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Conserved domains on  [gi|1009287601|ref|NP_001308398|]
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THUMP domain-containing protein 2 isoform 3 [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; ...
 181-326 4.20e-29

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: 4.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 181 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 249
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 250 KAAGLEDKIELLKISVIELPLPSESVDIIISDIPFGKKFKLGKDI----KSILQEMERVLHVGGTIVLLLSEdhHRRLTD 325
Cdd:pfam01170  84 ENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALealyPEFLREAKRVLRGGGWLVLLTAE--NKDFEK 161


                  .
gi 1009287601 326 C 326
Cdd:pfam01170 162 A 162
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 93-171 5.69e-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: 49.97  E-value: 5.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601   93 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 169
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 1009287601  170 GI 171
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 ...
 181-326 4.20e-29

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: 4.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 181 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 249
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 250 KAAGLEDKIELLKISVIELPLPSESVDIIISDIPFGKKFKLGKDI----KSILQEMERVLHVGGTIVLLLSEdhHRRLTD 325
Cdd:pfam01170  84 ENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALealyPEFLREAKRVLRGGGWLVLLTAE--NKDFEK 161


                  .
gi 1009287601 326 C 326
Cdd:pfam01170 162 A 162
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 193-325 8.27e-26

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: 8.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 193 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPS 272
Cdd:COG1041    14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI--GSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLAD 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1009287601 273 ESVDIIISDIPFGKKFKLGKD-----IKSILQEMERVLHVGGTIVLLLSEDHHRRLTD 325
Cdd:COG1041    91 ESVDAIVTDPPYGRSSKISGEellelYEKALEEAARVLKPGGRVVIVTPRDIDELLEE 148
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 135-312 4.06e-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: 4.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 135 KVIGiAIMKHFGWKADLRNPQLEIFI-HLNDIYSVVGIPVFRV-------SLASRAYIKTAGLRSTIAWAMASLADIKAG 206
Cdd:TIGR01177 105 RKIG-AILKKKGFKVSLRRPDIVVRVvITEDIFYLGRVLEERDkeqfierKPDRRPFFKPGSMDPKLARAMVNLARVTEG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 207 AFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDIIISDIPFGK 286
Cdd:TIGR01177 184 DRVLDPFCGTGGFLIEAGLMGAKVI--GCDIDWKMVAGARINLEHYGIED-FFVKRGDATKLPLSSESVDAIATDPPYGR 260

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1009287601 287 KFKLGKD-----IKSILQEMERVLHVGGTIV 312
Cdd:TIGR01177 261 STTAAGDgleslYERSLEEFHEVLKSEGWIV 291
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
128-318 2.19e-15

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


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 77.02  E-value: 2.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 128 FTAQEVGKVIGIAIMKHFG------WKADLRNPQLEIFIHLNDIYSVVGIPVF-RVSLASR---AYIKTAGLRSTIAWAM 197
Cdd:NF040721  104 FTSIDIGRVAGEAVIDSYLrdkgvrLKVNLDEPDVIVRVELIFDELLVGIDTTgDEGLHKRgyrVYQHPAHLNPTIASSL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 198 ASLADIKAGAFVLDPMCGLGTILLEAA---------------------------KEWPDVYY--VGADVSDSQLLGTWDN 248
Cdd:NF040721  184 IYLSGWKDEESLLDPMCGSGTILIEAAlikrnippgkfredfafkkifghelleKIKKDVELkiYGIEKFRKHLEGAKKN 263

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1009287601 249 LKAAGLEDKIELLKISVIELPLPSESVDIIISDIPFG----KKFKLGKDIKSILQEMERVLHVGGTIVLLLSED 318
Cdd:NF040721  264 AENAGVDDTIKFIQGDATKLDKYFDSVDVIVTNPPYGlrigKKRIIKKLYNNFLRSAKKILHKRSRIVVITAEK 337
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 209-313 2.98e-10

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 57.05  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 209 VLDPMCGLGTILLEAAkEWPDVYYVGADVSDSQLlGTWDNLKAAGLEDKIELLKISVIELPL-PSESVDIIISDIPFgkk 287
Cdd:cd02440     2 VLDLGCGTGALALALA-SGPGARVTGVDISPVAL-ELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPL--- 76

                          90       100
                  ....*....|....*....|....*.
gi 1009287601 288 FKLGKDIKSILQEMERVLHVGGTIVL 313
Cdd:cd02440    77 HHLVEDLARFLEEARRLLKPGGVLVL 102
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 190-314 7.10e-09

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: 7.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 190 RSTIAWAmaslaDIKAGAFVLDPMCGLGTILLEAAKEWPDV-YYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIEL 268
Cdd:PRK00216   41 RKTIKWL-----GVRPGDKVLDLACGTGDLAIALAKAVGKTgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEAL 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1009287601 269 PLPSESVDII-ISdipFGkkfkLG--KDIKSILQEMERVLHVGGTIVLL 314
Cdd:PRK00216  116 PFPDNSFDAVtIA---FG----LRnvPDIDKALREMYRVLKPGGRLVIL 157
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 93-171 5.69e-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: 49.97  E-value: 5.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601   93 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 169
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 1009287601  170 GI 171
Cdd:smart00981  81 SI 82
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 111-171 8.28e-07

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: 8.28e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009287601 111 DLTFRVSCRCSGTigKAFTAQEVGKVIGIAIMKHFG-----WKADLRNPQLEIFIHLNDIYSVVGI 171
Cdd:cd11715    85 DGTFAVRATRVGS--KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSL 148
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 113-162 7.75e-05

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: 7.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287601 113 TFRVSCRCSGTIGKaFTAQEVGKVIGIAIMKHFGWKADLRNPQLEIFIHL 162
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 ...
 181-326 4.20e-29

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: 4.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 181 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 249
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 250 KAAGLEDKIELLKISVIELPLPSESVDIIISDIPFGKKFKLGKDI----KSILQEMERVLHVGGTIVLLLSEdhHRRLTD 325
Cdd:pfam01170  84 ENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALealyPEFLREAKRVLRGGGWLVLLTAE--NKDFEK 161


                  .
gi 1009287601 326 C 326
Cdd:pfam01170 162 A 162
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 193-325 8.27e-26

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: 8.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 193 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPS 272
Cdd:COG1041    14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI--GSDIDPKMVEGARENLEHYGYED-ADVIRGDARDLPLAD 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1009287601 273 ESVDIIISDIPFGKKFKLGKD-----IKSILQEMERVLHVGGTIVLLLSEDHHRRLTD 325
Cdd:COG1041    91 ESVDAIVTDPPYGRSSKISGEellelYEKALEEAARVLKPGGRVVIVTPRDIDELLEE 148
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 135-312 4.06e-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: 4.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 135 KVIGiAIMKHFGWKADLRNPQLEIFI-HLNDIYSVVGIPVFRV-------SLASRAYIKTAGLRSTIAWAMASLADIKAG 206
Cdd:TIGR01177 105 RKIG-AILKKKGFKVSLRRPDIVVRVvITEDIFYLGRVLEERDkeqfierKPDRRPFFKPGSMDPKLARAMVNLARVTEG 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 207 AFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDIIISDIPFGK 286
Cdd:TIGR01177 184 DRVLDPFCGTGGFLIEAGLMGAKVI--GCDIDWKMVAGARINLEHYGIED-FFVKRGDATKLPLSSESVDAIATDPPYGR 260

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1009287601 287 KFKLGKD-----IKSILQEMERVLHVGGTIV 312
Cdd:TIGR01177 261 STTAAGDgleslYERSLEEFHEVLKSEGWIV 291
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
128-318 2.19e-15

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


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 77.02  E-value: 2.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 128 FTAQEVGKVIGIAIMKHFG------WKADLRNPQLEIFIHLNDIYSVVGIPVF-RVSLASR---AYIKTAGLRSTIAWAM 197
Cdd:NF040721  104 FTSIDIGRVAGEAVIDSYLrdkgvrLKVNLDEPDVIVRVELIFDELLVGIDTTgDEGLHKRgyrVYQHPAHLNPTIASSL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 198 ASLADIKAGAFVLDPMCGLGTILLEAA---------------------------KEWPDVYY--VGADVSDSQLLGTWDN 248
Cdd:NF040721  184 IYLSGWKDEESLLDPMCGSGTILIEAAlikrnippgkfredfafkkifghelleKIKKDVELkiYGIEKFRKHLEGAKKN 263

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1009287601 249 LKAAGLEDKIELLKISVIELPLPSESVDIIISDIPFG----KKFKLGKDIKSILQEMERVLHVGGTIVLLLSED 318
Cdd:NF040721  264 AENAGVDDTIKFIQGDATKLDKYFDSVDVIVTNPPYGlrigKKRIIKKLYNNFLRSAKKILHKRSRIVVITAEK 337
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 111-305 2.66e-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: 76.68  E-value: 2.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 111 DLTFRVSCRCSGTIGKA--FTAQEVGKVIGIAIMKHFGW--KADLRNPQLEIFIHL-NDIYSV----VGIPVFRvslasR 181
Cdd:COG0116    87 DGTFAVDATSVKSKLFHsqFAALRVKDAIVDRFREKYGArpSVDEDGPDVRIHVHLlKDRATLsldtSGESLHK-----R 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 182 AYIKTAG---LRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAA----------------KEWPD------------- 229
Cdd:COG0116   162 GYREAQGeapLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAAliaaniapglnrdfafEKWPDfdaelwqelreea 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 230 ---------VYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIELPLPSESvDIIISDIPFGKKFKLGKDIKSILQE 300
Cdd:COG0116   242 earikrdppLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPPAEP-GLIITNPPYGERLGEEEELEALYRE 320


                  ....*
gi 1009287601 301 MERVL 305
Cdd:COG0116   321 LGDVL 325
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 196-325 4.14e-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: 4.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 196 AMASLADIKAGAFVLDPMCGLGTILLEAAKEwpDVYYVGADVSDSQLLGTWDNLKAAGLedKIELLKISVIELPLPSESV 275
Cdd:COG2226    13 ALLAALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGL--NVEFVVGDAEDLPFPDGSF 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1009287601 276 DIIIS-----DIPfgkkfklgkDIKSILQEMERVLHVGGTIVLL-LSEDHHRRLTD 325
Cdd:COG2226    89 DLVISsfvlhHLP---------DPERALAEIARVLKPGGRLVVVdFSPPDLAELEE 135
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 209-313 2.98e-10

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 57.05  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 209 VLDPMCGLGTILLEAAkEWPDVYYVGADVSDSQLlGTWDNLKAAGLEDKIELLKISVIELPL-PSESVDIIISDIPFgkk 287
Cdd:cd02440     2 VLDLGCGTGALALALA-SGPGARVTGVDISPVAL-ELARKAAAALLADNVEVLKGDAEELPPeADESFDVIISDPPL--- 76

                          90       100
                  ....*....|....*....|....*.
gi 1009287601 288 FKLGKDIKSILQEMERVLHVGGTIVL 313
Cdd:cd02440    77 HHLVEDLARFLEEARRLLKPGGVLVL 102
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 210-313 3.03e-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: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 210 LDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLlgtwDNLKAAGLEDKIELLKISVIELPLPSESVDIIISdipfgkKFK 289
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVT--GVDISPEML----ELAREKAPREGLTFVVGDAEDLPFPDNSFDLVLS------SEV 68

                          90       100
                  ....*....|....*....|....*.
gi 1009287601 290 LG--KDIKSILQEMERVLHVGGTIVL 313
Cdd:pfam08241  69 LHhvEDPERALREIARVLKPGGILII 94
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 190-314 7.10e-09

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: 7.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 190 RSTIAWAmaslaDIKAGAFVLDPMCGLGTILLEAAKEWPDV-YYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIEL 268
Cdd:PRK00216   41 RKTIKWL-----GVRPGDKVLDLACGTGDLAIALAKAVGKTgEVVGLDFSEGMLAVGREKLRDLGLSGNVEFVQGDAEAL 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1009287601 269 PLPSESVDII-ISdipFGkkfkLG--KDIKSILQEMERVLHVGGTIVLL 314
Cdd:PRK00216  116 PFPDNSFDAVtIA---FG----LRnvPDIDKALREMYRVLKPGGRLVIL 157
PRK08317 PRK08317
hypothetical protein; Provisional
 199-314 2.00e-08

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 54.56  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 199 SLADIKAGAFVLDPMCGLGTILLEAAKE-WPDVYYVGADVSDSQLLGTwdNLKAAGLEDKIELLKISVIELPLPSESVDI 277
Cdd:PRK08317   13 ELLAVQPGDRVLDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALA--KERAAGLGPNVEFVRGDADGLPFPDGSFDA 90

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1009287601 278 IISDipfgKKFKLGKDIKSILQEMERVLHVGGTIVLL 314
Cdd:PRK08317   91 VRSD----RVLQHLEDPARALAEIARVLRPGGRVVVL 123
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 209-309 2.07e-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: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 209 VLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLedKIELLKISVIELPLPSESVDIIISDIPFGkkF 288
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAGL--NVEFVQGDAEDLPFPDGSFDLVVSSGVLH--H 75

                          90       100
                  ....*....|....*....|.
gi 1009287601 289 KLGKDIKSILQEMERVLHVGG 309
Cdd:pfam13649  76 LPDPDLEAALREIARVLKPGG 96
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 93-171 5.69e-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: 49.97  E-value: 5.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601   93 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 169
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 1009287601  170 GI 171
Cdd:smart00981  81 SI 82
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 197-313 1.93e-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: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 197 MASLADIKAGAFVLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIELPlPSESVD 276
Cdd:COG2230    43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVRLADYRDLP-ADGQFD 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1009287601 277 IIISdipfgkkfkLG-------KDIKSILQEMERVLHVGGTIVL 313
Cdd:COG2230   121 AIVS---------IGmfehvgpENYPAYFAKVARLLKPGGRLLL 155
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 150-285 2.43e-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: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 150 DLRNPQLEIFIHLNDIYSVVGIPVFRVSLASRAYIKTAG---LRSTIAWAMASLAD-IKAGAFVLDPMCGLGTILLEAA- 224
Cdd:PRK11783  131 DKEQPDIRINARLNKGEATISLDLSGESLHQRGYRQATGeapLKENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAAm 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 225 -----------KEW------------------------------PDVYYVGADvSDSQLLGT-WDNLKAAGLEDKIELLK 262
Cdd:PRK11783  211 maadiapglhrERWgfsgwlghdealwqelleeaqeraraglaeLPSKFYGSD-IDPRVIQAaRKNARRAGVAELITFEV 289

                         170       180
                  ....*....|....*....|....*
gi 1009287601 263 ISVIEL--PLPSESVDIIISDIPFG 285
Cdd:PRK11783  290 KDVADLknPLPKGPTGLVISNPPYG 314
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 203-313 4.19e-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: 4.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 203 IKAGAFVLDPMCGLGTILLEAAKEWPDVyyVGADVSDSQLlgtwDNLKAAGLEDKIELLKISVIELPLPSESVDIIIS-- 280
Cdd:COG2227    22 LPAGGRVLDVGCGTGRLALALARRGADV--TGVDISPEAL----EIARERAAELNVDFVQGDLEDLPLEDGSFDLVICse 95

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1009287601 281 ---DIPfgkkfklgkDIKSILQEMERVLHVGGTIVL 313
Cdd:COG2227    96 vleHLP---------DPAALLRELARLLKPGGLLLL 122
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 198-344 4.59e-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: 4.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 198 ASLADIKAGAFVLDPMCGLGTILLEAAKEwPDVYYVGADVSDSQLLGTWDNLKAAGLeDKIELLKISVIEL-PLPSESVD 276
Cdd:COG0500    19 ALLERLPKGGRVLDLGCGTGRNLLALAAR-FGGRVIGIDLSPEAIALARARAAKAGL-GNVEFLVADLAELdPLPAESFD 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009287601 277 IIIS-----DIPFGKkfklgkdIKSILQEMERVLHVGGtIVLLLSEDHHRRLTDCKESNIPFNSKDSHTDEPG 344
Cdd:COG0500    97 LVVAfgvlhHLPPEE-------REALLRELARALKPGG-VLLLSASDAAAALSLARLLLLATASLLELLLLLR 161
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 111-171 8.28e-07

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: 8.28e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009287601 111 DLTFRVSCRCSGTigKAFTAQEVGKVIGIAIMKHFG-----WKADLRNPQLEIFIHLNDIYSVVGI 171
Cdd:cd11715    85 DGTFAVRATRVGS--KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSL 148
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 203-313 1.64e-05

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 44.72  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 203 IKAGAFVLDPMCGLGTILLEAAKE-WPDVYYVGADVSDSQLLGTWDNLKAAGLED-KIELLKISVIELPLPSESVDIIIS 280
Cdd:pfam13847   1 IDKGMRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGFDNvEFEQGDIEELPELLEDDKFDVVIS 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1009287601 281 DipfgKKFKLGKDIKSILQEMERVLHVGGTIVL 313
Cdd:pfam13847  81 N----CVLNHIPDPDKVLQEILRVLKPGGRLII 109
Ubie_methyltran pfam01209
ubiE/COQ5 methyltransferase family;
204-314 4.67e-05

ubiE/COQ5 methyltransferase family;


Pssm-ID: 395966 [Multi-domain]  Cd Length: 228  Bit Score: 44.35  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 204 KAGAFVLDPMCGLGTI---LLEAAKEWPDVyyVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDIIIs 280
Cdd:pfam01209  41 KRGNKFLDVAGGTGDWtfgLSDSAGSSGKV--VGLDINENMLKEGEKKAKEEGKYN-IEFLQGNAEELPFEDDSFDIVT- 116

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1009287601 281 dIPFGkkFKLGKDIKSILQEMERVLHVGGTIVLL 314
Cdd:pfam01209 117 -ISFG--LRNFPDYLKVLKEAFRVLKPGGRVVCL 147
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 113-162 7.75e-05

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: 7.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287601 113 TFRVSCRCSGTIGKaFTAQEVGKVIGIAIMKHFGWKADLRNPQLEIFIHL 162
Cdd:pfam02926  84 TFAVRVKRRGKNHE-FTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEI 132
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
 193-313 1.25e-04

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


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 43.61  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 193 IAWAMAsLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKaAGLEDKIELLKISVIElPLPS 272
Cdd:PRK09328   97 VEWALE-ALLLKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAK-HGLGARVEFLQGDWFE-PLPG 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1009287601 273 ESVDIIISD---IPFGKKFKL---------------GKD----IKSILQEMERVLHVGGTIVL 313
Cdd:PRK09328  174 GRFDLIVSNppyIPEADIHLLqpevrdhephlalfgGEDgldfYRRIIEQAPRYLKPGGWLLL 236
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 193-280 1.92e-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: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 193 IAWAMASLADIKAgAFVLDpmcgLGT----ILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIEl 268
Cdd:COG2890   101 VELALALLPAGAP-PRVLD----LGTgsgaIALALAKERPDARVTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFE- 174

                          90
                  ....*....|...
gi 1009287601 269 PLPS-ESVDIIIS 280
Cdd:COG2890   175 PLPGdGRFDLIVS 187
arsM PRK11873
arsenite methyltransferase;
200-309 2.09e-04

arsenite methyltransferase;


Pssm-ID: 237007 [Multi-domain]  Cd Length: 272  Bit Score: 42.63  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 200 LADIKAGAFVLDPMCGLG-TILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIELPLPSESVDII 278
Cdd:PRK11873   72 LAELKPGETVLDLGSGGGfDCFLAARRVGPTGKVIGVDMTPEMLAKARANARKAGYTN-VEFRLGEIEALPVADNSVDVI 150

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1009287601 279 ISD--IpfgkkfKLGKDIKSILQEMERVLHVGG 309
Cdd:PRK11873  151 ISNcvI------NLSPDKERVFKEAFRVLKPGG 177
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 209-284 5.29e-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: 5.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009287601 209 VLDPMCGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIElPLPSESVDIIISDIPF 284
Cdd:pfam05175  35 VLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLEN-GEVVASDVYS-GVEDGKFDLIISNPPF 108
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 209-313 6.53e-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: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 209 VLDPMCGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLEDkIELLKISVIElPLPSESVDIIISDIPfgkkF 288
Cdd:COG2813    53 VLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARANAAANGLEN-VEVLWSDGLS-GVPDGSFDLILSNPP----F 126

                          90       100       110
                  ....*....|....*....|....*....|
gi 1009287601 289 KLGKDI-KSILQEM----ERVLHVGGTIVL 313
Cdd:COG2813   127 HAGRAVdKEVAHALiadaARHLRPGGELWL 156
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
193-292 7.01e-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: 7.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 193 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAK--------EWPDVYYVGADVSDSqllgTWD----NLKAAGLEDKIEL 260
Cdd:COG0286    31 VVRLMVELLDPKPGETVYDPACGSGGFLVEAAEylkehggdERKKLSLYGQEINPT----TYRlakmNLLLHGIGDPNIE 106

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1009287601 261 LKISVIELPLPSESVDIIISDIPFGKKFKLGK 292
Cdd:COG0286   107 LGDTLSNDGDELEKFDVVLANPPFGGKWKKEE 138
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 214-311 8.01e-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: 8.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 214 CGLGTILLEAAKEWPDVYYVGADVSDSQLLGTWDNLKAAGLED--KIELLKISVIELPLPseSVDIIISdipfgkkfkLG 291
Cdd:pfam08242   5 CGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNavRVELFQLDLGELDPG--SFDVVVA---------SN 73

                          90       100
                  ....*....|....*....|....*
gi 1009287601 292 -----KDIKSILQEMERVLHVGGTI 311
Cdd:pfam08242  74 vlhhlADPRAVLRNIRRLLKPGGVL 98
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 201-280 9.31e-04

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


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 40.77  E-value: 9.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 201 ADIKAGAFVLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELLKISVIELPlpsESVDIIIS 280
Cdd:pfam02353  57 LGLKPGMTLLDIGCGWGGLMRRAAERY-DVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLLQDYRDFD---EPFDRIVS 132
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 98-160 1.66e-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: 1.66e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1009287601  98 NDIEKA----IDTHNQNDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFI 160
Cdd:cd11716    82 EDIKEAalelLKEELKKGKTFKVRAKRADK-SFPFTSMEINREVGAALLENTPdLKVDLKNPDVTIRV 148
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
270-313 5.07e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 38.37  E-value: 5.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287601 270 LPSESVDIIISDIPF--GKKFKLGKD--------------IKSILQEMERVLHVGGTIVL 313
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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