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Conserved domains on  [gi|21357335|ref|NP_649577|]
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uncharacterized protein Dmel_CG1239, isoform A [Drosophila melanogaster]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 18605031)

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 Drosophila melanogaster RNA methyltransferases CG1239 and CG11342

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
 191-299 1.46e-57

Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif.


:

Pssm-ID: 462022  Cd Length: 109  Bit Score: 180.43  E-value: 1.46e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   191 FDVILCLSVTKWIHLNFCDSGLKQAFRRMYLQLRPGGKLILEPQSFDGYKRRKKLSEQIRDNYNAIKFRPDHFTEYLLSp 270
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLS- 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 21357335   271 EVGFAEMKLMG-IPEHCKVGFKRPIQIFTK 299
Cdd:pfam06859  80 EVGFESVEELGsTPEGKSKGFDRPIYLFRK 109
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 90-232 2.05e-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: 2.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335  90 NKDFHDIRLDVLgTQPDLFRNKQLLDIGCNSGHLSIQIARK-FEVkslVGLDIDRGLINDAQKTVSHLkrhatpgqgipH 168
Cdd:COG2227   6 ARDFWDRRLAAL-LARLLPAGGRVLDVGCGTGRLALALARRgADV---TGVDISPEALEIARERAAEL-----------N 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21357335 169 IQFVHGNyvLEDdvlLEIERPQFDVILCLSVtkWIHLnfcdSGLKQAFRRMYLQLRPGGKLILE 232
Cdd:COG2227  71 VDFVQGD--LED---LPLEDGSFDLVICSEV--LEHL----PDPAALLRELARLLKPGGLLLLS 123
 
Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
 191-299 1.46e-57

Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif.


Pssm-ID: 462022  Cd Length: 109  Bit Score: 180.43  E-value: 1.46e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   191 FDVILCLSVTKWIHLNFCDSGLKQAFRRMYLQLRPGGKLILEPQSFDGYKRRKKLSEQIRDNYNAIKFRPDHFTEYLLSp 270
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLS- 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 21357335   271 EVGFAEMKLMG-IPEHCKVGFKRPIQIFTK 299
Cdd:pfam06859  80 EVGFESVEELGsTPEGKSKGFDRPIYLFRK 109
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 90-232 2.05e-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: 2.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335  90 NKDFHDIRLDVLgTQPDLFRNKQLLDIGCNSGHLSIQIARK-FEVkslVGLDIDRGLINDAQKTVSHLkrhatpgqgipH 168
Cdd:COG2227   6 ARDFWDRRLAAL-LARLLPAGGRVLDVGCGTGRLALALARRgADV---TGVDISPEALEIARERAAEL-----------N 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21357335 169 IQFVHGNyvLEDdvlLEIERPQFDVILCLSVtkWIHLnfcdSGLKQAFRRMYLQLRPGGKLILE 232
Cdd:COG2227  71 VDFVQGD--LED---LPLEDGSFDLVICSEV--LEHL----PDPAALLRELARLLKPGGLLLLS 123
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 114-227 6.36e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 66.43  E-value: 6.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   114 LDIGCNSGHLSIQIARKFEVKsLVGLDIDRGLINDAQKTVSHLKrhatpgqgiPHIQFVHGNyvLEDdvlLEIERPQFDV 193
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGAR-VTGVDLSPEMLERARERAAEAG---------LNVEFVQGD--AED---LPFPDGSFDL 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 21357335   194 ILCLSVtkWIHLNfcDSGLKQAFRRMYLQLRPGG 227
Cdd:pfam13649  67 VVSSGV--LHHLP--DPDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 113-232 7.87e-12

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: 60.91  E-value: 7.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335 113 LLDIGCNSGHLSIQIARkFEVKSLVGLDIDRGLINDAQKTVSHLKRhatpgqgiPHIQFVHGNyvLEDDVLLEIERpqFD 192
Cdd:cd02440   2 VLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALLA--------DNVEVLKGD--AEELPPEADES--FD 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21357335 193 VILCLSVTKWIHLNFcdsglKQAFRRMYLQLRPGGKLILE 232
Cdd:cd02440  69 VIISDPPLHHLVEDL-----ARFLEEARRLLKPGGVLVLT 103
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 108-231 9.11e-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: 57.68  E-value: 9.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   108 FRNKQLLDIGCNSGHLSIQIARKFEVKSLVGLDIDRGLINDAQKTVShlkrhatpgqgiPHIQFVHGNyvLEDDVLLEie 187
Cdd:TIGR02072  33 FIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS------------ENVQFICGD--AEKLPLED-- 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 21357335   188 rPQFDVILCLSVTKWIHlnfcdsGLKQAFRRMYLQLRPGGKLIL 231
Cdd:TIGR02072  97 -SSFDLIVSNLALQWCD------DLSQALSELARVLKPGGLLAF 133
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 106-232 9.59e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 45.91  E-value: 9.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335  106 DLFRNKQLLDIGCNSGHLSIQIARK-FEVKSLVGLDIDRGLINDAQKTVSHLKRHatpgqgiPHIQFVHGNyVLEddvlL 184
Cdd:PRK00216  48 GVRPGDKVLDLACGTGDLAIALAKAvGKTGEVVGLDFSEGMLAVGREKLRDLGLS-------GNVEFVQGD-AEA----L 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21357335  185 EIERPQFDvilCLSVTkwihlnFcdsGL------KQAFRRMYLQLRPGGKL-ILE 232
Cdd:PRK00216 116 PFPDNSFD---AVTIA------F---GLrnvpdiDKALREMYRVLKPGGRLvILE 158
 
Name Accession Description Interval E-value
Bin3 pfam06859
Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of ...
 191-299 1.46e-57

Bicoid-interacting protein 3 (Bin3); This family represents a conserved region of approximately 120 residues within eukaryotic Bicoid-interacting protein 3 (Bin3). Bin3, which shows similarity to a number of protein methyltransferases that modify RNA-binding proteins, interacts with Bicoid, which itself directs pattern formation in the early Drosophila embryo. The interaction might allow Bicoid to switch between its dual roles in transcription and translation. Note that family members contain a conserved HLN motif.


Pssm-ID: 462022  Cd Length: 109  Bit Score: 180.43  E-value: 1.46e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   191 FDVILCLSVTKWIHLNFCDSGLKQAFRRMYLQLRPGGKLILEPQSFDGYKRRKKLSEQIRDNYNAIKFRPDHFTEYLLSp 270
Cdd:pfam06859   1 YDVILCLSVTKWIHLNWGDEGLKRFFKRIYSLLRPGGVLILEPQPWKSYKKAKRLSETIKANYKTIQLRPEDFEEYLLS- 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 21357335   271 EVGFAEMKLMG-IPEHCKVGFKRPIQIFTK 299
Cdd:pfam06859  80 EVGFESVEELGsTPEGKSKGFDRPIYLFRK 109
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 90-232 2.05e-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: 2.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335  90 NKDFHDIRLDVLgTQPDLFRNKQLLDIGCNSGHLSIQIARK-FEVkslVGLDIDRGLINDAQKTVSHLkrhatpgqgipH 168
Cdd:COG2227   6 ARDFWDRRLAAL-LARLLPAGGRVLDVGCGTGRLALALARRgADV---TGVDISPEALEIARERAAEL-----------N 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21357335 169 IQFVHGNyvLEDdvlLEIERPQFDVILCLSVtkWIHLnfcdSGLKQAFRRMYLQLRPGGKLILE 232
Cdd:COG2227  71 VDFVQGD--LED---LPLEDGSFDLVICSEV--LEHL----PDPAALLRELARLLKPGGLLLLS 123
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 105-246 8.89e-15

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 71.49  E-value: 8.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335 105 PDLFRNKQLLDIGCNSGHLSIQIARKFEVKsLVGLDIDRGLINDAQKTVSHlkrhatpgQGIPHIQFVHGNYvledDVLL 184
Cdd:COG0500  22 ERLPKGGRVLDLGCGTGRNLLALAARFGGR-VIGIDLSPEAIALARARAAK--------AGLGNVEFLVADL----AELD 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21357335 185 EIERPQFDVILCLSVtkWIHLNFcdSGLKQAFRRMYLQLRPGGKLILEPQSFDGYKRRKKLS 246
Cdd:COG0500  89 PLPAESFDLVVAFGV--LHHLPP--EEREALLRELARALKPGGVLLLSASDAAAALSLARLL 146
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 114-227 6.36e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 66.43  E-value: 6.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   114 LDIGCNSGHLSIQIARKFEVKsLVGLDIDRGLINDAQKTVSHLKrhatpgqgiPHIQFVHGNyvLEDdvlLEIERPQFDV 193
Cdd:pfam13649   2 LDLGCGTGRLTLALARRGGAR-VTGVDLSPEMLERARERAAEAG---------LNVEFVQGD--AED---LPFPDGSFDL 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 21357335   194 ILCLSVtkWIHLNfcDSGLKQAFRRMYLQLRPGG 227
Cdd:pfam13649  67 VVSSGV--LHHLP--DPDLEAALREIARVLKPGG 96
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
109-232 4.18e-13

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 64.07  E-value: 4.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335 109 RNKQLLDIGCNSGHLSIQIARKFEVKSLVGLDIDRGLINDAQKTVshlkrhatpgqgiPHIQFVHGNyvLEDdvlLEIER 188
Cdd:COG4106   1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL-------------PNVRFVVAD--LRD---LDPPE 62

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 21357335 189 PqFDVILCLSVTKWIHlnfcdsGLKQAFRRMYLQLRPGGKLILE 232
Cdd:COG4106  63 P-FDLVVSNAALHWLP------DHAALLARLAAALAPGGVLAVQ 99
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 114-229 1.12e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 62.77  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   114 LDIGCNSGHLSIQIARKFEVKSLVGLDIDRGLINDAQKTVSHLKRHAtpgqgIPHIQFVHGNyvleddvLLEIERPQFDV 193
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLN-----AVRVELFQLD-------LGELDPGSFDV 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 21357335   194 ILCLSVTKWIhlnfcdSGLKQAFRRMYLQLRPGGKL 229
Cdd:pfam08242  69 VVASNVLHHL------ADPRAVLRNIRRLLKPGGVL 98
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 113-232 7.87e-12

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: 60.91  E-value: 7.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335 113 LLDIGCNSGHLSIQIARkFEVKSLVGLDIDRGLINDAQKTVSHLKRhatpgqgiPHIQFVHGNyvLEDDVLLEIERpqFD 192
Cdd:cd02440   2 VLDLGCGTGALALALAS-GPGARVTGVDISPVALELARKAAAALLA--------DNVEVLKGD--AEELPPEADES--FD 68

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 21357335 193 VILCLSVTKWIHLNFcdsglKQAFRRMYLQLRPGGKLILE 232
Cdd:cd02440  69 VIISDPPLHHLVEDL-----ARFLEEARRLLKPGGVLVLT 103
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 92-231 3.23e-11

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: 60.01  E-value: 3.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335  92 DFHDIRLDVLGTQPdlfrNKQLLDIGCNSGHLSIQIARKFEvkSLVGLDIDRGLINDAQktvshlKRHATPGQgipHIQF 171
Cdd:COG2226   9 DGREALLAALGLRP----GARVLDLGCGTGRLALALAERGA--RVTGVDISPEMLELAR------ERAAEAGL---NVEF 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335 172 VHGNyvLEDdvlLEIERPQFDVILCLSVtkwihLNFCDSgLKQAFRRMYLQLRPGGKLIL 231
Cdd:COG2226  74 VVGD--AED---LPFPDGSFDLVISSFV-----LHHLPD-PERALAEIARVLKPGGRLVV 122
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 108-231 9.11e-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: 57.68  E-value: 9.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   108 FRNKQLLDIGCNSGHLSIQIARKFEVKSLVGLDIDRGLINDAQKTVShlkrhatpgqgiPHIQFVHGNyvLEDDVLLEie 187
Cdd:TIGR02072  33 FIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISAGMLAQAKTKLS------------ENVQFICGD--AEKLPLED-- 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 21357335   188 rPQFDVILCLSVTKWIHlnfcdsGLKQAFRRMYLQLRPGGKLIL 231
Cdd:TIGR02072  97 -SSFDLIVSNLALQWCD------DLSQALSELARVLKPGGLLAF 133
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 107-232 2.30e-09

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.12  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   107 LFRNKQLLDIGCNSGHLSIQIARKFEVKS-LVGLDIDRGLINDAQKtvsHLKRHatpgqGIPHIQFVHGNyVLEDDVLLE 185
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEELGPNAeVVGIDISEEAIEKARE---NAQKL-----GFDNVEFEQGD-IEELPELLE 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 21357335   186 IERpqFDVILCLSVTkwIHLNFCDSGLKQAFRrmylQLRPGGKLILE 232
Cdd:pfam13847  72 DDK--FDVVISNCVL--NHIPDPDKVLQEILR----VLKPGGRLIIS 110
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 114-231 3.96e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 53.05  E-value: 3.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   114 LDIGCNSGHLSIQIARKFevKSLVGLDIDRGLINDAQKTVshlkrhatpgqGIPHIQFVHGNYV---LEDDvlleierpQ 190
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG--ARVTGVDISPEMLELAREKA-----------PREGLTFVVGDAEdlpFPDN--------S 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 21357335   191 FDVILCLSVtkwihLNFCDSgLKQAFRRMYLQLRPGGKLIL 231
Cdd:pfam08241  60 FDLVLSSEV-----LHHVED-PERALREIARVLKPGGILII 94
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 113-241 5.02e-09

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: 54.81  E-value: 5.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335 113 LLDIGCNSGHLSIQIARKFEVKSLVGLDIDRGLINDAQKTVSHLkrhatpgqGIPHIQFVHgnyvleDDVLLEIERPQFD 192
Cdd:COG2813  53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAAN--------GLENVEVLW------SDGLSGVPDGSFD 118

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21357335 193 VILC-------LSVTKWIHLNFcdsgLKQAFRRmylqLRPGGKLILEPQSFDGYKR 241
Cdd:COG2813 119 LILSnppfhagRAVDKEVAHAL----IADAARH----LRPGGELWLVANRHLPYER 166
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 109-241 3.17e-08

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: 52.21  E-value: 3.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   109 RNKQLLDIGCNSGHLSIQIARKFEVKSLVGLDIDRGLINDAQKTvshLKRHatpgqGIPHIQFVHGnyvledDVLLEIER 188
Cdd:pfam05175  31 LSGKVLDLGCGAGVLGAALAKESPDAELTMVDINARALESAREN---LAAN-----GLENGEVVAS------DVYSGVED 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   189 PQFDVILC-------LSVTKWIHLNFcdsgLKQAFRRmylqLRPGGKLILEPQSFDGYKR 241
Cdd:pfam05175  97 GKFDLIISnppfhagLATTYNVAQRF----IADAKRH----LRPGGELWIVANRFLGYPP 148
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 98-231 8.30e-08

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 50.70  E-value: 8.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335  98 LDVLGTQPdlfrNKQLLDIGCNSGHLSIQIARKFEVKsLVGLDIDRGLINDAQKTVShlkrhatpGQGIPH-IQFVHGNY 176
Cdd:COG2230  44 LRKLGLKP----GMRVLDIGCGWGGLALYLARRYGVR-VTGVTLSPEQLEYARERAA--------EAGLADrVEVRLADY 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21357335 177 vleDDVLLEierPQFDVILCLSVTkwIHlnFCDSGLKQAFRRMYLQLRPGGKLIL 231
Cdd:COG2230 111 ---RDLPAD---GQFDAIVSIGMF--EH--VGPENYPAYFAKVARLLKPGGRLLL 155
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
109-241 3.00e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 49.61  E-value: 3.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335 109 RNKQLLDIGCNSGHLSIQIARKFevKSLVGLDIDRGLINDAQKTvshlkrhatpgqGIpHIQFVHGNYVLeddvlLEIER 188
Cdd:COG4976  46 PFGRVLDLGCGTGLLGEALRPRG--YRLTGVDLSEEMLAKAREK------------GV-YDRLLVADLAD-----LAEPD 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 21357335 189 PQFDVILCLSVTKWIHlnfcdsGLKQAFRRMYLQLRPGGKLILEPQSFDGYKR 241
Cdd:COG4976 106 GRFDLIVAADVLTYLG------DLAAVFAGVARALKPGGLFIFSVEDADGSGR 152
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 109-196 8.19e-06

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: 45.91  E-value: 8.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335 109 RNKQLLDIGCNSGHLSIQIARKFEVKSLVGLDIDRGLINDAQKTVSHLKRHAtpgqgipHIQFVHGNYvleDDVLLEIER 188
Cdd:COG4123  37 KGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLED-------RITVIHGDL---KEFAAELPP 106


                ....*...
gi 21357335 189 PQFDVILC 196
Cdd:COG4123 107 GSFDLVVS 114
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 106-232 9.59e-06

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 45.91  E-value: 9.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335  106 DLFRNKQLLDIGCNSGHLSIQIARK-FEVKSLVGLDIDRGLINDAQKTVSHLKRHatpgqgiPHIQFVHGNyVLEddvlL 184
Cdd:PRK00216  48 GVRPGDKVLDLACGTGDLAIALAKAvGKTGEVVGLDFSEGMLAVGREKLRDLGLS-------GNVEFVQGD-AEA----L 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21357335  185 EIERPQFDvilCLSVTkwihlnFcdsGL------KQAFRRMYLQLRPGGKL-ILE 232
Cdd:PRK00216 116 PFPDNSFD---AVTIA------F---GLrnvpdiDKALREMYRVLKPGGRLvILE 158
PRK08317 PRK08317
hypothetical protein; Provisional
 114-231 1.03e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 42.62  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335  114 LDIGCNSGHLSIQIARKFEVKS-LVGLDIDRGLINDAQktvshlkrhATPGQGIPHIQFVHGNyvlEDDVLLEIERpqFD 192
Cdd:PRK08317  24 LDVGCGPGNDARELARRVGPEGrVVGIDRSEAMLALAK---------ERAAGLGPNVEFVRGD---ADGLPFPDGS--FD 89

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 21357335  193 VILCLSVTKWIHlnfcdsGLKQAFRRMYLQLRPGGKLIL 231
Cdd:PRK08317  90 AVRSDRVLQHLE------DPARALAEIARVLRPGGRVVV 122
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 105-232 1.28e-04

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 41.64  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   105 PDLFRNKQLLDIGCNSGHLSIQIARKFevKSLVGLDIDRGLINDAQKTVSHlkrhatpgqgiphiqfvhgnyVLEDDVLL 184
Cdd:pfam13489  18 PKLPSPGRVLDFGCGTGIFLRLLRAQG--FSVTGVDPSPIAIERALLNVRF---------------------DQFDEQEA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 21357335   185 EIERPQFDVILCLSVTKWIHlNFCDsglkqAFRRMYLQLRPGGKLILE 232
Cdd:pfam13489  75 AVPAGKFDVIVAREVLEHVP-DPPA-----LLRQIAALLKPGGLLLLS 116
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
107-142 9.76e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 39.75  E-value: 9.76e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 21357335  107 LFRNKQLLDIGCNSGHLSIqIARKFEVKSLVGLDID 142
Cdd:PRK00517 117 VLPGKTVLDVGCGSGILAI-AAAKLGAKKVLAVDID 151
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 111-231 3.60e-03

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: 38.40  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335   111 KQLLDIGCNSGHLSIQIArKFEVKSLVGLDIDRGLINDAQktvSHLKRHatpgqGIPHIQFVHgnyvLEDDVLLEierpQ 190
Cdd:pfam06325 163 ESVLDVGCGSGILAIAAL-KLGAKKVVGVDIDPVAVRAAK---ENAELN-----GVEARLEVY----LPGDLPKE----K 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 21357335   191 FDVILCLsvtkwIHLNFCDSGLKQAFRRmylqLRPGGKLIL 231
Cdd:pfam06325 226 ADVVVAN-----ILADPLIELAPDIYAL----VKPGGYLIL 257
Methyltransf_2 pfam00891
O-methyltransferase domain; This family includes a range of O-methyltransferases. These ...
 99-231 6.19e-03

O-methyltransferase domain; This family includes a range of O-methyltransferases. These enzymes utilize S-adenosyl methionine.


Pssm-ID: 395719 [Multi-domain]  Cd Length: 208  Bit Score: 37.38  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357335    99 DVLgTQPDLFRNKQLLDIGCNSGHLSIQIARKFEVKSLVGLDIdrglindaQKTVSHLKRHATPGQGiPHIQFVHGNYVl 178
Cdd:pfam00891  51 DVL-TAFDLSGFRSLVDVGGGTGALAQAIVSLYPGCKGIVFDL--------PHVVEAAPTHFSAGEE-PRVTFHGGDFF- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 21357335   179 eDDVLleierPQFDVILclsvTKWIHLNFCDSGLKQAFRRMYLQLRPGGKLIL 231
Cdd:pfam00891 120 -KDSL-----PEADAYI----LKRVLHDWSDEKCVKLLKRCYKACPAGGKVIL 162
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
107-142 6.41e-03

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 37.46  E-value: 6.41e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 21357335 107 LFRNKQLLDIGCNSGHLSIqIARKFEVKSLVGLDID 142
Cdd:COG2264 146 LKPGKTVLDVGCGSGILAI-AAAKLGAKRVLAVDID 180
 
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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