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Conserved domains on  [gi|384496105|gb|EIE86596|]
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hypothetical protein RO3G_11307 [Rhizopus delemar RA 99-880]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10614797)

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

CATH:  2.20.25.110
EC:  2.1.-.-|2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 79-170 3.53e-17

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


:

Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.52  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   79 VLDIGCGSGVWIMDMINDYpNCTYHGCDI----VDTTNKVLKID--QFTYSHGNIVKgLPYKDNTFDFVHMRFFIFALRA 152
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLspemLERARERAAEAglNVEFVQGDAED-LPFPDGSFDLVVSSGVLHHLPD 78

                          90
                  ....*....|....*...
gi 384496105  153 EEWPIAIKEAIRVVKPGG 170
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 79-170 3.53e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.52  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   79 VLDIGCGSGVWIMDMINDYpNCTYHGCDI----VDTTNKVLKID--QFTYSHGNIVKgLPYKDNTFDFVHMRFFIFALRA 152
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLspemLERARERAAEAglNVEFVQGDAED-LPFPDGSFDLVVSSGVLHHLPD 78

                          90
                  ....*....|....*...
gi 384496105  153 EEWPIAIKEAIRVVKPGG 170
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 67-180 9.73e-13

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 63.86  E-value: 9.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105  67 VCNSLDFEKGISVLDIGCGSGVWIMDMINDypNCTYHGCDI----VDTTNKVLKIDQF--TYSHGNIVKgLPYKDNTFDF 140
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDIspemLELARERAAEAGLnvEFVVGDAED-LPFPDGSFDL 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 384496105 141 VHMRFFIFALraEEWPIAIKEAIRVVKPGGMV---------------QFYEAGFE 180
Cdd:COG2226   91 VISSFVLHHL--PDPERALAEIARVLKPGGRLvvvdfsppdlaeleeLLAEAGFE 143
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 50-172 1.10e-10

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 60.17  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105  50 GQHFAYKELFggnllssvCNSLDFEKGISVLDIGCGSGVWIMDMINDYP---NCTyhGCDIvdtTNKVLKI--------- 117
Cdd:PRK00216  34 GLHRVWRRKT--------IKWLGVRPGDKVLDLACGTGDLAIALAKAVGktgEVV--GLDF---SEGMLAVgreklrdlg 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384496105 118 --DQFTYSHGNIVKgLPYKDNTFDFVHMRffiFALR-AEEWPIAIKEAIRVVKPGGMV 172
Cdd:PRK00216 101 lsGNVEFVQGDAEA-LPFPDNSFDAVTIA---FGLRnVPDIDKALREMYRVLKPGGRL 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 79-177 1.35e-10

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: 57.05  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105  79 VLDIGCGSGVWIMDMInDYPNCTYHGCDIVDTTNKVLKI-------DQFTYSHGNIVKGLPYKDNTFDFVHMRFFIFALR 151
Cdd:cd02440    2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKaaaallaDNVEVLKGDAEELPPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*...
gi 384496105 152 AEEWPIaIKEAIRVVKPGG--MVQFYEA 177
Cdd:cd02440   81 EDLARF-LEEARRLLKPGGvlVLTLVLA 107
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 62-174 1.05e-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: 42.66  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   62 NLLSSVCNSLDFEKgISVLDIGCGSGVWIMDMINDYPNCTYHGCDIVDTTNKVLKID---QFTYSHGNIVKgLPYKDNTF 138
Cdd:TIGR02072  22 RLLALLKEKGIFIP-ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKlseNVQFICGDAEK-LPLEDSSF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 384496105  139 DfvhmrfFIFALRAEEW----PIAIKEAIRVVKPGGMVQF 174
Cdd:TIGR02072 100 D------LIVSNLALQWcddlSQALSELARVLKPGGLLAF 133
 
Name Accession Description Interval E-value
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 79-170 3.53e-17

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 74.52  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   79 VLDIGCGSGVWIMDMINDYpNCTYHGCDI----VDTTNKVLKID--QFTYSHGNIVKgLPYKDNTFDFVHMRFFIFALRA 152
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLspemLERARERAAEAglNVEFVQGDAED-LPFPDGSFDLVVSSGVLHHLPD 78

                          90
                  ....*....|....*...
gi 384496105  153 EEWPIAIKEAIRVVKPGG 170
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 80-172 1.63e-14

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 67.30  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   80 LDIGCGSGVWIMDMINDYPNCTyhGCDI----VDTTNKVLKIDQFTYSHGNIVKgLPYKDNTFDFVHMRFFIFALraEEW 155
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVT--GVDIspemLELAREKAPREGLTFVVGDAED-LPFPDNSFDLVLSSEVLHHV--EDP 75

                          90
                  ....*....|....*..
gi 384496105  156 PIAIKEAIRVVKPGGMV 172
Cdd:pfam08241  76 ERALREIARVLKPGGIL 92
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 67-180 9.73e-13

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 63.86  E-value: 9.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105  67 VCNSLDFEKGISVLDIGCGSGVWIMDMINDypNCTYHGCDI----VDTTNKVLKIDQF--TYSHGNIVKgLPYKDNTFDF 140
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDIspemLELARERAAEAGLnvEFVVGDAED-LPFPDGSFDL 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 384496105 141 VHMRFFIFALraEEWPIAIKEAIRVVKPGGMV---------------QFYEAGFE 180
Cdd:COG2226   91 VISSFVLHHL--PDPERALAEIARVLKPGGRLvvvdfsppdlaeleeLLAEAGFE 143
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 50-172 1.10e-10

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 60.17  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105  50 GQHFAYKELFggnllssvCNSLDFEKGISVLDIGCGSGVWIMDMINDYP---NCTyhGCDIvdtTNKVLKI--------- 117
Cdd:PRK00216  34 GLHRVWRRKT--------IKWLGVRPGDKVLDLACGTGDLAIALAKAVGktgEVV--GLDF---SEGMLAVgreklrdlg 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 384496105 118 --DQFTYSHGNIVKgLPYKDNTFDFVHMRffiFALR-AEEWPIAIKEAIRVVKPGGMV 172
Cdd:PRK00216 101 lsGNVEFVQGDAEA-LPFPDNSFDAVTIA---FGLRnVPDIDKALREMYRVLKPGGRL 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 79-177 1.35e-10

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: 57.05  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105  79 VLDIGCGSGVWIMDMInDYPNCTYHGCDIVDTTNKVLKI-------DQFTYSHGNIVKGLPYKDNTFDFVHMRFFIFALR 151
Cdd:cd02440    2 VLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKaaaallaDNVEVLKGDAEELPPEADESFDVIISDPPLHHLV 80

                         90       100
                 ....*....|....*....|....*...
gi 384496105 152 AEEWPIaIKEAIRVVKPGG--MVQFYEA 177
Cdd:cd02440   81 EDLARF-LEEARRLLKPGGvlVLTLVLA 107
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 80-172 5.35e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 52.37  E-value: 5.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   80 LDIGCGSGVWIMDMINDYPNCTYHGCDI-----VDTTNKV-----LKIDQFTYSHGNIVKGLPykdNTFDFVHMRFFIFA 149
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDIspaalEAARERLaalglLNAVRVELFQLDLGELDP---GSFDVVVASNVLHH 77

                          90       100
                  ....*....|....*....|...
gi 384496105  150 LraEEWPIAIKEAIRVVKPGGMV 172
Cdd:pfam08242  78 L--ADPRAVLRNIRRLLKPGGVL 98
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 73-172 4.85e-08

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: 50.40  E-value: 4.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105  73 FEKGISVLDIGCGSGvWIMDMINDYpNCTYHGCDI----VDTTNKVLKIDQFTYSHGNIVKgLPYKDNTFDFVHMRFFIF 148
Cdd:COG2227   22 LPAGGRVLDVGCGTG-RLALALARR-GADVTGVDIspeaLEIARERAAELNVDFVQGDLED-LPLEDGSFDLVICSEVLE 98

                         90       100
                 ....*....|....*....|....
gi 384496105 149 ALRaeEWPIAIKEAIRVVKPGGMV 172
Cdd:COG2227   99 HLP--DPAALLRELARLLKPGGLL 120
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 55-170 9.03e-08

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 51.07  E-value: 9.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105  55 YKELFGGNLLSSVCNSLDFEKGISVLDIGCGSGVWIMDMINdYPNCTYHGCDIVDT-------TNKVLKIDQFTYSHGNI 127
Cdd:COG0500    6 YSDELLPGLAALLALLERLPKGGRVLDLGCGTGRNLLALAA-RFGGRVIGIDLSPEaialaraRAAKAGLGNVEFLVADL 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 384496105 128 VKGLPYKDNTFDFVHMRFFIFALRAEEWPIAIKEAIRVVKPGG 170
Cdd:COG0500   85 AELDPLPAESFDLVVAFGVLHHLPPEEREALLRELARALKPGG 127
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 74-170 7.00e-07

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 47.81  E-value: 7.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   74 EKGISVLDIGCGSGVWIMDMinDYPNCTYHGCDIVDttNKVLKIDQFTYSHGNIVKGLPYKDNTFDFVHMRFFIFALRAe 153
Cdd:pfam13489  21 PSPGRVLDFGCGTGIFLRLL--RAQGFSVTGVDPSP--IAIERALLNVRFDQFDEQEAAVPAGKFDVIVAREVLEHVPD- 95

                          90
                  ....*....|....*..
gi 384496105  154 eWPIAIKEAIRVVKPGG 170
Cdd:pfam13489  96 -PPALLRQIAALLKPGG 111
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
75-172 2.43e-06

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 47.43  E-value: 2.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   75 KGISVLDIGCGSGVWIMDMINDY-PNCTYHGCDIVDTTNKVLK-------IDQFTYSHGNIVKgLPYKDNTFDFVHMRFf 146
Cdd:pfam01209  42 RGNKFLDVAGGTGDWTFGLSDSAgSSGKVVGLDINENMLKEGEkkakeegKYNIEFLQGNAEE-LPFEDDSFDIVTISF- 119

                          90       100
                  ....*....|....*....|....*..
gi 384496105  147 ifALR-AEEWPIAIKEAIRVVKPGGMV 172
Cdd:pfam01209 120 --GLRnFPDYLKVLKEAFRVLKPGGRV 144
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 74-170 2.63e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 46.26  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   74 EKGISVLDIGCGSGVWIMDMI-NDYPNCTYHGCDI------VDTTN-KVLKIDQFTYSHGNIVK-GLPYKDNTFDFVHMR 144
Cdd:pfam13847   2 DKGMRVLDLGCGTGHLSFELAeELGPNAEVVGIDIseeaieKARENaQKLGFDNVEFEQGDIEElPELLEDDKFDVVISN 81

                          90       100
                  ....*....|....*....|....*.
gi 384496105  145 FFIFALRAEewPIAIKEAIRVVKPGG 170
Cdd:pfam13847  82 CVLNHIPDP--DKVLQEILRVLKPGG 105
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
 79-174 2.09e-05

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 43.82  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   79 VLDIGCGSGVWIMDMINDYPNCTYHGCDI-VDTTNKVL-KIDQ-----FTYSHGNIVKGLPY--KDNTFDFVHMrFF--- 146
Cdd:pfam02390   5 FLEIGCGMGGFLVAMAKANPDKNFIGIEIrVPGVAKALkKIDAlglqnLRILCGNALDVLPNyfPPGSLQKIFI-NFpdp 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 384496105  147 IFALRAEEWPIA----IKEAIRVVKPGGMVQF 174
Cdd:pfam02390  84 WPKKRHHKRRLLqpefLKEYARVLKPGGVLHL 115
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 62-174 1.05e-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: 42.66  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   62 NLLSSVCNSLDFEKgISVLDIGCGSGVWIMDMINDYPNCTYHGCDIVDTTNKVLKID---QFTYSHGNIVKgLPYKDNTF 138
Cdd:TIGR02072  22 RLLALLKEKGIFIP-ASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKlseNVQFICGDAEK-LPLEDSSF 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 384496105  139 DfvhmrfFIFALRAEEW----PIAIKEAIRVVKPGGMVQF 174
Cdd:TIGR02072 100 D------LIVSNLALQWcddlSQALSELARVLKPGGLLAF 133
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
78-174 5.45e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 38.27  E-value: 5.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105  78 SVLDIGCGSGVWIMDMINDYPNCTYHGCDI----VDTTNKVLkiDQFTYSHGNIVKGLPykDNTFDFVHMRFFIFALraE 153
Cdd:COG4106    4 RVLDLGCGTGRLTALLAERFPGARVTGVDLspemLARARARL--PNVRFVVADLRDLDP--PEPFDLVVSNAALHWL--P 77

                         90       100
                 ....*....|....*....|...
gi 384496105 154 EWPIAIKEAIRVVKPGG--MVQF 174
Cdd:COG4106   78 DHAALLARLAAALAPGGvlAVQV 100
metW TIGR02081
methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that ...
 74-167 5.03e-03

methionine biosynthesis protein MetW; This protein is found alongside MetX, of the enzyme that acylates homoserine as a first step toward methionine biosynthesis, in many species. It appears to act in methionine biosynthesis but is not fully characterized. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273958  Cd Length: 194  Bit Score: 36.96  E-value: 5.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384496105   74 EKGISVLDIGCGSGVwIMDMINDYPNCTYHGCDIvdTTNKVLKIDQFTYS--HGNIVKGLP-YKDNTFDFVHMRffiFAL 150
Cdd:TIGR02081  12 PPGSRVLDLGCGDGE-LLALLRDEKQVRGYGIEI--DQDGVLACVARGVNviQGDLDEGLEaFPDKSFDYVILS---QTL 85

                          90
                  ....*....|....*...
gi 384496105  151 RAEEWPIAI-KEAIRVVK 167
Cdd:TIGR02081  86 QATRNPEEIlDEMLRVGR 103
 
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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