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Conserved domains on  [gi|1071575474|gb|OEP36894|]
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methyltransferase [Listeria monocytogenes]

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]; ...
 73-204 1.22e-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: 76.19  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  73 HLLDIGYGGGSNVKNLAELNknWTIYGVDISEESYKTATNLNKKAINNgtVKLSIQDVALMNYQADFFDLVYAIQTHMYW 152
Cdd:COG2226    25 RVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFPDGSFDLVISSFVLHHL 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1071575474 153 DNPQKGFEEIYRVMSQDGVLILssekdkIDYHMDEyktTASLTALLKEIGFR 204
Cdd:COG2226   101 PDPERALAEIARVLKPGGRLVV------VDFSPPD---LAELEELLAEAGFE 143
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 73-204 1.22e-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: 76.19  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  73 HLLDIGYGGGSNVKNLAELNknWTIYGVDISEESYKTATNLNKKAINNgtVKLSIQDVALMNYQADFFDLVYAIQTHMYW 152
Cdd:COG2226    25 RVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFPDGSFDLVISSFVLHHL 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1071575474 153 DNPQKGFEEIYRVMSQDGVLILssekdkIDYHMDEyktTASLTALLKEIGFR 204
Cdd:COG2226   101 PDPERALAEIARVLKPGGRLVV------VDFSPPD---LAELEELLAEAGFE 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-174 1.39e-17

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 74.62  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  75 LDIGYGGGSNVKNLAELNKNwtIYGVDISEESYKTAtnlnKKAINNGTVKLSIQDVALMNYQADFFDLVYAIQTHMYWDN 154
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR--VTGVDISPEMLELA----REKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVED 74

                          90       100
                  ....*....|....*....|
gi 1071575474 155 PQKGFEEIYRVMSQDGVLIL 174
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
PRK08317 PRK08317
hypothetical protein; Provisional
 75-175 4.54e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.56  E-value: 4.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  75 LDIGYGGGSNVKNLA-ELNKNWTIYGVDISEESYKTATNlnKKAINNGTVKLSIQDVALMNYQADFFDLVYAIQTHMYWD 153
Cdd:PRK08317   24 LDVGCGPGNDARELArRVGPEGRVVGIDRSEAMLALAKE--RAAGLGPNVEFVRGDADGLPFPDGSFDAVRSDRVLQHLE 101

                          90       100
                  ....*....|....*....|..
gi 1071575474 154 NPQKGFEEIYRVMSQDGVLILS 175
Cdd:PRK08317  102 DPARALAEIARVLRPGGRVVVL 123
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-178 1.38e-05

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: 42.80  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  74 LLDIGYGGGSNVKNLAELNKnWTIYGVDISEESYKTATNLNKKAINNGtVKLSIQDVALMNYQAD-FFDLVYAIQTHMYW 152
Cdd:cd02440     2 VLDLGCGTGALALALASGPG-ARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELPPEADeSFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|....*..
gi 1071575474 153 -DNPQKGFEEIYRVMSQDGVLILSSEK 178
Cdd:cd02440    80 vEDLARFLEEARRLLKPGGVLVLTLVL 106
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 65-176 1.01e-04

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: 41.89  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  65 NTELSNVNHLLDIGYGGGSNVKNLAELNKNWTIYGVDISEESYKTATNLNKKAINngtvklSIQ-DVALMNYQADFFDLV 143
Cdd:TIGR02072  29 EKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSENVQ------FICgDAEKLPLEDSSFDLI 102

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1071575474 144 Y---AIQthmyW-DNPQKGFEEIYRVMSQDGVLILSS 176
Cdd:TIGR02072 103 VsnlALQ----WcDDLSQALSELARVLKPGGLLAFST 135
 
Name Accession Description Interval E-value
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 73-204 1.22e-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: 76.19  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  73 HLLDIGYGGGSNVKNLAELNknWTIYGVDISEESYKTATNLNKKAINNgtVKLSIQDVALMNYQADFFDLVYAIQTHMYW 152
Cdd:COG2226    25 RVLDLGCGTGRLALALAERG--ARVTGVDISPEMLELARERAAEAGLN--VEFVVGDAEDLPFPDGSFDLVISSFVLHHL 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1071575474 153 DNPQKGFEEIYRVMSQDGVLILssekdkIDYHMDEyktTASLTALLKEIGFR 204
Cdd:COG2226   101 PDPERALAEIARVLKPGGRLVV------VDFSPPD---LAELEELLAEAGFE 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-174 1.39e-17

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 74.62  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  75 LDIGYGGGSNVKNLAELNKNwtIYGVDISEESYKTAtnlnKKAINNGTVKLSIQDVALMNYQADFFDLVYAIQTHMYWDN 154
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGAR--VTGVDISPEMLELA----REKAPREGLTFVVGDAEDLPFPDNSFDLVLSSEVLHHVED 74

                          90       100
                  ....*....|....*....|
gi 1071575474 155 PQKGFEEIYRVMSQDGVLIL 174
Cdd:pfam08241  75 PERALREIARVLKPGGILII 94
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 75-172 1.78e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 61.23  E-value: 1.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  75 LDIGYGGGSNVKNLAELNKNWTIYGVDISEESYKTATNLNKKAINNGTVKLSIQDVALMNYQADFFDLVYAIQTHMYWDN 154
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGELDPGSFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 1071575474 155 PQKGFEEIYRVMSQDGVL 172
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 75-170 5.34e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 59.88  E-value: 5.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  75 LDIGYGGGSNVKNLAELNkNWTIYGVDISEESYKTATNLNKKAINNgtVKLSIQDVALMNYQADFFDLVYAIQTHMYWDN 154
Cdd:pfam13649   2 LDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGLN--VEFVQGDAEDLPFPDGSFDLVVSSGVLHHLPD 78

                          90
                  ....*....|....*...
gi 1071575474 155 PQ--KGFEEIYRVMSQDG 170
Cdd:pfam13649  79 PDleAALREIARVLKPGG 96
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 73-175 2.17e-11

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: 59.26  E-value: 2.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  73 HLLDIGYGGGSNVKNLAELNknWTIYGVDISEESYKTAtnlnKKAINNGTVKLSIQDVALMNYQADFFDLVYAIQTHMYW 152
Cdd:COG2227    27 RVLDVGCGTGRLALALARRG--ADVTGVDISPEALEIA----RERAAELNVDFVQGDLEDLPLEDGSFDLVICSEVLEHL 100

                          90       100
                  ....*....|....*....|...
gi 1071575474 153 DNPQKGFEEIYRVMSQDGVLILS 175
Cdd:COG2227   101 PDPAALLRELARLLKPGGLLLLS 123
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 72-209 3.81e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 58.97  E-value: 3.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  72 NHLLDIGYGGGSNVKNLAE-LNKNWTIYGVDISEESYKTAT-NLNKKAINNgtVKLSIQDVALM--NYQADFFDLVYAIQ 147
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEeLGPNAEVVGIDISEEAIEKAReNAQKLGFDN--VEFEQGDIEELpeLLEDDKFDVVISNC 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1071575474 148 THMYWDNPQKGFEEIYRVMSQDGVLILSS-----EKDKIDYHMDEYKTTASLTALLKEIGFREVVEK 209
Cdd:pfam13847  83 VLNHIPDPDKVLQEILRVLKPGGRLIISDpdslaELPAHVKEDSTYYAGCVGGAILKKKLYELLEEA 149
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 73-176 1.73e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 54.55  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  73 HLLDIGYGGGSNVKNLAElNKNWTIYGVDISEESYKTATNLNKKAINNGTVKLSIQDVALMNYQaDFFDLVYAIQ--THM 150
Cdd:COG2230    54 RVLDIGCGWGGLALYLAR-RYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPAD-GQFDAIVSIGmfEHV 131

                          90       100
                  ....*....|....*....|....*.
gi 1071575474 151 YWDNPQKGFEEIYRVMSQDGVLILSS 176
Cdd:COG2230   132 GPENYPAYFAKVARLLKPGGRLLLHT 157
PRK08317 PRK08317
hypothetical protein; Provisional
 75-175 4.54e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.56  E-value: 4.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  75 LDIGYGGGSNVKNLA-ELNKNWTIYGVDISEESYKTATNlnKKAINNGTVKLSIQDVALMNYQADFFDLVYAIQTHMYWD 153
Cdd:PRK08317   24 LDVGCGPGNDARELArRVGPEGRVVGIDRSEAMLALAKE--RAAGLGPNVEFVRGDADGLPFPDGSFDAVRSDRVLQHLE 101

                          90       100
                  ....*....|....*....|..
gi 1071575474 154 NPQKGFEEIYRVMSQDGVLILS 175
Cdd:PRK08317  102 DPARALAEIARVLRPGGRVVVL 123
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 51-182 2.77e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 52.23  E-value: 2.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  51 WSSYFEDLSK-----WTISNTELSNVNHLLDIGYGGGSNVKNLAELNkNWTIYGVDISEESYKTATNLNKKAiNNGTVKL 125
Cdd:COG0500     2 WDSYYSDELLpglaaLLALLERLPKGGRVLDLGCGTGRNLLALAARF-GGRVIGIDLSPEAIALARARAAKA-GLGNVEF 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1071575474 126 SIQDVA-LMNYQADFFDLVYAIQTHmYWDNP---QKGFEEIYRVMSQDGVLILSSEKDKID 182
Cdd:COG0500    80 LVADLAeLDPLPAESFDLVVAFGVL-HHLPPeerEALLRELARALKPGGVLLLSASDAAAA 139
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
56-221 3.72e-08

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 51.54  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  56 EDLSKWTISNTELSNVNHLLDIGYGGGSNVKNLAELNKnwTIYGVDISEESyktatnLNKKAINNGTVKLSIQDVALMNY 135
Cdd:COG4976    32 ALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGY--RLTGVDLSEEM------LAKAREKGVYDRLLVADLADLAE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474 136 QADFFDLVYAIQTHMYWDNPQKGFEEIYRVMSQDGVLILSSEkdKIDYHMDEYKTTASLTALLKEIGFREvvekekgNWI 215
Cdd:COG4976   104 PDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVE--DADGSGRYAHSLDYVRDLLAAAGFEV-------PGL 174


                  ....*.
gi 1071575474 216 LYTVRK 221
Cdd:COG4976   175 LVVARK 180
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
73-175 1.74e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.90  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  73 HLLDIGYGGGSNVKNLAELNKNWTIYGVDISEESyktatnLNKKAINNGTVKLSIQDVALMNYQADfFDLVYAIQTHMYW 152
Cdd:COG4106     4 RVLDLGCGTGRLTALLAERFPGARVTGVDLSPEM------LARARARLPNVRFVVADLRDLDPPEP-FDLVVSNAALHWL 76

                          90       100
                  ....*....|....*....|...
gi 1071575474 153 DNPQKGFEEIYRVMSQDGVLILS 175
Cdd:COG4106    77 PDHAALLARLAAALAPGGVLAVQ 99
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 74-178 1.38e-05

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: 42.80  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  74 LLDIGYGGGSNVKNLAELNKnWTIYGVDISEESYKTATNLNKKAINNGtVKLSIQDVALMNYQAD-FFDLVYAIQTHMYW 152
Cdd:cd02440     2 VLDLGCGTGALALALASGPG-ARVTGVDISPVALELARKAAAALLADN-VEVLKGDAEELPPEADeSFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|....*..
gi 1071575474 153 -DNPQKGFEEIYRVMSQDGVLILSSEK 178
Cdd:cd02440    80 vEDLARFLEEARRLLKPGGVLVLTLVL 106
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-208 1.47e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 43.57  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  74 LLDIGYGGGSNVKNLAElnKNWTIYGVDISEEsyktatnlnKKAINNGTVKLSIQDVALMNYQADFFDLVYAIQT--HMy 151
Cdd:pfam13489  26 VLDFGCGTGIFLRLLRA--QGFSVTGVDPSPI---------AIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVleHV- 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1071575474 152 wDNPQKGFEEIYRVMSQDGVLILS-------SEKDKIDYHMDE-------YKTTASLTALLKEIGFrEVVE 208
Cdd:pfam13489  94 -PDPPALLRQIAALLKPGGLLLLStplasdeADRLLLEWPYLRprnghisLFSARSLKRLLEEAGF-EVVS 162
PTZ00098 PTZ00098
phosphoethanolamine N-methyltransferase; Provisional
 63-210 1.97e-05

phosphoethanolamine N-methyltransferase; Provisional


Pssm-ID: 173391 [Multi-domain]  Cd Length: 263  Bit Score: 44.19  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  63 ISNTELSNVNHLLDIGYGGGSNVKNLAElNKNWTIYGVDISEESYKTATNLNKkaiNNGTVKLSIQDVALMNYQADFFDL 142
Cdd:PTZ00098   45 LSDIELNENSKVLDIGSGLGGGCKYINE-KYGAHVHGVDICEKMVNIAKLRNS---DKNKIEFEANDILKKDFPENTFDM 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474 143 VYAIQT--HMYWDNPQKGFEEIYRVMSQDGVLILSSE-KDKIDYHMDEYK-----------TTASLTALLKEIGFREVVE 208
Cdd:PTZ00098  121 IYSRDAilHLSYADKKKLFEKCYKWLKPNGILLITDYcADKIENWDEEFKayikkrkytliPIQEYGDLIKSCNFQNVVA 200


                  ..
gi 1071575474 209 KE 210
Cdd:PTZ00098  201 KD 202
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 65-176 1.01e-04

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: 41.89  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071575474  65 NTELSNVNHLLDIGYGGGSNVKNLAELNKNWTIYGVDISEESYKTATNLNKKAINngtvklSIQ-DVALMNYQADFFDLV 143
Cdd:TIGR02072  29 EKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLSENVQ------FICgDAEKLPLEDSSFDLI 102

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1071575474 144 Y---AIQthmyW-DNPQKGFEEIYRVMSQDGVLILSS 176
Cdd:TIGR02072 103 VsnlALQ----WcDDLSQALSELARVLKPGGLLAFST 135
 
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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