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Conserved domains on  [gi|1308682697|gb|PKM52701|]
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class I SAM-dependent methyltransferase [Firmicutes bacterium HGW-Firmicutes-7]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10789277)

class I SAM-dependent methyltransferase is an enzyme that uses S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyl transfer, creating the product S-adenosyl-L-homocysteine (AdoHcy)

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047
PubMed:  12826405
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 40-145 2.68e-17

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


:

Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 75.03  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  40 INDGMVILEIGCSDGHNLSQLTKdRKCVAYGIDPSQDAIKDGKHRFPD----LKLMVGTADELNLPDESIDIVIFGFCLY 115
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDLPFPDGSFDLVISSFVLH 98

                          90       100       110
                  ....*....|....*....|....*....|
gi 1308682697 116 LVDRklLAKVVAETDRVTKDNAYVGITDFD 145
Cdd:COG2226    99 HLPD--PERALAEIARVLKPGGRLVVVDFS 126
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 40-145 2.68e-17

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 75.03  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  40 INDGMVILEIGCSDGHNLSQLTKdRKCVAYGIDPSQDAIKDGKHRFPD----LKLMVGTADELNLPDESIDIVIFGFCLY 115
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDLPFPDGSFDLVISSFVLH 98

                          90       100       110
                  ....*....|....*....|....*....|
gi 1308682697 116 LVDRklLAKVVAETDRVTKDNAYVGITDFD 145
Cdd:COG2226    99 HLPD--PERALAEIARVLKPGGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-136 1.98e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 68.74  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  46 ILEIGCSDGHNLSQLTKDRKCVAYGIDPSQDAIKDGKHRF----PDLKLMVGTADELNLPDESIDIVIFGFCLYLVDRKL 121
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*
gi 1308682697 122 LAKVVAETDRVTKDN 136
Cdd:pfam13649  81 LEAALREIARVLKPG 95
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 46-142 2.56e-08

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 52.61  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  46 ILEIGCSDG---HNLSQ-LTKDRKCVAYGIDPSQDAIKDGKHRFPDLKLMVGTADELNLPDESIDIV--IFGFCLylvdr 119
Cdd:PRK11088   89 LLDIGCGEGyytHALADaLPEITTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIirIYAPCK----- 163

                          90       100
                  ....*....|....*....|...
gi 1308682697 120 kllakvVAETDRVTKDNAYVgIT 142
Cdd:PRK11088  164 ------AEELARVVKPGGIV-IT 179
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 46-146 5.64e-06

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: 43.96  E-value: 5.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  46 ILEIGCSDGHNLSQLTKDRKCVAYGIDPSQDAIKDGK-----HRFPDLKLMVGTADELNL-PDESIDIVIFGFCLYLVDR 119
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARkaaaaLLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*..
gi 1308682697 120 kLLAKVVAETDRVTKDNAYVGITDFDV 146
Cdd:cd02440    82 -DLARFLEEARRLLKPGGVLVLTLVLA 107
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 40-145 2.68e-17

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 75.03  E-value: 2.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  40 INDGMVILEIGCSDGHNLSQLTKdRKCVAYGIDPSQDAIKDGKHRFPD----LKLMVGTADELNLPDESIDIVIFGFCLY 115
Cdd:COG2226    20 LRPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEaglnVEFVVGDAEDLPFPDGSFDLVISSFVLH 98

                          90       100       110
                  ....*....|....*....|....*....|
gi 1308682697 116 LVDRklLAKVVAETDRVTKDNAYVGITDFD 145
Cdd:COG2226    99 HLPD--PERALAEIARVLKPGGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 46-136 1.98e-15

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 68.74  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  46 ILEIGCSDGHNLSQLTKDRKCVAYGIDPSQDAIKDGKHRF----PDLKLMVGTADELNLPDESIDIVIFGFCLYLVDRKL 121
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAaeagLNVEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPDPD 80

                          90
                  ....*....|....*
gi 1308682697 122 LAKVVAETDRVTKDN 136
Cdd:pfam13649  81 LEAALREIARVLKPG 95
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-139 7.16e-13

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 62.30  E-value: 7.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  47 LEIGCSDGHNLSQLTKdRKCVAYGIDPSQDAIKDGKHRFPD--LKLMVGTADELNLPDESIDIVIFGFCLYLVDRklLAK 124
Cdd:pfam08241   1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPRegLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVED--PER 77

                          90
                  ....*....|....*
gi 1308682697 125 VVAETDRVTKDNAYV 139
Cdd:pfam08241  78 ALREIARVLKPGGIL 92
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 37-145 7.93e-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: 60.03  E-value: 7.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  37 KKYINDGMVILEIGCSDGHNLSQLtKDRKCVAYGIDPSQDAIKDGKHRFPDLKL--MVGTADELNLPDESIDIVIFGFCL 114
Cdd:COG2227    19 ARLLPAGGRVLDVGCGTGRLALAL-ARRGADVTGVDISPEALEIARERAAELNVdfVQGDLEDLPLEDGSFDLVICSEVL 97

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1308682697 115 YLVDRklLAKVVAETDRVTKDNAYVGITDFD 145
Cdd:COG2227    98 EHLPD--PAALLRELARLLKPGGLLLLSTPN 126
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 46-145 1.41e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 55.69  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  46 ILEIGCSDGHNLSQLTK-DRKCVaYGIDPSQDAIKDGKHRFPDLKL-----MVGTADELN-LPDESIDIVIFGFCLYLVD 118
Cdd:COG0500    30 VLDLGCGTGRNLLALAArFGGRV-IGIDLSPEAIALARARAAKAGLgnvefLVADLAELDpLPAESFDLVVAFGVLHHLP 108

                          90       100
                  ....*....|....*....|....*..
gi 1308682697 119 RKLLAKVVAETDRVTKDNAYVGITDFD 145
Cdd:COG0500   109 PEEREALLRELARALKPGGVLLLSASD 135
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
46-127 7.55e-09

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 51.36  E-value: 7.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  46 ILEIGCSDGHNLSQLTK-DRKCVAYGIDPSQDAIKDGKHRFPDLKLMVGTADELNlPDESIDIVIFGFCLYLVD--RKLL 122
Cdd:COG4106     5 VLDLGCGTGRLTALLAErFPGARVTGVDLSPEMLARARARLPNVRFVVADLRDLD-PPEPFDLVVSNAALHWLPdhAALL 83


                  ....*
gi 1308682697 123 AKVVA 127
Cdd:COG4106    84 ARLAA 88
rrmA PRK11088
23S rRNA methyltransferase A; Provisional
 46-142 2.56e-08

23S rRNA methyltransferase A; Provisional


Pssm-ID: 236841 [Multi-domain]  Cd Length: 272  Bit Score: 52.61  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  46 ILEIGCSDG---HNLSQ-LTKDRKCVAYGIDPSQDAIKDGKHRFPDLKLMVGTADELNLPDESIDIV--IFGFCLylvdr 119
Cdd:PRK11088   89 LLDIGCGEGyytHALADaLPEITTMQLFGLDISKVAIKYAAKRYPQVTFCVASSHRLPFADQSLDAIirIYAPCK----- 163

                          90       100
                  ....*....|....*....|...
gi 1308682697 120 kllakvVAETDRVTKDNAYVgIT 142
Cdd:PRK11088  164 ------AEELARVVKPGGIV-IT 179
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 47-139 5.74e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 46.21  E-value: 5.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  47 LEIGCSDGHNLSQLTKDRKCVAY-GIDPSQDAIKDGKHRFPDLKLMVGTA------DELNLPDESIDIVIFGFCL-YLVD 118
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYtGLDISPAALEAARERLAALGLLNAVRvelfqlDLGELDPGSFDVVVASNVLhHLAD 80

                          90       100
                  ....*....|....*....|.
gi 1308682697 119 RKllaKVVAETDRVTKDNAYV 139
Cdd:pfam08242  81 PR---AVLRNIRRLLKPGGVL 98
PRK08317 PRK08317
hypothetical protein; Provisional
 46-145 1.54e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 47.24  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  46 ILEIGCSDGHNLSQLtKDRKCV---AYGIDPSQDAIKDGKHRF----PDLKLMVGTADELNLPDESIDIVIfgfclylVD 118
Cdd:PRK08317   23 VLDVGCGPGNDAREL-ARRVGPegrVVGIDRSEAMLALAKERAaglgPNVEFVRGDADGLPFPDGSFDAVR-------SD 94

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1308682697 119 RKL-----LAKVVAETDRVTKDNAYVGITDFD 145
Cdd:PRK08317   95 RVLqhledPARALAEIARVLRPGGRVVVLDTD 126
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 68-144 4.24e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 45.91  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  68 AYGIDPSQDAIKDGKHRFPD------LKLMVGTADELNLPDESIDIVIFGFCLY-LVDRKllaKVVAETDRVTKDNAYVG 140
Cdd:PRK00216   79 VVGLDFSEGMLAVGREKLRDlglsgnVEFVQGDAEALPFPDNSFDAVTIAFGLRnVPDID---KALREMYRVLKPGGRLV 155


                  ....
gi 1308682697 141 ITDF 144
Cdd:PRK00216  156 ILEF 159
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 46-146 5.64e-06

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: 43.96  E-value: 5.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  46 ILEIGCSDGHNLSQLTKDRKCVAYGIDPSQDAIKDGK-----HRFPDLKLMVGTADELNL-PDESIDIVIFGFCLYLVDR 119
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARkaaaaLLADNVEVLKGDAEELPPeADESFDVIISDPPLHHLVE 81

                          90       100
                  ....*....|....*....|....*..
gi 1308682697 120 kLLAKVVAETDRVTKDNAYVGITDFDV 146
Cdd:cd02440    82 -DLARFLEEARRLLKPGGVLVLTLVLA 107
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 40-145 1.48e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.48  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  40 INDGMVILEIGCSDGHNLSQL-TKDR-KCVAYGIDPSQDAIKDGKHR-----FPDLKLMVGTADEL--NLPDESIDIVI- 109
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELaEELGpNAEVVGIDISEEAIEKARENaqklgFDNVEFEQGDIEELpeLLEDDKFDVVIs 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1308682697 110 FGFCLYLVDrklLAKVVAETDRVTKDNAYVGITDFD 145
Cdd:pfam13847  81 NCVLNHIPD---PDKVLQEILRVLKPGGRLIISDPD 113
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-143 3.32e-04

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 39.53  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  40 INDGMVILEIGCSDGHNLSQLTKDRKCVAYGIDPSQDAIKDGKHRFPDLKL----MVGTADELNLP-DESIDIVIFGFCL 114
Cdd:COG2230    49 LKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLadrvEVRLADYRDLPaDGQFDAIVSIGMF 128

                          90       100
                  ....*....|....*....|....*....
gi 1308682697 115 YLVDRKLLAKVVAETDRVTKDNAYVGITD 143
Cdd:COG2230   129 EHVGPENYPAYFAKVARLLKPGGRLLLHT 157
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 38-109 3.82e-03

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


Pssm-ID: 399779  Cd Length: 193  Bit Score: 37.05  E-value: 3.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1308682697  38 KYINDGMVILEIGCSDGHNLSQLTKDRKCVAYGIDPSQDAIKDGKHRfpDLKLMVGTADE--LNLPDESIDIVI 109
Cdd:pfam07021   9 EWIPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAAGVAECVAK--GLYVIQGDLDEglEHFPDKSFDYVI 80
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
46-142 5.14e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 36.51  E-value: 5.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  46 ILEIGCSDGHNLSQLTKDRKCVAyGIDPSQDAIKDGKHRFPDLKLMVGTADELNLPDESIDIVI-FGFCLYLVDrklLAK 124
Cdd:COG4976    50 VLDLGCGTGLLGEALRPRGYRLT-GVDLSEEMLAKAREKGVYDRLLVADLADLAEPDGRFDLIVaADVLTYLGD---LAA 125

                          90
                  ....*....|....*...
gi 1308682697 125 VVAETDRVTKDNAYVGIT 142
Cdd:COG4976   126 VFAGVARALKPGGLFIFS 143
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-160 6.88e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 35.87  E-value: 6.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1308682697  39 YINDGMVILEIGCSDGHNLSQLtKDRKCVAYGIDPSQDAIkDGKHRFPDLKLMVgtADELNLPDESIDIVIFGFCLYLVD 118
Cdd:pfam13489  19 KLPSPGRVLDFGCGTGIFLRLL-RAQGFSVTGVDPSPIAI-ERALLNVRFDQFD--EQEAAVPAGKFDVIVAREVLEHVP 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1308682697 119 ------RKLLAKVvaetdrvtKDNAYVGITDFDVKIPRKRRYKHYEDI 160
Cdd:pfam13489  95 dppallRQIAALL--------KPGGLLLLSTPLASDEADRLLLEWPYL 134
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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