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Conserved domains on  [gi|2177571864|ref|WP_234350375|]
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trans-aconitate 2-methyltransferase [Streptomyces sp. WM4235]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11467871)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
27-121 2.26e-21

Trans-aconitate methyltransferase [Energy production and conversion];


:

Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 85.26  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  27 PPRTALEIGAGTGKATRLFARR--GVAVTATEPDGAMLAELRKHVPaHVRAVRAAFEDVREGERYGLVYAAAALHW-TTP 103
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLP-NVRFVVADLRDLDPPEPFDLVVSNAALHWlPDH 79

                          90
                  ....*....|....*...
gi 2177571864 104 QGRWSRMAGLLEPGGVFA 121
Cdd:COG4106    80 AALLARLAAALAPGGVLA 97
 
Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
27-121 2.26e-21

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 85.26  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  27 PPRTALEIGAGTGKATRLFARR--GVAVTATEPDGAMLAELRKHVPaHVRAVRAAFEDVREGERYGLVYAAAALHW-TTP 103
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLP-NVRFVVADLRDLDPPEPFDLVVSNAALHWlPDH 79

                          90
                  ....*....|....*...
gi 2177571864 104 QGRWSRMAGLLEPGGVFA 121
Cdd:COG4106    80 AALLARLAAALAPGGVLA 97
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 32-118 2.96e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.04  E-value: 2.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  32 LEIGAGTGKATRLFARRGVA-VTATEPDGAMLAELRKHVPAH---VRAVRAAFEDVR-EGERYGLVYAAAALHWTTPQGR 106
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAglnVEFVQGDAEDLPfPDGSFDLVVSSGVLHHLPDPDL 81

                          90
                  ....*....|....*
gi 2177571864 107 ---WSRMAGLLEPGG 118
Cdd:pfam13649  82 eaaLREIARVLKPGG 96
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 14-124 9.59e-10

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: 56.91  E-value: 9.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  14 DRLFDMVAAYAGHPPRTALEIGAGTGKATRLFARRGVAVTATEPDGA--MLAELRKHVPAHVRAVRAAFED-VREGERYG 90
Cdd:TIGR02072  21 KRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISagMLAQAKTKLSENVQFICGDAEKlPLEDSSFD 100

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2177571864  91 LVYAAAALHW-TTPQGRWSRMAGLLEPGGV--FASFG 124
Cdd:TIGR02072 101 LIVSNLALQWcDDLSQALSELARVLKPGGLlaFSTFG 137
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 6-121 1.57e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 48.02  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864   6 ERFRPGYpdrlfDMVAAYAGHPPRTALEIGAGTGKATRLFARR--GVAVTATEPDGAMLAELRKHVPaHVRAVRAAFEDV 83
Cdd:PRK01683   15 ERTRPAR-----DLLARVPLENPRYVVDLGCGPGNSTELLVERwpAARITGIDSSPAMLAEARSRLP-DCQFVEADIASW 88

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2177571864  84 REGERYGLVYAAAALHWTTP-QGRWSRMAGLLEPGGVFA 121
Cdd:PRK01683   89 QPPQALDLIFANASLQWLPDhLELFPRLVSLLAPGGVLA 127
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 30-120 4.15e-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: 41.65  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  30 TALEIGAGTGKATRLFARRGVA-VTATEPDGAMLAELRK------HVPAHVRAVRAAFEDVREGERYGLVYAAAALHWTT 102
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKaaaallADNVEVLKGDAEELPPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|
gi 2177571864 103 P-QGRW-SRMAGLLEPGGVF 120
Cdd:cd02440    81 EdLARFlEEARRLLKPGGVL 100
rADc smart00650
Ribosomal RNA adenine dimethylases;
20-72 1.33e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 41.34  E-value: 1.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2177571864   20 VAAYAGHPPRTALEIGAGTGKATRLFARRGVAVTATEPDGAMLAELRKHVPAH 72
Cdd:smart00650   6 VRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAA 58
 
Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
27-121 2.26e-21

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 85.26  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  27 PPRTALEIGAGTGKATRLFARR--GVAVTATEPDGAMLAELRKHVPaHVRAVRAAFEDVREGERYGLVYAAAALHW-TTP 103
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARARARLP-NVRFVVADLRDLDPPEPFDLVVSNAALHWlPDH 79

                          90
                  ....*....|....*...
gi 2177571864 104 QGRWSRMAGLLEPGGVFA 121
Cdd:COG4106    80 AALLARLAAALAPGGVLA 97
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 14-120 1.04e-15

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: 71.20  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  14 DRLFDMVAAYAGhPPRTALEIGAGTGKATRLFARRGVAVTATEPDGAMLAELRKHVPA-HVRAVRAAFEDV-REGERYGL 91
Cdd:COG2227    12 RRLAALLARLLP-AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIARERAAElNVDFVQGDLEDLpLEDGSFDL 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 2177571864  92 VYAAAALHWTTPQGRW-SRMAGLLEPGGVF 120
Cdd:COG2227    91 VICSEVLEHLPDPAALlRELARLLKPGGLL 120
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 5-141 4.54e-14

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


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 67.33  E-value: 4.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864   5 YERFRPGYpDRLFDMVAAYAGHPPRTALEIGAGTGKATRLFARRGVAVTATEPDGAMLAELRKHVPAH---VRAVRAAFE 81
Cdd:COG2226     1 FDRVAARY-DGREALLAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAglnVEFVVGDAE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2177571864  82 DVR-EGERYGLVYAAAALHWTT-PQGRWSRMAGLLEPGGVFAsFGGPFRLADPAVEEAVRAA 141
Cdd:COG2226    80 DLPfPDGSFDLVISSFVLHHLPdPERALAEIARVLKPGGRLV-VVDFSPPDLAELEELLAEA 140
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
1-121 1.39e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 64.25  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864   1 MAQAYERF---RPGY--PDRLFD-MVAAYAGHPPRTALEIGAGTGKATRLFARRGVAVTATEPDGAMLAELRKHvPAHVR 74
Cdd:COG4976    14 YADSYDAAlveDLGYeaPALLAEeLLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKAREK-GVYDR 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2177571864  75 AVRAAFEDVRE-GERYGLVYAAAALHWTTPQGRW-SRMAGLLEPGGVFA 121
Cdd:COG4976    93 LLVADLADLAEpDGRFDLIVAADVLTYLGDLAAVfAGVARALKPGGLFI 141
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 32-118 2.96e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.04  E-value: 2.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  32 LEIGAGTGKATRLFARRGVA-VTATEPDGAMLAELRKHVPAH---VRAVRAAFEDVR-EGERYGLVYAAAALHWTTPQGR 106
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGArVTGVDLSPEMLERARERAAEAglnVEFVQGDAEDLPfPDGSFDLVVSSGVLHHLPDPDL 81

                          90
                  ....*....|....*
gi 2177571864 107 ---WSRMAGLLEPGG 118
Cdd:pfam13649  82 eaaLREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 32-121 6.16e-11

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 57.29  E-value: 6.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  32 LEIGAGTGKATRLFARRGVAVTATEPDGAMLAELRKHVP-AHVRAVRAAFEDVR-EGERYGLVYAAAALHWTTPQGR-WS 108
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPrEGLTFVVGDAEDLPfPDNSFDLVLSSEVLHHVEDPERaLR 80

                          90
                  ....*....|...
gi 2177571864 109 RMAGLLEPGGVFA 121
Cdd:pfam08241  81 EIARVLKPGGILI 93
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 4-120 1.46e-10

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 58.77  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864   4 AYERFRPGYPDRLFDMVAAYAGH--PPRTALEIGAGTGKATRLFARR-GVAVTATEPDGAMLAELRKHVPA------HVR 74
Cdd:COG0500     1 PWDSYYSDELLPGLAALLALLERlpKGGRVLDLGCGTGRNLLALAARfGGRVIGIDLSPEAIALARARAAKaglgnvEFL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2177571864  75 AVRAAFEDVREGERYGLVYAAAALHWTTPQGR---WSRMAGLLEPGGVF 120
Cdd:COG0500    81 VADLAELDPLPAESFDLVVAFGVLHHLPPEERealLRELARALKPGGVL 129
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 14-124 9.59e-10

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: 56.91  E-value: 9.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  14 DRLFDMVAAYAGHPPRTALEIGAGTGKATRLFARRGVAVTATEPDGA--MLAELRKHVPAHVRAVRAAFED-VREGERYG 90
Cdd:TIGR02072  21 KRLLALLKEKGIFIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISagMLAQAKTKLSENVQFICGDAEKlPLEDSSFD 100

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2177571864  91 LVYAAAALHW-TTPQGRWSRMAGLLEPGGV--FASFG 124
Cdd:TIGR02072 101 LIVSNLALQWcDDLSQALSELARVLKPGGLlaFSTFG 137
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 32-120 1.11e-07

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 48.52  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  32 LEIGAGTGKATRLFAR--RGVAVTATEPDGAMLAELRKHVPA----HVRAVRAAFEDV--REGERYGLVYAAAALHWT-T 102
Cdd:pfam08242   1 LEIGCGTGTLLRALLEalPGLEYTGLDISPAALEAARERLAAlgllNAVRVELFQLDLgeLDPGSFDVVVASNVLHHLaD 80

                          90
                  ....*....|....*...
gi 2177571864 103 PQGRWSRMAGLLEPGGVF 120
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
PRK01683 PRK01683
trans-aconitate 2-methyltransferase; Provisional
 6-121 1.57e-06

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 234970  Cd Length: 258  Bit Score: 48.02  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864   6 ERFRPGYpdrlfDMVAAYAGHPPRTALEIGAGTGKATRLFARR--GVAVTATEPDGAMLAELRKHVPaHVRAVRAAFEDV 83
Cdd:PRK01683   15 ERTRPAR-----DLLARVPLENPRYVVDLGCGPGNSTELLVERwpAARITGIDSSPAMLAEARSRLP-DCQFVEADIASW 88

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2177571864  84 REGERYGLVYAAAALHWTTP-QGRWSRMAGLLEPGGVFA 121
Cdd:PRK01683   89 QPPQALDLIFANASLQWLPDhLELFPRLVSLLAPGGVLA 127
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 13-121 3.05e-05

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.99  E-value: 3.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  13 PDRLFDMVAAYAGHPP-RTALEIGAGTGKATRLFARR-GVAVTATEPDGAMLAELRKHVPAH-----VRAVRAAFEDVRE 85
Cdd:COG2230    36 QEAKLDLILRKLGLKPgMRVLDIGCGWGGLALYLARRyGVRVTGVTLSPEQLEYARERAAEAgladrVEVRLADYRDLPA 115

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2177571864  86 GERYGLVYAAAALHWTTPQGRW---SRMAGLLEPGGVFA 121
Cdd:COG2230   116 DGQFDAIVSIGMFEHVGPENYPayfAKVARLLKPGGRLL 154
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 30-120 4.15e-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: 41.65  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  30 TALEIGAGTGKATRLFARRGVA-VTATEPDGAMLAELRK------HVPAHVRAVRAAFEDVREGERYGLVYAAAALHWTT 102
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGArVTGVDISPVALELARKaaaallADNVEVLKGDAEELPPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|
gi 2177571864 103 P-QGRW-SRMAGLLEPGGVF 120
Cdd:cd02440    81 EdLARFlEEARRLLKPGGVL 100
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 5-120 5.14e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 42.42  E-value: 5.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864   5 YERFRPGYPDRLFDMVAAYaGHPPRTALEIGAGTGKATRLFARRGVAVTATEPDGAMLAELRKHVPAHVraVRAAFEDVR 84
Cdd:pfam13489   1 YAHQRERLLADLLLRLLPK-LPSPGRVLDFGCGTGIFLRLLRAQGFSVTGVDPSPIAIERALLNVRFDQ--FDEQEAAVP 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2177571864  85 EGeRYGLVYAAAALHWTTPQGRWSRMAG-LLEPGGVF 120
Cdd:pfam13489  78 AG-KFDVIVAREVLEHVPDPPALLRQIAaLLKPGGLL 113
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 1-121 5.70e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 43.14  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864   1 MAQAYERFRPgypdrLFDMVAAYAGHPPRTALEIGAGTGKATRLFARR--GVAVTATEPDGAMLAELRkhvPAHVRAVRA 78
Cdd:PRK14103    8 LAFADHRGRP-----FYDLLARVGAERARRVVDLGCGPGNLTRYLARRwpGAVIEALDSSPEMVAAAR---ERGVDARTG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2177571864  79 AFEDVREGERYGLVYAAAALHWTTPQG-RWSRMAGLLEPGGVFA 121
Cdd:PRK14103   80 DVRDWKPKPDTDVVVSNAALQWVPEHAdLLVRWVDELAPGSWIA 123
rADc smart00650
Ribosomal RNA adenine dimethylases;
20-72 1.33e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 41.34  E-value: 1.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2177571864   20 VAAYAGHPPRTALEIGAGTGKATRLFARRGVAVTATEPDGAMLAELRKHVPAH 72
Cdd:smart00650   6 VRAANLRPGDTVLEIGPGKGALTEELLERAKRVTAIEIDPRLAPRLREKFAAA 58
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 18-92 2.02e-04

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 41.65  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2177571864  18 DMVAAYAGHPPRTALEIGAGTGKATRLFARRGVAVTATEPDGAMLAELRKHVPAHVR-------AVRAAFEDVREGERYG 90
Cdd:COG0030    28 RIVDAAGITPGDTVLEIGPGLGALTRALLERAARVTAVEIDRRLAAILRETFAAYPNltviegdALKVDLPALAAGEPLK 107


                  ..
gi 2177571864  91 LV 92
Cdd:COG0030   108 VV 109
RrnaAD pfam00398
Ribosomal RNA adenine dimethylase;
30-69 3.59e-03

Ribosomal RNA adenine dimethylase;


Pssm-ID: 395321 [Multi-domain]  Cd Length: 263  Bit Score: 37.73  E-value: 3.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2177571864  30 TALEIGAGTGKATRLFARRGVAVTATEPDGAMLAELRKHV 69
Cdd:pfam00398  33 TVLEIGPGKGALTVILAKRAKQVVAIEIDPRLAKLLQKKL 72
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
29-67 4.99e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 37.19  E-value: 4.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2177571864  29 RTALEIGAGTGKATRLFARRGVAVTATEPDGAMLAELRK 67
Cdd:PRK14896   31 DPVLEIGPGKGALTDELAKRAKKVYAIELDPRLAEFLRD 69
 
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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