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Conserved domains on  [gi|254553431|ref|NP_079540|]
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THUMP domain-containing protein 2 isoform 1 [Homo sapiens]

Protein Classification

THUMP domain-containing class I SAM-dependent methyltransferase( domain architecture ID 10659626)

THUMP domain-containing 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; may be an RNA methylase

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047|GO:0003723
PubMed:  12504684|12826405|11295541
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 274-419 1.20e-28

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.).


The actual alignment was detected with superfamily member pfam01170:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 184  Bit Score: 111.68  E-value: 1.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  274 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 342
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  343 KAAGLEDKIELLKISVIELPLPSESVDIIISDIPFGKKFKLGKDI----KSILQEMERVLHVGGTIVLLLSEdhHRRLTD 418
Cdd:pfam01170  84 ENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALealyPEFLREAKRVLRGGGWLVLLTAE--NKDFEK 161


                  .
gi 254553431  419 C 419
Cdd:pfam01170 162 A 162
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 186-264 4.27e-08

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


:

Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 50.35  E-value: 4.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431   186 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 262
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 254553431   263 GI 264
Cdd:smart00981  81 SI 82
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 274-419 1.20e-28

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 111.68  E-value: 1.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  274 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 342
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  343 KAAGLEDKIELLKISVIELPLPSESVDIIISDIPFGKKFKLGKDI----KSILQEMERVLHVGGTIVLLLSEdhHRRLTD 418
Cdd:pfam01170  84 ENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALealyPEFLREAKRVLRGGGWLVLLTAE--NKDFEK 161


                  .
gi 254553431  419 C 419
Cdd:pfam01170 162 A 162
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 286-418 1.93e-25

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: 102.33  E-value: 1.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 286 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPS 365
Cdd:COG1041   14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI--GSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLAD 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254553431 366 ESVDIIISDIPFGKKFKLGKD-----IKSILQEMERVLHVGGTIVLLLSEDHHRRLTD 418
Cdd:COG1041   91 ESVDAIVTDPPYGRSSKISGEellelYEKALEEAARVLKPGGRVVIVTPRDIDELLEE 148
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 228-405 7.40e-19

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 87.49  E-value: 7.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  228 KVIGiAIMKHFGWKADLRNPQLEIFI-HLNDIYSVVGIPVFRV-------SLASRAYIKTAGLRSTIAWAMASLADIKAG 299
Cdd:TIGR01177 105 RKIG-AILKKKGFKVSLRRPDIVVRVvITEDIFYLGRVLEERDkeqfierKPDRRPFFKPGSMDPKLARAMVNLARVTEG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  300 AFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDIIISDIPFGK 379
Cdd:TIGR01177 184 DRVLDPFCGTGGFLIEAGLMGAKVI--GCDIDWKMVAGARINLEHYGIED-FFVKRGDATKLPLSSESVDAIATDPPYGR 260

                         170       180       190
                  ....*....|....*....|....*....|.
gi 254553431  380 KFKLGKD-----IKSILQEMERVLHVGGTIV 405
Cdd:TIGR01177 261 STTAAGDgleslYERSLEEFHEVLKSEGWIV 291
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
221-411 3.04e-15

tRNA (guanine(6)-N2)-methyltransferase;


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 77.02  E-value: 3.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 221 FTAQEVGKVIGIAIMKHFG------WKADLRNPQLEIFIHLNDIYSVVGIPVF-RVSLASR---AYIKTAGLRSTIAWAM 290
Cdd:NF040721 104 FTSIDIGRVAGEAVIDSYLrdkgvrLKVNLDEPDVIVRVELIFDELLVGIDTTgDEGLHKRgyrVYQHPAHLNPTIASSL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 291 ASLADIKAGAFVLDPMCGLGTILLEAA---------------------------KEWPDVYY--VGADVSDSQLLGTWDN 341
Cdd:NF040721 184 IYLSGWKDEESLLDPMCGSGTILIEAAlikrnippgkfredfafkkifghelleKIKKDVELkiYGIEKFRKHLEGAKKN 263

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254553431 342 LKAAGLEDKIELLKISVIELPLPSESVDIIISDIPFG----KKFKLGKDIKSILQEMERVLHVGGTIVLLLSED 411
Cdd:NF040721 264 AENAGVDDTIKFIQGDATKLDKYFDSVDVIVTNPPYGlrigKKRIIKKLYNNFLRSAKKILHKRSRIVVITAEK 337
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 302-406 3.88e-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: 3.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 302 VLDPMCGLGTILLEAAkEWPDVYYVGADVSDSQLlGTWDNLKAAGLEDKIELLKISVIELPL-PSESVDIIISDIPFgkk 380
Cdd:cd02440    2 VLDLGCGTGALALALA-SGPGARVTGVDISPVAL-ELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPL--- 76

                         90       100
                 ....*....|....*....|....*.
gi 254553431 381 FKLGKDIKSILQEMERVLHVGGTIVL 406
Cdd:cd02440   77 HHLVEDLARFLEEARRLLKPGGVLVL 102
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 283-407 1.11e-08

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 55.93  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 283 RSTIAWAmaslaDIKAGAFVLDPMCGLGTILLEAAKEWPDV-YYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIEL 361
Cdd:PRK00216  41 RKTIKWL-----GVRPGDKVLDLACGTGDLAIALAKAVGKTgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEAL 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 254553431 362 PLPSESVDII-ISdipFGkkfkLG--KDIKSILQEMERVLHVGGTIVLL 407
Cdd:PRK00216 116 PFPDNSFDAVtIA---FG----LRnvPDIDKALREMYRVLKPGGRLVIL 157
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 186-264 4.27e-08

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 50.35  E-value: 4.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431   186 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 262
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 254553431   263 GI 264
Cdd:smart00981  81 SI 82
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 204-264 1.14e-06

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 48.35  E-value: 1.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254553431 204 DLTFRVSCRCSGTigKAFTAQEVGKVIGIAIMKHFG-----WKADLRNPQLEIFIHLNDIYSVVGI 264
Cdd:cd11715   85 DGTFAVRATRVGS--KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSL 148
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 206-255 1.06e-04

THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 460749  Cd Length: 143  Bit Score: 42.43  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 254553431  206 TFRVSCRCSGTIGKaFTAQEVGKVIGIAIMKHFGWKADLRNPQLEIFIHL 255
Cdd:pfam02926  84 TFAVRVKRRGKNHE-FTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEI 132
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 274-419 1.20e-28

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 111.68  E-value: 1.20e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  274 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 342
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  343 KAAGLEDKIELLKISVIELPLPSESVDIIISDIPFGKKFKLGKDI----KSILQEMERVLHVGGTIVLLLSEdhHRRLTD 418
Cdd:pfam01170  84 ENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALealyPEFLREAKRVLRGGGWLVLLTAE--NKDFEK 161


                  .
gi 254553431  419 C 419
Cdd:pfam01170 162 A 162
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 286-418 1.93e-25

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: 102.33  E-value: 1.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 286 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPS 365
Cdd:COG1041   14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI--GSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLAD 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 254553431 366 ESVDIIISDIPFGKKFKLGKD-----IKSILQEMERVLHVGGTIVLLLSEDHHRRLTD 418
Cdd:COG1041   91 ESVDAIVTDPPYGRSSKISGEellelYEKALEEAARVLKPGGRVVIVTPRDIDELLEE 148
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 228-405 7.40e-19

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 87.49  E-value: 7.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  228 KVIGiAIMKHFGWKADLRNPQLEIFI-HLNDIYSVVGIPVFRV-------SLASRAYIKTAGLRSTIAWAMASLADIKAG 299
Cdd:TIGR01177 105 RKIG-AILKKKGFKVSLRRPDIVVRVvITEDIFYLGRVLEERDkeqfierKPDRRPFFKPGSMDPKLARAMVNLARVTEG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  300 AFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDIIISDIPFGK 379
Cdd:TIGR01177 184 DRVLDPFCGTGGFLIEAGLMGAKVI--GCDIDWKMVAGARINLEHYGIED-FFVKRGDATKLPLSSESVDAIATDPPYGR 260

                         170       180       190
                  ....*....|....*....|....*....|.
gi 254553431  380 KFKLGKD-----IKSILQEMERVLHVGGTIV 405
Cdd:TIGR01177 261 STTAAGDgleslYERSLEEFHEVLKSEGWIV 291
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
221-411 3.04e-15

tRNA (guanine(6)-N2)-methyltransferase;


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 77.02  E-value: 3.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 221 FTAQEVGKVIGIAIMKHFG------WKADLRNPQLEIFIHLNDIYSVVGIPVF-RVSLASR---AYIKTAGLRSTIAWAM 290
Cdd:NF040721 104 FTSIDIGRVAGEAVIDSYLrdkgvrLKVNLDEPDVIVRVELIFDELLVGIDTTgDEGLHKRgyrVYQHPAHLNPTIASSL 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 291 ASLADIKAGAFVLDPMCGLGTILLEAA---------------------------KEWPDVYY--VGADVSDSQLLGTWDN 341
Cdd:NF040721 184 IYLSGWKDEESLLDPMCGSGTILIEAAlikrnippgkfredfafkkifghelleKIKKDVELkiYGIEKFRKHLEGAKKN 263

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254553431 342 LKAAGLEDKIELLKISVIELPLPSESVDIIISDIPFG----KKFKLGKDIKSILQEMERVLHVGGTIVLLLSED 411
Cdd:NF040721 264 AENAGVDDTIKFIQGDATKLDKYFDSVDVIVTNPPYGlrigKKRIIKKLYNNFLRSAKKILHKRSRIVVITAEK 337
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 204-398 6.60e-15

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 76.29  E-value: 6.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 204 DLTFRVSCRCSGTIGKA--FTAQEVGKVIGIAIMKHFGW--KADLRNPQLEIFIHL-NDIYSV----VGIPVFRvslasR 274
Cdd:COG0116   87 DGTFAVDATSVKSKLFHsqFAALRVKDAIVDRFREKYGArpSVDEDGPDVRIHVHLlKDRATLsldtSGESLHK-----R 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 275 AYIKTAG---LRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAA----------------KEWPD------------- 322
Cdd:COG0116  162 GYREAQGeapLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAAliaaniapglnrdfafEKWPDfdaelwqelreea 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 323 ---------VYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIELPLPSESvDIIISDIPFGKKFKLGKDIKSILQE 393
Cdd:COG0116  242 earikrdppLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEP-GLIITNPPYGERLGEEEELEALYRE 320


                 ....*
gi 254553431 394 MERVL 398
Cdd:COG0116  321 LGDVL 325
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 289-418 5.39e-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: 63.47  E-value: 5.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 289 AMASLADIKAGAFVLDPMCGLGTILLEAAKEwpDVYYVGADVSDSQLLGTWDNLKAAGLedKIELLKISVIELPLPSESV 368
Cdd:COG2226   13 ALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPDGSF 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 254553431 369 DIIIS-----DIPfgkkfklgkDIKSILQEMERVLHVGGTIVLL-LSEDHHRRLTD 418
Cdd:COG2226   89 DLVISsfvlhHLP---------DPERALAEIARVLKPGGRLVVVdFSPPDLAELEE 135
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 302-406 3.88e-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: 3.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 302 VLDPMCGLGTILLEAAkEWPDVYYVGADVSDSQLlGTWDNLKAAGLEDKIELLKISVIELPL-PSESVDIIISDIPFgkk 380
Cdd:cd02440    2 VLDLGCGTGALALALA-SGPGARVTGVDISPVAL-ELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPL--- 76

                         90       100
                 ....*....|....*....|....*.
gi 254553431 381 FKLGKDIKSILQEMERVLHVGGTIVL 406
Cdd:cd02440   77 HHLVEDLARFLEEARRLLKPGGVLVL 102
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 303-406 4.15e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 53.82  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  303 LDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLlgtwDNLKAAGLEDKIELLKISVIELPLPSESVDIIISdipfgkKFK 382
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVT--GVDISPEML----ELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLS------SEV 68

                          90       100
                  ....*....|....*....|....*.
gi 254553431  383 LG--KDIKSILQEMERVLHVGGTIVL 406
Cdd:pfam08241  69 LHhvEDPERALREIARVLKPGGILII 94
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 283-407 1.11e-08

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 55.93  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 283 RSTIAWAmaslaDIKAGAFVLDPMCGLGTILLEAAKEWPDV-YYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIEL 361
Cdd:PRK00216  41 RKTIKWL-----GVRPGDKVLDLACGTGDLAIALAKAVGKTgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEAL 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 254553431 362 PLPSESVDII-ISdipFGkkfkLG--KDIKSILQEMERVLHVGGTIVLL 407
Cdd:PRK00216 116 PFPDNSFDAVtIA---FG----LRnvPDIDKALREMYRVLKPGGRLVIL 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 302-402 2.60e-08

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 51.41  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  302 VLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLedKIELLKISVIELPLPSESVDIIISDIPFGkkF 381
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLH--H 75

                          90       100
                  ....*....|....*....|.
gi 254553431  382 KLGKDIKSILQEMERVLHVGG 402
Cdd:pfam13649  76 LPDPDLEAALREIARVLKPGG 96
PRK08317 PRK08317
hypothetical protein; Provisional
 292-407 2.71e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.56  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 292 SLADIKAGAFVLDPMCGLGTILLEAAKE-WPDVYYVGADVSDSQLLGTwdNLKAAGLEDKIELLKISVIELPLPSESVDI 370
Cdd:PRK08317  13 ELLAVQPGDRVLDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALA--KERAAGLGPNVEFVRGDADGLPFPDGSFDA 90

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 254553431 371 IISDipfgKKFKLGKDIKSILQEMERVLHVGGTIVLL 407
Cdd:PRK08317  91 VRSD----RVLQHLEDPARALAEIARVLRPGGRVVVL 123
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 186-264 4.27e-08

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 50.35  E-value: 4.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431   186 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 262
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 254553431   263 GI 264
Cdd:smart00981  81 SI 82
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 290-406 2.50e-07

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 50.31  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 290 MASLADIKAGAFVLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIELPlPSESVD 369
Cdd:COG2230   43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADGQFD 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 254553431 370 IIISdipfgkkfkLG-------KDIKSILQEMERVLHVGGTIVL 406
Cdd:COG2230  121 AIVS---------IGmfehvgpENYPAYFAKVARLLKPGGRLLL 155
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 243-378 3.27e-07

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 52.88  E-value: 3.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 243 DLRNPQLEIFIHLNDIYSVVGIPVFRVSLASRAYIKTAG---LRSTIAWAMASLAD-IKAGAFVLDPMCGLGTILLEAA- 317
Cdd:PRK11783 131 DKEQPDIRINARLNKGEATISLDLSGESLHQRGYRQATGeapLKENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAAm 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 318 -----------KEW------------------------------PDVYYVGADvSDSQLLGT-WDNLKAAGLEDKIELLK 355
Cdd:PRK11783 211 maadiapglhrERWgfsgwlghdealwqelleeaqeraraglaeLPSKFYGSD-IDPRVIQAaRKNARRAGVAELITFEV 289

                        170       180
                 ....*....|....*....|....*
gi 254553431 356 ISVIEL--PLPSESVDIIISDIPFG 378
Cdd:PRK11783 290 KDVADLknPLPKGPTGLVISNPPYG 314
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 296-406 5.32e-07

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: 48.48  E-value: 5.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 296 IKAGAFVLDPMCGLGTILLEAAKEWPDVyyVGADVSDSQLlgtwDNLKAAGLEDKIELLKISVIELPLPSESVDIIIS-- 373
Cdd:COG2227   22 LPAGGRVLDVGCGTGRLALALARRGADV--TGVDISPEAL----EIARERAAELNVDFVQGDLEDLPLEDGSFDLVICse 95

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 254553431 374 ---DIPfgkkfklgkDIKSILQEMERVLHVGGTIVL 406
Cdd:COG2227   96 vleHLP---------DPAALLRELARLLKPGGLLLL 122
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 291-437 6.05e-07

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 49.91  E-value: 6.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 291 ASLADIKAGAFVLDPMCGLGTILLEAAKEwPDVYYVGADVSDSQLLGTWDNLKAAGLeDKIELLKISVIEL-PLPSESVD 369
Cdd:COG0500   19 ALLERLPKGGRVLDLGCGTGRNLLALAAR-FGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELdPLPAESFD 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254553431 370 IIIS-----DIPFGKkfklgkdIKSILQEMERVLHVGGtIVLLLSEDHHRRLTDCKESNIPFNSKDSHTDEPG 437
Cdd:COG0500   97 LVVAfgvlhHLPPEE-------REALLRELARALKPGG-VLLLSASDAAAALSLARLLLLATASLLELLLLLR 161
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 204-264 1.14e-06

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 48.35  E-value: 1.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254553431 204 DLTFRVSCRCSGTigKAFTAQEVGKVIGIAIMKHFG-----WKADLRNPQLEIFIHLNDIYSVVGI 264
Cdd:cd11715   85 DGTFAVRATRVGS--KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSL 148
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 296-406 1.68e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.72  E-value: 1.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  296 IKAGAFVLDPMCGLGTILLEAAKE-WPDVYYVGADVSDSQLLGTWDNLKAAGLED-KIELLKISVIELPLPSESVDIIIS 373
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGFDNvEFEQGDIEELPELLEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 254553431  374 DipfgKKFKLGKDIKSILQEMERVLHVGGTIVL 406
Cdd:pfam13847  81 N----CVLNHIPDPDKVLQEILRVLKPGGRLII 109
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
297-407 7.23e-05

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 44.35  E-value: 7.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  297 KAGAFVLDPMCGLGTI---LLEAAKEWPDVyyVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDIIIs 373
Cdd:pfam01209  41 KRGNKFLDVAGGTGDWtfgLSDSAGSSGKV--VGLDINENMLKEGEKKAKEEGKYN-IEFLQGNAEELPFEDDSFDIVT- 116

                          90       100       110
                  ....*....|....*....|....*....|....
gi 254553431  374 dIPFGkkFKLGKDIKSILQEMERVLHVGGTIVLL 407
Cdd:pfam01209 117 -ISFG--LRNFPDYLKVLKEAFRVLKPGGRVVCL 147
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 206-255 1.06e-04

THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 460749  Cd Length: 143  Bit Score: 42.43  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 254553431  206 TFRVSCRCSGTIGKaFTAQEVGKVIGIAIMKHFGWKADLRNPQLEIFIHL 255
Cdd:pfam02926  84 TFAVRVKRRGKNHE-FTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEI 132
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 286-406 1.64e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 43.61  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 286 IAWAMAsLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKaAGLEDKIELLKISVIElPLPS 365
Cdd:PRK09328  97 VEWALE-ALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAK-HGLGARVEFLQGDWFE-PLPG 173

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254553431 366 ESVDIIISD---IPFGKKFKL---------------GKD----IKSILQEMERVLHVGGTIVL 406
Cdd:PRK09328 174 GRFDLIVSNppyIPEADIHLLqpevrdhephlalfgGEDgldfYRRIIEQAPRYLKPGGWLLL 236
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 286-373 2.58e-04

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 42.83  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 286 IAWAMASLADIKAgAFVLDpmcgLGT----ILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIEl 361
Cdd:COG2890  101 VELALALLPAGAP-PRVLD----LGTgsgaIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFE- 174

                         90
                 ....*....|...
gi 254553431 362 PLPS-ESVDIIIS 373
Cdd:COG2890  175 PLPGdGRFDLIVS 187
arsM PRK11873
arsenite methyltransferase;
293-402 3.34e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 42.63  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 293 LADIKAGAFVLDPMCGLG-TILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDII 371
Cdd:PRK11873  72 LAELKPGETVLDLGSGGGfDCFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTN-VEFRLGEIEALPVADNSVDVI 150

                         90       100       110
                 ....*....|....*....|....*....|...
gi 254553431 372 ISD--IpfgkkfKLGKDIKSILQEMERVLHVGG 402
Cdd:PRK11873 151 ISNcvI------NLSPDKERVFKEAFRVLKPGG 177
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 302-377 6.84e-04

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: 40.65  E-value: 6.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254553431  302 VLDPMCGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIElPLPSESVDIIISDIPF 377
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLEN-GEVVASDVYS-GVEDGKFDLIISNPPF 108
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 302-406 8.50e-04

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: 40.56  E-value: 8.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 302 VLDPMCGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIElPLPSESVDIIISDIPfgkkF 381
Cdd:COG2813   53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLS-GVPDGSFDLILSNPP----F 126

                         90       100       110
                 ....*....|....*....|....*....|
gi 254553431 382 KLGKDI-KSILQEM----ERVLHVGGTIVL 406
Cdd:COG2813  127 HAGRAVdKEVAHALiadaARHLRPGGELWL 156
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
286-385 9.53e-04

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 40.94  E-value: 9.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 286 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAK--------EWPDVYYVGADVSDSqllgTWD----NLKAAGLEDKIEL 353
Cdd:COG0286   31 VVRLMVELLDPKPGETVYDPACGSGGFLVEAAEylkehggdERKKLSLYGQEINPT----TYRlakmNLLLHGIGDPNIE 106

                         90       100       110
                 ....*....|....*....|....*....|..
gi 254553431 354 LKISVIELPLPSESVDIIISDIPFGKKFKLGK 385
Cdd:COG0286  107 LGDTLSNDGDELEKFDVVLANPPFGGKWKKEE 138
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 307-404 9.86e-04

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.50  E-value: 9.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  307 CGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLED--KIELLKISVIELPLPseSVDIIISdipfgkkfkLG 384
Cdd:pfam08242   5 CGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELDPG--SFDVVVA---------SN 73

                          90       100
                  ....*....|....*....|....*
gi 254553431  385 -----KDIKSILQEMERVLHVGGTI 404
Cdd:pfam08242  74 vlhhlADPRAVLRNIRRLLKPGGVL 98
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 294-373 1.24e-03

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


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 40.77  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431  294 ADIKAGAFVLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIELPlpsESVDIIIS 373
Cdd:pfam02353  57 LGLKPGMTLLDIGCGWGGLMRRAAERY-DVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFD---EPFDRIVS 132
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 191-253 2.20e-03

THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the formation of the modified base S(4)U (4-thiouridine) found at position 8 in some prokaryotic tRNAs. This modification acts as a signal for UV exposure, triggering a response that provides protection against its damaging effects. ThiI consists of an N-terminal THUMP domain, followed by an NFLD domain, and a C-terminal PP-loop pyrophosphatase domain. The N-terminal THUMP domain has been implicated in the recognition of the acceptor-stem region. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212585  Cd Length: 166  Bit Score: 38.97  E-value: 2.20e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254553431 191 NDIEKA----IDTHNQNDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFI 253
Cdd:cd11716   82 EDIKEAalelLKEELKKGKTFKVRAKRADK-SFPFTSMEINREVGAALLENTPdLKVDLKNPDVTIRV 148
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
363-406 5.92e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 38.37  E-value: 5.92e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553431 363 LPSESVDIIISDIPF--GKKFKLGKD--------------IKSILQEMERVLHVGGTIVL 406
Cdd:COG0863   14 LPDESVDLIVTDPPYnlGKKYGLGRReignelsfeeylefLREWLAECYRVLKPGGSLYV 73
 
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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