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Conserved domains on  [gi|749818228|ref|WP_040297061|]
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cyclopropane-fatty-acyl-phospholipid synthase family protein [Alcanivorax hongdengensis]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 11454891)

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

CATH:  2.20.25.110
EC:  2.1.-.-
Gene Ontology:  GO:0032259|GO:0008757|GO:1904047|GO:0008168
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CMAS super family cl47167
Mycolic acid cyclopropane synthetase; This family consist of ...
 129-396 2.37e-100

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.


The actual alignment was detected with superfamily member pfam02353:

Pssm-ID: 481507 [Multi-domain]  Cd Length: 272  Bit Score: 299.63  E-value: 2.37e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  129 SLRGSRRNIAAHYDLGNDFFALFLDRTMMYSSAVYPTEQASLEEASAHKMDLICQKLDLQPGMSLLEVGTGWGGLALHAA 208
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  209 RHYGVQVTTTTISREQARYARERVREAGLDDRITVLEEDYRDLTGVYDRVVSVEMIEAVGAEYLDGYFRQLGERLKSNGV 288
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  289 LLLQAITVPDQRY-HYALKQVDFIKRYIFPGGFLPSISvMCDKLTRHTDLVVIGLQDIGLDYARTLHDWRERFLTERGRI 367
Cdd:pfam02353 161 MLLHTITGLHPDEtSERGLPLKFIDKYIFPGGELPSIS-MIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEA 239

                         250       260
                  ....*....|....*....|....*....
gi 749818228  368 ERLgFDERFMRMWDYYLCYCEGAFLERAI 396
Cdd:pfam02353 240 IAL-QSEEFYRMWMLYLTGCAVAFRIGYI 267
 
Name Accession Description Interval E-value
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 129-396 2.37e-100

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: 299.63  E-value: 2.37e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  129 SLRGSRRNIAAHYDLGNDFFALFLDRTMMYSSAVYPTEQASLEEASAHKMDLICQKLDLQPGMSLLEVGTGWGGLALHAA 208
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  209 RHYGVQVTTTTISREQARYARERVREAGLDDRITVLEEDYRDLTGVYDRVVSVEMIEAVGAEYLDGYFRQLGERLKSNGV 288
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  289 LLLQAITVPDQRY-HYALKQVDFIKRYIFPGGFLPSISvMCDKLTRHTDLVVIGLQDIGLDYARTLHDWRERFLTERGRI 367
Cdd:pfam02353 161 MLLHTITGLHPDEtSERGLPLKFIDKYIFPGGELPSIS-MIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEA 239

                         250       260
                  ....*....|....*....|....*....
gi 749818228  368 ERLgFDERFMRMWDYYLCYCEGAFLERAI 396
Cdd:pfam02353 240 IAL-QSEEFYRMWMLYLTGCAVAFRIGYI 267
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
51-396 2.43e-98

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 298.30  E-value: 2.43e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  51 GNAPAIITVNNWDTYRMMMSGGSLGAAEAYMENGWDSPDLVAVI-RYFAANINalNALEGGLAVLsqpaLKLL--HVYNR 127
Cdd:PRK11705  33 GSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFsRVLRAGLD--EKLPHHLKDT----LRILraRLFNL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 128 NSLRGSRRNIAAHYDLGNDFFALFLDRTMMYSSAvYPTEQASLEEASAHKMDLICQKLDLQPGMSLLEVGTGWGGLALHA 207
Cdd:PRK11705 107 QSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCG-YWKDADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 208 ARHYGVQVTTTTISREQARYARERVreAGLDdrITVLEEDYRDLTGVYDRVVSVEMIEAVGAEYLDGYFRQLGERLKSNG 287
Cdd:PRK11705 186 AEHYGVSVVGVTISAEQQKLAQERC--AGLP--VEIRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDG 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 288 VLLLQAITVPDQRYHyalkqVD-FIKRYIFPGGFLPSISVMCDKLTRHtdLVVIGLQDIGLDYARTLHDWRERFLTERGR 366
Cdd:PRK11705 262 LFLLHTIGSNKTDTN-----VDpWINKYIFPNGCLPSVRQIAQASEGL--FVMEDWHNFGADYDRTLMAWHENFEAAWPE 334

                        330       340       350
                 ....*....|....*....|....*....|
gi 749818228 367 IERlGFDERFMRMWDYYLCYCEGAFLERAI 396
Cdd:PRK11705 335 LAD-NYSERFYRMWRYYLLSCAGAFRARDI 363
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 139-293 1.86e-74

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 229.05  E-value: 1.86e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 139 AHYDLGNDFFALFLDRTMMYSSAVYPTEQASLEEASAHKMDLICQKLDLQPGMSLLEVGTGWGGLALHAARHYGVQVTTT 218
Cdd:COG2230    1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749818228 219 TISREQARYARERVREAGLDDRITVLEEDYRDL--TGVYDRVVSVEMIEAVGAEYLDGYFRQLGERLKSNGVLLLQA 293
Cdd:COG2230   81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
 130-391 1.25e-50

cyclopropane mycolic acid synthase family methyltransferase; Members of this family include tailoring enzymes that make site-specific modifications to mycolic acid precursor molecules. These include Mycobacterium tuberculosis enzymes MmaA1-MmaA4, CmaA1-CmaA2, and PcaA. The family also includes UmaA, reported to be the lone member of this family not involved in mycolic acid biosynthesis. No members of this family are found in species that lack mycolic acids. This model excludes two more distantly related paralogs, Rv0447c (UfaA1 ) and Rv3720, that are also encoded in the Mycobacterium tuberculosis H37Rv genome.


Pssm-ID: 468626  Cd Length: 283  Bit Score: 171.88  E-value: 1.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 130 LRGSRRNIAAHYDLGNDFFALFLDRTMMYSSAVYPTEQASLEEASAHKMDLICQKLDLQPGMSLLEVGTGWGGLALHAAR 209
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 210 HYGVQVTTTTISREQARYARERVREAGLDDRITVLEEDYRDLTGVYDRVVSVEMIEAVGAEYLDGYFRQLGERLKSNGVL 289
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 290 LLQAITVPDQRY---------HYALKQVDFIKRYIFPGGFLPSISVMCDKLTRhTDLVVIGLQDIGLDYARTLHDWRERF 360
Cdd:NF040660 161 LLHTITGLHRKEmherglpltMELARFIKFIVTEIFPGGRLPSIEMVVEHAEK-AGFTVTRVQSLQPHYARTLDLWADAL 239

                        250       260       270
                 ....*....|....*....|....*....|....
gi 749818228 361 LTERGR---IERLGFDERFMRmwdyYLCYCEGAF 391
Cdd:NF040660 240 QAHKDEaiaIQSEEVYERYMK----YLTGCAKLF 269
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 193-296 1.94e-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: 60.52  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 193 LLEVGTGWGGLALHAARHYGVQVTTTTISREQARYAReRVREAGLDDRITVLEEDYRDLTGV----YDRVVSVEMIEAVg 268
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPEadesFDVIISDPPLHHL- 79

                         90       100
                 ....*....|....*....|....*...
gi 749818228 269 AEYLDGYFRQLGERLKSNGVLLLQAITV 296
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVLTLVLA 107
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
194-407 3.58e-09

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 56.66  E-value: 3.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228   194 LEVGTGWG-GLALHAARHYGVQVTTTTISREQARYARERVREAGLDDRITVLeedYRDLT-----GVYDRVVSVEMIEAV 267
Cdd:smart00828   4 LDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAkdpfpDTYDLVFGFEVIHHI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228   268 GAEylDGYFRQLGERLKSNGVLL--------LQAITVPDQRyhyalkqvdfikryifpgGFLPSISVMCDKLTRHTDLVV 339
Cdd:smart00828  81 KDK--MDLFSNISRHLKDGGHLVladfianlLSAIEHEETT------------------SYLVTREEWAELLARNNLRVV 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749818228   340 IGLqDIGLDYARTLHDwrERFLTERGRIERLGFDERFMRMWDYYLCYCEGafLERAISTVHLVAAGPD 407
Cdd:smart00828 141 EGV-DASLEIANFLYD--PGFEDNLERLYQDDLDEVTKRHFRGIANLGKL--LEKGLASYALLIVQKD 203
 
Name Accession Description Interval E-value
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 129-396 2.37e-100

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: 299.63  E-value: 2.37e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  129 SLRGSRRNIAAHYDLGNDFFALFLDRTMMYSSAVYPTEQASLEEASAHKMDLICQKLDLQPGMSLLEVGTGWGGLALHAA 208
Cdd:pfam02353   1 SKTRDAENIQAHYDLSNDFFALFLDPTMTYSCAYFERPDMTLEEAQQAKLDLILDKLGLKPGMTLLDIGCGWGGLMRRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  209 RHYGVQVTTTTISREQARYARERVREAGLDDRITVLEEDYRDLTGVYDRVVSVEMIEAVGAEYLDGYFRQLGERLKSNGV 288
Cdd:pfam02353  81 ERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFDEPFDRIVSVGMFEHVGHENYDTFFKKLYNLLPPGGL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  289 LLLQAITVPDQRY-HYALKQVDFIKRYIFPGGFLPSISvMCDKLTRHTDLVVIGLQDIGLDYARTLHDWRERFLTERGRI 367
Cdd:pfam02353 161 MLLHTITGLHPDEtSERGLPLKFIDKYIFPGGELPSIS-MIVESSSEAGFTVEDVESLRPHYAKTLDLWAENLQANKDEA 239

                         250       260
                  ....*....|....*....|....*....
gi 749818228  368 ERLgFDERFMRMWDYYLCYCEGAFLERAI 396
Cdd:pfam02353 240 IAL-QSEEFYRMWMLYLTGCAVAFRIGYI 267
PRK11705 PRK11705
cyclopropane fatty acyl phospholipid synthase;
51-396 2.43e-98

cyclopropane fatty acyl phospholipid synthase;


Pssm-ID: 183282  Cd Length: 383  Bit Score: 298.30  E-value: 2.43e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  51 GNAPAIITVNNWDTYRMMMSGGSLGAAEAYMENGWDSPDLVAVI-RYFAANINalNALEGGLAVLsqpaLKLL--HVYNR 127
Cdd:PRK11705  33 GSRPWDIQVHNPRFFKRVLQEGSLGLGESYMDGWWDCDRLDEFFsRVLRAGLD--EKLPHHLKDT----LRILraRLFNL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 128 NSLRGSRRNIAAHYDLGNDFFALFLDRTMMYSSAvYPTEQASLEEASAHKMDLICQKLDLQPGMSLLEVGTGWGGLALHA 207
Cdd:PRK11705 107 QSKKRAWIVGKEHYDLGNDLFEAMLDPRMQYSCG-YWKDADTLEEAQEAKLDLICRKLQLKPGMRVLDIGCGWGGLARYA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 208 ARHYGVQVTTTTISREQARYARERVreAGLDdrITVLEEDYRDLTGVYDRVVSVEMIEAVGAEYLDGYFRQLGERLKSNG 287
Cdd:PRK11705 186 AEHYGVSVVGVTISAEQQKLAQERC--AGLP--VEIRLQDYRDLNGQFDRIVSVGMFEHVGPKNYRTYFEVVRRCLKPDG 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 288 VLLLQAITVPDQRYHyalkqVD-FIKRYIFPGGFLPSISVMCDKLTRHtdLVVIGLQDIGLDYARTLHDWRERFLTERGR 366
Cdd:PRK11705 262 LFLLHTIGSNKTDTN-----VDpWINKYIFPNGCLPSVRQIAQASEGL--FVMEDWHNFGADYDRTLMAWHENFEAAWPE 334

                        330       340       350
                 ....*....|....*....|....*....|
gi 749818228 367 IERlGFDERFMRMWDYYLCYCEGAFLERAI 396
Cdd:PRK11705 335 LAD-NYSERFYRMWRYYLLSCAGAFRARDI 363
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 139-293 1.86e-74

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 229.05  E-value: 1.86e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 139 AHYDLGNDFFALFLDRTMMYSSAVYPTEQASLEEASAHKMDLICQKLDLQPGMSLLEVGTGWGGLALHAARHYGVQVTTT 218
Cdd:COG2230    1 HHYDLGNDFYRLFLDPTMTYSCAYFEDPDDTLEEAQEAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749818228 219 TISREQARYARERVREAGLDDRITVLEEDYRDL--TGVYDRVVSVEMIEAVGAEYLDGYFRQLGERLKSNGVLLLQA 293
Cdd:COG2230   81 TLSPEQLEYARERAAEAGLADRVEVRLADYRDLpaDGQFDAIVSIGMFEHVGPENYPAYFAKVARLLKPGGRLLLHT 157
mycolic_MTase NF040660
cyclopropane mycolic acid synthase family methyltransferase; Members of this family include ...
 130-391 1.25e-50

cyclopropane mycolic acid synthase family methyltransferase; Members of this family include tailoring enzymes that make site-specific modifications to mycolic acid precursor molecules. These include Mycobacterium tuberculosis enzymes MmaA1-MmaA4, CmaA1-CmaA2, and PcaA. The family also includes UmaA, reported to be the lone member of this family not involved in mycolic acid biosynthesis. No members of this family are found in species that lack mycolic acids. This model excludes two more distantly related paralogs, Rv0447c (UfaA1 ) and Rv3720, that are also encoded in the Mycobacterium tuberculosis H37Rv genome.


Pssm-ID: 468626  Cd Length: 283  Bit Score: 171.88  E-value: 1.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 130 LRGSRRNIAAHYDLGNDFFALFLDRTMMYSSAVYPTEQASLEEASAHKMDLICQKLDLQPGMSLLEVGTGWGGLALHAAR 209
Cdd:NF040660   1 LRPHFEDVQAHYDLSDDFFALFLDPTQTYSCAYFERDDMTLEEAQIAKIDLALGKLNLEPGMTLLDIGCGWGATMRRAVE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 210 HYGVQVTTTTISREQARYARERVREAGLDDRITVLEEDYRDLTGVYDRVVSVEMIEAVGAEYLDGYFRQLGERLKSNGVL 289
Cdd:NF040660  81 KYDVNVVGLTLSKNQAAHVQQVLDEIDTPRSRRVLLQGWEEFDEPVDRIVSIGAFEHFGHERYDDFFKRAYNILPADGRM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 290 LLQAITVPDQRY---------HYALKQVDFIKRYIFPGGFLPSISVMCDKLTRhTDLVVIGLQDIGLDYARTLHDWRERF 360
Cdd:NF040660 161 LLHTITGLHRKEmherglpltMELARFIKFIVTEIFPGGRLPSIEMVVEHAEK-AGFTVTRVQSLQPHYARTLDLWADAL 239

                        250       260       270
                 ....*....|....*....|....*....|....
gi 749818228 361 LTERGR---IERLGFDERFMRmwdyYLCYCEGAF 391
Cdd:NF040660 240 QAHKDEaiaIQSEEVYERYMK----YLTGCAKLF 269
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 194-287 6.65e-16

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 72.60  E-value: 6.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  194 LEVGTGWGGLALHAARHYGVQVTTTTISREQARYARERVREAGLddRITVLEEDYRDL---TGVYDRVVSVEMIEAVGAE 270
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLpfpDGSFDLVVSSGVLHHLPDP 79

                          90
                  ....*....|....*..
gi 749818228  271 YLDGYFRQLGERLKSNG 287
Cdd:pfam13649  80 DLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 179-300 1.77e-13

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: 67.33  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 179 DLICQKLDLQPGMSLLEVGTGWGGLALHAARHyGVQVTTTTISREQARYARERVREAGLddRITVLEEDYRDL---TGVY 255
Cdd:COG2226   12 EALLAALGLRPGARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLpfpDGSF 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 749818228 256 DRVVSVEMIEAVgaEYLDGYFRQLGERLKSNGVLLLQAITVPDQR 300
Cdd:COG2226   89 DLVISSFVLHHL--PDPERALAEIARVLKPGGRLVVVDFSPPDLA 131
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 171-293 4.44e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 67.63  E-value: 4.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 171 EEASAHKMDLICQKLDLQPGMSLLEVGTGWGGLALHAARHYGVQVTTTTISREQARYARERVREAGLdDRITVLEEDYRD 250
Cdd:COG0500    8 DELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAE 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 749818228 251 LTGV----YDRVVSVEMIEAVGAEYLDGYFRQLGERLKSNGVLLLQA 293
Cdd:COG0500   87 LDPLpaesFDLVVAFGVLHHLPPEEREALLRELARALKPGGVLLLSA 133
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 187-298 2.58e-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: 63.50  E-value: 2.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 187 LQPGMSLLEVGTGWGGLALHAARHyGVQVTTTTISREQARYARERVREAglddRITVLEEDYRDL---TGVYDRVVSVEM 263
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARR-GADVTGVDISPEALEIARERAAEL----NVDFVQGDLEDLpleDGSFDLVICSEV 96

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 749818228 264 IEAVgaEYLDGYFRQLGERLKSNGVLLlqaITVPD 298
Cdd:COG2227   97 LEHL--PDPAALLRELARLLKPGGLLL---LSTPN 126
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 193-296 1.94e-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: 60.52  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 193 LLEVGTGWGGLALHAARHYGVQVTTTTISREQARYAReRVREAGLDDRITVLEEDYRDLTGV----YDRVVSVEMIEAVg 268
Cdd:cd02440    2 VLDLGCGTGALALALASGPGARVTGVDISPVALELAR-KAAAALLADNVEVLKGDAEELPPEadesFDVIISDPPLHHL- 79

                         90       100
                 ....*....|....*....|....*...
gi 749818228 269 AEYLDGYFRQLGERLKSNGVLLLQAITV 296
Cdd:cd02440   80 VEDLARFLEEARRLLKPGGVLVLTLVLA 107
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 194-291 1.04e-09

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: 57.12  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 194 LEVGTGWG--GLALHAARHYGVQVTTTTISREQARYARERVREAGLDDRITVLEEDYRD-----LTGVYDRVVsvemIEA 266
Cdd:COG4122   21 LEIGTGTGysTLWLARALPDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGDALEvlprlADGPFDLVF----IDA 96

                         90       100
                 ....*....|....*....|....*
gi 749818228 267 VGAEYLDgYFRQLGERLKSNGVLLL 291
Cdd:COG4122   97 DKSNYPD-YLELALPLLRPGGLIVA 120
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
194-407 3.58e-09

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 56.66  E-value: 3.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228   194 LEVGTGWG-GLALHAARHYGVQVTTTTISREQARYARERVREAGLDDRITVLeedYRDLT-----GVYDRVVSVEMIEAV 267
Cdd:smart00828   4 LDFGCGYGsDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIF---YRDSAkdpfpDTYDLVFGFEVIHHI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228   268 GAEylDGYFRQLGERLKSNGVLL--------LQAITVPDQRyhyalkqvdfikryifpgGFLPSISVMCDKLTRHTDLVV 339
Cdd:smart00828  81 KDK--MDLFSNISRHLKDGGHLVladfianlLSAIEHEETT------------------SYLVTREEWAELLARNNLRVV 140

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749818228   340 IGLqDIGLDYARTLHDwrERFLTERGRIERLGFDERFMRMWDYYLCYCEGafLERAISTVHLVAAGPD 407
Cdd:smart00828 141 EGV-DASLEIANFLYD--PGFEDNLERLYQDDLDEVTKRHFRGIANLGKL--LEKGLASYALLIVQKD 203
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
188-251 2.68e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 54.27  E-value: 2.68e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749818228 188 QPGMSLLEVGTGWGGLALHAARHYGVQVTTTTISREQARYARERVREAGLDDRITVLEEDYRDL 251
Cdd:COG4076   34 KPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVNPDIAAVARRIIAANGLSDRITVINADATDL 97
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 180-290 5.96e-08

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: 53.24  E-value: 5.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 180 LICQKLDLQPGMSLLEVGTGWGGLALHAARH---YGvQVTTTTISREQARYARERVREAGLDDRITVLEEDYRDLT--GV 254
Cdd:COG2519   82 YIIARLDIFPGARVLEAGTGSGALTLALARAvgpEG-KVYSYERREDFAEIARKNLERFGLPDNVELKLGDIREGIdeGD 160

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 749818228 255 YDRVVsVEMIEAVgaEYLDgyfrQLGERLKSNGVLL 290
Cdd:COG2519  161 VDAVF-LDMPDPW--EALE----AVAKALKPGGVLV 189
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 194-291 1.30e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 49.20  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  194 LEVGTGWGGLALHAARhYGVQVTTTTISREQARYARERVREAGLDDRITVLEE-DYRDltGVYDRVVSVEMIEAVgaEYL 272
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREGLTFVVGDAEDlPFPD--NSFDLVLSSEVLHHV--EDP 75

                          90       100
                  ....*....|....*....|
gi 749818228  273 DGYFRQLgER-LKSNGVLLL 291
Cdd:pfam08241  76 ERALREI-ARvLKPGGILII 94
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 183-259 1.78e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 51.76  E-value: 1.78e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749818228 183 QKLDLQPGMSLLEVGTGWGGLALHAARHyGVQVTTTTISREQARYARERVREAGLDDRITVLEEDYRDLTGVYDRVV 259
Cdd:PRK07580  57 PADGDLTGLRILDAGCGVGSLSIPLARR-GAKVVASDISPQMVEEARERAPEAGLAGNITFEVGDLESLLGRFDTVV 132
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 136-247 3.72e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 50.92  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 136 NIAAHYDLGNDFFALFLDRT---MMyssavypteqasleeasahkmdliCQKLDLQPGMSLLEVGTGWGGLALHAARHYG 212
Cdd:PRK00216  19 SIAPKYDLMNDLLSFGLHRVwrrKT------------------------IKWLGVRPGDKVLDLACGTGDLAIALAKAVG 74

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 749818228 213 V--QVTTTTISREQARYARERVREAGLDDRITVLEED 247
Cdd:PRK00216  75 KtgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGD 111
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 194-289 1.15e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 46.59  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  194 LEVGTGWGGLALHAARHY-GVQVTTTTISREQARYARERVREAGLDD----RITVLEEDYRDLTGvYDRVVSVEMIEAVg 268
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALpGLEYTGLDISPAALEAARERLAALGLLNavrvELFQLDLGELDPGS-FDVVVASNVLHHL- 78

                          90       100
                  ....*....|....*....|.
gi 749818228  269 aEYLDGYFRQLGERLKSNGVL 289
Cdd:pfam08242  79 -ADPRAVLRNIRRLLKPGGVL 98
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 189-304 1.47e-06

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 47.81  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  189 PGMSLLEVGTGWGGLALHaARHYGVQVTTTTISREQARYARERVREAGLDdritvlEEDYRDLTGVYDRVVSVEMIEAVg 268
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRL-LRAQGFSVTGVDPSPIAIERALLNVRFDQFD------EQEAAVPAGKFDVIVAREVLEHV- 93

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 749818228  269 aEYLDGYFRQLGERLKSNGVLLLQaitVPDQRYHYA 304
Cdd:pfam13489  94 -PDPPALLRQIAALLKPGGLLLLS---TPLASDEAD 125
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
172-308 2.81e-06

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 47.30  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 172 EASAHKMDLICQKLDLQPGMSLLEVGTGwGGLALHAARHYGVQVTTTTISREQARYARERvreaGLDDRitVLEEDYRDL 251
Cdd:COG4976   29 EAPALLAEELLARLPPGPFGRVLDLGCG-TGLLGEALRPRGYRLTGVDLSEEMLAKAREK----GVYDR--LLVADLADL 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749818228 252 T---GVYDRVVSVEMIEAVGAeyLDGYFRQLGERLKSNGVLllqAITVPD----QRYHYALKQV 308
Cdd:COG4976  102 AepdGRFDLIVAADVLTYLGD--LAAVFAGVARALKPGGLF---IFSVEDadgsGRYAHSLDYV 160
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 186-260 3.61e-06

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: 47.83  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 186 DLQPGMSLLEVGTGWG--GLALhAARHYGVQVTTTTISREQARYARERVREAGLDDRITVLEEDYRDL-----TGVYDRV 258
Cdd:COG4123   34 PVKKGGRVLDLGTGTGviALML-AQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFaaelpPGSFDLV 112


                 ..
gi 749818228 259 VS 260
Cdd:COG4123  113 VS 114
PRK13942 PRK13942
protein-L-isoaspartate O-methyltransferase; Provisional
 176-246 5.57e-06

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 184409  Cd Length: 212  Bit Score: 46.93  E-value: 5.57e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749818228 176 HKMDLICQKLDLQPGMSLLEVGTGWGGLALHAARHYGVQVTTTTISR--EQARYARERVREAGLDDRITVLEE 246
Cdd:PRK13942  63 HMVAIMCELLDLKEGMKVLEIGTGSGYHAAVVAEIVGKSGKVVTIERipELAEKAKKTLKKLGYDNVEVIVGD 135
PLN02244 PLN02244
tocopherol O-methyltransferase
 194-262 1.22e-05

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 47.05  E-value: 1.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749818228 194 LEVGTGWGGLALHAARHYGVQVTTTTISREQARYARERVREAGLDDRITV-----LEEDYRDltGVYDRVVSVE 262
Cdd:PLN02244 123 VDVGCGIGGSSRYLARKYGANVKGITLSPVQAARANALAAAQGLSDKVSFqvadaLNQPFED--GQFDLVWSME 194
PRK14967 PRK14967
putative methyltransferase; Provisional
 186-260 2.06e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 45.43  E-value: 2.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749818228 186 DLQPGMSLLEVGTGWGGLALHAARHYGVQVTTTTISREQARYARERVREAGLDdrITVLEEDYRDL--TGVYDRVVS 260
Cdd:PRK14967  33 GLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAVDISRRAVRSARLNALLAGVD--VDVRRGDWARAveFRPFDVVVS 107
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
176-309 5.03e-05

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 43.90  E-value: 5.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  176 HKMDLICQKLDLQPGMSLLEVGTGWGGLALHAARHYGVQVTTTTI--SREQARYARERVREAGLDDRITVLEEDYRdltG 253
Cdd:pfam01135  60 HMHAMMLELLELKPGMRVLEIGSGSGYLTACFARMVGEVGRVVSIehIPELVEIARRNLEKLGLENVIVVVGDGRQ---G 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749818228  254 V-----YDRVVsvemieaVGAEyLDGYFRQLGERLKSNGVLLlqaitVP-DQRYHYALKQVD 309
Cdd:pfam01135 137 WpefapYDAIH-------VGAA-APEIPEALIDQLKEGGRLV-----IPvGPNGNQVLQQFD 185
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 180-290 7.16e-05

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 43.54  E-value: 7.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 180 LICQKLDLQPGMSLLEVGTGWG---GLALHAARHygvqVTTTTISREQARYARERVREAGLdDRITVLeedYRDLT---- 252
Cdd:COG2518   57 RMLEALDLKPGDRVLEIGTGSGyqaAVLARLAGR----VYSVERDPELAERARERLAALGY-DNVTVR---VGDGAlgwp 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 749818228 253 --GVYDRVVsvemIEAVGAEYLDGYFRQlgerLKSNGVLL 290
Cdd:COG2518  129 ehAPFDRII----VTAAAPEVPEALLEQ----LAPGGRLV 160
GCD14 pfam08704
tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase ...
 180-258 9.81e-05

tRNA methyltransferase complex GCD14 subunit; GCD14 is a subunit of the tRNA methyltransferase complex and is required for 1-methyladenosine modification and maturation of initiator methionyl-tRNA.


Pssm-ID: 312288  Cd Length: 242  Bit Score: 43.63  E-value: 9.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  180 LICQKLDLQPGMSLLEVGTGWGGLALHAARHYGVQVTTTTISREQARY--ARERVREAGLDDRITVLEED------YRDL 251
Cdd:pfam08704  31 LITMMLELRPGSVVCESGTGSGSLSHAIIRTVAPTGHLFTFEFHEQRAdkAREEFREHGIDQLVTVTHRDvckegfLTEV 110


                  ....*..
gi 749818228  252 TGVYDRV 258
Cdd:pfam08704 111 SGKADAV 117
Qor COG0604
NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and ...
 183-282 7.61e-04

NADPH:quinone reductase or related Zn-dependent oxidoreductase [Energy production and conversion, General function prediction only];


Pssm-ID: 440369 [Multi-domain]  Cd Length: 322  Bit Score: 41.29  E-value: 7.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 183 QKLDLQPGMSLLEVGTGwGGLALHA---ARHYGVQVTTTTISREQAryarERVREAGLDDRI----TVLEEDYRDLTGV- 254
Cdd:COG0604  133 DRGRLKPGETVLVHGAA-GGVGSAAvqlAKALGARVIATASSPEKA----ELLRALGADHVIdyreEDFAERVRALTGGr 207

                         90       100
                 ....*....|....*....|....*....
gi 749818228 255 -YDRVvsvemIEAVGAEYLDGYFRQLGER 282
Cdd:COG0604  208 gVDVV-----LDTVGGDTLARSLRALAPG 231
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 164-269 8.04e-04

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 41.06  E-value: 8.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 164 PTEQASLEEASA---HKMDLIcqklDLQPGMSLLEVGTG-WGGLALHAARHYGV-QVTTTTISREQARYARErvreAGLD 238
Cdd:cd08236  135 DYEEAAMIEPAAvalHAVRLA----GITLGDTVVVIGAGtIGLLAIQWLKILGAkRVIAVDIDDEKLAVARE----LGAD 206

                         90       100       110
                 ....*....|....*....|....*....|.
gi 749818228 239 DRITVLEEDYRDLTGVYDRVVSVEMIEAVGA 269
Cdd:cd08236  207 DTINPKEEDVEKVRELTEGRGADLVIEAAGS 237
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
185-325 1.31e-03

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 39.80  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 185 LDLQPGMSLLEVGTGWGGLAL---HAARHygvqvtTTTISR--EQARYARERVREAGLDDRITVLEEDYRDLT--GVYDR 257
Cdd:PRK00312  74 LELKPGDRVLEIGTGSGYQAAvlaHLVRR------VFSVERikTLQWEAKRRLKQLGLHNVSVRHGDGWKGWPayAPFDR 147

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 258 VVSVEMIEAVGAEYLdgyfrqlgERLKSNGVlLLQAITVPDQRYHYALKQVD--FIKRYIFPGGFLPSIS 325
Cdd:PRK00312 148 ILVTAAAPEIPRALL--------EQLKEGGI-LVAPVGGEEQQLLTRVRKRGgrFEREVLEEVRFVPLVK 208
SpeE COG0421
Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];
194-304 1.32e-03

Spermidine synthase (polyamine aminopropyltransferase) [Amino acid transport and metabolism];


Pssm-ID: 440190 [Multi-domain]  Cd Length: 195  Bit Score: 39.81  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 194 LEVGTGWGGLALHAARHYGV-QVTTTTISREQARYARER---VREAGLDDRITVLEED---Y-RDLTGVYDrVVSVEMIE 265
Cdd:COG0421   42 LIIGGGDGGLARELLKHPPVeRVDVVEIDPEVVELAREYfplLAPAFDDPRLRVVIGDgraFlREAEESYD-VIIVDLTD 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 749818228 266 AVG-AEYLDG--YFRQLGERLKSNGVLLLQAITVPDQRYHYA 304
Cdd:COG0421  121 PVGpAEGLFTreFYEDCRRALKPGGVLVVNLGSPFYGLDLLR 162
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 189-292 3.33e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 37.78  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  189 PGMSLLEVGTGWGGLALHAARHYG--VQVTTTTISREQARYARERVREAGLDD------RITVLEEDYRDLTgvYDRVVS 260
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELGpnAEVVGIDISEEAIEKARENAQKLGFDNvefeqgDIEELPELLEDDK--FDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 749818228  261 VEMIEAVGAeyLDGYFRQLGERLKSNGVLLLQ 292
Cdd:pfam13847  81 NCVLNHIPD--PDKVLQEILRVLKPGGRLIIS 110
PRK13944 PRK13944
protein-L-isoaspartate O-methyltransferase; Provisional
 176-249 4.57e-03

protein-L-isoaspartate O-methyltransferase; Provisional


Pssm-ID: 140001  Cd Length: 205  Bit Score: 38.26  E-value: 4.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749818228 176 HKMDLICQKLDLQPGMSLLEVGTGWGGLALHAARHYGVQ--VTTTTISREQARYARERVREAGLDDRITVLEEDYR 249
Cdd:PRK13944  59 HMVAMMCELIEPRPGMKILEVGTGSGYQAAVCAEAIERRgkVYTVEIVKELAIYAAQNIERLGYWGVVEVYHGDGK 134
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 184-231 6.59e-03

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 38.58  E-value: 6.59e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 749818228 184 KLDLQPGMSLLEVGTGWGGLALHAARHYGVQVTTTTISREQARYARER 231
Cdd:PLN02336 261 KLDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALER 308
rumB PRK03522
23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;
159-238 7.60e-03

23S rRNA (uracil(747)-C(5))-methyltransferase RlmC;


Pssm-ID: 235128 [Multi-domain]  Cd Length: 315  Bit Score: 37.93  E-value: 7.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228 159 SSAVYPTEQASLEEASAHKM-DLICqkldlqpgmsllevgtGWGGLALHAARHyGVQVTTTTISREQARYARERVREAGL 237
Cdd:PRK03522 158 AAQLYATARDWVRELPPRSMwDLFC----------------GVGGFGLHCATP-GMQLTGIEISAEAIACAKQSAAELGL 220


                 .
gi 749818228 238 D 238
Cdd:PRK03522 221 T 221
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 183-308 9.80e-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: 36.80  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749818228  183 QKLDLQPGMSLLEVGTGWGGLALHAARHYG-VQVTTTTISREQARYARERVREAGLDDrITVLEED-YRDLT-GVYDRVV 259
Cdd:pfam05175  25 EHLPKDLSGKVLDLGCGAGVLGAALAKESPdAELTMVDINARALESARENLAANGLEN-GEVVASDvYSGVEdGKFDLII 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 749818228  260 SVEMIEAVGAEYLD---GYFRQLGERLKSNGVLLLqaITVPDQRYHYALKQV 308
Cdd:pfam05175 104 SNPPFHAGLATTYNvaqRFIADAKRHLRPGGELWI--VANRFLGYPPLLEEL 153
 
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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