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Conserved domains on  [gi|1418394052|gb|AWZ21157|]
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Phosphoethanolamine N-methyltransferase [Roseovarius sp. AK1035]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 1009176)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Caenorhabditis elegans phosphoethanolamine N-methyltransferase 1

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12504684|12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02336 super family cl31863
phosphoethanolamine N-methyltransferase
 3-165 2.45e-23

phosphoethanolamine N-methyltransferase


The actual alignment was detected with superfamily member PLN02336:

Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 98.28  E-value: 2.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052   3 EDILYDQSHIGFLEDLWGEGFLSPGGQDEVARVLDGVDLT-GAKVLDIGCGSGAIAVLMVRVHGAaHVTGIDVEDPVCAA 81
Cdd:PLN02336  226 DNVQYKSSGILRYERVFGEGFVSTGGLETTKEFVDKLDLKpGQKVLDVGCGIGGGDFYMAENFDV-HVVGIDLSVNMISF 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  82 ARARATAAGLAGQITIDKVTPGPfpYPDQSFDVVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASDWLRAhDGAPSPEM 161
Cdd:PLN02336  305 ALERAIGRKCSVEFEVADCTKKT--YPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRS-PGTPSPEF 381


                  ....
gi 1418394052 162 AHYI 165
Cdd:PLN02336  382 AEYI 385
 
Name Accession Description Interval E-value
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 3-165 2.45e-23

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 98.28  E-value: 2.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052   3 EDILYDQSHIGFLEDLWGEGFLSPGGQDEVARVLDGVDLT-GAKVLDIGCGSGAIAVLMVRVHGAaHVTGIDVEDPVCAA 81
Cdd:PLN02336  226 DNVQYKSSGILRYERVFGEGFVSTGGLETTKEFVDKLDLKpGQKVLDVGCGIGGGDFYMAENFDV-HVVGIDLSVNMISF 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  82 ARARATAAGLAGQITIDKVTPGPfpYPDQSFDVVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASDWLRAhDGAPSPEM 161
Cdd:PLN02336  305 ALERAIGRKCSVEFEVADCTKKT--YPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRS-PGTPSPEF 381


                  ....
gi 1418394052 162 AHYI 165
Cdd:PLN02336  382 AEYI 385
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 30-151 2.11e-19

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 81.58  E-value: 2.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  30 DEVARVLDGVDLT-GAKVLDIGCGSGAIAVLMVRVhgAAHVTGIDVEDP---VCAAARARATAAGLAGQITIDKvtpgpF 105
Cdd:COG2226     9 DGREALLAALGLRpGARVLDLGCGTGRLALALAER--GARVTGVDISPEmleLARERAAEAGLNVEFVVGDAED-----L 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1418394052 106 PYPDQSFDVVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASDWLR 151
Cdd:COG2226    82 PFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-142 1.90e-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: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  46 VLDIGCGSGAIAVLMVRVHGAaHVTGIDVEDPVCAAARARATAAGLAGQITIDKVTPgpFPYPDQSFDVVFSKDSIIHI- 124
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGA-RVTGVDLSPEMLERARERAAEAGLNVEFVQGDAED--LPFPDGSFDLVVSSGVLHHLp 77

                          90
                  ....*....|....*....
gi 1418394052 125 -PDKEALAAEVFRVLKPGG 142
Cdd:pfam13649  78 dPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-150 2.78e-12

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: 61.68  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  45 KVLDIGCGSGAIAVLMVRvHGAAHVTGIDVeDPVCAAARARATAAGLAGQITIDKVTPGPFP-YPDQSFDVVFSKDSIIH 123
Cdd:cd02440     1 RVLDLGCGTGALALALAS-GPGARVTGVDI-SPVALELARKAAAALLADNVEVLKGDAEELPpEADESFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|....*...
gi 1418394052 124 I-PDKEALAAEVFRVLKPGGVFAASDWL 150
Cdd:cd02440    79 LvEDLARFLEEARRLLKPGGVLVLTLVL 106
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 32-148 2.60e-08

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 53.06  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  32 VARVLDGVDLTGAKVLDIGCGSGAIAVLMVRVHGAAHVTGIDVEDPVCAAARARATAAGLAGQITIDKvtpgpFPYPDQS 111
Cdd:TIGR02072  24 LALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSENVQFICGDAEK-----LPLEDSS 98

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1418394052 112 FDVVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASD 148
Cdd:TIGR02072  99 FDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFST 135
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
45-150 1.08e-05

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 45.10  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052   45 KVLDIGCGSGAIAVLMVRVHGAAHVTGIDVEDPVCAAARARATAAGLAGQITI--DKVTPGPFPypdQSFDVVFSKDSII 122
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIfyRDSAKDPFP---DTYDLVFGFEVIH 78

                           90       100
                   ....*....|....*....|....*...
gi 1418394052  123 HIPDKEALAAEVFRVLKPGGVFAASDWL 150
Cdd:smart00828  79 HIKDKMDLFSNISRHLKDGGHLVLADFI 106
 
Name Accession Description Interval E-value
PLN02336 PLN02336
phosphoethanolamine N-methyltransferase
 3-165 2.45e-23

phosphoethanolamine N-methyltransferase


Pssm-ID: 177970 [Multi-domain]  Cd Length: 475  Bit Score: 98.28  E-value: 2.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052   3 EDILYDQSHIGFLEDLWGEGFLSPGGQDEVARVLDGVDLT-GAKVLDIGCGSGAIAVLMVRVHGAaHVTGIDVEDPVCAA 81
Cdd:PLN02336  226 DNVQYKSSGILRYERVFGEGFVSTGGLETTKEFVDKLDLKpGQKVLDVGCGIGGGDFYMAENFDV-HVVGIDLSVNMISF 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  82 ARARATAAGLAGQITIDKVTPGPfpYPDQSFDVVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASDWLRAhDGAPSPEM 161
Cdd:PLN02336  305 ALERAIGRKCSVEFEVADCTKKT--YPDNSFDVIYSRDTILHIQDKPALFRSFFKWLKPGGKVLISDYCRS-PGTPSPEF 381


                  ....
gi 1418394052 162 AHYI 165
Cdd:PLN02336  382 AEYI 385
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 30-151 2.11e-19

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 81.58  E-value: 2.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  30 DEVARVLDGVDLT-GAKVLDIGCGSGAIAVLMVRVhgAAHVTGIDVEDP---VCAAARARATAAGLAGQITIDKvtpgpF 105
Cdd:COG2226     9 DGREALLAALGLRpGARVLDLGCGTGRLALALAER--GARVTGVDISPEmleLARERAAEAGLNVEFVVGDAED-----L 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1418394052 106 PYPDQSFDVVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASDWLR 151
Cdd:COG2226    82 PFPDGSFDLVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSP 127
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 30-148 2.84e-18

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: 78.14  E-value: 2.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  30 DEVARVLDGVDLTGAKVLDIGCGSGAIAVLMVRvHGAaHVTGIDV-EDPVCAAARARATAAGLAGQITIDKvtpgpFPYP 108
Cdd:COG2227    12 RRLAALLARLLPAGGRVLDVGCGTGRLALALAR-RGA-DVTGVDIsPEALEIARERAAELNVDFVQGDLED-----LPLE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1418394052 109 DQSFDVVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASD 148
Cdd:COG2227    85 DGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLST 124
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-142 1.90e-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: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  46 VLDIGCGSGAIAVLMVRVHGAaHVTGIDVEDPVCAAARARATAAGLAGQITIDKVTPgpFPYPDQSFDVVFSKDSIIHI- 124
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGA-RVTGVDLSPEMLERARERAAEAGLNVEFVQGDAED--LPFPDGSFDLVVSSGVLHHLp 77

                          90
                  ....*....|....*....
gi 1418394052 125 -PDKEALAAEVFRVLKPGG 142
Cdd:pfam13649  78 dPDLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-145 3.73e-16

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 71.54  E-value: 3.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  47 LDIGCGSGAIAVLMVRVhgAAHVTGIDVEDPVCAAARARATAAGLAGQI-TIDKVtpgpfPYPDQSFDVVFSKDSIIHIP 125
Cdd:pfam08241   1 LDVGCGTGLLTELLARL--GARVTGVDISPEMLELAREKAPREGLTFVVgDAEDL-----PFPDNSFDLVLSSEVLHHVE 73

                          90       100
                  ....*....|....*....|
gi 1418394052 126 DKEALAAEVFRVLKPGGVFA 145
Cdd:pfam08241  74 DPERALREIARVLKPGGILI 93
PRK08317 PRK08317
hypothetical protein; Provisional
 43-156 1.31e-13

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 68.42  E-value: 1.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  43 GAKVLDIGCGSGAIAVLM-VRVHGAAHVTGIDVEDPVCAAARARATAAGLAGQITIDKVTPGPFPypDQSFDVVFSKDSI 121
Cdd:PRK08317   20 GDRVLDVGCGPGNDARELaRRVGPEGRVVGIDRSEAMLALAKERAAGLGPNVEFVRGDADGLPFP--DGSFDAVRSDRVL 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1418394052 122 IHIPDKEALAAEVFRVLKPGG--VFAASDW----LRAHDGA 156
Cdd:PRK08317   98 QHLEDPARALAEIARVLRPGGrvVVLDTDWdtlvWHSGDRA 138
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 24-148 2.09e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 66.11  E-value: 2.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  24 LSPGGQDEVARVLDGVDLT-GAKVLDIGCGSGAIAVLMVRVHGaAHVTGIDVEDPVCAAARARATAAGLAGQITIDKVTP 102
Cdd:COG2230    32 LEEAQEAKLDLILRKLGLKpGMRVLDIGCGWGGLALYLARRYG-VRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADY 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1418394052 103 GPFPyPDQSFDVVFSKDSIIHIPDK--EALAAEVFRVLKPGGVFAASD 148
Cdd:COG2230   111 RDLP-ADGQFDAIVSIGMFEHVGPEnyPAYFAKVARLLKPGGRLLLHT 157
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
43-148 3.13e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 64.07  E-value: 3.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  43 GAKVLDIGCGSGAIAVLMVRVHGAAHVTGIDVeDPVCAAARARATAAGLAGQITIDKVTpgpfpyPDQSFDVVFSKDSII 122
Cdd:COG4106     2 PRRVLDLGCGTGRLTALLAERFPGARVTGVDL-SPEMLARARARLPNVRFVVADLRDLD------PPEPFDLVVSNAALH 74

                          90       100
                  ....*....|....*....|....*.
gi 1418394052 123 HIPDKEALAAEVFRVLKPGGVFAASD 148
Cdd:COG4106    75 WLPDHAALLARLAAALAPGGVLAVQV 100
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 45-150 2.78e-12

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: 61.68  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  45 KVLDIGCGSGAIAVLMVRvHGAAHVTGIDVeDPVCAAARARATAAGLAGQITIDKVTPGPFP-YPDQSFDVVFSKDSIIH 123
Cdd:cd02440     1 RVLDLGCGTGALALALAS-GPGARVTGVDI-SPVALELARKAAAALLADNVEVLKGDAEELPpEADESFDVIISDPPLHH 78

                          90       100
                  ....*....|....*....|....*...
gi 1418394052 124 I-PDKEALAAEVFRVLKPGGVFAASDWL 150
Cdd:cd02440    79 LvEDLARFLEEARRLLKPGGVLVLTLVL 106
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 3-149 3.16e-12

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 64.61  E-value: 3.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052   3 EDILYDQSHIGFLEDLWGEGFLSPGGQDEVARVLDGVDLT-GAKVLDIGCGSGAIAVLMVRVHGAaHVTGIDVEDPVCAA 81
Cdd:PTZ00098   12 ENNQYSDEGIKAYEFIFGEDYISSGGIEATTKILSDIELNeNSKVLDIGSGLGGGCKYINEKYGA-HVHGVDICEKMVNI 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  82 ARARATAAGLAGQITIDKVTPgpfPYPDQSFDVVFSKDSIIHIP--DKEALAAEVFRVLKPGGVFAASDW 149
Cdd:PTZ00098   91 AKLRNSDKNKIEFEANDILKK---DFPENTFDMIYSRDAILHLSyaDKKKLFEKCYKWLKPNGILLITDY 157
PLN02244 PLN02244
tocopherol O-methyltransferase
 6-142 4.02e-12

tocopherol O-methyltransferase


Pssm-ID: 215135 [Multi-domain]  Cd Length: 340  Bit Score: 65.15  E-value: 4.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052   6 LYDQSHiGFLEDLWGE----GFLSPGGQD---------------EVARVLDGVDLTGAKVLDIGCGSGAIAVLMVRVHGA 66
Cdd:PLN02244   64 FYDESS-GVWEDVWGEhmhhGYYDPGASRgdhrqaqirmieeslAWAGVPDDDEKRPKRIVDVGCGIGGSSRYLARKYGA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  67 AhVTGIDVEdPVcaaaRARATAAGLAGQITIDKVTpgpF--------PYPDQSFDVVFSKDSIIHIPDKEALAAEVFRVL 138
Cdd:PLN02244  143 N-VKGITLS-PV----QAARANALAAAQGLSDKVS---FqvadalnqPFEDGQFDLVWSMESGEHMPDKRKFVQELARVA 213


                  ....
gi 1418394052 139 KPGG 142
Cdd:PLN02244  214 APGG 217
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 43-148 8.34e-12

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 61.28  E-value: 8.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  43 GAKVLDIGCGSGAIA-VLMVRVHGAAHVTGID-VEDPVCAAARARATAAGLAGQITIDKVTPGPFPYPDQSFDVVFSKDS 120
Cdd:pfam13847   4 GMRVLDLGCGTGHLSfELAEELGPNAEVVGIDiSEEAIEKARENAQKLGFDNVEFEQGDIEELPELLEDDKFDVVISNCV 83

                          90       100
                  ....*....|....*....|....*...
gi 1418394052 121 IIHIPDKEALAAEVFRVLKPGGVFAASD 148
Cdd:pfam13847  84 LNHIPDPDKVLQEILRVLKPGGRLIISD 111
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 43-149 1.51e-11

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 61.86  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  43 GAKVLDIGCGSGAIAVLMVRVHGAaHVTGIDVEDPVCAAARARATaaglagQITIDKVT------PGPFPYPDQSFDVVF 116
Cdd:COG0500    27 GGRVLDLGCGTGRNLLALAARFGG-RVIGIDLSPEAIALARARAA------KAGLGNVEflvadlAELDPLPAESFDLVV 99

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1418394052 117 SKDSIIHIPDKE--ALAAEVFRVLKPGGVFAASDW 149
Cdd:COG0500   100 AFGVLHHLPPEEreALLRELARALKPGGVLLLSAS 134
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
43-163 1.92e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 61.17  E-value: 1.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  43 GAKVLDIGCGSGAIAVLMVRVhgAAHVTGIDV---------EDPVcaaararataaglagQITIDKVTPGPFPYPDQSFD 113
Cdd:COG4976    47 FGRVLDLGCGTGLLGEALRPR--GYRLTGVDLseemlakarEKGV---------------YDRLLVADLADLAEPDGRFD 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1418394052 114 VVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASdwlrAHDGAPSPEMAH 163
Cdd:COG4976   110 LIVAADVLTYLGDLAAVFAGVARALKPGGLFIFS----VEDADGSGRYAH 155
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-144 7.38e-11

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 57.38  E-value: 7.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  47 LDIGCGSGAIAVLMVRVHGAAHVTGIDVEDPVCAAARARATAAGLAGQITIDKVTPGPFPYPDQSFDVVFSKDSIIHIPD 126
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 1418394052 127 KEALAAEVFRVLKPGGVF 144
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
36-147 1.36e-09

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 57.11  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  36 LDGVDLTGAKVLDIGCGSG--AIAVLMvrvHGAAHVTGIDVeDPVCaaararataaglaGQITID-----------KVTP 102
Cdd:COG2264   142 LEKLLKPGKTVLDVGCGSGilAIAAAK---LGAKRVLAVDI-DPVA-------------VEAAREnaelngvedriEVVL 204

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1418394052 103 GPFpYPDQSFDVVFS---KDSIIhipdkeALAAEVFRVLKPGGVFAAS 147
Cdd:COG2264   205 GDL-LEDGPYDLVVAnilANPLI------ELAPDLAALLKPGGYLILS 245
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 43-145 5.54e-09

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 55.16  E-value: 5.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  43 GAKVLDIGCGSGAIAVLMVRVHGA-AHVTGID-------VedpvcaaararataaglAGQITIDKVTPGPF--------- 105
Cdd:PRK00216   52 GDKVLDLACGTGDLAIALAKAVGKtGEVVGLDfsegmlaV-----------------GREKLRDLGLSGNVefvqgdaea 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1418394052 106 -PYPDQSFDVVfskdSI---I-HIPDKEALAAEVFRVLKPGGVFA 145
Cdd:PRK00216  115 lPFPDNSFDAV----TIafgLrNVPDIDKALREMYRVLKPGGRLV 155
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
36-79 1.68e-08

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 53.62  E-value: 1.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1418394052  36 LDGVDLTGAKVLDIGCGSG--AIAVLMVrvhGAAHVTGIDVeDPVC 79
Cdd:PRK00517  113 LEKLVLPGKTVLDVGCGSGilAIAAAKL---GAKKVLAVDI-DPQA 154
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 30-154 1.69e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 52.43  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  30 DEVARVLDGvDLTGAKVLDIGCGSGAIAVLMVRVhgAAHVTGIDVeDPVCAAARARATAAGLAGQITIDkvtpgpfpYPD 109
Cdd:pfam13489  11 DLLLRLLPK-LPSPGRVLDFGCGTGIFLRLLRAQ--GFSVTGVDP-SPIAIERALLNVRFDQFDEQEAA--------VPA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1418394052 110 QSFDVVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASDWLRAHD 154
Cdd:pfam13489  79 GKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPLASDE 123
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 32-148 2.60e-08

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 53.06  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  32 VARVLDGVDLTGAKVLDIGCGSGAIAVLMVRVHGAAHVTGIDVEDPVCAAARARATAAGLAGQITIDKvtpgpFPYPDQS 111
Cdd:TIGR02072  24 LALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSENVQFICGDAEK-----LPLEDSS 98

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1418394052 112 FDVVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASD 148
Cdd:TIGR02072  99 FDLIVSNLALQWCDDLSQALSELARVLKPGGLLAFST 135
arsM PRK11873
arsenite methyltransferase;
106-148 2.72e-08

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 53.41  E-value: 2.72e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1418394052 106 PYPDQSFDVVFSKDSIIHIPDKEALAAEVFRVLKPGGVFAASD 148
Cdd:PRK11873  141 PVADNSVDVIISNCVINLSPDKERVFKEAFRVLKPGGRFAISD 183
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 36-147 8.01e-08

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 52.27  E-value: 8.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  36 LDGVDLTGAKVLDIGCGSG--AIAVLMVrvhGAAHVTGIDVeDPVcaaararaTAAGLAGQITIDKVTPGPFPY-----P 108
Cdd:pfam06325 155 LERLVKPGESVLDVGCGSGilAIAALKL---GAKKVVGVDI-DPV--------AVRAAKENAELNGVEARLEVYlpgdlP 222

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1418394052 109 DQSFDVVFSK---DSIIHipdkeaLAAEVFRVLKPGGVFAAS 147
Cdd:pfam06325 223 KEKADVVVANilaDPLIE------LAPDIYALVKPGGYLILS 258
COG4627 COG4627
Predicted SAM-depedendent methyltransferase [General function prediction only];
104-144 2.34e-07

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


Pssm-ID: 443666 [Multi-domain]  Cd Length: 161  Bit Score: 49.09  E-value: 2.34e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1418394052 104 PFPYPDQSFDVVFSKDSIIHIPDKEALAA--EVFRVLKPGGVF 144
Cdd:COG4627    39 PLPFPDNSVDAIYSSHVLEHLDYEEAPLAlkECYRVLKPGGIL 81
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 43-145 3.83e-07

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 49.57  E-value: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  43 GAKVLDIGCGSGAIAVLMVRVHGA-AHVTGIDVEDPVCAAARARATAAGLAGQITIDKVTpgpFPYPDQSFDVVFSKDSI 121
Cdd:TIGR01934  40 GQKVLDVACGTGDLAIELAKSAPDrGKVTGVDFSSEMLEVAKKKSELPLNIEFIQADAEA---LPFEDNSFDAVTIAFGL 116

                          90       100
                  ....*....|....*....|....
gi 1418394052 122 IHIPDKEALAAEVFRVLKPGGVFA 145
Cdd:TIGR01934 117 RNVTDIQKALREMYRVLKPGGRLV 140
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
40-144 1.80e-06

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 47.43  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  40 DLTGAKVLDIGCGSGAIAVLMVRVHGAA-HVTGIDVeDPVCAAARARATAAGLAGQITIDKVTPGPFPYPDQSFDVVFSK 118
Cdd:pfam01209  40 VKRGNKFLDVAGGTGDWTFGLSDSAGSSgKVVGLDI-NENMLKEGEKKAKEEGKYNIEFLQGNAEELPFEDDSFDIVTIS 118

                          90       100
                  ....*....|....*....|....*.
gi 1418394052 119 DSIIHIPDKEALAAEVFRVLKPGGVF 144
Cdd:pfam01209 119 FGLRNFPDYLKVLKEAFRVLKPGGRV 144
UbiG TIGR01983
ubiquinone biosynthesis O-methyltransferase; This model represents an O-methyltransferase ...
 40-142 3.72e-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: 46.52  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  40 DLTGAKVLDIGCGSGAIAVLMVRvHGAAhVTGIDV-------------EDPVcaaararataAGLAGQITIDKVTPGPfp 106
Cdd:TIGR01983  44 PLDGLRVLDVGCGGGLLSEPLAR-LGAN-VTGIDAseenievaklhakKDPL----------QIDYRCTTVEDLAEKK-- 109

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1418394052 107 ypDQSFDVVFSKDSIIHIPDKEALAAEVFRVLKPGG 142
Cdd:TIGR01983 110 --AGSFDVVTCMEVLEHVPDPQAFIRACAQLLKPGG 143
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 18-75 6.30e-06

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: 46.03  E-value: 6.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1418394052  18 LWGegFLSPGGQdEVAR-VLDGVDLTGAKVLDIGCGSGAIAVLMVRvHGAAHVTGIDVE 75
Cdd:COG3897    48 FWA--FLWPSGQ-ALARyLLDHPEVAGKRVLELGCGLGLVGIAAAK-AGAADVTATDYD 102
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
45-150 1.08e-05

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 45.10  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052   45 KVLDIGCGSGAIAVLMVRVHGAAHVTGIDVEDPVCAAARARATAAGLAGQITI--DKVTPGPFPypdQSFDVVFSKDSII 122
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIfyRDSAKDPFP---DTYDLVFGFEVIH 78

                           90       100
                   ....*....|....*....|....*...
gi 1418394052  123 HIPDKEALAAEVFRVLKPGGVFAASDWL 150
Cdd:smart00828  79 HIKDKMDLFSNISRHLKDGGHLVLADFI 106
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 32-74 3.46e-05

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 43.99  E-value: 3.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1418394052  32 VARVLDGV-DLTGAKVLDIGCGSGAIAVLMVRVHGAAHVTGIDV 74
Cdd:COG2890   101 VELALALLpAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDI 144
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 36-145 4.50e-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: 43.59  E-value: 4.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  36 LDGVDL-------TGAKVLDIGCGSGAIAVLMVRVHGAAHVTGIDVEDPVCAAARARATAAGLAGQITI--DKVTPGPFP 106
Cdd:COG4123    24 TDAVLLaafapvkKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVihGDLKEFAAE 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1418394052 107 YPDQSFDVV------FSKDSIIHIPDK-------------EALAAEVFRVLKPGGVFA 145
Cdd:COG4123   104 LPPGSFDLVvsnppyFKAGSGRKSPDEaraiarhedaltlEDLIRAAARLLKPGGRFA 161
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 43-74 3.34e-04

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: 40.56  E-value: 3.34e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1418394052  43 GAKVLDIGCGSGAIAVLMVRVHGAAHVTGIDV 74
Cdd:COG2813    50 GGRVLDLGCGYGVIGLALAKRNPEARVTLVDV 81
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 43-74 7.62e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 40.15  E-value: 7.62e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1418394052  43 GAKVLDIGCGSGAIAVLMVRVHGAAHVTGIDV 74
Cdd:PRK09328  109 PLRVLDLGTGSGAIALALAKERPDAEVTAVDI 140
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
34-73 8.84e-04

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 39.84  E-value: 8.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1418394052  34 RVLDGV-DLTGAKVLDIGCGSGAIAVLMVRvHGAAHVTGID 73
Cdd:PRK15068  113 RVLPHLsPLKGRTVLDVGCGNGYHMWRMLG-AGAKLVVGID 152
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
34-74 1.10e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 39.25  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1418394052  34 RVLDGVDLTGAKVLDIGCGSGAIAVLMVRvHGAAHVTGIDV 74
Cdd:COG4076    27 AAIERVVKPGDVVLDIGTGSGLLSMLAAR-AGAKKVYAVEV 66
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 43-147 1.64e-03

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 37.69  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  43 GAKVLDIGCGSGAIAVLMVRVHGAAHVTGIDVEDPVCAAARARATAAGLAGQITIDKVTPGPFPYPDQSFDVVFSKDSII 122
Cdd:TIGR02469  20 GDVLWDIGAGTGSVTIEAARLVPNGRVYAIERNPEALDLIERNLRRFGVSNIVIVEGDAPEAPEALLPDPDAVFVGGSGG 99

                          90       100
                  ....*....|....*....|....*
gi 1418394052 123 HIpdkEALAAEVFRVLKPGGVFAAS 147
Cdd:TIGR02469 100 LL---QEILEAVERRLRPGGRIVLN 121
PLN02233 PLN02233
ubiquinone biosynthesis methyltransferase
 39-141 1.95e-03

ubiquinone biosynthesis methyltransferase


Pssm-ID: 177877 [Multi-domain]  Cd Length: 261  Bit Score: 38.72  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  39 VDLTGAK----VLDIGCGSGAIAVLMV-RVHGAAHVTGIDVEDPVCAAARARATAAGLAGQITIDKVTPGP--FPYPDQS 111
Cdd:PLN02233   66 VSWSGAKmgdrVLDLCCGSGDLAFLLSeKVGSDGKVMGLDFSSEQLAVAASRQELKAKSCYKNIEWIEGDAtdLPFDDCY 145

                          90       100       110
                  ....*....|....*....|....*....|
gi 1418394052 112 FDVVFSKDSIIHIPDKEALAAEVFRVLKPG 141
Cdd:PLN02233  146 FDAITMGYGLRNVVDRLKAMQEMYRVLKPG 175
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
40-77 2.73e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 37.96  E-value: 2.73e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1418394052  40 DLTGAKVLDIGCGSG--AIAVLMVrvhGAAHVTGIDVeDP 77
Cdd:COG2263    43 DIEGKTVLDLGCGTGmlAIGAALL---GAKKVVGVDI-DP 78
PRK14967 PRK14967
putative methyltransferase; Provisional
 33-74 2.87e-03

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 38.11  E-value: 2.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1418394052  33 ARVLDGVDL-TGAKVLDIGCGSGAIAVLMVRVhGAAHVTGIDV 74
Cdd:PRK14967   26 ADALAAEGLgPGRRVLDLCTGSGALAVAAAAA-GAGSVTAVDI 67
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 27-132 4.11e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 37.51  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418394052  27 GGQDEVARVL----DGVDLTGAKVLDIGCGSGAIAVLMVRvHGaAHVTGIDVEDPVCAAARARATAAGLAGQIT-----I 97
Cdd:PRK07580   44 GHQRMRDTVLswlpADGDLTGLRILDAGCGVGSLSIPLAR-RG-AKVVASDISPQMVEEARERAPEAGLAGNITfevgdL 121

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1418394052  98 DKVTpGpfpypdqSFDVVFSKDSIIHIPDKEALAA 132
Cdd:PRK07580  122 ESLL-G-------RFDTVVCLDVLIHYPQEDAARM 148
PCMT pfam01135
Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT);
32-73 4.81e-03

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


Pssm-ID: 395902 [Multi-domain]  Cd Length: 205  Bit Score: 37.35  E-value: 4.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1418394052  32 VARVLDGVDLT-GAKVLDIGCGSGAIAVLMVRVHGA-AHVTGID 73
Cdd:pfam01135  62 HAMMLELLELKpGMRVLEIGSGSGYLTACFARMVGEvGRVVSIE 105
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 32-74 5.06e-03

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


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 36.99  E-value: 5.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1418394052  32 VARVLDGVDLT-GAKVLDIGCGSGAIAVLMVRVhgAAHVTGIDV 74
Cdd:COG2518    55 VARMLEALDLKpGDRVLEIGTGSGYQAAVLARL--AGRVYSVER 96
PRK14968 PRK14968
putative methyltransferase; Provisional
 33-74 5.38e-03

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 36.80  E-value: 5.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1418394052  33 ARVLDGVDltGAKVLDIGCGSGAIAVLMVRvhGAAHVTGIDV 74
Cdd:PRK14968   16 AENAVDKK--GDRVLEVGTGSGIVAIVAAK--NGKKVVGVDI 53
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 32-74 6.05e-03

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: 37.46  E-value: 6.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1418394052  32 VARVLDGVDLTGAK-VLDIGCGSGAIAVLMVRvhGAAHVTGIDV 74
Cdd:COG2265   222 YAAALEWLDLTGGErVLDLYCGVGTFALPLAR--RAKKVIGVEI 263
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
26-73 6.55e-03

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


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 36.72  E-value: 6.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1418394052  26 PGGQ-----DEVARVLDGVDLT-GAKVLDIGCGSGAIAVLMVRVhgAAHVTGID 73
Cdd:PRK00312   56 GCGQtisqpYMVARMTELLELKpGDRVLEIGTGSGYQAAVLAHL--VRRVFSVE 107
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 40-77 7.29e-03

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 37.22  E-value: 7.29e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1418394052  40 DLTGAKVLDIGCGS-GAIAVLMVRVHGAAHVTGIDVEDP 77
Cdd:cd08232   163 DLAGKRVLVTGAGPiGALVVAAARRAGAAEIVATDLADA 201
 
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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