NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24647025|ref|NP_731984|]
View 

arginine methyltransferase 3, isoform B [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG4076 super family cl44002
Predicted RNA methylase [General function prediction only];
176-374 7.46e-34

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: 127.07  E-value: 7.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 176 HHEMLSDKVRTSTYRASLlqNEAVVRGKTVLDVGCGTGILSIFASKAGAARVVGID-NSDIVYTAMDIIRKNKV-ENVEL 253
Cdd:COG4076  12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEvNPDIAAVARRIIAANGLsDRITV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 254 IKGRLEDTDLPEtKYDIIISEWMGYFLLYESMLDSIIYARENHLNPNGIILPSRCTL--SLLGYGDDTLYADEVEFWSNV 331
Cdd:COG4076  90 INADATDLDLPE-KADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNaaQPVESPVDAEGFEDWQFDGFD 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24647025 332 YEVDMSDLRKQSIEEPLMQVVDAEFMLTEPEQIANFDIMTVDM 374
Cdd:COG4076 169 FRLFGFLLYAEPLLHLTRLVRTPLLLLLLPTAFDEFPFDLASQ 211
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
176-374 7.46e-34

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 127.07  E-value: 7.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 176 HHEMLSDKVRTSTYRASLlqNEAVVRGKTVLDVGCGTGILSIFASKAGAARVVGID-NSDIVYTAMDIIRKNKV-ENVEL 253
Cdd:COG4076  12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEvNPDIAAVARRIIAANGLsDRITV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 254 IKGRLEDTDLPEtKYDIIISEWMGYFLLYESMLDSIIYARENHLNPNGIILPSRCTL--SLLGYGDDTLYADEVEFWSNV 331
Cdd:COG4076  90 INADATDLDLPE-KADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNaaQPVESPVDAEGFEDWQFDGFD 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24647025 332 YEVDMSDLRKQSIEEPLMQVVDAEFMLTEPEQIANFDIMTVDM 374
Cdd:COG4076 169 FRLFGFLLYAEPLLHLTRLVRTPLLLLLLPTAFDEFPFDLASQ 211
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 204-307 7.84e-16

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: 73.23  E-value: 7.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 204 TVLDVGCGTGILSIFASKAGAARVVGIDNSDIVY-TAMDIIRKNKVENVELIKGRLED-TDLPETKYDIIISeWMGYFLL 281
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALeLARKAAAALLADNVEVLKGDAEElPPEADESFDVIIS-DPPLHHL 79

                        90       100
                ....*....|....*....|....*.
gi 24647025 282 YESMLDSIIYAREnHLNPNGIILPSR 307
Cdd:cd02440  80 VEDLARFLEEARR-LLKPGGVLVLTL 104
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 205-301 1.03e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.51  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   205 VLDVGCGTGILSIFASKAGAARVVGIDNSDivyTAMDIIRKNKVE---NVELIKGRLEDTDLPETKYDIIISeWMGYFLL 281
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSP---EMLERARERAAEaglNVEFVQGDAEDLPFPDGSFDLVVS-SGVLHHL 76

                          90       100
                  ....*....|....*....|..
gi 24647025   282 YESMLDSIIyaRE--NHLNPNG 301
Cdd:pfam13649  77 PDPDLEAAL--REiaRVLKPGG 96
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
197-272 3.09e-14

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 72.49  E-value: 3.09e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24647025  197 EAVVRGKTVLDVGCGTGILSIFASKAGAARVVGIDNSDIVYtamdiirKNKVENVELiKGRLEDTDLPE--TKYDIII 272
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAV-------EAARENAEL-NGVELNVYLPQgdLKADVIV 184
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 199-272 1.70e-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: 58.69  E-value: 1.70e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24647025   199 VVRGKTVLDVGCGTGILSIFASKAGAARVVGIDNSDI-VYTAMDIIRKNKVENVELIKgRLEDTDLPETKYDIII 272
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLaVESARKNAELNQVSDRLQVK-LIYLEQPIEGKADVIV 230
 
Name Accession Description Interval E-value
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
176-374 7.46e-34

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 127.07  E-value: 7.46e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 176 HHEMLSDKVRTSTYRASLlqNEAVVRGKTVLDVGCGTGILSIFASKAGAARVVGID-NSDIVYTAMDIIRKNKV-ENVEL 253
Cdd:COG4076  12 HHPMLNDVERNDAFKAAI--ERVVKPGDVVLDIGTGSGLLSMLAARAGAKKVYAVEvNPDIAAVARRIIAANGLsDRITV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 254 IKGRLEDTDLPEtKYDIIISEWMGYFLLYESMLDSIIYARENHLNPNGIILPSRCTL--SLLGYGDDTLYADEVEFWSNV 331
Cdd:COG4076  90 INADATDLDLPE-KADVIISEMLDTALLDEGQVPILNHARKRLLKPGGRIIPERITNaaQPVESPVDAEGFEDWQFDGFD 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 24647025 332 YEVDMSDLRKQSIEEPLMQVVDAEFMLTEPEQIANFDIMTVDM 374
Cdd:COG4076 169 FRLFGFLLYAEPLLHLTRLVRTPLLLLLLPTAFDEFPFDLASQ 211
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
197-272 2.17e-17

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


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 82.14  E-value: 2.17e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24647025 197 EAVVRGKTVLDVGCGTGILSIFASKAGAARVVGIDNSDI-VYTAMDIIRKNKVEN-VELIKGrledTDLPETKYDIII 272
Cdd:COG2264 144 KLLKPGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVaVEAARENAELNGVEDrIEVVLG----DLLEDGPYDLVV 217
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 204-307 7.84e-16

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: 73.23  E-value: 7.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 204 TVLDVGCGTGILSIFASKAGAARVVGIDNSDIVY-TAMDIIRKNKVENVELIKGRLED-TDLPETKYDIIISeWMGYFLL 281
Cdd:cd02440   1 RVLDLGCGTGALALALASGPGARVTGVDISPVALeLARKAAAALLADNVEVLKGDAEElPPEADESFDVIIS-DPPLHHL 79

                        90       100
                ....*....|....*....|....*.
gi 24647025 282 YESMLDSIIYAREnHLNPNGIILPSR 307
Cdd:cd02440  80 VEDLARFLEEARR-LLKPGGVLVLTL 104
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 196-304 3.33e-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: 71.97  E-value: 3.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 196 NEAVVRGKTVLDVGCGTGILSIFASKAGaARVVGIDNSDivyTAMDIIRKNKVE-NVELIKGRLEDTDLPETKYDIIISe 274
Cdd:COG2227  19 ARLLPAGGRVLDVGCGTGRLALALARRG-ADVTGVDISP---EALEIARERAAElNVDFVQGDLEDLPLEDGSFDLVIC- 93

                        90       100       110
                ....*....|....*....|....*....|..
gi 24647025 275 wMGYFllyESMLDSIIYARE--NHLNPNGIIL 304
Cdd:COG2227  94 -SEVL---EHLPDPAALLRElaRLLKPGGLLL 121
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 205-301 1.03e-14

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 69.51  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   205 VLDVGCGTGILSIFASKAGAARVVGIDNSDivyTAMDIIRKNKVE---NVELIKGRLEDTDLPETKYDIIISeWMGYFLL 281
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSP---EMLERARERAAEaglNVEFVQGDAEDLPFPDGSFDLVVS-SGVLHHL 76

                          90       100
                  ....*....|....*....|..
gi 24647025   282 YESMLDSIIyaRE--NHLNPNG 301
Cdd:pfam13649  77 PDPDLEAAL--REiaRVLKPGG 96
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
 197-272 1.77e-14

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: 73.84  E-value: 1.77e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24647025   197 EAVVR-GKTVLDVGCGTGILSIFASKAGAARVVGIDNSDI-VYTAMDIIRKNKVEnvELIKGRLEDtDLPETKYDIII 272
Cdd:pfam06325 156 ERLVKpGESVLDVGCGSGILAIAALKLGAKKVVGVDIDPVaVRAAKENAELNGVE--ARLEVYLPG-DLPKEKADVVV 230
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
197-272 3.09e-14

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 72.49  E-value: 3.09e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24647025  197 EAVVRGKTVLDVGCGTGILSIFASKAGAARVVGIDNSDIVYtamdiirKNKVENVELiKGRLEDTDLPE--TKYDIII 272
Cdd:PRK00517 115 KLVLPGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAV-------EAARENAEL-NGVELNVYLPQgdLKADVIV 184
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 201-346 4.41e-13

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 68.02  E-value: 4.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 201 RGKTVLDVGCGTGILSIFASKAGAARVVGIDNS-DIVYTAMDIIRKNKVENVELIKGRLEDT-DLPETKYDIIISewMGY 278
Cdd:COG0500  26 KGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSpEAIALARARAAKAGLGNVEFLVADLAELdPLPAESFDLVVA--FGV 103

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24647025 279 F-LLYESMLDSIIYARENHLNPNGIIL-----PSRCTLSLLGYGDDTLYADEVEFWSNVYEVDMSDLRKQSIEE 346
Cdd:COG0500 104 LhHLPPEEREALLRELARALKPGGVLLlsasdAAAALSLARLLLLATASLLELLLLLRLLALELYLRALLAAAA 177
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 193-307 4.94e-13

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: 67.99  E-value: 4.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 193 LLQNEAVvRGKTVLDVGCGTGILSIFASKAGAARVVGIDNSDIVYTAMDI-IRKNKVEnVELIKGRLEDTDlPETKYDII 271
Cdd:COG3897  63 LLDHPEV-AGKRVLELGCGLGLVGIAAAKAGAADVTATDYDPEALAALRLnAALNGVA-ITTRLGDWRDPP-AAGGFDLI 139

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 24647025 272 I-SEwmgyfLLYE-SMLDSIIYARENHLNPNGIIL---PSR 307
Cdd:COG3897 140 LgGD-----VLYErDLAEPLLPFLDRLAAPGGEVLigdPGR 175
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 190-304 1.28e-12

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: 65.02  E-value: 1.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 190 RASLLQNEAVVRGKTVLDVGCGTGILSIFASKAGaARVVGIDNSDivyTAMDIIRKN---KVENVELIKGRLEDTDLPET 266
Cdd:COG2226  11 REALLAALGLRPGARVLDLGCGTGRLALALAERG-ARVTGVDISP---EMLELARERaaeAGLNVEFVVGDAEDLPFPDG 86

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 24647025 267 KYDIIISEWMGYFLLY-ESMLDSIiyARenHLNPNGIIL 304
Cdd:COG2226  87 SFDLVISSFVLHHLPDpERALAEI--AR--VLKPGGRLV 121
PRK14968 PRK14968
putative methyltransferase; Provisional
 193-304 2.36e-12

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 65.31  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025  193 LLQNEAVVRGKTVLDVGCGTGILSIFASKAGaARVVGID-NSDIVYTAMDIIRKNKVEN--VELIKGRLEDtDLPETKYD 269
Cdd:PRK14968  15 LAENAVDKKGDRVLEVGTGSGIVAIVAAKNG-KKVVGVDiNPYAVECAKCNAKLNNIRNngVEVIRSDLFE-PFRGDKFD 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24647025  270 III--------------SEWMGYFLlyeS-------MLDSIIYARENHLNPNGIIL 304
Cdd:PRK14968  93 VILfnppylpteeeeewDDWLNYAL---SggkdgreVIDRFLDEVGRYLKPGGRIL 145
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
189-304 7.77e-12

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 63.86  E-value: 7.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 189 YRASLLQNEAVVRGKTVLDVGCGTGILSIFASKAGaARVVGIDNSDivytAM-DIIRKNKVEnVELIKGRLEDTDLPETK 267
Cdd:COG4976  34 LAEELLARLPPGPFGRVLDLGCGTGLLGEALRPRG-YRLTGVDLSE----EMlAKAREKGVY-DRLLVADLADLAEPDGR 107

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24647025 268 YDIIISewmgyfllyesmLDSIIYARE---------NHLNPNGIIL 304
Cdd:COG4976 108 FDLIVA------------ADVLTYLGDlaavfagvaRALKPGGLFI 141
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
200-273 2.10e-11

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 63.00  E-value: 2.10e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24647025 200 VRGKTVLDVGCGTGILSIFASKAGAARVVGIdnsDIVYTAMDIIRKN---KVENVELIKGRLEDTDLPETkYDIIIS 273
Cdd:COG2263  44 IEGKTVLDLGCGTGMLAIGAALLGAKKVVGV---DIDPEALEIARENaerLGVRVDFIRADVTRIPLGGS-VDTVVM 116
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
201-304 2.48e-11

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 60.22  E-value: 2.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 201 RGKTVLDVGCGTGILS-IFASKAGAARVVGIDNSDivytAMdiIR--KNKVENVELIKGRLEDTDLPEtKYDIIISEWMG 277
Cdd:COG4106   1 PPRRVLDLGCGTGRLTaLLAERFPGARVTGVDLSP----EM--LAraRARLPNVRFVVADLRDLDPPE-PFDLVVSNAAL 73

                        90       100       110
                ....*....|....*....|....*....|..
gi 24647025 278 YFL-----LYESMLDsiiyarenHLNPNGIIL 304
Cdd:COG4106  74 HWLpdhaaLLARLAA--------ALAPGGVLA 97
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 202-304 3.06e-11

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 61.48  E-value: 3.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 202 GKTVLDVGCGTGILSIFASKAGAARVVGIDNSDivyTAMDIIRKNKVE-----NVELIKGRLEDTDLPETkYDIIIS--- 273
Cdd:COG2230  52 GMRVLDIGCGWGGLALYLARRYGVRVTGVTLSP---EQLEYARERAAEagladRVEVRLADYRDLPADGQ-FDAIVSigm 127

                        90       100       110
                ....*....|....*....|....*....|..
gi 24647025 274 -EWMGYfLLYESMLDSIiyARenHLNPNGIIL 304
Cdd:COG2230 128 fEHVGP-ENYPAYFAKV--AR--LLKPGGRLL 154
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 202-346 5.02e-11

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 60.89  E-value: 5.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   202 GKTVLDVGCGTGILSIF-ASKAGA-ARVVGIDNS-DIVYTAMDIIRKNKVENVELIKGRLED--TDLPETKYDIIISEwm 276
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFElAEELGPnAEVVGIDISeEAIEKARENAQKLGFDNVEFEQGDIEElpELLEDDKFDVVISN-- 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   277 gYFLLYESMLDSIIYARENHLNPNGIILPSRCtlSLLGYGDDTLYADEVEFWSNVYEVDMSDLRKQSIEE 346
Cdd:pfam13847  82 -CVLNHIPDPDKVLQEILRVLKPGGRLIISDP--DSLAELPAHVKEDSTYYAGCVGGAILKKKLYELLEE 148
prmA TIGR00406
ribosomal protein L11 methyltransferase; Ribosomal protein L11 methyltransferase is an ...
 199-272 1.70e-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: 58.69  E-value: 1.70e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24647025   199 VVRGKTVLDVGCGTGILSIFASKAGAARVVGIDNSDI-VYTAMDIIRKNKVENVELIKgRLEDTDLPETKYDIII 272
Cdd:TIGR00406 157 DLKDKNVIDVGCGSGILSIAALKLGAAKVVGIDIDPLaVESARKNAELNQVSDRLQVK-LIYLEQPIEGKADVIV 230
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 181-303 8.12e-09

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: 55.09  E-value: 8.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 181 SDKVRTSTYraSLLQNEavVRGKTVLDVGCGTGILSI-FASKaGAARVVGIDNSdivYTAMDIIRKNK-----VENVELI 254
Cdd:COG0742  25 TDRVREALF--NILGPD--IEGARVLDLFAGSGALGLeALSR-GAASVVFVEKD---RKAAAVIRKNLeklglEDRARVI 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 24647025 255 KGRLED--TDLPETKYDIIisewmgyFL-------LYESMLDSIiyARENHLNPNGII 303
Cdd:COG0742  97 RGDALRflKRLAGEPFDLV-------FLdppyakgLLEKALELL--AENGLLAPGGLI 145
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 206-276 2.96e-08

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 51.13  E-value: 2.96e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24647025   206 LDVGCGTGILSIFASKAGaARVVGIDNSDivyTAMDIIRKNKVEN-VELIKGRLEDTDLPETKYDIIISEWM 276
Cdd:pfam08241   1 LDVGCGTGLLTELLARLG-ARVTGVDISP---EMLELAREKAPREgLTFVVGDAEDLPFPDNSFDLVLSSEV 68
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 201-304 5.47e-08

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 52.43  E-value: 5.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   201 RGKTVLDVGCGTGILSIFASKAGaARVVGIDNSDIVYTAMDIIRKNKVENVELIkgrledtDLPETKYDIIISewmgyFL 280
Cdd:pfam13489  22 SPGRVLDFGCGTGIFLRLLRAQG-FSVTGVDPSPIAIERALLNVRFDQFDEQEA-------AVPAGKFDVIVA-----RE 88

                          90       100
                  ....*....|....*....|....*.
gi 24647025   281 LYESMLDSIIYARE--NHLNPNGIIL 304
Cdd:pfam13489  89 VLEHVPDPPALLRQiaALLKPGGLLL 114
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 193-273 5.52e-08

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: 52.88  E-value: 5.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 193 LLQNEAVVRGKTVLDVGCGTGILSIFASKAGA-ARVVGIDNSdivYTAMDIIRKN----KVENVELIKGrleD--TDLPE 265
Cdd:COG2813  41 LLEHLPEPLGGRVLDLGCGYGVIGLALAKRNPeARVTLVDVN---ARAVELARANaaanGLENVEVLWS---DglSGVPD 114


                ....*...
gi 24647025 266 TKYDIIIS 273
Cdd:COG2813 115 GSFDLILS 122
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
181-303 1.15e-07

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 51.47  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   181 SDKVRTSTYraSLLQNEavVRGKTVLDVGCGTGILSIFASKAGAARVVGIDNSDIVYTamdIIRKN----KVENVELIKG 256
Cdd:pfam03602  25 TDRVREALF--NWLAPY--IEGARVLDLFAGSGALGLEALSRGAKRVTLVEKDKRAVQ---ILKENlqllGLPGAVLVMD 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24647025   257 RLEDTD-LPETK--YDIIisewmgyFL-------LYESMLDSIiyARENHLNPNGII 303
Cdd:pfam03602  98 ALLALLrLAGKGpvFDIV-------FLdppyakgLIEEVLDLL--AEKGWLKPNALI 145
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 194-273 1.42e-07

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 52.86  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025  194 LQNEAVVRGKTVLDVGCGTGILSI-FASKAGAARVVGIDNSDIvytAMDIIRKN----KVENVELIKGRLEDtDLPETKY 268
Cdd:PRK09328 101 LEALLLKEPLRVLDLGTGSGAIALaLAKERPDAEVTAVDISPE---ALAVARRNakhgLGARVEFLQGDWFE-PLPGGRF 176


                 ....*
gi 24647025  269 DIIIS 273
Cdd:PRK09328 177 DLIVS 181
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 193-273 1.43e-07

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: 51.05  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   193 LLQNEAVVRGKTVLDVGCGTGILSIFASKAGA-ARVVGIDNSdivYTAMDIIRK----NKVENVELIKGRLEDtDLPETK 267
Cdd:pfam05175  23 LLEHLPKDLSGKVLDLGCGAGVLGAALAKESPdAELTMVDIN---ARALESAREnlaaNGLENGEVVASDVYS-GVEDGK 98


                  ....*.
gi 24647025   268 YDIIIS 273
Cdd:pfam05175  99 FDLIIS 104
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 201-273 6.25e-07

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: 50.53  E-value: 6.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 201 RGKTVLDVGCGTGILSIF-ASKAGAARVVGIDNSDIVYtamDIIRKNKVEN-----VELIKGRLED--TDLPETKYDIII 272
Cdd:COG4123  37 KGGRVLDLGTGTGVIALMlAQRSPGARITGVEIQPEAA---ELARRNVALNgledrITVIHGDLKEfaAELPPGSFDLVV 113


                .
gi 24647025 273 S 273
Cdd:COG4123 114 S 114
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 200-272 1.38e-06

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 50.18  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 200 VRGKTVLDVGCGTGILSIFASKAGAARVVGIDNSDivyTAMDIIRKNKVEN-----VELIKGR----LEDTDLPETKYDI 270
Cdd:COG1092 215 AKGKRVLNLFSYTGGFSVHAAAGGAKSVTSVDLSA---TALEWAKENAALNglddrHEFVQADafdwLRELAREGERFDL 291


                ..
gi 24647025 271 II 272
Cdd:COG1092 292 II 293
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 191-274 2.11e-06

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 47.64  E-value: 2.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 191 ASLLQNEAVVR-GKTVLDVGCGTGILSIFASKAGaARVVGID-NSDIVYTAMDIIRKNKVENVELIKGRLEDTDLPETKY 268
Cdd:COG1041  15 ARALVNLAGAKeGDTVLDPFCGTGTILIEAGLLG-RRVIGSDiDPKMVEGARENLEHYGYEDADVIRGDARDLPLADESV 93


                ....*.
gi 24647025 269 DIIISE 274
Cdd:COG1041  94 DAIVTD 99
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 201-273 2.91e-06

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 48.61  E-value: 2.91e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24647025 201 RGKTVLDVGCGTGILSI-FASKAGAARVVGIDNSDivyTAMDIIRKN----KVEN-VELIKGRLEDTDLPETKYDIIIS 273
Cdd:COG2890 112 APPRVLDLGTGSGAIALaLAKERPDARVTAVDISP---DALAVARRNaerlGLEDrVRFLQGDLFEPLPGDGRFDLIVS 187
CbiT TIGR02469
precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes ...
 201-304 3.25e-06

precorrin-6Y C5,15-methyltransferase (decarboxylating), CbiT subunit; This model recognizes the CbiT methylase which is responsible, in part (along with CbiE), for methylating precorrin-6y (or cobalt-precorrin-6y) at both the 5 and 15 positions as well as the concomitant decarbozylation at C-12. In many organisms, this protein is fused to the CbiE subunit. The fused protein, when found in organisms catalyzing the oxidative version of the cobalamin biosynthesis pathway, is called CobL. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 274148 [Multi-domain]  Cd Length: 124  Bit Score: 46.17  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   201 RGKTVLDVGCGTGILSIFASKA-GAARVVGIDNSDivyTAMDIIRKN----KVENVELIKGrledtDLPETKYDIIISEW 275
Cdd:TIGR02469  19 PGDVLWDIGAGTGSVTIEAARLvPNGRVYAIERNP---EALDLIERNlrrfGVSNIVIVEG-----DAPEAPEALLPDPD 90

                          90       100
                  ....*....|....*....|....*....
gi 24647025   276 MGYFLLYESMLDSIIYARENHLNPNGIIL 304
Cdd:TIGR02469  91 AVFVGGSGGLLQEILEAVERRLRPGGRIV 119
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 206-303 4.13e-06

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 45.05  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   206 LDVGCGTG-ILSIFASKAGAARVVGIDNSDIvytAMDIIRK-------NKVENVELIKGRLEDTDLPetKYDIIIsewMG 277
Cdd:pfam08242   1 LEIGCGTGtLLRALLEALPGLEYTGLDISPA---ALEAARErlaalglLNAVRVELFQLDLGELDPG--SFDVVV---AS 72

                          90       100
                  ....*....|....*....|....*.
gi 24647025   278 YFLLYESMLDSIIYARENHLNPNGII 303
Cdd:pfam08242  73 NVLHHLADPRAVLRNIRRLLKPGGVL 98
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 199-304 5.73e-06

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: 46.81  E-value: 5.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   199 VVRGKTVLDVGCGTGILSIFASKAGAARVVGIdnsDIVYtaMDIIRKNKVENVELIKG---RLEDTDLPET----KYDII 271
Cdd:pfam01728  19 LKPGKTVLDLGAAPGGWSQVALQRGAGKVVGV---DLGP--MQLWKPRNDPGVTFIQGdirDPETLDLLEEllgrKVDLV 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 24647025   272 ISEwMGYFLLYESMLDSIIYAR---------ENHLNPNGIIL 304
Cdd:pfam01728  94 LSD-GSPFISGNKVLDHLRSLDlvkaalevaLELLRKGGNFV 134
arsM PRK11873
arsenite methyltransferase;
202-273 6.23e-06

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 47.64  E-value: 6.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24647025  202 GKTVLDVGCGTGILSIFASKA-GA-ARVVGIDNSD-IVYTAMDIIRKNKVENVELIKGRLEDTDLPETKYDIIIS 273
Cdd:PRK11873  78 GETVLDLGSGGGFDCFLAARRvGPtGKVIGVDMTPeMLAKARANARKAGYTNVEFRLGEIEALPVADNSVDVIIS 152
PRK08317 PRK08317
hypothetical protein; Provisional
 189-274 1.43e-05

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 46.47  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025  189 YRASLLQNEAVVRGKTVLDVGCGTGILSI-FASKAGAA-RVVGIDNSDivytAMDIIRKNKVE----NVELIKGRLEDTD 262
Cdd:PRK08317   7 YRARTFELLAVQPGDRVLDVGCGPGNDAReLARRVGPEgRVVGIDRSE----AMLALAKERAAglgpNVEFVRGDADGLP 82

                         90
                 ....*....|..
gi 24647025  263 LPETKYDIIISE 274
Cdd:PRK08317  83 FPDGSFDAVRSD 94
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
 190-265 1.52e-05

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: 47.08  E-value: 1.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 190 RASLLQNEAVVRGKTVLDVGCGTGILSIFASKAG-AARVVGIDNSDivyTAMDIIRKNK----VENVELIKGRLED--TD 262
Cdd:COG2242 236 RALTLAKLALRPGDVLWDIGAGSGSVSIEAARLApGGRVYAIERDP---ERAALIRANArrfgVPNVEVVEGEAPEalAD 312


                ...
gi 24647025 263 LPE 265
Cdd:COG2242 313 LPD 315
PRK14967 PRK14967
putative methyltransferase; Provisional
 191-273 2.40e-05

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 45.43  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025  191 ASLLQNEAVVRGKTVLDVGCGTGILSIFASKAGAARVVGIdnsDIVYTAMDIIRKNKVEN---VELIKGRLEDTdLPETK 267
Cdd:PRK14967  26 ADALAAEGLGPGRRVLDLCTGSGALAVAAAAAGAGSVTAV---DISRRAVRSARLNALLAgvdVDVRRGDWARA-VEFRP 101


                 ....*.
gi 24647025  268 YDIIIS 273
Cdd:PRK14967 102 FDVVVS 107
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
 192-233 2.46e-05

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 45.60  E-value: 2.46e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 24647025  192 SLLQNEAVVRGKTVLDVGCGTGILSIFASKAGaARVVGIDNS 233
Cdd:PRK07580  54 SWLPADGDLTGLRILDAGCGVGSLSIPLARRG-AKVVASDIS 94
COG2521 COG2521
Predicted archaeal methyltransferase [General function prediction only];
174-272 3.15e-05

Predicted archaeal methyltransferase [General function prediction only];


Pssm-ID: 442011 [Multi-domain]  Cd Length: 285  Bit Score: 45.67  E-value: 3.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 174 GIHheMLSDKVRT----STYRASLLqneAVVRGKTVLDVGCGTGILSIFASKAGAARVVGIDNSDIVytaMDIIRKN--- 246
Cdd:COG2521 106 GIH--MHRIKGTDpledARRKVKLV---GVRRGDRVLDTCTGLGYTAIEALKRGAREVITVEKDPNV---LELAELNpws 177

                        90       100       110
                ....*....|....*....|....*....|.
gi 24647025 247 ---KVENVELIKGRLED--TDLPETKYDIII 272
Cdd:COG2521 178 relANERIKIILGDASEviKTFPDESFDAII 208
PRK15068 PRK15068
tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;
202-282 4.02e-05

tRNA 5-methoxyuridine(34)/uridine 5-oxyacetic acid(34) synthase CmoB;


Pssm-ID: 237898  Cd Length: 322  Bit Score: 45.62  E-value: 4.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025  202 GKTVLDVGCGTG-----ILSifaskAGAARVVGIDNSDIVYTAMDIIRK--NKVENVELIKGRLEdtDLPET-KYDIIIS 273
Cdd:PRK15068 123 GRTVLDVGCGNGyhmwrMLG-----AGAKLVVGIDPSQLFLCQFEAVRKllGNDQRAHLLPLGIE--QLPALkAFDTVFS 195


                 ....*....
gi 24647025  274 ewMGyfLLY 282
Cdd:PRK15068 196 --MG--VLY 200
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
 202-272 4.16e-05

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: 45.55  E-value: 4.16e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24647025 202 GKTVLDVGCGTGILSIFASKAgAARVVGID-NSDIVYTAMDIIRKNKVENVELIKGRLED---TDLPETKYDIII 272
Cdd:COG2265 234 GERVLDLYCGVGTFALPLARR-AKKVIGVEiVPEAVEDARENARLNGLKNVEFVAGDLEEvlpELLWGGRPDVVV 307
Methyltransf_9 pfam08003
Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It ...
 201-301 1.33e-04

Protein of unknown function (DUF1698); This family contains many hypothetical proteins. It also includes two putative methyltransferase proteins, Swiss:Q8EEE6 and Swiss:Q88MX8.


Pssm-ID: 429781 [Multi-domain]  Cd Length: 315  Bit Score: 43.93  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   201 RGKTVLDVGCGTGILSIFASKAGAARVVGIDNSDIVYTAMDIIRK--NKVENVELIKGRLEdtDLPETK-YDIIISewMG 277
Cdd:pfam08003 115 KGRTILDVGCGNGYHMWRMLGEGAAMVVGIDPSELFLCQFEAVRKllGNDQRAHLLPLGIE--QLPALAaFDTVFS--MG 190

                          90       100
                  ....*....|....*....|....*.
gi 24647025   278 yfLLY--ESMLDSIIyARENHLNPNG 301
Cdd:pfam08003 191 --VLYhrRSPLDHLL-QLKDQLVKGG 213
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 192-321 1.53e-04

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 43.04  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   192 SLLQNEAVVRGKTVLDVGCGTGILS-IFASKAGAARVVGIDNSDivytAMDIIRKNKV-ENVELIKGRLEDTDLPETKYD 269
Cdd:TIGR02072  25 ALLKEKGIFIPASVLDIGCGTGYLTrALLKRFPQAEFIALDISA----GMLAQAKTKLsENVQFICGDAEKLPLEDSSFD 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24647025   270 IIIS----EWMGYFllyESMLDSIiyARenHLNPNGIILPSrcTLsllgyGDDTLY 321
Cdd:TIGR02072 101 LIVSnlalQWCDDL---SQALSEL--AR--VLKPGGLLAFS--TF-----GPGTLH 142
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
190-301 1.99e-04

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 42.30  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025  190 RASLLQNEAVVRGKTVLDVGCGTGILSIFASKA-GAARVVGID-NSDivytAMDIIRKNK----VENVELIKGrLEDTDL 263
Cdd:PRK08287  20 RALALSKLELHRAKHLIDVGAGTGSVSIEAALQfPSLQVTAIErNPD----ALRLIKENRqrfgCGNIDIIPG-EAPIEL 94

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 24647025  264 PETKYDIIISEWMGYfllyesmLDSIIYARENHLNPNG 301
Cdd:PRK08287  95 PGKADAIFIGGSGGN-------LTAIIDWSLAHLHPGG 125
cbiT PRK00377
cobalt-precorrin-6Y C(15)-methyltransferase; Provisional
 190-320 2.72e-04

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


Pssm-ID: 234740  Cd Length: 198  Bit Score: 42.09  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025  190 RASLLQNEAVVRGKTVLDVGCGTGILSIFAS--KAGAARVVGIDNSDivyTAMDIIRKN-----KVENVELIKGrledtD 262
Cdd:PRK00377  29 RALALSKLRLRKGDMILDIGCGTGSVTVEASllVGETGKVYAVDKDE---KAINLTRRNaekfgVLNNIVLIKG-----E 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24647025  263 LPETkYDIIISEWMGYFLLYESM-LDSIIYARENHLNPNGIILPSRCTLSLLGYGDDTL 320
Cdd:PRK00377 101 APEI-LFTINEKFDRIFIGGGSEkLKEIISASWEIIKKGGRIVIDAILLETVNNALSAL 158
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
202-273 8.06e-04

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 41.04  E-value: 8.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24647025  202 GKTVLDVGCGTGILSIF-ASKAGAARVVGIDnSDIVYTAMDiiRKNKVENVELIKGRLEDTDLPEtkYDIIIS 273
Cdd:PRK14896  30 GDPVLEIGPGKGALTDElAKRAKKVYAIELD-PRLAEFLRD--DEIAAGNVEIIEGDALKVDLPE--FNKVVS 97
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 201-271 1.23e-03

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 40.52  E-value: 1.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24647025  201 RGKTVLDVGCGTGILSIFASKAG--AARVVGIDNSdivyTAM-DIIRK-----NKVENVELIKGRLEDTDLPETKYDII 271
Cdd:PRK00216  51 PGDKVLDLACGTGDLAIALAKAVgkTGEVVGLDFS----EGMlAVGREklrdlGLSGNVEFVQGDAEALPFPDNSFDAV 125
PLN02585 PLN02585
magnesium protoporphyrin IX methyltransferase
 192-235 1.45e-03

magnesium protoporphyrin IX methyltransferase


Pssm-ID: 215319 [Multi-domain]  Cd Length: 315  Bit Score: 40.61  E-value: 1.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 24647025  192 SLLQNEAVVRGKTVLDVGCGTGILSIFASKAGAArvvgIDNSDI 235
Cdd:PLN02585 135 LWLAEDGSLAGVTVCDAGCGTGSLAIPLALEGAI----VSASDI 174
Pcm COG2518
Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, ...
 191-272 1.62e-03

Protein-L-isoaspartate O-methyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442008 [Multi-domain]  Cd Length: 197  Bit Score: 39.69  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 191 ASLLQNEAVVRGKTVLDVGCGTG----ILSifaskAGAARVVGID-NSDIVYTAMDIIRKNKVENVELIKGRLEDTDLPE 265
Cdd:COG2518  56 ARMLEALDLKPGDRVLEIGTGSGyqaaVLA-----RLAGRVYSVErDPELAERARERLAALGYDNVTVRVGDGALGWPEH 130


                ....*..
gi 24647025 266 TKYDIII 272
Cdd:COG2518 131 APFDRII 137
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
 191-273 2.31e-03

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: 40.03  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   191 ASLLQNEAVVRgktVLDVGCGTGILSI-FASKAGAARVVGIDNS-DIVYTAMDIIRKNKVE-NVELIKGRLEDtDLPETK 267
Cdd:TIGR00536 107 ASLISQPPILH---ILDLGTGSGCIALaLAYEFPNAEVIAVDISpDALAVAEENAEKNQLEhRVEFIQSNLFE-PLAGQK 182


                  ....*.
gi 24647025   268 YDIIIS 273
Cdd:TIGR00536 183 IDIIVS 188
Gcd14 COG2519
tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 ...
 202-272 2.81e-03

tRNA A58 N-methylase Trm61 [Translation, ribosomal structure and biogenesis]; tRNA A58 N-methylase Trm61 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442009 [Multi-domain]  Cd Length: 249  Bit Score: 39.37  E-value: 2.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 202 GKTVLDVGCGTGILSIFaskagAARVVGidNSDIVYT------AMDIIRKN-----KVENVELIKGRLEDtDLPETKYDI 270
Cdd:COG2519  92 GARVLEAGTGSGALTLA-----LARAVG--PEGKVYSyerredFAEIARKNlerfgLPDNVELKLGDIRE-GIDEGDVDA 163


                ..
gi 24647025 271 II 272
Cdd:COG2519 164 VF 165
MenG_MenH_UbiE TIGR01934
ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of ...
 173-271 2.94e-03

ubiquinone/menaquinone biosynthesis methyltransferases; This model represents a family of methyltransferases involved in the biosynthesis of menaquinone and ubiqinone. Some members such as the UbiE enzyme from E. coli are believed to act in both pathways, while others may act in only the menaquinone pathway. These methyltransferases are members of the UbiE/CoQ family of methyltransferases (pfam01209) which also contains ubiquinone methyltransferases and other methyltransferases. Members of this clade include a wide distribution of bacteria and eukaryotes, but no archaea. An outgroup for this clade is provided by the phosphatidylethanolamine methyltransferase (EC 2.1.1.17) from Rhodobacter sphaeroides. Note that a number of non-orthologous genes which are members of pfam03737 have been erroneously annotated as MenG methyltransferases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273884 [Multi-domain]  Cd Length: 223  Bit Score: 39.17  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025   173 FGIHHemlsdkvrtsTYRASLLQNEAVVRGKTVLDVGCGTGILSIFASKAGAAR--VVGIDNSdivyTAM-DIIRKNKV- 248
Cdd:TIGR01934  21 FGLHR----------LWRRRAVKLIGVFKGQKVLDVACGTGDLAIELAKSAPDRgkVTGVDFS----SEMlEVAKKKSEl 86

                          90       100
                  ....*....|....*....|....
gi 24647025   249 -ENVELIKGRLEDTDLPETKYDII 271
Cdd:TIGR01934  87 pLNIEFIQADAEALPFEDNSFDAV 110
idonate-5-DH cd08232
L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of ...
 157-245 8.58e-03

L-idonate 5-dehydrogenase; L-idonate 5-dehydrogenase (L-ido 5-DH ) catalyzes the conversion of L-lodonate to 5-ketogluconate in the metabolism of L-Idonate to 6-P-gluconate. In E. coli, this GntII pathway is a subsidiary pathway to the canonical GntI system, which also phosphorylates and transports gluconate. L-ido 5-DH is found in an operon with a regulator indR, transporter idnT, 5-keto-D-gluconate 5-reductase, and Gnt kinase. L-ido 5-DH is a zinc-dependent alcohol dehydrogenase-like protein. The alcohol dehydrogenase ADH-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) which displays a broad range of activities and are distinguished from the smaller short chain dehydrogenases(~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176194 [Multi-domain]  Cd Length: 339  Bit Score: 38.37  E-value: 8.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647025 157 RNNVCLDNEYFKSYAHFGIHHEMLSDKV------------RTSTYRASLLQNEAV----------VRGKTVLDVGCGT-G 213
Cdd:cd08232  99 RPNLCLNMRFLGSAMRFPHVQGGFREYLvvdasqcvplpdGLSLRRAALAEPLAValhavnragdLAGKRVLVTGAGPiG 178

                        90       100       110
                ....*....|....*....|....*....|...
gi 24647025 214 ILSIFASK-AGAARVVGidnSDIVYTAMDIIRK 245
Cdd:cd08232 179 ALVVAAARrAGAAEIVA---TDLADAPLAVARA 208
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH