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Conserved domains on  [gi|32566195|ref|NP_502174|]
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THUMP domain-containing protein [Caenorhabditis elegans]

Protein Classification

class I SAM-dependent methyltransferase; bifunctional glycosyltransferase/class I SAM-dependent methyltransferase( domain architecture ID 1915406)

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| bifunctional glycosyltransferase/class I SAM-dependent methyltransferase catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds and/or the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

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; ...
 212-381 8.78e-35

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: 126.70  E-value: 8.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195   212 GPTTMRSTMCHCMLQLADIKPGDIIVDAMCGGGSIPIEGAISWKNS-----------LFLGGDNHEmAMSRCLQNWSANS 280
Cdd:pfam01170   8 GPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIapgkfdarvraPLYGSDIDR-RMVQGARLNAENA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195   281 SSSRSNcDFLTWDATNLPLRDNSIDALVTDLPFGKKIGSTTDNRLLYPRLLAEWKRVLRKGGRLVLMTHDKRSLEnSFLK 360
Cdd:pfam01170  87 GVGDLI-EFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRGGGWLVLLTAENKDFE-KAAR 164

                         170       180
                  ....*....|....*....|.
gi 32566195   361 DRSSWQTdasHVVNVgGLSCL 381
Cdd:pfam01170 165 ERAWRKK---KEFNV-HIGGT 181
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 58-196 4.72e-18

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: 80.17  E-value: 4.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195    58 DNLYMVFYEETIE-KLSEMQKEDALKTIQSQISFCNWKLAIEAYQLARG-------NAINGGSEKILKQIQQFKKDRIYS 129
Cdd:pfam02926   1 KEIEELLKKGGINvEVVRSGRGRILVVLKGENPEEDRELLKEALEKAPGierfpvaETCEADLEDILELAKEIIKDKFKK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32566195   130 EvtddSPKFRVTCKRCGEKeiHKFSSMDAASKFGAEINNAFGWKCSVKEFDIEVVLRIDRNNMTVMM 196
Cdd:pfam02926  81 E----GETFAVRVKRRGKN--HEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 212-381 8.78e-35

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: 126.70  E-value: 8.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195   212 GPTTMRSTMCHCMLQLADIKPGDIIVDAMCGGGSIPIEGAISWKNS-----------LFLGGDNHEmAMSRCLQNWSANS 280
Cdd:pfam01170   8 GPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIapgkfdarvraPLYGSDIDR-RMVQGARLNAENA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195   281 SSSRSNcDFLTWDATNLPLRDNSIDALVTDLPFGKKIGSTTDNRLLYPRLLAEWKRVLRKGGRLVLMTHDKRSLEnSFLK 360
Cdd:pfam01170  87 GVGDLI-EFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRGGGWLVLLTAENKDFE-KAAR 164

                         170       180
                  ....*....|....*....|.
gi 32566195   361 DRSSWQTdasHVVNVgGLSCL 381
Cdd:pfam01170 165 ERAWRKK---KEFNV-HIGGT 181
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 213-351 1.32e-24

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: 98.87  E-value: 1.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195 213 PTTMRSTMCHCMLQLADIKPGDIIVDAMCGGGSIPIEGAISWKNSLflGGD-NHEMA-MSRclqnwSANSSSSRSNCDFL 290
Cdd:COG1041   7 PGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI--GSDiDPKMVeGAR-----ENLEHYGYEDADVI 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32566195 291 TWDATNLPLRDNSIDALVTDLPFGKKIGSTTDNRL-LYPRLLAEWKRVLRKGGRLVLMTHDK 351
Cdd:COG1041  80 RGDARDLPLADESVDAIVTDPPYGRSSKISGEELLeLYEKALEEAARVLKPGGRVVIVTPRD 141
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 58-196 4.72e-18

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: 80.17  E-value: 4.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195    58 DNLYMVFYEETIE-KLSEMQKEDALKTIQSQISFCNWKLAIEAYQLARG-------NAINGGSEKILKQIQQFKKDRIYS 129
Cdd:pfam02926   1 KEIEELLKKGGINvEVVRSGRGRILVVLKGENPEEDRELLKEALEKAPGierfpvaETCEADLEDILELAKEIIKDKFKK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32566195   130 EvtddSPKFRVTCKRCGEKeiHKFSSMDAASKFGAEINNAFGWKCSVKEFDIEVVLRIDRNNMTVMM 196
Cdd:pfam02926  81 E----GETFAVRVKRRGKN--HEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 7-198 3.27e-13

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: 66.83  E-value: 3.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195   7 ICAAVITGFEKVAAKEISKLFsPKKCHPGRGNVRFSIDLE---RVNetLQLRSIDNLYMVfyeetieklsemqkedalkt 83
Cdd:cd11715   1 FFATCPPGLEELLAAELKALG-AEDVEVGPGGVSFEGDLEdayRAN--LWLRTAHRVLLL-------------------- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195  84 iqsqisfcnwklaieayqLARGNAINggsekiLKQIQQFKKDRIYSEVTDDSPKFRVTCKRCGEkeiHKFSSMDAASKFG 163
Cdd:cd11715  58 ------------------LAEFEAED------FDDLYELAKAIDWEDYLDPDGTFAVRATRVGS---KLFHSQFAALRVK 110

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 32566195 164 AEINNAFG-----WKCSVKEFDIEVVLRIDRNNMTVMMAL 198
Cdd:cd11715 111 DAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSLDL 150
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 14-251 7.69e-13

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: 68.97  E-value: 7.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195  14 GFEKVAAKEISKLfSPKKCHPGRGNVRFSIDLE---RVNetLQLRSIDNLYMVFYEETIEKlsemqkEDALktiqsqisf 90
Cdd:COG0116  10 GLEALLADELKEL-GAEDVKVENGGVSFEGDLEdiyRAN--LWLRTASRVLLPLAEFKART------FDDL--------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195  91 cnwklaieaYQLARgnAINggsekilkqiqqfkkdriYSEVTDDSPKFRVTCKRCGEKEihkFSSMDAASKFGAEINNAF 170
Cdd:COG0116  72 ---------YEGAK--AIP------------------WEEYLPPDGTFAVDATSVKSKL---FHSQFAALRVKDAIVDRF 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195 171 GWKCSVKEF------DIEVVLRIDRNNMTVMMALNEESLFKRNicaY----GPTTMRSTMCHCMLQLADIKPGDIIVDAM 240
Cdd:COG0116 120 REKYGARPSvdedgpDVRIHVHLLKDRATLSLDTSGESLHKRG---YreaqGEAPLKETLAAALLLLSGWDGDRPLVDPM 196

                       250
                ....*....|.
gi 32566195 241 CGGGSIPIEGA 251
Cdd:COG0116 197 CGSGTILIEAA 207
PRK08317 PRK08317
hypothetical protein; Provisional
 225-354 2.03e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 57.64  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195  225 LQLADIKPGDIIVDAMCGGGSIPIEGAI-SWKNSLFLGGDNHE----MAMSRCLQNWSAnssssrsnCDFLTWDATNLPL 299
Cdd:PRK08317  12 FELLAVQPGDRVLDVGCGPGNDARELARrVGPEGRVVGIDRSEamlaLAKERAAGLGPN--------VEFVRGDADGLPF 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32566195  300 RDNSIDALVTDlpfgkkigsttdNRLLY----PRLLAEWKRVLRKGGRLVLMTHDKRSL 354
Cdd:PRK08317  84 PDGSFDAVRSD------------RVLQHledpARALAEIARVLRPGGRVVVLDTDWDTL 130
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 137-194 7.65e-07

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: 46.50  E-value: 7.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 32566195    137 KFRVTCKRCGEKeiHKFSSMDAASKFGAEINNAFG-WKCSVKEFDIEVVLRIDRNNMTV 194
Cdd:smart00981  24 TFAVRAKRRGKN--HEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 212-381 8.78e-35

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: 126.70  E-value: 8.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195   212 GPTTMRSTMCHCMLQLADIKPGDIIVDAMCGGGSIPIEGAISWKNS-----------LFLGGDNHEmAMSRCLQNWSANS 280
Cdd:pfam01170   8 GPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIapgkfdarvraPLYGSDIDR-RMVQGARLNAENA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195   281 SSSRSNcDFLTWDATNLPLRDNSIDALVTDLPFGKKIGSTTDNRLLYPRLLAEWKRVLRKGGRLVLMTHDKRSLEnSFLK 360
Cdd:pfam01170  87 GVGDLI-EFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRGGGWLVLLTAENKDFE-KAAR 164

                         170       180
                  ....*....|....*....|.
gi 32566195   361 DRSSWQTdasHVVNVgGLSCL 381
Cdd:pfam01170 165 ERAWRKK---KEFNV-HIGGT 181
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 213-351 1.32e-24

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: 98.87  E-value: 1.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195 213 PTTMRSTMCHCMLQLADIKPGDIIVDAMCGGGSIPIEGAISWKNSLflGGD-NHEMA-MSRclqnwSANSSSSRSNCDFL 290
Cdd:COG1041   7 PGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI--GSDiDPKMVeGAR-----ENLEHYGYEDADVI 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32566195 291 TWDATNLPLRDNSIDALVTDLPFGKKIGSTTDNRL-LYPRLLAEWKRVLRKGGRLVLMTHDK 351
Cdd:COG1041  80 RGDARDLPLADESVDAIVTDPPYGRSSKISGEELLeLYEKALEEAARVLKPGGRVVIVTPRD 141
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 58-196 4.72e-18

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: 80.17  E-value: 4.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195    58 DNLYMVFYEETIE-KLSEMQKEDALKTIQSQISFCNWKLAIEAYQLARG-------NAINGGSEKILKQIQQFKKDRIYS 129
Cdd:pfam02926   1 KEIEELLKKGGINvEVVRSGRGRILVVLKGENPEEDRELLKEALEKAPGierfpvaETCEADLEDILELAKEIIKDKFKK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32566195   130 EvtddSPKFRVTCKRCGEKeiHKFSSMDAASKFGAEINNAFGWKCSVKEFDIEVVLRIDRNNMTVMM 196
Cdd:pfam02926  81 E----GETFAVRVKRRGKN--HEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 7-198 3.27e-13

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: 66.83  E-value: 3.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195   7 ICAAVITGFEKVAAKEISKLFsPKKCHPGRGNVRFSIDLE---RVNetLQLRSIDNLYMVfyeetieklsemqkedalkt 83
Cdd:cd11715   1 FFATCPPGLEELLAAELKALG-AEDVEVGPGGVSFEGDLEdayRAN--LWLRTAHRVLLL-------------------- 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195  84 iqsqisfcnwklaieayqLARGNAINggsekiLKQIQQFKKDRIYSEVTDDSPKFRVTCKRCGEkeiHKFSSMDAASKFG 163
Cdd:cd11715  58 ------------------LAEFEAED------FDDLYELAKAIDWEDYLDPDGTFAVRATRVGS---KLFHSQFAALRVK 110

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 32566195 164 AEINNAFG-----WKCSVKEFDIEVVLRIDRNNMTVMMAL 198
Cdd:cd11715 111 DAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSLDL 150
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 14-251 7.69e-13

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: 68.97  E-value: 7.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195  14 GFEKVAAKEISKLfSPKKCHPGRGNVRFSIDLE---RVNetLQLRSIDNLYMVFYEETIEKlsemqkEDALktiqsqisf 90
Cdd:COG0116  10 GLEALLADELKEL-GAEDVKVENGGVSFEGDLEdiyRAN--LWLRTASRVLLPLAEFKART------FDDL--------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195  91 cnwklaieaYQLARgnAINggsekilkqiqqfkkdriYSEVTDDSPKFRVTCKRCGEKEihkFSSMDAASKFGAEINNAF 170
Cdd:COG0116  72 ---------YEGAK--AIP------------------WEEYLPPDGTFAVDATSVKSKL---FHSQFAALRVKDAIVDRF 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195 171 GWKCSVKEF------DIEVVLRIDRNNMTVMMALNEESLFKRNicaY----GPTTMRSTMCHCMLQLADIKPGDIIVDAM 240
Cdd:COG0116 120 REKYGARPSvdedgpDVRIHVHLLKDRATLSLDTSGESLHKRG---YreaqGEAPLKETLAAALLLLSGWDGDRPLVDPM 196

                       250
                ....*....|.
gi 32566195 241 CGGGSIPIEGA 251
Cdd:COG0116 197 CGSGTILIEAA 207
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 224-355 2.37e-11

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 61.16  E-value: 2.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195 224 MLQLADIKPGDIIVDAMCGGGSIPIegAISWKNSLFLGGD-NHEMamsrcLQNWSANSSSSRSNCDFLTWDATNLPLRDN 302
Cdd:COG2226  14 LLAALGLRPGARVLDLGCGTGRLAL--ALAERGARVTGVDiSPEM-----LELARERAAEAGLNVEFVVGDAEDLPFPDG 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 32566195 303 SIDALVTdlpfgkkigsttdNRLLY-----PRLLAEWKRVLRKGGRLVLMTHDKRSLE 355
Cdd:COG2226  87 SFDLVIS-------------SFVLHhlpdpERALAEIARVLKPGGRLVVVDFSPPDLA 131
PRK08317 PRK08317
hypothetical protein; Provisional
 225-354 2.03e-09

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 57.64  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195  225 LQLADIKPGDIIVDAMCGGGSIPIEGAI-SWKNSLFLGGDNHE----MAMSRCLQNWSAnssssrsnCDFLTWDATNLPL 299
Cdd:PRK08317  12 FELLAVQPGDRVLDVGCGPGNDARELARrVGPEGRVVGIDRSEamlaLAKERAAGLGPN--------VEFVRGDADGLPF 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32566195  300 RDNSIDALVTDlpfgkkigsttdNRLLY----PRLLAEWKRVLRKGGRLVLMTHDKRSL 354
Cdd:PRK08317  84 PDGSFDAVRSD------------RVLQHledpARALAEIARVLRPGGRVVVLDTDWDTL 130
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 137-194 7.65e-07

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: 46.50  E-value: 7.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 32566195    137 KFRVTCKRCGEKeiHKFSSMDAASKFGAEINNAFG-WKCSVKEFDIEVVLRIDRNNMTV 194
Cdd:smart00981  24 TFAVRAKRRGKN--HEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 293-346 1.78e-05

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 43.04  E-value: 1.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 32566195   293 DATNLPLRDNSIDALVTDLPFgkkigSTTDNRllyPRLLAEWKRVLRKGGRLVL 346
Cdd:pfam08241  49 DAEDLPFPDNSFDLVLSSEVL-----HHVEDP---ERALREIARVLKPGGILII 94
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 224-345 1.24e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 43.22  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32566195  224 MLQLADIKPGDIIVDAMCGGGSIpiegAISWKNSL-----FLGGD-NHEM---AMSRCLQNWSANSsssrsnCDFLTWDA 294
Cdd:PRK00216  43 TIKWLGVRPGDKVLDLACGTGDL----AIALAKAVgktgeVVGLDfSEGMlavGREKLRDLGLSGN------VEFVQGDA 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 32566195  295 TNLPLRDNSIDAL--------VTDlpfgkkigsttdnrllYPRLLAEWKRVLRKGGRLV 345
Cdd:PRK00216 113 EALPFPDNSFDAVtiafglrnVPD----------------IDKALREMYRVLKPGGRLV 155
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 287-342 1.34e-04

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 40.62  E-value: 1.34e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 32566195   287 CDFLTWDATNLPLRDNSIDALVTDLPFgkkiGSTTDNRLlyPRLLAEWKRVLRKGG 342
Cdd:pfam13649  47 VEFVQGDAEDLPFPDGSFDLVVSSGVL----HHLPDPDL--EAALREIARVLKPGG 96
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 180-251 6.81e-04

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: 41.71  E-value: 6.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32566195  180 DIEVVLRIDRNNMTVMMALNEESLFKRnicAY----GPTTMRSTMCHCMLQLAD-IKPGDIIVDAMCGGGSIPIEGA 251
Cdd:PRK11783 136 DIRINARLNKGEATISLDLSGESLHQR---GYrqatGEAPLKENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAA 209
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 298-346 1.69e-03

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: 39.02  E-value: 1.69e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 32566195 298 PLRDNSIDALVTDLPFgkKIGSTTDNRLLYpRLLAEWKRVLRKGGRLVL 346
Cdd:COG2813 111 GVPDGSFDLILSNPPF--HAGRAVDKEVAH-ALIADAARHLRPGGELWL 156
YhdJ COG0863
DNA modification methylase [Replication, recombination and repair];
299-347 5.24e-03

DNA modification methylase [Replication, recombination and repair];


Pssm-ID: 440623  Cd Length: 236  Bit Score: 37.98  E-value: 5.24e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32566195 299 LRDNSIDALVTDLPFGKKIGSTTDNRLL--------YPRLLAEW----KRVLRKGGRLVLM 347
Cdd:COG0863  14 LPDESVDLIVTDPPYNLGKKYGLGRREIgnelsfeeYLEFLREWlaecYRVLKPGGSLYVN 74
 
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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