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Conserved domains on  [gi|66770921|gb|AAY54772|]
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IP11481p [Drosophila melanogaster]

Protein Classification

SAM-dependent methyltransferase( domain architecture ID 1905023)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
22-161 1.81e-37

Predicted RNA methylase [General function prediction only];


The actual alignment was detected with superfamily member COG4076:

Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 134.01  E-value: 1.81e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  22 SYSRLETHMNMLRDSVRMQAFRDAIvqDGGLFQDKIVLDVGCGTGILSLFAAEAGASKVIAVEC-TDIADIAEEIIRDNQ 100
Cdd:COG4076   5 QFFVPRWHHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVnPDIAAVARRIIAANG 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66770921 101 KENVVKVVKGLVEQVELPdgiEKVDIIVSEWMGNALYMEAMINSVLFARDKWLTRGGRILP 161
Cdd:COG4076  83 LSDRITVINADATDLDLP---EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIP 140
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
22-161 1.81e-37

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 134.01  E-value: 1.81e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  22 SYSRLETHMNMLRDSVRMQAFRDAIvqDGGLFQDKIVLDVGCGTGILSLFAAEAGASKVIAVEC-TDIADIAEEIIRDNQ 100
Cdd:COG4076   5 QFFVPRWHHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVnPDIAAVARRIIAANG 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66770921 101 KENVVKVVKGLVEQVELPdgiEKVDIIVSEWMGNALYMEAMINSVLFARDKWLTRGGRILP 161
Cdd:COG4076  83 LSDRITVINADATDLDLP---EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIP 140
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
52-128 8.83e-14

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 70.18  E-value: 8.83e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66770921   52 LFQDKIVLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKENvvkvvkGLVEQVELPDGIEKVDIIV 128
Cdd:PRK00517 117 VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV---DIDPQAVEAARENAELN------GVELNVYLPQGDLKADVIV 184
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 54-128 1.47e-10

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 61.13  E-value: 1.47e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66770921    54 QDKIVLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKENVVKvvkgLVEQVELPDGI--EKVDIIV 128
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGV---DIDPVAVRAAKENAELNGVE----ARLEVYLPGDLpkEKADVVV 230
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 58-160 2.59e-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: 2.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  58 VLDVGCGTGILSLFAAEAGASKVIAVECTDIA-DIAEEIIRDNQKENvVKVVKGLVEQVeLPDGIEKVDIIVSEWMGNAL 136
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEEL-PPEADESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....*.
gi 66770921 137 --YMEAMINSVLfardKWLTRGGRIL 160
Cdd:cd02440  80 veDLARFLEEAR----RLLKPGGVLV 101
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 55-128 5.04e-09

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 56.38  E-value: 5.04e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66770921    55 DKIVLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKENVVKVVKgLVEQVELPDGIE-KVDIIV 128
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAAKVVGI---DIDPLAVESARKNAELNQVSDRL-QVKLIYLEQPIEgKADVIV 230
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
22-161 1.81e-37

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 134.01  E-value: 1.81e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  22 SYSRLETHMNMLRDSVRMQAFRDAIvqDGGLFQDKIVLDVGCGTGILSLFAAEAGASKVIAVEC-TDIADIAEEIIRDNQ 100
Cdd:COG4076   5 QFFVPRWHHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEVnPDIAAVARRIIAANG 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66770921 101 KENVVKVVKGLVEQVELPdgiEKVDIIVSEWMGNALYMEAMINSVLFARDKWLTRGGRILP 161
Cdd:COG4076  83 LSDRITVINADATDLDLP---EKADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIP 140
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
52-128 8.83e-14

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 70.18  E-value: 8.83e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66770921   52 LFQDKIVLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKENvvkvvkGLVEQVELPDGIEKVDIIV 128
Cdd:PRK00517 117 VLPGKTVLDVGCGSGILAIAAAKLGAKKVLAV---DIDPQAVEAARENAELN------GVELNVYLPQGDLKADVIV 184
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
52-128 5.26e-13

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 68.28  E-value: 5.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  52 LFQDKIVLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKENvvkvvkGLVEQVE--LPDGI--EKVDII 127
Cdd:COG2264 146 LKPGKTVLDVGCGSGILAIAAAKLGAKRVLAV---DIDPVAVEAARENAELN------GVEDRIEvvLGDLLedGPYDLV 216


                .
gi 66770921 128 V 128
Cdd:COG2264 217 V 217
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 40-160 2.43e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 61.10  E-value: 2.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  40 QAFRDAIVQDGGLFQDKIVLDVGCGTGILSLFAAEAGASKVIAVectDI----ADIAEEIIRDNQKENVVKVVKGLVEQV 115
Cdd:COG2230  37 EAKLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGV---TLspeqLEYARERAAEAGLADRVEVRLADYRDL 113

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 66770921 116 ELPdgiEKVDIIVS----EWMGNALYMEaminsvLFAR-DKWLTRGGRIL 160
Cdd:COG2230 114 PAD---GQFDAIVSigmfEHVGPENYPA------YFAKvARLLKPGGRLL 154
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 54-128 1.47e-10

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 61.13  E-value: 1.47e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66770921    54 QDKIVLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKENVVKvvkgLVEQVELPDGI--EKVDIIV 128
Cdd:pfam06325 161 PGESVLDVGCGSGILAIAALKLGAKKVVGV---DIDPVAVRAAKENAELNGVE----ARLEVYLPGDLpkEKADVVV 230
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 58-129 1.66e-10

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 57.19  E-value: 1.66e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66770921    58 VLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKENVVKV--VKGLVEQVELPDGieKVDIIVS 129
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGV---DLSPEMLERARERAAEAGLNVefVQGDAEDLPFPDG--SFDLVVS 69
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 58-160 2.59e-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: 2.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  58 VLDVGCGTGILSLFAAEAGASKVIAVECTDIA-DIAEEIIRDNQKENvVKVVKGLVEQVeLPDGIEKVDIIVSEWMGNAL 136
Cdd:cd02440   2 VLDLGCGTGALALALASGPGARVTGVDISPVAlELARKAAAALLADN-VEVLKGDAEEL-PPEADESFDVIISDPPLHHL 79

                        90       100
                ....*....|....*....|....*.
gi 66770921 137 --YMEAMINSVLfardKWLTRGGRIL 160
Cdd:cd02440  80 veDLARFLEEAR----RLLKPGGVLV 101
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 38-160 3.31e-10

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: 57.33  E-value: 3.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  38 RMQAFRDAIVQDGGLfqdkiVLDVGCGTGILSLFAAEAGAsKVIAVectDIADIAEEIIRDNQKENVVKVVKGLVEQVEL 117
Cdd:COG2227  13 RLAALLARLLPAGGR-----VLDVGCGTGRLALALARRGA-DVTGV---DISPEALEIARERAAELNVDFVQGDLEDLPL 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 66770921 118 PDGieKVDIIVS----EWMGNAlymEAMINSVLfardKWLTRGGRIL 160
Cdd:COG2227  84 EDG--SFDLVICsevlEHLPDP---AALLRELA----RLLKPGGLLL 121
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
51-129 6.62e-10

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 57.99  E-value: 6.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  51 GLFQDKIVLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKE--NVVKVVKGLVEQVELpdgIEKVDIIV 128
Cdd:COG2263  42 GDIEGKTVLDLGCGTGMLAIGAALLGAKKVVGV---DIDPEALEIARENAERlgVRVDFIRADVTRIPL---GGSVDTVV 115


                .
gi 66770921 129 S 129
Cdd:COG2263 116 M 116
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 53-183 4.12e-09

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 56.05  E-value: 4.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  53 FQDKIVLDVGCGTGILSLFAAEAGASKVIAvecTDIADIAEEIIRDNQKENVVKvVKGLVEQVELPDGIEKVDIIvseWM 132
Cdd:COG3897  69 VAGKRVLELGCGLGLVGIAAAKAGAADVTA---TDYDPEALAALRLNAALNGVA-ITTRLGDWRDPPAAGGFDLI---LG 141

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 66770921 133 GNALYMEAMINSVLfardKWLTR----GGRIlpstgnlwLMGayDPHRRTNLNFW 183
Cdd:COG3897 142 GDVLYERDLAEPLL----PFLDRlaapGGEV--------LIG--DPGRGYLPAFR 182
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 55-128 5.04e-09

ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an S-adenosyl-L-methionine-dependent methyltransferase required for the modification of ribosomal protein L11. This protein is found in bacteria and (with a probable transit peptide) in Arabidopsis. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273061  Cd Length: 288  Bit Score: 56.38  E-value: 5.04e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66770921    55 DKIVLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKENVVKVVKgLVEQVELPDGIE-KVDIIV 128
Cdd:TIGR00406 160 DKNVIDVGCGSGILSIAALKLGAAKVVGI---DIDPLAVESARKNAELNQVSDRL-QVKLIYLEQPIEgKADVIV 230
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 42-129 2.97e-08

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: 51.92  E-value: 2.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  42 FRDAIVQDGGLFQDKIVLDVGCGTGILSLFAAEAGAsKVIAVectdiaDIAEEII-----RDNQKENVVKVVKGLVEQVE 116
Cdd:COG2226  10 GREALLAALGLRPGARVLDLGCGTGRLALALAERGA-RVTGV------DISPEMLelareRAAEAGLNVEFVVGDAEDLP 82

                        90
                ....*....|...
gi 66770921 117 LPDGieKVDIIVS 129
Cdd:COG2226  83 FPDG--SFDLVIS 93
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 58-129 5.60e-08

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: 52.84  E-value: 5.60e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66770921  58 VLDVGCGTGILSLF-AAEAGASKVIAVEC-TDIADIAEEIIRDNQKENVVKVVKGLVEQVELPDGIEKVDIIVS 129
Cdd:COG4123  41 VLDLGTGTGVIALMlAQRSPGARITGVEIqPEAAELARRNVALNGLEDRITVIHGDLKEFAAELPPGSFDLVVS 114
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 59-132 1.39e-07

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 48.82  E-value: 1.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66770921    59 LDVGCGTGILSLFAAEAGAsKVIAVectDIADIAEEIIRDNQKENVVKVVKGLVEQVELPDgiEKVDIIVSEWM 132
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGA-RVTGV---DISPEMLELAREKAPREGLTFVVGDAEDLPFPD--NSFDLVLSSEV 68
PRK14968 PRK14968
putative methyltransferase; Provisional
 45-136 1.77e-07

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 50.67  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921   45 AIVQDGglfqdKIVLDVGCGTGILSLFAAEAGASkviaVECTDIADIAEEIIRDNQKENVVKVVKGLVEQVELPDGI--E 122
Cdd:PRK14968  19 AVDKKG-----DRVLEVGTGSGIVAIVAAKNGKK----VVGVDINPYAVECAKCNAKLNNIRNNGVEVIRSDLFEPFrgD 89

                         90       100
                 ....*....|....*....|....*...
gi 66770921  123 KVDII--------------VSEWMGNAL 136
Cdd:PRK14968  90 KFDVIlfnppylpteeeeeWDDWLNYAL 117
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 58-129 3.68e-07

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 50.92  E-value: 3.68e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66770921  58 VLDVGCGTGILSL-FAAEAGASKVIAVECTDIA-DIAEEIIRDNQKENVVKVVKG-LVEQVelpDGIEKVDIIVS 129
Cdd:COG2890 116 VLDLGTGSGAIALaLAKERPDARVTAVDISPDAlAVARRNAERLGLEDRVRFLQGdLFEPL---PGDGRFDLIVS 187
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 44-129 2.30e-06

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 48.23  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921   44 DAIVQDGGLFQDKIVLDVGCGTGILSL-FAAEAGASKVIAVectDIADIAEEIIRDNQKENV---VKVVKG-LVEqvelP 118
Cdd:PRK09328  98 EWALEALLLKEPLRVLDLGTGSGAIALaLAKERPDAEVTAV---DISPEALAVARRNAKHGLgarVEFLQGdWFE----P 170

                         90
                 ....*....|.
gi 66770921  119 DGIEKVDIIVS 129
Cdd:PRK09328 171 LPGGRFDLIVS 181
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
42-129 5.72e-06

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 47.20  E-value: 5.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921   42 FRDAIVQDGGLFQDKIVLDVGCGTGILSLFAAEAgASKVIAVEC-TDIADIAEEIIrdnQKENVVKVVKGLVEQVELPdg 120
Cdd:PRK14896  17 VVDRIVEYAEDTDGDPVLEIGPGKGALTDELAKR-AKKVYAIELdPRLAEFLRDDE---IAAGNVEIIEGDALKVDLP-- 90


                 ....*....
gi 66770921  121 ieKVDIIVS 129
Cdd:PRK14896  91 --EFNKVVS 97
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 58-160 1.15e-05

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 45.68  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  58 VLDVGCGTGILSLFAAEAGASKVIAVECTDIA-DIAEEIIRDNQKENVVKVVKGLVEQVELPDgiEKVDIIVS----EWM 132
Cdd:COG0500  30 VLDLGCGTGRNLLALAARFGGRVIGIDLSPEAiALARARAAKAGLGNVEFLVADLAELDPLPA--ESFDLVVAfgvlHHL 107

                        90       100
                ....*....|....*....|....*...
gi 66770921 133 gNALYMEAMINSVLfardKWLTRGGRIL 160
Cdd:COG0500 108 -PPEEREALLRELA----RALKPGGVLL 130
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 45-129 1.24e-05

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: 45.74  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921    45 AIVQDGGLFQDKIVLDVGCGTGILS-LFAAEAGASKVIAVectDIADIAEEIIRDNQKENvVKVVKGLVEQVELPDgiEK 123
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTrALLKRFPQAEFIAL---DISAGMLAQAKTKLSEN-VQFICGDAEKLPLED--SS 98


                  ....*.
gi 66770921   124 VDIIVS 129
Cdd:TIGR02072  99 FDLIVS 104
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 58-129 2.69e-05

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 44.12  E-value: 2.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66770921    58 VLDVGCGTGILSLFAAEagASKVIAVECTDIA----DIAEEIIRDNQKENVVKVVKGLVEQVElpdgIEKVDIIVS 129
Cdd:pfam05175  35 VLDLGCGAGVLGAALAK--ESPDAELTMVDINaralESARENLAANGLENGEVVASDVYSGVE----DGKFDLIIS 104
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 58-129 4.15e-05

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: 43.64  E-value: 4.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  58 VLDVGCGTGILSLFAAEagASKVIAVECTDI---A-DIAEEIIRDNQKENVvkvvkglveQVELPDGIEKV-----DIIV 128
Cdd:COG2813  53 VLDLGCGYGVIGLALAK--RNPEARVTLVDVnarAvELARANAAANGLENV---------EVLWSDGLSGVpdgsfDLIL 121


                .
gi 66770921 129 S 129
Cdd:COG2813 122 S 122
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 1-96 8.95e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 43.29  E-value: 8.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921    1 MSFNANQKLPFLEgkdsDYF-----QSYSRL--ETHMNMLRDSVRM--QAFRDAIV---QDGGLFQDKIVLDVGCGTGIL 68
Cdd:PRK07580   2 MMFNYLEHKSEVR----TYFnrtgfDRWARIysDAPVSKVRATVRAghQRMRDTVLswlPADGDLTGLRILDAGCGVGSL 77

                         90       100
                 ....*....|....*....|....*...
gi 66770921   69 SLFAAEAGAsKVIAVectdiaDIAEEII 96
Cdd:PRK07580  78 SIPLARRGA-KVVAS------DISPQMV 98
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 51-128 1.49e-04

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 43.24  E-value: 1.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  51 GLFQDKIVLDVGCGTGILSLFAAEAGAsKVIAVECTD--IADiAEEIIRDNQKENvVKVVKGLVEQVeLPD--GIEKVDI 126
Cdd:COG2265 230 DLTGGERVLDLYCGVGTFALPLARRAK-KVIGVEIVPeaVED-ARENARLNGLKN-VEFVAGDLEEV-LPEllWGGRPDV 305


                ..
gi 66770921 127 IV 128
Cdd:COG2265 306 VV 307
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 57-129 2.08e-04

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 40.76  E-value: 2.08e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66770921    57 IVLDVGCGTGILSLFAAEAGA-SKVIAVECT-DIADIAEEIIRDNQKENVVkvvkglVEQVELPDGIEKVDIIVS 129
Cdd:TIGR01444   1 VVIDVGANIGDTSLYFARKGAeGRVIAFEPLpDAYEILEENVKLNNLPNVV------LLNAAVGDRDGELEFNVS 69
PRK14967 PRK14967
putative methyltransferase; Provisional
 58-129 2.11e-04

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 41.96  E-value: 2.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66770921   58 VLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKEN--VVKVVKG-LVEQVELpdgiEKVDIIVS 129
Cdd:PRK14967  40 VLDLCTGSGALAVAAAAAGAGSVTAV---DISRRAVRSARLNALLAgvDVDVRRGdWARAVEF----RPFDVVVS 107
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 39-129 3.35e-04

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 41.96  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921    39 MQAFRDAIVQDGGLFqdkiVLDVGCGTGILSL-FAAEAGASKVIAVEC-TDIADIAEEIIRDNQKENVVKVVkglveQVE 116
Cdd:TIGR00536 103 EKALASLISQPPILH----ILDLGTGSGCIALaLAYEFPNAEVIAVDIsPDALAVAEENAEKNQLEHRVEFI-----QSN 173

                          90
                  ....*....|....*
gi 66770921   117 LPDGIE--KVDIIVS 129
Cdd:TIGR00536 174 LFEPLAgqKIDIIVS 188
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
58-160 5.90e-04

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 38.65  E-value: 5.90e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  58 VLDVGCGTGILS-LFAAEAGASKVIAVectdiaDIAEEIIRDNQKENV-VKVVKGLVEQVELPdgiEKVDIIVS----EW 131
Cdd:COG4106   5 VLDLGCGTGRLTaLLAERFPGARVTGV------DLSPEMLARARARLPnVRFVVADLRDLDPP---EPFDLVVSnaalHW 75

                        90       100
                ....*....|....*....|....*....
gi 66770921 132 MGNalyMEAMINSVLfardKWLTRGGRIL 160
Cdd:COG4106  76 LPD---HAALLARLA----AALAPGGVLA 97
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 55-129 5.92e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 39.71  E-value: 5.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66770921    55 DKIVLDVGCGTGILSLFAAE--AGASKVIAVECTDIA-DIAEEIIRDNQKENvVKVVKGLVEQVELPDGIEKVDIIVS 129
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEelGPNAEVVGIDISEEAiEKARENAQKLGFDN-VEFEQGDIEELPELLEDDKFDVVIS 80
arsM PRK11873
arsenite methyltransferase;
57-129 6.45e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 40.70  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921   57 IVLDVGCGTGILSLFAA-EAGAS-KVIAVectdiaDIAEEII---RDNQK----ENvVKVVKGLVEQVELPDGIekVDII 127
Cdd:PRK11873  80 TVLDLGSGGGFDCFLAArRVGPTgKVIGV------DMTPEMLakaRANARkagyTN-VEFRLGEIEALPVADNS--VDVI 150


                 ..
gi 66770921  128 VS 129
Cdd:PRK11873 151 IS 152
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 48-129 7.00e-04

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 39.88  E-value: 7.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921    48 QDGGLFQDKIVLDVGCGTGILSLFAAEAGASKVIAVectDIADIAEEIIRDNQKenvVKVVKG-----LVEQVELPDGIE 122
Cdd:pfam01728  15 KFGLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGV---DLGPMQLWKPRNDPG---VTFIQGdirdpETLDLLEELLGR 88


                  ....*..
gi 66770921   123 KVDIIVS 129
Cdd:pfam01728  89 KVDLVLS 95
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 31-110 1.16e-03

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: 40.11  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  31 NMLRDsvrmQAFRDAIVQDGGLFQDKIVLDVGCGTGILSLFAAEAGAsKVIAVEC-TDIADIAEEIIRDNQKenvVKVVK 109
Cdd:COG0030  18 NFLID----PNIIRRIVDAAGITPGDTVLEIGPGLGALTRALLERAA-RVTAVEIdRRLAAILRETFAAYPN---LTVIE 89


                .
gi 66770921 110 G 110
Cdd:COG0030  90 G 90
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
12-129 1.29e-03

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 39.21  E-value: 1.29e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  12 LEGKDSDYFQSYSRL-ETHMNMLRDSVRMQAFRDAIVQDGGLFQDKIVLDVGCGTGILSLFAAEAGASkviaVECTDI-- 88
Cdd:COG4976   3 LDAYVEALFDQYADSyDAALVEDLGYEAPALLAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYR----LTGVDLse 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 66770921  89 --ADIAEEiirdnqKENVVKVVKGLVEQVELPDGieKVDIIVS 129
Cdd:COG4976  79 emLAKARE------KGVYDRLLVADLADLAEPDG--RFDLIVA 113
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 59-159 1.46e-03

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 37.35  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921    59 LDVGCGTGILSLFAAEAGASkvIAVECTDIA----DIAEEIIRDNQKENVVKvVKGLVEQVELPDGiEKVDIIVsewMGN 134
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPG--LEYTGLDISpaalEAARERLAALGLLNAVR-VELFQLDLGELDP-GSFDVVV---ASN 73

                          90       100
                  ....*....|....*....|....*....
gi 66770921   135 AL----YMEAMINSVLfardKWLTRGGRI 159
Cdd:pfam08242  74 VLhhlaDPRAVLRNIR----RLLKPGGVL 98
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 51-159 1.59e-03

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 40.15  E-value: 1.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  51 GLFQDKIVLDVGCGTGILSLFAA-EAGASKVIAVECtDIADIaeEIIRDN-QKENV--VKVVKGlveqvELPDGIEKVD- 125
Cdd:COG2242 244 ALRPGDVLWDIGAGSGSVSIEAArLAPGGRVYAIER-DPERA--ALIRANaRRFGVpnVEVVEG-----EAPEALADLPd 315

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 66770921 126 ---IIVSewmGNALYMEAMINSVLfardKWLTRGGRI 159
Cdd:COG2242 316 pdaVFIG---GSGGNLPEILEACW----ARLRPGGRL 345
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 32-160 1.86e-03

cobalt-precorrin-6Y C(15)-methyltransferase; Provisional


Pssm-ID: 234740  Cd Length: 198  Bit Score: 39.01  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921   32 MLRDSVRMQAFRDAIVQDGGLFqdkivLDVGCGTGILSLfaaEAG-----ASKVIAVectDIADIAEEIIRDNQKE---- 102
Cdd:PRK00377  23 MTKEEIRALALSKLRLRKGDMI-----LDIGCGTGSVTV---EASllvgeTGKVYAV---DKDEKAINLTRRNAEKfgvl 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 66770921  103 NVVKVVKGLVEQVeLPDGIEKVDIIVSEwmGNALYMEAMINSVlfarDKWLTRGGRIL 160
Cdd:PRK00377  92 NNIVLIKGEAPEI-LFTINEKFDRIFIG--GGSEKLKEIISAS----WEIIKKGGRIV 142
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 43-119 2.23e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 38.98  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921   43 RDAIVQDGGLFQDKIVLDVGCGTGILSLFAAEAGAS--KVIAVectDIA----DIAEEIIRDNQKENVVKVVKGLVEQVE 116
Cdd:PRK00216  40 RRKTIKWLGVRPGDKVLDLACGTGDLAIALAKAVGKtgEVVGL---DFSegmlAVGREKLRDLGLSGNVEFVQGDAEALP 116


                 ...
gi 66770921  117 LPD 119
Cdd:PRK00216 117 FPD 119
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-129 3.20e-03

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 37.79  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921    39 MQAFRDAIVQD------GGLFQDKIVLDVGCGTGILSLFAAEAGASkVIAVectDIADIAEEIIRDNqkenvvkVVKGLV 112
Cdd:pfam13489   1 YAHQRERLLADlllrllPKLPSPGRVLDFGCGTGIFLRLLRAQGFS-VTGV---DPSPIAIERALLN-------VRFDQF 69

                          90
                  ....*....|....*..
gi 66770921   113 EQVELPDGIEKVDIIVS 129
Cdd:pfam13489  70 DEQEAAVPAGKFDVIVA 86
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 53-110 4.78e-03

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 37.37  E-value: 4.78e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66770921  53 FQDKIVLDVGCGTGILSLfaaEA---GASKVIAVEctdIADIAEEIIRDNQK----ENVVKVVKG 110
Cdd:COG0742  40 IEGARVLDLFAGSGALGL---EAlsrGAASVVFVE---KDRKAAAVIRKNLEklglEDRARVIRG 98
PRK04338 PRK04338
N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional
 29-103 6.22e-03

N(2),N(2)-dimethylguanosine tRNA methyltransferase; Provisional


Pssm-ID: 235286  Cd Length: 382  Bit Score: 37.97  E-value: 6.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66770921   29 HMNMLRD-SVR-MQAFRDaivqdggLFQDKIVLDVGCGTGILSL-FAAEAGASKVIaveCTDIADIAEEIIRDNQKEN 103
Cdd:PRK04338  37 RMELNRDiSVLvLRAFGP-------KLPRESVLDALSASGIRGIrYALETGVEKVT---LNDINPDAVELIKKNLELN 104
PRK08317 PRK08317
hypothetical protein; Provisional
 36-130 7.31e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 37.61  E-value: 7.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921   36 SVRMQAFRDAIVQDGGlfqdkIVLDVGCGTGILSL-FAAEAGA-SKVIAVectdiaDIAEEII-----RDNQKENVVKVV 108
Cdd:PRK08317   6 RYRARTFELLAVQPGD-----RVLDVGCGPGNDAReLARRVGPeGRVVGI------DRSEAMLalakeRAAGLGPNVEFV 74

                         90       100
                 ....*....|....*....|..
gi 66770921  109 KGLVEQVELPDgiEKVDIIVSE 130
Cdd:PRK08317  75 RGDADGLPFPD--GSFDAVRSD 94
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
 44-136 7.35e-03

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 37.63  E-value: 7.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66770921  44 DAIVQDGGLFQDKIVLDVGCGTGILSLFAAEAGASK--VIAVECTDIADIAEEIIRDNQKENVVKVVKGLVEQVELPDGI 121
Cdd:COG5459  70 AELAEAGPDFAPLTVLDVGAGPGTAAWAAADAWPSLldATLLERSAAALALGRRLARAAANPALETAEWRLADLAAALPA 149

                        90
                ....*....|....*
gi 66770921 122 EKVDIIVsewMGNAL 136
Cdd:COG5459 150 PPADLVV---ASYVL 161
 
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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