDTVQYKCSGILRYERVFGPGFVSTGGIETTKEFVGKLDLKPGQRVLDVGCGIGGGDFYMAENFDV 338
Cdd:PLN02336  212 KV-SSTNDKGFQRFLDNVQYKSSGILRYERVFGEGFVSTGGLETTKEFVDKLDLKPGQKVLDVGCGIGGGDFYMAENFDV 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 339 EVVGIDLSINMISLALERAIGLKCAVEFEVADCTKKVYPDNAFDVIYSRDTILHIQDKPALFRSFYKWVKPGGKILITDY 418
Cdd:PLN02336  291 HVVGIDLSVNMISFALERAIGRKCSVEFEVADCTKKTYPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDY 370
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 419 CKSSGAPSPAFAEYIKQRGYDLHDVKSYGQMLEEAGFKDVVAEDRTDQFMSVLQRELDAVEKEKDAFIHDFSEEDYNDIV 498
Cdd:PLN02336  371 CRSPGTPSPEFAEYIKQRGYDLHDVQAYGQMLKDAGFDDVIAEDRTDQFLQVLQRELDAVEKEKDEFISDFSEEDYNDIV 450
                         490       500
                  ....*....|....*....|....
gi 1280981287 499 GGWKAKLERCWCGEQKWGLFIAHK 522
Cdd:PLN02336  451 GGWKAKLVRSSSGEQKWGLFIAKK 474
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
271-522 1.36e-66

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 215.99  E-value: 1.36e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 271 RFLDTVQYKCSGILRYERVFGPGFVSTGGIETTKEFVGKLDLKPGQRVLDVGCGIGGGDFYMAENFDVEVVGIDLSINMI 350
Cdd:PTZ00098    9 TYLENNQYSDEGIKAYEFIFGEDYISSGGIEATTKILSDIELNENSKVLDIGSGLGGGCKYINEKYGAHVHGVDICEKMV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 351 SLALERAIGlKCAVEFEVADCTKKVYPDNAFDVIYSRDTILHI--QDKPALFRSFYKWVKPGGKILITDYCKSSGAP-SP 427
Cdd:PTZ00098   89 NIAKLRNSD-KNKIEFEANDILKKDFPENTFDMIYSRDAILHLsyADKKKLFEKCYKWLKPNGILLITDYCADKIENwDE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 428 AFAEYIKQRGYDLHDVKSYGQMLEEAGFKDVVAEDRTDQFMSVLQRELDAVEKEKDAFIHDFSEEDYNDIVGGWKAKLER 507
Cdd:PTZ00098  168 EFKAYIKKRKYTLIPIQEYGDLIKSCNFQNVVAKDISDYWLELLQVELKKLEEKKEEFLKLYSEKEYNSLKDGWTRKIKD 247
                         250
                  ....*....|....*
gi 1280981287 508 CWCGEQKWGLFIAHK 522
Cdd:PTZ00098  248 TKRKLQKWGYFKAQK 262
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
301-456 1.45e-30

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: 115.86  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 301 ETTKEFVGKLDLKPGQRVLDVGCGIGGGDFYMAENfDVEVVGIDLSINMISLALERAIGLKCAVEFEVADCTKKVYPDNA 380
Cdd:COG2226     9 DGREALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPDGS 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1280981287 381 FDVIYSRDTILHIQDKPALFRSFYKWVKPGGKILITDyckssgapspafaeyikqrgYDLHDVKSYGQMLEEAGFK 456
Cdd:COG2226    88 FDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVD--------------------FSPPDLAELEELLAEAGFE 143
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
263-417 1.64e-30

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 116.18  E-value: 1.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 263 SNDDrgFQRFLD-TVQYKCSGILRYERVFGPGfvstgGIETTKEFVGKLDLKPGQRVLDVGCGIGGGDFYMAENFDVEVV 341
Cdd:COG2230     6 GNDF--YRLFLDpTMTYSCAYFEDPDDTLEEA-----QEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 342 GIDLSINMISLALERA--IGLKCAVEFEVADCTkKVYPDNAFDVIYSRDTILHIQDK--PALFRSFYKWVKPGGKILITD 417
Cdd:COG2230    79 GVTLSPEQLEYARERAaeAGLADRVEVRLADYR-DLPADGQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
318-411 2.29e-25

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 99.95  E-value: 2.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 318 VLDVGCGIGGGDFYMAENFDVEVVGIDLSINMISLALERAIGLKCAVEFEVADCTKKVYPDNAFDVIYSRDTILHI--QD 395
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLpdPD 80
                          90
                  ....*....|....*.
gi 1280981287 396 KPALFRSFYKWVKPGG 411
Cdd:pfam13649  81 LEAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
305-418 4.74e-25

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: 100.09  E-value: 4.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 305 EFVGKLdLKPGQRVLDVGCGIGGGDFYMAENFdVEVVGIDLSINMISLALERAIGLKcaVEFEVADCTKKVYPDNAFDVI 384
Cdd:COG2227    16 ALLARL-LPAGGRVLDVGCGTGRLALALARRG-ADVTGVDISPEALEIARERAAELN--VDFVQGDLEDLPLEDGSFDLV 91
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1280981287 385 YSRDTILHIQDKPALFRSFYKWVKPGGKILITDY 418
Cdd:COG2227    92 ICSEVLEHLPDPAALLRELARLLKPGGLLLLSTP 125
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
314-417 1.46e-21

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 89.11  E-value: 1.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 314 PGQRVLDVGCGIGGGDFYMAENF-DVEVVGIDLSINMISLALERAIGlkcaVEFEVADCTKkVYPDNAFDVIYSRDTILH 392
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFpGARVTGVDLSPEMLARARARLPN----VRFVVADLRD-LDPPEPFDLVVSNAALHW 75
                          90       100
                  ....*....|....*....|....*
gi 1280981287 393 IQDKPALFRSFYKWVKPGGKILITD 417
Cdd:COG4106    76 LPDHAALLARLAAALAPGGVLAVQV 100
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
319-415 3.21e-21

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 88.11  E-value: 3.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 319 LDVGCGIGGGDFYMAENFdVEVVGIDLSINMISLALERAIGLKcaVEFEVADCTKKVYPDNAFDVIYSRDTILHIQDKPA 398
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG-ARVTGVDISPEMLELAREKAPREG--LTFVVGDAEDLPFPDNSFDLVLSSEVLHHVEDPER 77
                          90
                  ....*....|....*..
gi 1280981287 399 LFRSFYKWVKPGGKILI 415
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
PRK08317 PRK08317
hypothetical protein; Provisional
299-417 5.46e-21

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 91.92  E-value: 5.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 299 GIETTKEFV-GKLDLKPGQRVLDVGCGIGGGDFYMAENF--DVEVVGIDLSINMISLALERAIGLKCAVEFEVADCTKKV 375
Cdd:PRK08317    3 DFRRYRARTfELLAVQPGDRVLDVGCGPGNDARELARRVgpEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLP 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1280981287 376 YPDNAFDVIYSRDTILHIQDKPALFRSFYKWVKPGGKILITD 417
Cdd:PRK08317   83 FPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLD 124
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
310-458 1.27e-20

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 88.64  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 310 LDLKPGQRVLDVGCGIGggdfYMAENFD---VEVVGIDLSINMISLALEraiglkcAVEFEVADCTKKVYPDNAFDVIYS 386
Cdd:pfam13489  18 PKLPSPGRVLDFGCGTG----IFLRLLRaqgFSVTGVDPSPIAIERALL-------NVRFDQFDEQEAAVPAGKFDVIVA 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1280981287 387 RDTILHIQDKPALFRSFYKWVKPGGKILITDYCKSSGAPSPA-FAEYIKQRG--YDLHDVKSYGQMLEEAGFKDV 458
Cdd:pfam13489  87 REVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDEADRLLlEWPYLRPRNghISLFSARSLKRLLEEAGFEVV 161
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
304-455 1.98e-20

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 88.90  E-value: 1.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 304 KEFVGKLDLKPGQRVLDVGCGIGGGDFYMAENFDvEVVGIDLSINMISLALERAIGlkcaVEFEVADCTKKVYPDNAFDV 383
Cdd:COG4976    36 EELLARLPPGPFGRVLDLGCGTGLLGEALRPRGY-RLTGVDLSEEMLAKAREKGVY----DRLLVADLADLAEPDGRFDL 110
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1280981287 384 IYSRDTILHIQDKPALFRSFYKWVKPGGKILITdyckssgapspafAEYIKQRGYDLHDVKSYGQMLEEAGF 455
Cdd:COG4976   111 IVAADVLTYLGDLAAVFAGVARALKPGGLFIFS-------------VEDADGSGRYAHSLDYVRDLLAAAGF 169
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
33-160 2.69e-20

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: 87.36  E-value: 2.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  33 DSNASDLDkeERPEVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAGQVIALDFIEGVIKK-NESINGHHKNVKFMCADVT 111
Cdd:COG2226     2 DRVAARYD--GREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELaRERAAEAGLNVEFVVGDAE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1280981287 112 spELKVSENSVDLIFSNWLLMYLSDKEvKNLAErMVKWLKVGGYIFFRE 160
Cdd:COG2226    80 --DLPFPDGSFDLVISSFVLHHLPDPE-RALAE-IARVLKPGGRLVVVD 124
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
312-454 2.69e-19

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 84.78  E-value: 2.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 312 LKPGQRVLDVGCGIGGGDFYMAE--NFDVEVVGIDLSINMISLALERAIGLKCA-VEFEVADCTK--KVYPDNAFDVIYS 386
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEElpELLEDDKFDVVIS 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 387 RDTILHIQDKPALFRSFYKWVKPGGKILITDYCKSSGAPSPAFAE--YIKQRGYDLHDVKSYGQMLEEAG 454
Cdd:pfam13847  81 NCVLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELPAHVKEDstYYAGCVGGAILKKKLYELLEEAG 150
PLN02244 PLN02244
tocopherol O-methyltransferase
300-462 2.71e-19

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 89.03  E-value: 2.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 300 IETTKEFVG--KLDLKPGQRVLDVGCGIGGGDFYMAENFDVEVVGIDLSINMISLA--LERAIGLKCAVEFEVADCTKKV 375
Cdd:PLN02244  102 IEESLAWAGvpDDDEKRPKRIVDVGCGIGGSSRYLARKYGANVKGITLSPVQAARAnaLAAAQGLSDKVSFQVADALNQP 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 376 YPDNAFDVIYSRDTILHIQDKPALFRSFYKWVKPGGKILITDYCKSSGAPS-----PAFAEYIKQ--RGYDLHD---VKS 445
Cdd:PLN02244  182 FEDGQFDLVWSMESGEHMPDKRKFVQELARVAAPGGRIIIVTWCHRDLEPGetslkPDEQKLLDKicAAYYLPAwcsTSD 261
                         170
                  ....*....|....*..
gi 1280981287 446 YGQMLEEAGFKDVVAED 462
Cdd:PLN02244  262 YVKLAESLGLQDIKTED 278
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
311-418 3.56e-19

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 85.74  E-value: 3.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 311 DLKPGQRVLDVGCGIGGGDFYMAENFDVEVVGIDLSINMISLALERAIGLKCA-VEFEVADCTK-KVYPDNAFDVIYSRD 388
Cdd:COG0500    23 RLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAElDPLPAESFDLVVAFG 102
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1280981287 389 TILHIQDKP--ALFRSFYKWVKPGGKILITDY 418
Cdd:COG0500   103 VLHHLPPEEreALLRELARALKPGGVLLLSAS 134
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
59-154 4.99e-18

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 79.14  E-value: 4.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  59 VLELGAGIGRFTGDLAEKAG-QVIALDFIEGVIKK-NESINGHHKNVKFMCADVTspELKVSENSVDLIFSNWLLMYLSD 136
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGaRVTGVDLSPEMLERaRERAAEAGLNVEFVQGDAE--DLPFPDGSFDLVVSSGVLHHLPD 78
                          90
                  ....*....|....*...
gi 1280981287 137 KEVKNLAERMVKWLKVGG 154
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
319-413 2.91e-16

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 74.33  E-value: 2.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 319 LDVGCGIGGGDFYMAENF-DVEVVGIDLSINMISLALER--AIGLKCAVEFEVADCTKKVYPDNAFDVIYSRDTILHIQD 395
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERlaALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80
                          90
                  ....*....|....*...
gi 1280981287 396 KPALFRSFYKWVKPGGKI 413
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
308-495 1.49e-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: 76.98  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 308 GKLDLKPGQRVLDVGCGIGGGDFYMAENFDVEVVGIDLSINMISLALER--AIGLKCAVEFEVADctkkvYPD--NAFDV 383
Cdd:pfam02353  55 DKLGLKPGMTLLDIGCGWGGLMRRAAERYDVNVVGLTLSKNQYKLARKRvaAEGLARKVEVLLQD-----YRDfdEPFDR 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 384 IYSRDTILHIQDK--PALFRSFYKWVKPGGKILI-------TDYCKSSGAPSPAFAEYIKQRGY--DLHDVKSYGQmleE 452
Cdd:pfam02353 130 IVSVGMFEHVGHEnyDTFFKKLYNLLPPGGLMLLhtitglhPDETSERGLPLKFIDKYIFPGGElpSISMIVESSS---E 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1280981287 453 AGFKDVVAEDRTDQFMSVLQRELDAVEKEKDAFIHDFSEEDYN 495
Cdd:pfam02353 207 AGFTVEDVESLRPHYAKTLDLWAENLQANKDEAIALQSEEFYR 249
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
60-158 1.99e-15

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.54  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  60 LELGAGIGRFTGDLAEKAGQVIALDFIEGVIKKNESiNGHHKNVKFMCADVTspELKVSENSVDLIFSNWLLMYLSDKEv 139
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELARE-KAPREGLTFVVGDAE--DLPFPDNSFDLVLSSEVLHHVEDPE- 76
                          90
                  ....*....|....*....
gi 1280981287 140 KNLAErMVKWLKVGGYIFF 158
Cdd:pfam08241  77 RALRE-IARVLKPGGILII 94
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
317-418 2.11e-15

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: 72.08  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 317 RVLDVGCGIGGGDFYMAENFDVEVVGIDLSINMISLALERAIGLKCA-VEFEVADCTK-KVYPDNAFDVIYSRDTILHI- 393
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADnVEVLKGDAEElPPEADESFDVIISDPPLHHLv 80
                          90       100
                  ....*....|....*....|....*
gi 1280981287 394 QDKPALFRSFYKWVKPGGKILITDY 418
Cdd:cd02440    81 EDLARFLEEARRLLKPGGVLVLTLV 105
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
304-458 1.29e-14

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 73.26  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 304 KEFVGKLDLKPGQRVLDVGCGIggGD--FYMAENFDV--EVVGIDLSINMISLALERAIGLKCA--VEFEVADCTKKVYP 377
Cdd:PRK00216   41 RKTIKWLGVRPGDKVLDLACGT--GDlaIALAKAVGKtgEVVGLDFSEGMLAVGREKLRDLGLSgnVEFVQGDAEALPFP 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 378 DNAFDVIysrdTI---L-HIQDKPALFRSFYKWVKPGGKILITDYCKSSGAPspafaeyIKQrGYDLH------------ 441
Cdd:PRK00216  119 DNSFDAV----TIafgLrNVPDIDKALREMYRVLKPGGRLVILEFSKPTNPP-------LKK-AYDFYlfkvlpligkli 186
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1280981287 442 --DVKSY----------------GQMLEEAGFKDV 458
Cdd:PRK00216  187 skNAEAYsylaesirafpdqeelAAMLEEAGFERV 221
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
44-158 1.34e-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: 70.43  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  44 RPEVLSLLPPH--EGKSVLELGAGIGRFTGDLAEKAGQVIALDFIEGVIKKNESiNGHHKNVKFMCADVTspELKVSENS 121
Cdd:COG2227    11 DRRLAALLARLlpAGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARE-RAAELNVDFVQGDLE--DLPLEDGS 87
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1280981287 122 VDLIFSNWLLMYLSDkeVKNLAERMVKWLKVGGYIFF 158
Cdd:COG2227    88 FDLVICSEVLEHLPD--PAALLRELARLLKPGGLLLL 122
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
309-386 4.32e-14

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 73.73  E-value: 4.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 309 KLDLKPGQRVLDVGCGIGGGDFYMAENFDVEVVGIDLSINMISLALERAIGLkcAVEFEVADctkkvYPD--NAFDVIYS 386
Cdd:PRK11705  162 KLQLKPGMRVLDIGCGWGGLARYAAEHYGVSVVGVTISAEQQKLAQERCAGL--PVEIRLQD-----YRDlnGQFDRIVS 234
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
55-158 2.61e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 66.00  E-value: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  55 EGKSVLELGAGIGRFTGDLAEK--AGQVIALDFIEGVIkknESINGHHKNVKFMCADVTSPELkvsENSVDLIFSNWLLM 132
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEML---ARARARLPNVRFVVADLRDLDP---PEPFDLVVSNAALH 74
                          90       100
                  ....*....|....*....|....*.
gi 1280981287 133 YLSDKEVknLAERMVKWLKVGGYIFF 158
Cdd:COG4106    75 WLPDHAA--LLARLAAALAPGGVLAV 98
arsM PRK11873
arsenite methyltransferase;
312-464 4.21e-12

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 66.51  E-value: 4.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 312 LKPGQRVLDVGCGIGggdfymaenFDV-----------EVVGIDLSINMISLALERAIGLKCA-VEFEVADCTKKVYPDN 379
Cdd:PRK11873   75 LKPGETVLDLGSGGG---------FDCflaarrvgptgKVIGVDMTPEMLAKARANARKAGYTnVEFRLGEIEALPVADN 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 380 AFDVIYSRDTILHIQDKPALFRSFYKWVKPGGKILITDYCksSGAPSPafaEYIKQRGyDLH--------DVKSYGQMLE 451
Cdd:PRK11873  146 SVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFAISDVV--LRGELP---EEIRNDA-ELYagcvagalQEEEYLAMLA 219
                         170
                  ....*....|....
gi 1280981287 452 EAGFKDV-VAEDRT 464
Cdd:PRK11873  220 EAGFVDItIQPKRE 233
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
304-464 1.15e-11

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 64.38  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 304 KEFVGKLD-LKPGQRVLDVGCGIGGGDFYMAENFDV--EVVGIDLSINMISLALERAI-GLKCAVEFEVADCTKKVYPDN 379
Cdd:pfam01209  31 KDFTMKCMgVKRGNKFLDVAGGTGDWTFGLSDSAGSsgKVVGLDINENMLKEGEKKAKeEGKYNIEFLQGNAEELPFEDD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 380 AFDVIYSRDTILHIQDKPALFRSFYKWVKPGGKILITDYCKSSGAP-SPAFAEYIKQ-------------RGY------- 438
Cdd:pfam01209 111 SFDIVTISFGLRNFPDYLKVLKEAFRVLKPGGRVVCLEFSKPENPLlSQAYELYFKYvmpfmgkmfaksyKSYqylqesi 190
                         170       180
                  ....*....|....*....|....*..
gi 1280981287 439 -DLHDVKSYGQMLEEAGFKDVVAEDRT 464
Cdd:pfam01209 191 rDFPDQKTLASMFEKAGFKSVGYESLT 217
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
316-478 2.79e-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: 63.46  E-value: 2.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 316 QRVLDVGCGIGGGDFYMAENF-DVEVVGIDLSINMISLALERaigLKCAVEFEVADCTKKVYPDNAFDVIYSRDTILHIQ 394
Cdd:TIGR02072  36 ASVLDIGCGTGYLTRALLKRFpQAEFIALDISAGMLAQAKTK---LSENVQFICGDAEKLPLEDSSFDLIVSNLALQWCD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 395 DKPALFRSFYKWVKPGGKILITDYCKSSgapspaFAEY---IKQRGYDLHDVKSYGQMLEEAgFKDVVAEDR--TDQFMS 469
Cdd:TIGR02072 113 DLSQALSELARVLKPGGLLAFSTFGPGT------LHELrqsFGQHGLRYLSLDELKALLKNS-FELLTLEEEliTLSFDD 185
                         170
                  ....*....|.
gi 1280981287 470 VLQ--RELDAV 478
Cdd:TIGR02072 186 PLDvlRHLKKT 196
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
53-165 3.75e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 61.28  E-value: 3.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  53 PHEGKSVLELGAGIGRFTGDLAEKAG---QVIALDFIEGVIKKNESINGHH--KNVKFMCADVTSPELKVSENSVDLIFS 127
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGpnaEVVGIDISEEAIEKARENAQKLgfDNVEFEQGDIEELPELLEDDKFDVVIS 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1280981287 128 NWLLMYLSDKeVKNLaERMVKWLKVGGYIFFRESCFHQ 165
Cdd:pfam13847  81 NCVLNHIPDP-DKVL-QEILRVLKPGGRLIISDPDSLA 116
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
59-158 7.77e-11

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: 58.98  E-value: 7.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  59 VLELGAGIGRFTGDLAE-KAGQVIALDFIEGVIKKNESI--NGHHKNVKFMCADVTSPeLKVSENSVDLIFSNWLLMYLS 135
Cdd:cd02440     2 VLDLGCGTGALALALASgPGARVTGVDISPVALELARKAaaALLADNVEVLKGDAEEL-PPEADESFDVIISDPPLHHLV 80
                          90       100
                  ....*....|....*....|...
gi 1280981287 136 DkEVKNLAERMVKWLKVGGYIFF 158
Cdd:cd02440    81 E-DLARFLEEARRLLKPGGVLVL 102
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
28-158 8.34e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 61.17  E-value: 8.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  28 EGMLLDSNASDLDKEERPEVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAGQVIALDFIEGVIKKNESINGHhknVKFMC 107
Cdd:COG4976    19 DAALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREKGVY---DRLLV 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1280981287 108 ADVTspELKVSENSVDLIFSNWLLMYLSDkeVKNLAERMVKWLKVGGYIFF 158
Cdd:COG4976    96 ADLA--DLAEPDGRFDLIVAADVLTYLGD--LAAVFAGVARALKPGGLFIF 142
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
37-158 5.68e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 59.16  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  37 SDLDKEERPEVLSLLPPHE----GKSVLELGAGIGRFTGDLAEKAG-QVIALDFIEGVI---KKNESINGHHkNVKFMCA 108
Cdd:COG0500     4 SYYSDELLPGLAALLALLErlpkGGRVLDLGCGTGRNLLALAARFGgRVIGIDLSPEAIalaRARAAKAGLG-NVEFLVA 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1280981287 109 DVTSPElKVSENSVDLIFSNWLLMYLSDKEVKNLAERMVKWLKVGGYIFF 158
Cdd:COG0500    83 DLAELD-PLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLL 131
PRK08317 PRK08317
hypothetical protein; Provisional
44-156 2.26e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 58.02  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  44 RPEVLSLLPPHEGKSVLELGAGIGRFTGDLAE---KAGQVIALDFIEGVIK-KNESINGHHKNVKFMCADVTSpeLKVSE 119
Cdd:PRK08317    8 RARTFELLAVQPGDRVLDVGCGPGNDARELARrvgPEGRVVGIDRSEAMLAlAKERAAGLGPNVEFVRGDADG--LPFPD 85
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1280981287 120 NSVDLIFSNWLLMYLSDKEvKNLAErMVKWLKVGGYI 156
Cdd:PRK08317   86 GSFDAVRSDRVLQHLEDPA-RALAE-IARVLRPGGRV 120
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
48-158 1.72e-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: 55.37  E-value: 1.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  48 LSLLPPH---EGKSVLELGAGIGRFTGDLAEK--AGQVIALDFIEGVIKKNESINGhhKNVKFMCADVTspELKVSENSV 122
Cdd:TIGR02072  24 LALLKEKgifIPASVLDIGCGTGYLTRALLKRfpQAEFIALDISAGMLAQAKTKLS--ENVQFICGDAE--KLPLEDSSF 99
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1280981287 123 DLIFSNWLLMYLSDKE--VKNLAErmvkWLKVGGYIFF 158
Cdd:TIGR02072 100 DLIVSNLALQWCDDLSqaLSELAR----VLKPGGLLAF 133
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
317-491 2.00e-08

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 54.73  E-value: 2.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  317 RVLDVGCGIGGGDFYMAENF-DVEVVGIDLSINMISLALER--AIGLKCAVEFEVADCTKKVYPDNaFDVIYSRDTILHI 393
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHpHLQLHGYTISPEQAEVGRERirALGLQGRIRIFYRDSAKDPFPDT-YDLVFGFEVIHHI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  394 QDKPALFRSFYKWVKPGGKILITDYCKSSGAP---------SPAFAEYIKQ---RGYDLHDVKSYGQ----MLEEAGFkd 457
Cdd:smart00828  81 KDKMDLFSNISRHLKDGGHLVLADFIANLLSAieheettsyLVTREEWAELlarNNLRVVEGVDASLeianFLYDPGF-- 158
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1280981287  458 vvaedrTDQFMSVLQRELDAVEKEKDAFIHDFSE 491
Cdd:smart00828 159 ------EDNLERLYQDDLDEVTKRHFRGIANLGK 186
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
46-158 6.26e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 52.24  E-value: 6.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  46 EVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAG-QVIALDF----IEGVIKKNESInGHHKNVKFMCADVTSPELkvsEN 120
Cdd:COG2230    42 LILRKLGLKPGMRVLDIGCGWGGLALYLARRYGvRVTGVTLspeqLEYARERAAEA-GLADRVEVRLADYRDLPA---DG 117
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1280981287 121 SVDLIFSNWLLMYLSDKEVKNLAERMVKWLKVGGYIFF 158
Cdd:COG2230   118 QFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLL 155
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
312-443 1.88e-07

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: 51.10  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 312 LKPGQRVLDVGCGIGGgdfymaenFDVE-------VVGIDLSINMISLA---LERAigLKCAVEFEVADCTKKVYPDNAF 381
Cdd:COG1041    24 AKEGDTVLDPFCGTGT--------ILIEagllgrrVIGSDIDPKMVEGArenLEHY--GYEDADVIRGDARDLPLADESV 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1280981287 382 DVI-----------YSRDTILHIQDKpaLFRSFYKWVKPGGKILITdyckssgAPSPaFAEYIKQRGYDLHDV 443
Cdd:COG1041    94 DAIvtdppygrsskISGEELLELYEK--ALEEAARVLKPGGRVVIV-------TPRD-IDELLEEAGFKVLER 156
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
46-111 1.28e-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: 1.28e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1280981287  46 EVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAGQVIAldfIEGV---I---KKNESINGhHKNVKFMCADVT 111
Cdd:COG2265   224 AALEWLDLTGGERVLDLYCGVGTFALPLARRAKKVIG---VEIVpeaVedaRENARLNG-LKNVEFVAGDLE 291
PRK10258 PRK10258
biotin biosynthesis protein BioC; Provisional
310-422 1.31e-06

biotin biosynthesis protein BioC; Provisional


Pssm-ID: 182340 [Multi-domain]  Cd Length: 251  Bit Score: 49.76  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 310 LDLKPGQR---VLDVGCGIGGGDFYMAENfDVEVVGIDLSINMISLALERaiglKCAVEFEVADCTKKVYPDNAFDVIYS 386
Cdd:PRK10258   35 LAMLPQRKfthVLDAGCGPGWMSRYWRER-GSQVTALDLSPPMLAQARQK----DAADHYLAGDIESLPLATATFDLAWS 109
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1280981287 387 RDTILHIQDKPALFRSFYKWVKPGGKILITDYCKSS 422
Cdd:PRK10258  110 NLAVQWCGNLSTALRELYRVVRPGGVVAFTTLVQGS 145
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
289-415 1.50e-06

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


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 48.65  E-value: 1.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 289 VFGPGFVSTGgietTKEFVGKLDLKPGQRVLDVGCGIGG-GDFYMAENFDVEVVGIDLSINMISLALE--RAIGLKcAVE 365
Cdd:COG2813    28 VFSRDRLDIG----TRLLLEHLPEPLGGRVLDLGCGYGViGLALAKRNPEARVTLVDVNARAVELARAnaAANGLE-NVE 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 366 FEVADCTKKVyPDNAFDVIYS----------RDTILHiqdkpALFRSFYKWVKPGGKILI 415
Cdd:COG2813   103 VLWSDGLSGV-PDGSFDLILSnppfhagravDKEVAH-----ALIADAARHLRPGGELWL 156
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
313-455 1.96e-06

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 49.50  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 313 KPGQRVLDVGCGIGGGDFYMAENF--DVEVVGIDLSINMISLALERA-----IGLKCaVEFEVADCTKKVYPDNAFDVIY 385
Cdd:PLN02233   72 KMGDRVLDLCCGSGDLAFLLSEKVgsDGKVMGLDFSSEQLAVAASRQelkakSCYKN-IEWIEGDATDLPFDDCYFDAIT 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 386 SRDTILHIQDKPALFRSFYKWVKPGGKILITDYCKSSGAPSPAFAEYIKQR-------GYDLHDVKSY----------GQ 448
Cdd:PLN02233  151 MGYGLRNVVDRLKAMQEMYRVLKPGSRVSILDFNKSTQPFTTSMQEWMIDNvvvpvatGYGLAKEYEYlkssineyltGE 230
                         170
                  ....*....|.
gi 1280981287 449 MLE----EAGF 455
Cdd:PLN02233  231 ELEklalEAGF 241
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
303-456 3.03e-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: 48.44  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 303 TKEFVGKLDlkpGQRVLDVGCGIGGGDFYMAENfDVEVVGIDLSINMISLALERAIGLKCAVEFE---VADCTKKvyPDN 379
Cdd:TIGR01983  38 RKNFKNPLD---GLRVLDVGCGGGLLSEPLARL-GANVTGIDASEENIEVAKLHAKKDPLQIDYRcttVEDLAEK--KAG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 380 AFDVIYSRDTILHIQDKPALFRSFYKWVKPGGKILITDYCKS--SGAPSPAFAEYIKQ---RGydLHDVKSY------GQ 448
Cdd:TIGR01983 112 SFDVVTCMEVLEHVPDPQAFIRACAQLLKPGGILFFSTINRTpkSYLLAIVGAEYILRivpKG--THDWEKFikpselLS 189

                  ....*...
gi 1280981287 449 MLEEAGFK 456
Cdd:TIGR01983 190 WLESAGLR 197
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
60-156 4.02e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 45.44  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  60 LELGAGIGRFTGDLAEKA--GQVIALDFIEGVIKKNESINGHHKNVKFMCADVTSPEL-KVSENSVDLIFSNWLLMYLSD 136
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpgLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLgELDPGSFDVVVASNVLHHLAD 80
                          90       100
                  ....*....|....*....|
gi 1280981287 137 KEVknLAERMVKWLKVGGYI 156
Cdd:pfam08242  81 PRA--VLRNIRRLLKPGGVL 98
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
46-195 1.19e-05

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 46.89  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  46 EVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAG-QVIALDFIEGVIKKNESINGHHKNVKFMCADVTSPELkvSENSVDL 124
Cdd:PTZ00098   43 KILSDIELNENSKVLDIGSGLGGGCKYINEKYGaHVHGVDICEKMVNIAKLRNSDKNKIEFEANDILKKDF--PENTFDM 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 125 IFSNWLLMYLSDKEVKNLAERMVKWLKVGGYIFFRESCFHQSGDC---------KRKYNPTHYREprfYTKVFKECHMQD 195
Cdd:PTZ00098  121 IYSRDAILHLSYADKKKLFEKCYKWLKPNGILLITDYCADKIENWdeefkayikKRKYTLIPIQE---YGDLIKSCNFQN 197
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
311-386 3.70e-05

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: 45.14  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 311 DLKPGQRVLDVGCGIGGGDFYMAENF-DVEVVGIDLSINMISLALE--RAIGLKCAVEFEVADCT--KKVYPDNAFDVIY 385
Cdd:COG4123    34 PVKKGGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEAAELARRnvALNGLEDRITVIHGDLKefAAELPPGSFDLVV 113

                  .
gi 1280981287 386 S 386
Cdd:COG4123   114 S 114
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
55-128 5.71e-05

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 44.12  E-value: 5.71e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1280981287  55 EGKSVLELGAGIGRFT-GDLAEKAGQVIALD----FIEgVIKKNESinGHHKNVKFMCADVTSPELkvsENSVDLIFSN 128
Cdd:COG2263    45 EGKTVLDLGCGTGMLAiGAALLGAKKVVGVDidpeALE-IARENAE--RLGVRVDFIRADVTRIPL---GGSVDTVVMN 117
PRK06202 PRK06202
hypothetical protein; Provisional
317-401 6.74e-05

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 44.22  E-value: 6.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 317 RVLDVGCgiGGGDF-----YMAE--NFDVEVVGIDLSINMISLALERAIGLKCAVEFEVADCTkkVYPDNAFDVIYSrDT 389
Cdd:PRK06202   63 TLLDIGC--GGGDLaidlaRWARrdGLRLEVTAIDPDPRAVAFARANPRRPGVTFRQAVSDEL--VAEGERFDVVTS-NH 137
                          90
                  ....*....|..
gi 1280981287 390 ILHIQDKPALFR 401
Cdd:PRK06202  138 FLHHLDDAEVVR 149
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
310-384 1.39e-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: 44.01  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 310 LDLKPGQRVLDVGCGIGGgdF--YMAENFDvEVVGIDLSINMISLALE--RAIGLKcAVEFEVADCTK---KVYPDNAFD 382
Cdd:COG2265   229 LDLTGGERVLDLYCGVGT--FalPLARRAK-KVIGVEIVPEAVEDAREnaRLNGLK-NVEFVAGDLEEvlpELLWGGRPD 304

                  ..
gi 1280981287 383 VI 384
Cdd:COG2265   305 VV 306
PRK14968 PRK14968
putative methyltransferase; Provisional
310-384 1.49e-04

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.96  E-value: 1.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1280981287 310 LDLKPGQRVLDVGCGIGGGDFYMAENfDVEVVGIDLSINMISLALERAIGLKCA---VEFEVADCTKKVYpDNAFDVI 384
Cdd:PRK14968   19 AVDKKGDRVLEVGTGSGIVAIVAAKN-GKKVVGVDINPYAVECAKCNAKLNNIRnngVEVIRSDLFEPFR-GDKFDVI 94
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
314-441 1.54e-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: 42.95  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 314 PGQRVLDVGCGIGGGDFYMAENFDVEVVGIDLSinmiSLALErAIGLKCA-----VEFEVADCTKKVyPDNAFDVI---- 384
Cdd:COG3897    70 AGKRVLELGCGLGLVGIAAAKAGAADVTATDYD----PEALA-ALRLNAAlngvaITTRLGDWRDPP-AAGGFDLIlggd 143
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1280981287 385 --YSRDTILHIqdkPALFRSFykwVKPGGKILITDYckssG-APSPAFAEY-IKQRGYDLH 441
Cdd:COG3897   144 vlYERDLAEPL---LPFLDRL---AAPGGEVLIGDP----GrGYLPAFRERlEALAGYEVV 194
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
309-370 1.97e-04

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 42.90  E-value: 1.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1280981287 309 KLDLKPGQRVLDVGCGIGGGDFYMAENfDVEVVGIDLSINMISLALERA--IGLKCAVEFEVAD 370
Cdd:PRK07580   58 ADGDLTGLRILDAGCGVGSLSIPLARR-GAKVVASDISPQMVEEARERApeAGLAGNITFEVGD 120
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
312-390 1.98e-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: 42.44  E-value: 1.98e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1280981287 312 LKPGQRVLDVGCGIGGGDFYMAENFDVEVVGIDLSINMISLALERAIglkcAVEFEVADCTKKVYPDNAFDVIYSRDTI 390
Cdd:pfam07021  11 IPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAAGVAECVAKGL----YVIQGDLDEGLEHFPDKSFDYVILSQTL 85
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
312-417 2.36e-04

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: 42.09  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 312 LKPGQRVLDVGCGIGGGDFYMAENF--DVEVVGIDLSINMISLA---LERAiGLKCAVEFEVADCTK--KVYPDNAFDVI 384
Cdd:COG4122    14 LLGAKRILEIGTGTGYSTLWLARALpdDGRLTTIEIDPERAAIArenFARA-GLADRIRLILGDALEvlPRLADGPFDLV 92
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1280981287 385 YSrDTilhiqDK---PALFRSFYKWVKPGGkILITD 417
Cdd:COG4122    93 FI-DA-----DKsnyPDYLELALPLLRPGG-LIVAD 121
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
44-125 3.77e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 42.06  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  44 RPEVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAG---QVIALDFIEG---VIKKNESINGHHKNVKFMCADVTspELKV 117
Cdd:PRK00216   40 RRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGktgEVVGLDFSEGmlaVGREKLRDLGLSGNVEFVQGDAE--ALPF 117

                  ....*...
gi 1280981287 118 SENSVDLI 125
Cdd:PRK00216  118 PDNSFDAV 125
Methyltransf_PK pfam05891
AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron ...
15-160 3.78e-04

AdoMet dependent proline di-methyltransferase; This protein is expressed in the tail neuron PVT and in uterine cells in C. elegans [worm-base]. In Saccharomyces cerevisiae this is AdoMet dependent proline di-methyltransferase. This enzyme catalyzes the di-methylation of ribosomal proteins Rpl12 and Rps25 at N-terminal proline residues. The methyltransferases described here specifically recognize the N-terminal X-Pro-Lys sequence motif, and they may account for nearly all previously described eukaryotic protein N-terminal methylation reactions. A number of other yeast and human proteins also share the recognition motif and may be similarly modified. As with other methyltransferases, this family carries the characteriztic GxGxG motif.


Pssm-ID: 461771  Cd Length: 218  Bit Score: 41.98  E-value: 3.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  15 KKYWMEHSAglTLEGML--------LDSNASD-----LDKEERPEVlsllppHEGKSVLELGAGIGRFTGDLAEK-AGQV 80
Cdd:pfam05891  10 IDYWEGVSA--TVDGMLggyghvsdIDVNGSRnflrrLLRERLPGK------NRHLVALDCGAGIGRVTKNLLLPlFSKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  81 IALDFIEGVIKK--NESINGHHKNVKFMCADVT--SPElkvsENSVDLIFSNWLLMYLSDKEVKNLAERMVKWLKVGGYI 156
Cdd:pfam05891  82 DLVEPVEDFIEKakEYLAEGKKKVGNFFCVGLQdfTPE----EGRYDLIWIQWCIGHLTDEDLVAFLKRCKGGLKPNGFI 157

                  ....
gi 1280981287 157 FFRE 160
Cdd:pfam05891 158 VVKE 161
PRK06922 PRK06922
class I SAM-dependent methyltransferase;
310-417 4.55e-04

class I SAM-dependent methyltransferase;


Pssm-ID: 180751 [Multi-domain]  Cd Length: 677  Bit Score: 42.93  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 310 LDLKPGQRVLDVGCGigGG---DFYMAENFDVEVVGIDLSINMISlALER---------------AIGLKCAVEFEVADC 371
Cdd:PRK06922  414 LDYIKGDTIVDVGAG--GGvmlDMIEEETEDKRIYGIDISENVID-TLKKkkqnegrswnvikgdAINLSSSFEKESVDT 490
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 372 tkkvypdnafdVIYSrdTILH-----IQDKPALF---------RSFYKWVKPGGKILITD 417
Cdd:PRK06922  491 -----------IVYS--SILHelfsyIEYEGKKFnhevikkglQSAYEVLKPGGRIIIRD 537
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
368-446 4.95e-04

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 41.01  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 368 VADCTKKV-YPDNAFDVIYSRDTILHIQDK--PALFRSFYKWVKPGGKILIT--D---YCKSSGAPSPAFAEYIKQRGYD 439
Cdd:COG4627    33 VGDLTDPLpFPDNSVDAIYSSHVLEHLDYEeaPLALKECYRVLKPGGILRIVvpDlehVARLYLAEYDAALDVAELRLAG 112

                  ....*..
gi 1280981287 440 LHDVKSY 446
Cdd:COG4627   113 PIDPLGI 119
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
54-157 5.99e-04

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 41.56  E-value: 5.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  54 HEGKSVLELGAGIGRFTGdLAEKAG--QVIALD---FIEGVIKKNESINGHHKNVKFMCADVTSPELK------VSEnsv 122
Cdd:COG4076    34 KPGDVVLDIGTGSGLLSM-LAARAGakKVYAVEvnpDIAAVARRIIAANGLSDRITVINADATDLDLPekadviISE--- 109
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1280981287 123 dlIFSNWLlmyLSDKEVKNLAERMVKWLKVGGYIF 157
Cdd:COG4076   110 --MLDTAL---LDEGQVPILNHARKRLLKPGGRII 139
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
312-411 6.25e-04

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 41.47  E-value: 6.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 312 LKPGQRVLDVGCGIGGGDFYMAENF-DVEVVGIDLSINMISLALERAIGlkcaVEFEVADCTKKVyPDNAFDVIYSRDTI 390
Cdd:PRK01683   29 LENPRYVVDLGCGPGNSTELLVERWpAARITGIDSSPAMLAEARSRLPD----CQFVEADIASWQ-PPQALDLIFANASL 103
                          90       100
                  ....*....|....*....|.
gi 1280981287 391 LHIQDKPALFRSFYKWVKPGG 411
Cdd:PRK01683  104 QWLPDHLELFPRLVSLLAPGG 124
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
292-415 7.12e-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: 40.65  E-value: 7.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 292 PGFVSTGGIET-TKEFVGKLDLKPGQRVLDVGCGIGG-GDFYMAENFDVEVVGIDlsINMISLALER----AIGLKcAVE 365
Cdd:pfam05175   8 PGVFSHGRLDIgSRLLLEHLPKDLSGKVLDLGCGAGVlGAALAKESPDAELTMVD--INARALESARenlaANGLE-NGE 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1280981287 366 FEVADCTKKVyPDNAFDVIYS-------RDTILHIQDkpALFRSFYKWVKPGGKILI 415
Cdd:pfam05175  85 VVASDVYSGV-EDGKFDLIISnppfhagLATTYNVAQ--RFIADAKRHLRPGGELWI 138
arsM PRK11873
arsenite methyltransferase;
54-154 8.03e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 41.47  E-value: 8.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  54 HEGKSVLELGAGIGrFTGDLAEKA----GQVIALDFIEGVI---KKNESINGHhKNVKFMCADVTspELKVSENSVDLIF 126
Cdd:PRK11873   76 KPGETVLDLGSGGG-FDCFLAARRvgptGKVIGVDMTPEMLakaRANARKAGY-TNVEFRLGEIE--ALPVADNSVDVII 151
                          90       100
                  ....*....|....*....|....*...
gi 1280981287 127 SNWLLMYLSDKEvKNLAErMVKWLKVGG 154
Cdd:PRK11873  152 SNCVINLSPDKE-RVFKE-AFRVLKPGG 177
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
52-128 1.40e-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: 40.51  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  52 PPHEGKSVLELGAGIG--------RFtgdlaeKAGQVIALDFIEGVI---KKNESINGHHKNVKFMCADVTSPELKVSEN 120
Cdd:COG4123    34 PVKKGGRVLDLGTGTGvialmlaqRS------PGARITGVEIQPEAAelaRRNVALNGLEDRITVIHGDLKEFAAELPPG 107

                  ....*...
gi 1280981287 121 SVDLIFSN 128
Cdd:COG4123   108 SFDLVVSN 115
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
310-385 1.89e-03

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 39.69  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 310 LDLKPGQRVLDVGCGIGggdfY----MAENFDvEVVGIDLSINMISLALER--AIGLKcAVEFEVADCTkKVYPDNA-FD 382
Cdd:COG2518    62 LDLKPGDRVLEIGTGSG----YqaavLARLAG-RVYSVERDPELAERARERlaALGYD-NVTVRVGDGA-LGWPEHApFD 134

                  ...
gi 1280981287 383 VIY 385
Cdd:COG2518   135 RII 137
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
31-147 2.25e-03

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: 40.11  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  31 LLDSNAsdLDKeerpeVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAGQVIA--LDfiEGVIKKNESINGHHKNVKFMCA 108
Cdd:COG0030    20 LIDPNI--IRR-----IVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAveID--RRLAAILRETFAAYPNLTVIEG 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1280981287 109 DVtspeLKVSENSVDL-----IFSN-----------WLLMYLSD---------KEVknlAERMV 147
Cdd:COG0030    91 DA----LKVDLPALAAgeplkVVGNlpynistpilfKLLEARPPiedavlmvqKEV---AERLV 147
rADc smart00650
Ribosomal RNA adenine dimethylases;
46-147 2.27e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 39.03  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287   46 EVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAGQVIAL----DFIEGVIKKNEsingHHKNVK-----FMCADVTS-PEL 115
Cdd:smart00650   4 KIVRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIeidpRLAPRLREKFA----AADNLTvihgdALKFDLPKlQPY 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1280981287  116 KVSEN-----SVDLIFsnWLL--------MYL-SDKEVknlAERMV 147
Cdd:smart00650  80 KVVGNlpyniSTPILF--KLLeeppafrdAVLmVQKEV---ARRLA 120
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
305-413 2.68e-03

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 39.67  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 305 EFVGKLDLKPGQRVLDVGCGIGGGDFYMAENF-DVEVVGIDLSINMISLALERAIGlkcAVEFEVADCTkkvyPDNAFDV 383
Cdd:PRK14103   20 DLLARVGAERARRVVDLGCGPGNLTRYLARRWpGAVIEALDSSPEMVAAARERGVD---ARTGDVRDWK----PKPDTDV 92
                          90       100       110
                  ....*....|....*....|....*....|
gi 1280981287 384 IYSRDTILHIQDKPALFRSFYKWVKPGGKI 413
Cdd:PRK14103   93 VVSNAALQWVPEHADLLVRWVDELAPGSWI 122
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
330-415 3.83e-03

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: 39.19  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  330 FYMAENFDVEVVGIDLSINMISLA-----LERAIG-----------------------LKCAVEFEVADCTKKVYPDNAF 381
Cdd:smart00138 125 LPKGREPDVKILATDIDLKALEKAragiyPERELEdlpkallaryfkevedkyrvkpeLKERVRFAKHNLLAESPPLGDF 204
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1280981287  382 DVIYSRDTILHI--QDKPALFRSFYKWVKPGGKILI 415
Cdd:smart00138 205 DLIFCRNVLIYFdePTQRKLLNRFAEALKPGGYLFL 240
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
314-391 4.57e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 38.35  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 314 PGQRVLDVGCGIG----GGDFYMAEnfdvEVVGIDLSINMISLALERAIGLKCAVEFEVADCTKkvypdnaFDVIYSRDT 389
Cdd:COG2263    45 EGKTVLDLGCGTGmlaiGAALLGAK----KVVGVDIDPEALEIARENAERLGVRVDFIRADVTR-------IPLGGSVDT 113

                  ..
gi 1280981287 390 IL 391
Cdd:COG2263   114 VV 115
rumA PRK13168
23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;
310-370 4.59e-03

23S rRNA (uracil(1939)-C(5))-methyltransferase RlmD;


Pssm-ID: 237291 [Multi-domain]  Cd Length: 443  Bit Score: 39.37  E-value: 4.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 310 LDLKPGQRVLDVGCGIGggdfymaeNFDV-------EVVGIDLSINMISLALERAI--GLKcAVEFEVAD 370
Cdd:PRK13168  293 LDPQPGDRVLDLFCGLG--------NFTLplarqaaEVVGVEGVEAMVERARENARrnGLD-NVTFYHAN 353
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
45-155 4.96e-03

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 38.56  E-value: 4.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  45 PEVLSLLPPHEGKSVLELGAGIGRFTGDLAEKAGQVIALD----FIEGV--IKKNESINGHHKNVKfmcaDVTSPELkvs 118
Cdd:PRK11207   20 SEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGFDVTAWDknpmSIANLerIKAAENLDNLHTAVV----DLNNLTF--- 92
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1280981287 119 ENSVDLIFSNWLLMYLSDKEVKNLAERMVKWLKVGGY 155
Cdd:PRK11207   93 DGEYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGY 129
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
43-151 4.99e-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: 38.71  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  43 ERPEVlsllpphEGKSVLELGAGIGrFTGDLAEKAG--QVIALDFIEGV---IKKNESINGHHknVKFMCADVTSPELkv 117
Cdd:COG3897    65 DHPEV-------AGKRVLELGCGLG-LVGIAAAKAGaaDVTATDYDPEAlaaLRLNAALNGVA--ITTRLGDWRDPPA-- 132
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1280981287 118 sENSVDLIFsnwllmyLSDkeV---KNLAERMVKWLK 151
Cdd:COG3897   133 -AGGFDLIL-------GGD--VlyeRDLAEPLLPFLD 159
trmB PRK00121
tRNA (guanine-N(7)-)-methyltransferase; Reviewed
59-158 7.06e-03

tRNA (guanine-N(7)-)-methyltransferase; Reviewed


Pssm-ID: 234649  Cd Length: 202  Bit Score: 37.83  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287  59 VLELGAGIGRFTGDLAEKAGQV--IALD-FIEGVIKKNESINGHH-KNVKFMCADVTSP-ELKVSENSVD---LIFSN-W 129
Cdd:PRK00121   44 HLEIGFGKGEFLVEMAKANPDInfIGIEvHEPGVGKALKKIEEEGlTNLRLLCGDAVEVlLDMFPDGSLDriyLNFPDpW 123
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1280981287 130 L--------LMYlsdkevKNLAERMVKWLKVGGYIFF 158
Cdd:PRK00121  124 PkkrhhkrrLVQ------PEFLALYARKLKPGGEIHF 154
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
307-419 9.59e-03

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: 37.83  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1280981287 307 VGKLDLKPGQRVLDVGCGIGGGDFYMAeNFdV----EVVGIDLSINMISLALE--RAIGLKCAVEFEVADcTKKVYPDNA 380
Cdd:COG2519    84 IARLDIFPGARVLEAGTGSGALTLALA-RA-VgpegKVYSYERREDFAEIARKnlERFGLPDNVELKLGD-IREGIDEGD 160
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1280981287 381 FDVIysrdtILHIQDKPALFRSFYKWVKPGGKILItdYC 419
Cdd:COG2519   161 VDAV-----FLDMPDPWEALEAVAKALKPGGVLVA--YV 192
 
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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