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Conserved domains on  [gi|15597230|ref|NP_250724|]
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hypothetical protein PA2034 [Pseudomonas aeruginosa PAO1]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11423066)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Saccharomyces cerevisiae trans-aconitate 3-methyltransferase

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 27-137 6.94e-16

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


:

Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 73.03  E-value: 6.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230  27 HLLSRAQLLARLPERARLLSVGCGAGGELAELAGlRPGWRFVAADLSADMLALARQRCARLGlLERIELHCGDVAGLP-- 104
Cdd:COG0500  13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAA-RFGGRVIGIDLSPEAIALARARAAKAG-LGNVEFLVADLAELDpl 90

                        90       100       110
                ....*....|....*....|....*....|...
gi 15597230 105 PAPPCDAALVLLVLHFLrgDQAKRRFLEAVAER 137
Cdd:COG0500  91 PAESFDLVVAFGVLHHL--PPEEREALLRELAR 121
 
Name Accession Description Interval E-value
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 27-137 6.94e-16

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 73.03  E-value: 6.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230  27 HLLSRAQLLARLPERARLLSVGCGAGGELAELAGlRPGWRFVAADLSADMLALARQRCARLGlLERIELHCGDVAGLP-- 104
Cdd:COG0500  13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAA-RFGGRVIGIDLSPEAIALARARAAKAG-LGNVEFLVADLAELDpl 90

                        90       100       110
                ....*....|....*....|....*....|...
gi 15597230 105 PAPPCDAALVLLVLHFLrgDQAKRRFLEAVAER 137
Cdd:COG0500  91 PAESFDLVVAFGVLHHL--PPEEREALLRELAR 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 47-135 6.27e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 65.28  E-value: 6.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230    47 VGCGAGGELAELAGlRPGWRFVAADLSADMLALARQRCARLGLleRIELHCGDVAGLPPAP-PCDAALVLLVLHFLrGDQ 125
Cdd:pfam13649   4 LGCGTGRLTLALAR-RGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDgSFDLVVSSGVLHHL-PDP 79

                          90
                  ....*....|
gi 15597230   126 AKRRFLEAVA 135
Cdd:pfam13649  80 DLEAALREIA 89
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 43-137 5.25e-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: 54.74  E-value: 5.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230  43 RLLSVGCGAGGELAELAgLRPGWRFVAADLSADMLALARQRCARlGLLERIELHCGDVAGLPPAPP--CDAALVLLVLHF 120
Cdd:cd02440   1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAA-LLADNVEVLKGDAEELPPEADesFDVIISDPPLHH 78

                        90
                ....*....|....*..
gi 15597230 121 LRGDQakRRFLEAVAER 137
Cdd:cd02440  79 LVEDL--ARFLEEARRL 93
PRK08317 PRK08317
hypothetical protein; Provisional
 30-121 1.16e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 56.48  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230   30 SRAQLLARLPERArlLSVGCGAGGELAELAGL-RPGWRFVAADLSADMLALARQRCArlGLLERIELHCGDVAGLP-PAP 107
Cdd:PRK08317  11 TFELLAVQPGDRV--LDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALAKERAA--GLGPNVEFVRGDADGLPfPDG 86

                         90
                 ....*....|....
gi 15597230  108 PCDAALVLLVLHFL 121
Cdd:PRK08317  87 SFDAVRSDRVLQHL 100
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
43-122 2.31e-07

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 49.72  E-value: 2.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230     43 RLLSVGCGAGGELAELAGLRPGWRFVAADLSADMLALARQRCARLGLLERIELHCGDVAGLPPAPPCDAALVLLVLHFLR 122
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTYDLVFGFEVIHHIK 81
 
Name Accession Description Interval E-value
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 27-137 6.94e-16

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 73.03  E-value: 6.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230  27 HLLSRAQLLARLPERARLLSVGCGAGGELAELAGlRPGWRFVAADLSADMLALARQRCARLGlLERIELHCGDVAGLP-- 104
Cdd:COG0500  13 GLAALLALLERLPKGGRVLDLGCGTGRNLLALAA-RFGGRVIGIDLSPEAIALARARAAKAG-LGNVEFLVADLAELDpl 90

                        90       100       110
                ....*....|....*....|....*....|...
gi 15597230 105 PAPPCDAALVLLVLHFLrgDQAKRRFLEAVAER 137
Cdd:COG0500  91 PAESFDLVVAFGVLHHL--PPEEREALLRELAR 121
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
42-135 8.94e-15

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 67.54  E-value: 8.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230  42 ARLLSVGCGAGGELAELAGLRPGWRFVAADLSADMLALARQRcarlglLERIELHCGDVAGLPPAPPCDAALVLLVLHFL 121
Cdd:COG4106   3 RRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARAR------LPNVRFVVADLRDLDPPEPFDLVVSNAALHWL 76

                        90
                ....*....|....*.
gi 15597230 122 RgDQAK--RRFLEAVA 135
Cdd:COG4106  77 P-DHAAllARLAAALA 91
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 47-135 6.27e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 65.28  E-value: 6.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230    47 VGCGAGGELAELAGlRPGWRFVAADLSADMLALARQRCARLGLleRIELHCGDVAGLPPAP-PCDAALVLLVLHFLrGDQ 125
Cdd:pfam13649   4 LGCGTGRLTLALAR-RGGARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDgSFDLVVSSGVLHHL-PDP 79

                          90
                  ....*....|
gi 15597230   126 AKRRFLEAVA 135
Cdd:pfam13649  80 DLEAALREIA 89
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 36-137 1.06e-13

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 66.11  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230  36 ARLPERARLLSVGCGAGGeLAELAGLRPGWRFVAADLSADMLALARQRCARLGLLERIELHCGDVAGLPPAPPCDAALVL 115
Cdd:COG2230  47 LGLKPGMRVLDIGCGWGG-LALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLPADGQFDAIVSI 125

                        90       100
                ....*....|....*....|..
gi 15597230 116 LVLHFLrGDQAKRRFLEAVAER 137
Cdd:COG2230 126 GMFEHV-GPENYPAYFAKVARL 146
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 31-126 1.15e-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: 65.79  E-value: 1.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230  31 RAQLLARLPER--ARLLSVGCGAGGELAELAglRPGWRFVAADLSADMLALARQRCARLGLleRIELHCGDVAGLP-PAP 107
Cdd:COG2226  11 REALLAALGLRpgARVLDLGCGTGRLALALA--ERGARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPfPDG 86

                        90
                ....*....|....*....
gi 15597230 108 PCDAALVLLVLHFLRGDQA 126
Cdd:COG2226  87 SFDLVISSFVLHHLPDPER 105
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 34-136 7.96e-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: 60.42  E-value: 7.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230  34 LLARLPERARLLSVGCGAGGELAELAGLrpGWRFVAADLSADMLALARQRCARLglleRIELHCGDVAGLPPAP-PCDAA 112
Cdd:COG2227  18 LARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAEL----NVDFVQGDLEDLPLEDgSFDLV 91

                        90       100
                ....*....|....*....|....
gi 15597230 113 LVLLVLHFLRGDQAkrrFLEAVAE 136
Cdd:COG2227  92 ICSEVLEHLPDPAA---LLRELAR 112
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 43-137 5.25e-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: 54.74  E-value: 5.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230  43 RLLSVGCGAGGELAELAgLRPGWRFVAADLSADMLALARQRCARlGLLERIELHCGDVAGLPPAPP--CDAALVLLVLHF 120
Cdd:cd02440   1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAA-LLADNVEVLKGDAEELPPEADesFDVIISDPPLHH 78

                        90
                ....*....|....*..
gi 15597230 121 LRGDQakRRFLEAVAER 137
Cdd:cd02440  79 LVEDL--ARFLEEARRL 93
PRK08317 PRK08317
hypothetical protein; Provisional
 30-121 1.16e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 56.48  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230   30 SRAQLLARLPERArlLSVGCGAGGELAELAGL-RPGWRFVAADLSADMLALARQRCArlGLLERIELHCGDVAGLP-PAP 107
Cdd:PRK08317  11 TFELLAVQPGDRV--LDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALAKERAA--GLGPNVEFVRGDADGLPfPDG 86

                         90
                 ....*....|....
gi 15597230  108 PCDAALVLLVLHFL 121
Cdd:PRK08317  87 SFDAVRSDRVLQHL 100
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 45-136 1.33e-09

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 53.53  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230    45 LSVGCGAGGELAELAGLRPGWRFVAADLSADMLALARQRCARLGLL--ERIELHCGDVAGLPPAPPcDAALVLLVLHFLR 122
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLnaVRVELFQLDLGELDPGSF-DVVVASNVLHHLA 79

                          90
                  ....*....|....
gi 15597230   123 GdqaKRRFLEAVAE 136
Cdd:pfam08242  80 D---PRAVLRNIRR 90
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
9-136 9.23e-09

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 53.08  E-value: 9.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230   9 ADGYETRIGRLLpGYELLHLLsRAQLLARLP--ERARLLSVGCGAGGELAELAGLrpGWRFVAADLSADMLALARQRCAr 86
Cdd:COG4976  15 ADSYDAALVEDL-GYEAPALL-AEELLARLPpgPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKAREKGV- 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15597230  87 lglleRIELHCGDVAGLPPAP-PCDAALVLLVLHFLrGDQakRRFLEAVAE 136
Cdd:COG4976  90 -----YDRLLVADLADLAEPDgRFDLIVAADVLTYL-GDL--AAVFAGVAR 132
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 27-110 1.03e-07

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 51.30  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230  27 HLLSRAQLLARLPERARLLSVGCGAGGELAELAGLRPGWRFVAADLSADMLALARQRCARLGLLERIELHCGDV-AGLPP 105
Cdd:COG2890  99 ELVELALALLPAGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLfEPLPG 178


                ....*
gi 15597230 106 APPCD 110
Cdd:COG2890 179 DGRFD 183
PKS_MT smart00828
Methyltransferase in polyketide synthase (PKS) enzymes;
43-122 2.31e-07

Methyltransferase in polyketide synthase (PKS) enzymes;


Pssm-ID: 214839 [Multi-domain]  Cd Length: 224  Bit Score: 49.72  E-value: 2.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230     43 RLLSVGCGAGGELAELAGLRPGWRFVAADLSADMLALARQRCARLGLLERIELHCGDVAGLPPAPPCDAALVLLVLHFLR 122
Cdd:smart00828   2 RVLDFGCGYGSDLIDLAERHPHLQLHGYTISPEQAEVGRERIRALGLQGRIRIFYRDSAKDPFPDTYDLVFGFEVIHHIK 81
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 31-99 2.48e-07

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 49.84  E-value: 2.48e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597230   31 RAQLLARLPER-----ARLLSVGCGAGGELAELAglRPGWRFVAADLSADMLALARQRCARLGLLERIELHCGD 99
Cdd:PRK07580  49 RDTVLSWLPADgdltgLRILDAGCGVGSLSIPLA--RRGAKVVASDISPQMVEEARERAPEAGLAGNITFEVGD 120
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 45-121 4.09e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 46.50  E-value: 4.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597230    45 LSVGCGAGGELAELAglRPGWRFVAADLSADMLALARQRCARLGLleriELHCGDVAGLP-PAPPCDAALVLLVLHFL 121
Cdd:pfam08241   1 LDVGCGTGLLTELLA--RLGARVTGVDISPEMLELAREKAPREGL----TFVVGDAEDLPfPDNSFDLVLSSEVLHHV 72
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 36-104 9.92e-07

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 47.84  E-value: 9.92e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597230   36 ARLPERARLLSVGCGAG---GELAELAGlRPGWrFVAADLSADMLALARQRCARLGLLERIELHCGDVAGLP 104
Cdd:PRK00216  47 LGVRPGDKVLDLACGTGdlaIALAKAVG-KTGE-VVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEALP 116
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 43-104 4.67e-06

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 45.10  E-value: 4.67e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597230    43 RLLSVGCGAGGELAELAG-LRPGWRFVAADLSADMLALARQRCARLGlLERIELHCGDVAGLP 104
Cdd:pfam13847   6 RVLDLGCGTGHLSFELAEeLGPNAEVVGIDISEEAIEKARENAQKLG-FDNVEFEQGDIEELP 67
PRK14103 PRK14103
trans-aconitate 2-methyltransferase; Provisional
 34-123 1.34e-05

trans-aconitate 2-methyltransferase; Provisional


Pssm-ID: 184509  Cd Length: 255  Bit Score: 44.68  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230   34 LLARLPERA--RLLSVGCGAGGELAELAGLRPGWRFVAADLSADMLALARQRcarlglleRIELHCGDVAGLPPAPPCDA 111
Cdd:PRK14103  21 LLARVGAERarRVVDLGCGPGNLTRYLARRWPGAVIEALDSSPEMVAAARER--------GVDARTGDVRDWKPKPDTDV 92

                         90
                 ....*....|..
gi 15597230  112 ALVLLVLHFLRG 123
Cdd:PRK14103  93 VVSNAALQWVPE 104
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 27-100 1.75e-05

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 44.38  E-value: 1.75e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597230   27 HLLSRAQLLARLPERARLLSVGCGAGGELAELAGLRPGWRFVAADLSADMLALARqRCARLGLLERIELHCGDV 100
Cdd:PRK09328  95 ELVEWALEALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVAR-RNAKHGLGARVEFLQGDW 167
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 35-108 2.45e-04

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 40.90  E-value: 2.45e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597230  35 LARLPERARLLSVGCGAGGELAELAGLRPGWRFVAADLSADMLALARQRCARLGLLERIELHCGDVAGLPPAPP 108
Cdd:COG4123  32 FAPVKKGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGDLKEFAAELP 105
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
 24-99 2.86e-04

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 40.17  E-value: 2.86e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597230  24 ELLHLLSRAQllarlpeRA-RLLSVGCGAGGELAELA-GLRPGWRFVAADLSADMLALARQRCARLGLLERIELHCGD 99
Cdd:COG4122   6 RLLYLLARLL-------GAkRILEIGTGTGYSTLWLArALPDDGRLTTIEIDPERAAIARENFARAGLADRIRLILGD 76
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 36-95 4.53e-04

Mycolic acid cyclopropane synthetase; This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyze the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid.


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 40.39  E-value: 4.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230    36 ARLPERARLLSVGCGAGGeLAELAGLRPGWRFVAADLSADMLALARQRCARLGLLERIEL 95
Cdd:pfam02353  57 LGLKPGMTLLDIGCGWGG-LMRRAAERYDVNVVGLTLSKNQYKLARKRVAAEGLARKVEV 115
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
 19-98 5.56e-04

unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 40.45  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230   19 LLPGYELLHLLSraQLLARLPERARLLSVGCGAGGELAELAGLRPGWRFVAADLSADMLALARQRCARLGllERIELHCG 98
Cdd:PRK14966 232 LIPRPETEHLVE--AVLARLPENGRVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNAADLG--ARVEFAHG 307
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
33-97 9.62e-04

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 39.18  E-value: 9.62e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597230   33 QLLARLPERA-RLLSVGCGAGGELAELAGLrpGWRFVAADLSADMLALARQRCARLGLLERIEL-HC 97
Cdd:PRK11036  36 RLLAELPPRPlRVLDAGGGEGQTAIKLAEL--GHQVILCDLSAEMIQRAKQAAEAKGVSDNMQFiHC 100
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 34-100 1.23e-03

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 38.63  E-value: 1.23e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597230  34 LLARLPERA--RLLSVGCGAGGELAELAGLRPGWRFVAADLSADMLALARQRCARLGlLERIELHCGDV 100
Cdd:COG2813  41 LLEHLPEPLggRVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANG-LENVEVLWSDG 108
MeTrc smart00138
Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to ...
 13-82 1.92e-03

Methyltransferase, chemotaxis proteins; Methylates methyl-accepting chemotaxis proteins to form gamma-glutamyl methyl ester residues.


Pssm-ID: 214534 [Multi-domain]  Cd Length: 264  Bit Score: 38.42  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230     13 ETRIGRLLPGYELL--HLLSRAQLLARLPERARLLSVGCGAGGE-------LAEL--AGLRPGWRFVAADLSADMLALAR 81
Cdd:smart00138  70 ETRFFRESKHFEALeeKVLPLLIASRRHGRRVRIWSAGCSTGEEpyslamlLAETlpKGREPDVKILATDIDLKALEKAR 149


                   .
gi 15597230     82 Q 82
Cdd:smart00138 150 A 150
CheR pfam01739
CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling ...
 23-166 5.36e-03

CheR methyltransferase, SAM binding domain; CheR proteins are part of the chemotaxis signaling mechanism in bacteria. CheR methylates the chemotaxis receptor at specific glutamate residues. CheR is an S-adenosylmethionine- dependent methyltransferase - the C-terminal domain (this one) binds SAM.


Pssm-ID: 426403  Cd Length: 190  Bit Score: 36.49  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597230    23 YELLHLLSRAQLLARLperaRLLSVGCGAGGE-------LAELAGLRPGWRF--VAADLSADMLALARQrcarlGLLERI 93
Cdd:pfam01739  17 KYVLPLLAKAKNGKRV----RIWSAGCSSGEEpyslamlLKETFPNAARWDFkiLATDIDLSVLEKARA-----GVYPER 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597230    94 ELhcgdvAGLPPAppcdaalvLLVLHFLRGDQAKRRFLEAVAERlapaAPLLLANLMEARDAFeRPVQAEACR 166
Cdd:pfam01739  88 EL-----EGLPEE--------LLRRYFEKTAGGGYTVKPEIKSM----VLFEYLNLLDEYPPL-GDFDVIFCR 142
 
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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