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Conserved domains on  [gi|2527967767|ref|WP_288922918|]
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class I SAM-dependent RNA methyltransferase [uncultured Ottowia sp.]

Protein Classification

THUMP domain-containing class I SAM-dependent RNA methyltransferase( domain architecture ID 11414754)

THUMP domain-containing class I SAM-dependent RNA methyltransferase catalyzes the methylation of a specific RNA substrate using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor, such as ribosomal RNA large subunit methyltransferase L that specifically methylates the guanine in position 2445 (m2G2445) of 23S rRNA

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0001510|GO:0008757|GO:1904047
PubMed:  11295541|12826405|12504684
SCOP:  3000118

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 6-421 3.37e-175

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: 494.23  E-value: 3.37e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767   6 LTLFLPCAAGVQDFLADEvhgLTGLAGQDLLIERGGIYARGRWRDVMRLNLHSRLAQRVLLELAHVPCESEDALYALARR 85
Cdd:COG0116     1 FELFATCARGLEALLADE---LKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767  86 VPWEDWFGTRHTFRVDVTARGSAFKSLQFAALRVKDAVADRFRERSGARPSVQTQQPDVRIHLHLDGAHASLLLDTSGEP 165
Cdd:COG0116    78 IPWEEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 166 LFKRGWRQDKGDAPLKETLAAAMLAASGwWQPARravaaqPLYDPCCGSGTIVIEAAQLALGLPPGGQRRFAFERLPLFK 245
Cdd:COG0116   158 LHKRGYREAQGEAPLKETLAAALLLLSG-WDGDR------PLVDPMCGSGTILIEAALIAANIAPGLNRDFAFEKWPDFD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 246 RDEWQAMKDeAEAAARPAPAAPRIFGSDVSHRMVDFAQRNAERAGVAQAVQLRGGDALQRQPPcAGPGLILMNPPYGERI 325
Cdd:COG0116   231 AELWQELRE-EAEARIKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPP-AEPGLIITNPPYGERL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 326 avvgkagagketgwktgqgretfqtatlrrGDEnspgqESAHDFFEQLSQHWKTHFGGWTAWLLTPDARLSARLRLKESR 405
Cdd:COG0116   309 ------------------------------GEE-----EELEALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASK 353

                         410
                  ....*....|....*.
gi 2527967767 406 RVPLFNGPIECRLLRF 421
Cdd:COG0116   354 RRKLYNGGLECRLLQY 369
 
Name Accession Description Interval E-value
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 6-421 3.37e-175

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: 494.23  E-value: 3.37e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767   6 LTLFLPCAAGVQDFLADEvhgLTGLAGQDLLIERGGIYARGRWRDVMRLNLHSRLAQRVLLELAHVPCESEDALYALARR 85
Cdd:COG0116     1 FELFATCARGLEALLADE---LKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767  86 VPWEDWFGTRHTFRVDVTARGSAFKSLQFAALRVKDAVADRFRERSGARPSVQTQQPDVRIHLHLDGAHASLLLDTSGEP 165
Cdd:COG0116    78 IPWEEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 166 LFKRGWRQDKGDAPLKETLAAAMLAASGwWQPARravaaqPLYDPCCGSGTIVIEAAQLALGLPPGGQRRFAFERLPLFK 245
Cdd:COG0116   158 LHKRGYREAQGEAPLKETLAAALLLLSG-WDGDR------PLVDPMCGSGTILIEAALIAANIAPGLNRDFAFEKWPDFD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 246 RDEWQAMKDeAEAAARPAPAAPRIFGSDVSHRMVDFAQRNAERAGVAQAVQLRGGDALQRQPPcAGPGLILMNPPYGERI 325
Cdd:COG0116   231 AELWQELRE-EAEARIKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPP-AEPGLIITNPPYGERL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 326 avvgkagagketgwktgqgretfqtatlrrGDEnspgqESAHDFFEQLSQHWKTHFGGWTAWLLTPDARLSARLRLKESR 405
Cdd:COG0116   309 ------------------------------GEE-----EELEALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASK 353

                         410
                  ....*....|....*.
gi 2527967767 406 RVPLFNGPIECRLLRF 421
Cdd:COG0116   354 RRKLYNGGLECRLLQY 369
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 6-432 1.02e-124

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: 377.22  E-value: 1.02e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767   6 LTLFLPCAAGVQDFLADEvhgLTGLAGQDLLIERGGIYARGRWRDVMRLNLHSRLAQRVLLELAHVPCESEDALYALARR 85
Cdd:PRK11783    2 NSLFASCAKGLEELLKDE---LEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767  86 VPWEDWFGTRHTFRVDVTARGSAFKSLQFAALRVKDAVADRFRERSGARPSVQTQQPDVRIHLHLDGAHASLLLDTSGEP 165
Cdd:PRK11783   79 IDWTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGES 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 166 LFKRGWRQDKGDAPLKETLAAAMLAASGWWQParravaAQPLYDPCCGSGTIVIEAAQLALGLPPGGQR-RFAFERLPLF 244
Cdd:PRK11783  159 LHQRGYRQATGEAPLKENLAAAILLRSGWPQE------GTPLLDPMCGSGTLLIEAAMMAADIAPGLHReRWGFSGWLGH 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 245 KRDEWQAMKD--EAEAAARPAPAAPRIFGSDVSHRMVDFAQRNAERAGVAQAVQLRGGDALQRQPPCAG--PGLILMNPP 320
Cdd:PRK11783  233 DEALWQELLEeaQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKgpTGLVISNPP 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 321 YGERIavvgkagagketgwktgqgretfqtatlrrGDENSPGQesahdFFEQLSQHWKTHFGGWTAWLLTPDARLSARLR 400
Cdd:PRK11783  313 YGERL------------------------------GEEPALIA-----LYSQLGRRLKQQFGGWNAALFSSSPELLSCLG 357

                         410       420       430
                  ....*....|....*....|....*....|..
gi 2527967767 401 LKESRRVPLFNGPIECRLLRFELTARRPASAP 432
Cdd:PRK11783  358 LRADKQYKLKNGALECVLKNYTIAEESTSSDA 389
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 8-163 2.44e-54

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: 177.77  E-value: 2.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767   8 LFLPCAAGVQDFLADEvhgLTGLAGQDLLIERGGIYARGRWRDVMRLNLHSRLAQRVLLELAHVPCESEDALYALARRVP 87
Cdd:cd11715     1 FFATCPPGLEELLAAE---LKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAID 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527967767  88 WEDWFGTRHTFRVDVTARGSAFKSLQFAALRVKDAVADRFRERsGARPSVQTQQPDVRIHLHLDGAHASLLLDTSG 163
Cdd:cd11715    78 WEDYLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREK-GKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 169-420 2.08e-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: 113.22  E-value: 2.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 169 RGWRQDKGDAPLKETLAAAMLAASGWwQPArravaaQPLYDPCCGSGTIVIEAAQLALGLPPGgqrrfaferlplfkrde 248
Cdd:pfam01170   1 RGYRPFNGPAPLKETLAAAMVNLAGW-KPG------DPLLDPMCGSGTILIEAALMGANIAPG----------------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 249 wqamkdeaeaaARPAPAAPRIFGSDVSHRMVDFAQRNAERAGVAQAVQLRGGDALQRQPPCAGPGLILMNPPYGERIavv 328
Cdd:pfam01170  57 -----------KFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRL--- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 329 GKAGAGketgwktgqgrETFQTATLRrgdenspgqeSAHDFFEQlsqhwkthfGGWTAWLLTPDARLSARLRLKESRRVP 408
Cdd:pfam01170 123 GSKGAL-----------EALYPEFLR----------EAKRVLRG---------GGWLVLLTAENKDFEKAARERAWRKKK 172

                         250
                  ....*....|..
gi 2527967767 409 LFNGPIECRLLR 420
Cdd:pfam01170 173 EFNVHIGGTRVI 184
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 75-157 5.36e-17

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: 75.39  E-value: 5.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767   75 SEDALYALARR-VPWEDWFGTRHTFRVDVTARGsafKSLQFAALRVKDAVADRFRERSGARPsVQTQQPDVRIHLHLDGA 153
Cdd:smart00981   1 DLEDLYETALElIRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKLLEKTGGRK-VDLKNPDVVIRVELRKD 76


                   ....
gi 2527967767  154 HASL 157
Cdd:smart00981  77 KAYL 80
 
Name Accession Description Interval E-value
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 6-421 3.37e-175

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: 494.23  E-value: 3.37e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767   6 LTLFLPCAAGVQDFLADEvhgLTGLAGQDLLIERGGIYARGRWRDVMRLNLHSRLAQRVLLELAHVPCESEDALYALARR 85
Cdd:COG0116     1 FELFATCARGLEALLADE---LKELGAEDVKVENGGVSFEGDLEDIYRANLWLRTASRVLLPLAEFKARTFDDLYEGAKA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767  86 VPWEDWFGTRHTFRVDVTARGSAFKSLQFAALRVKDAVADRFRERSGARPSVQTQQPDVRIHLHLDGAHASLLLDTSGEP 165
Cdd:COG0116    78 IPWEEYLPPDGTFAVDATSVKSKLFHSQFAALRVKDAIVDRFREKYGARPSVDEDGPDVRIHVHLLKDRATLSLDTSGES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 166 LFKRGWRQDKGDAPLKETLAAAMLAASGwWQPARravaaqPLYDPCCGSGTIVIEAAQLALGLPPGGQRRFAFERLPLFK 245
Cdd:COG0116   158 LHKRGYREAQGEAPLKETLAAALLLLSG-WDGDR------PLVDPMCGSGTILIEAALIAANIAPGLNRDFAFEKWPDFD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 246 RDEWQAMKDeAEAAARPAPAAPRIFGSDVSHRMVDFAQRNAERAGVAQAVQLRGGDALQRQPPcAGPGLILMNPPYGERI 325
Cdd:COG0116   231 AELWQELRE-EAEARIKRDPPLPIFGSDIDPRAIEAARENAERAGVADLIEFEQADFRDLEPP-AEPGLIITNPPYGERL 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 326 avvgkagagketgwktgqgretfqtatlrrGDEnspgqESAHDFFEQLSQHWKTHFGGWTAWLLTPDARLSARLRLKESR 405
Cdd:COG0116   309 ------------------------------GEE-----EELEALYRELGDVLKQRFKGWSAYILTSDPELEKAIGLKASK 353

                         410
                  ....*....|....*.
gi 2527967767 406 RVPLFNGPIECRLLRF 421
Cdd:COG0116   354 RRKLYNGGLECRLLQY 369
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 6-432 1.02e-124

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: 377.22  E-value: 1.02e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767   6 LTLFLPCAAGVQDFLADEvhgLTGLAGQDLLIERGGIYARGRWRDVMRLNLHSRLAQRVLLELAHVPCESEDALYALARR 85
Cdd:PRK11783    2 NSLFASCAKGLEELLKDE---LEALGASECKVVQGGVHFEGDLELAYRSCLWSRLASRILLPLAEFKVYSDLDLYLGVQA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767  86 VPWEDWFGTRHTFRVDVTARGSAFKSLQFAALRVKDAVADRFRERSGARPSVQTQQPDVRIHLHLDGAHASLLLDTSGEP 165
Cdd:PRK11783   79 IDWTEHFSPDKTFAVDFSGTNDEIRNTQFGALKVKDAIVDRFRRKGGPRPSVDKEQPDIRINARLNKGEATISLDLSGES 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 166 LFKRGWRQDKGDAPLKETLAAAMLAASGWWQParravaAQPLYDPCCGSGTIVIEAAQLALGLPPGGQR-RFAFERLPLF 244
Cdd:PRK11783  159 LHQRGYRQATGEAPLKENLAAAILLRSGWPQE------GTPLLDPMCGSGTLLIEAAMMAADIAPGLHReRWGFSGWLGH 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 245 KRDEWQAMKD--EAEAAARPAPAAPRIFGSDVSHRMVDFAQRNAERAGVAQAVQLRGGDALQRQPPCAG--PGLILMNPP 320
Cdd:PRK11783  233 DEALWQELLEeaQERARAGLAELPSKFYGSDIDPRVIQAARKNARRAGVAELITFEVKDVADLKNPLPKgpTGLVISNPP 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 321 YGERIavvgkagagketgwktgqgretfqtatlrrGDENSPGQesahdFFEQLSQHWKTHFGGWTAWLLTPDARLSARLR 400
Cdd:PRK11783  313 YGERL------------------------------GEEPALIA-----LYSQLGRRLKQQFGGWNAALFSSSPELLSCLG 357

                         410       420       430
                  ....*....|....*....|....*....|..
gi 2527967767 401 LKESRRVPLFNGPIECRLLRFELTARRPASAP 432
Cdd:PRK11783  358 LRADKQYKLKNGALECVLKNYTIAEESTSSDA 389
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 8-163 2.44e-54

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: 177.77  E-value: 2.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767   8 LFLPCAAGVQDFLADEvhgLTGLAGQDLLIERGGIYARGRWRDVMRLNLHSRLAQRVLLELAHVPCESEDALYALARRVP 87
Cdd:cd11715     1 FFATCPPGLEELLAAE---LKALGAEDVEVGPGGVSFEGDLEDAYRANLWLRTAHRVLLLLAEFEAEDFDDLYELAKAID 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527967767  88 WEDWFGTRHTFRVDVTARGSAFKSLQFAALRVKDAVADRFRERsGARPSVQTQQPDVRIHLHLDGAHASLLLDTSG 163
Cdd:cd11715    78 WEDYLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREK-GKRPSVDLDNPDVRIRVHLSKDRATLSLDLSG 152
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 169-420 2.08e-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: 113.22  E-value: 2.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 169 RGWRQDKGDAPLKETLAAAMLAASGWwQPArravaaQPLYDPCCGSGTIVIEAAQLALGLPPGgqrrfaferlplfkrde 248
Cdd:pfam01170   1 RGYRPFNGPAPLKETLAAAMVNLAGW-KPG------DPLLDPMCGSGTILIEAALMGANIAPG----------------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 249 wqamkdeaeaaARPAPAAPRIFGSDVSHRMVDFAQRNAERAGVAQAVQLRGGDALQRQPPCAGPGLILMNPPYGERIavv 328
Cdd:pfam01170  57 -----------KFDARVRAPLYGSDIDRRMVQGARLNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRL--- 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 329 GKAGAGketgwktgqgrETFQTATLRrgdenspgqeSAHDFFEQlsqhwkthfGGWTAWLLTPDARLSARLRLKESRRVP 408
Cdd:pfam01170 123 GSKGAL-----------EALYPEFLR----------EAKRVLRG---------GGWLVLLTAENKDFEKAARERAWRKKK 172

                         250
                  ....*....|..
gi 2527967767 409 LFNGPIECRLLR 420
Cdd:pfam01170 173 EFNVHIGGTRVI 184
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 75-157 5.36e-17

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: 75.39  E-value: 5.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767   75 SEDALYALARR-VPWEDWFGTRHTFRVDVTARGsafKSLQFAALRVKDAVADRFRERSGARPsVQTQQPDVRIHLHLDGA 153
Cdd:smart00981   1 DLEDLYETALElIRWEKIFKEGKTFAVRAKRRG---KNHEFTSLEVKRAIGDKLLEKTGGRK-VDLKNPDVVIRVELRKD 76


                   ....
gi 2527967767  154 HASL 157
Cdd:smart00981  77 KAYL 80
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 33-161 8.55e-12

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: 62.46  E-value: 8.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767  33 QDLLIERGGIYARGRWRDVMRLNLHSRLAQRvlLELAHVPCESEDALYALARRVPWEDWFGTRHTFRVDVTARGsafKSL 112
Cdd:pfam02926  22 GRILVVLKGENPEEDRELLKEALEKAPGIER--FPVAETCEADLEDILELAKEIIKDKFKKEGETFAVRVKRRG---KNH 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2527967767 113 QFAALRVKDAVADRFRERSGARpsVQTQQPDVRIHLHLDGAHASLLLDT 161
Cdd:pfam02926  97 EFTSLEINREVGKAIVEKTGLK--VDLENPDIVVHVEIIKDKAYISIDR 143
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 180-322 8.18e-08

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: 51.87  E-value: 8.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767 180 LKETLAAAMLAASGWWQPARravaaqpLYDPCCGSGTIVIEAAqlALGLPpggqrrfaferlplfkrdewqamkdeaeaa 259
Cdd:COG1041    10 LDPRLARALVNLAGAKEGDT-------VLDPFCGTGTILIEAG--LLGRR------------------------------ 50

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2527967767 260 arpapaaprIFGSDVSHRMVDFAQRNAERAGVAQAVQLRgGDALQRQPPCAGPGLILMNPPYG 322
Cdd:COG1041    51 ---------VIGSDIDPKMVEGARENLEHYGYEDADVIR-GDARDLPLADESVDAIVTDPPYG 103
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 272-321 8.37e-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: 40.17  E-value: 8.37e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2527967767 272 SDVSHRMVDFAQRNAERAGVAQaVQLRGGDALQRQPPcAGPGLILMNPPY 321
Cdd:COG2813    79 VDVNARAVELARANAAANGLEN-VEVLWSDGLSGVPD-GSFDLILSNPPF 126
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
 269-321 1.43e-03

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


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 40.13  E-value: 1.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2527967767 269 IFGSDVSHRMVDFAQRNAERAGVAQAVQLRGGDALQrqpPCAGPG---LILMNPPY 321
Cdd:COG2890   139 VTAVDISPDALAVARRNAERLGLEDRVRFLQGDLFE---PLPGDGrfdLIVSNPPY 191
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 321-379 2.72e-03

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 38.20  E-value: 2.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2527967767 321 YGERIAVVGKAGAGKETGWKTGQGRETFQTATLRRGDENSPGqesahdFFEQLSQHWKT 379
Cdd:cd03221    25 PGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG------YFEQLSGGEKM 77
THUMP cd11688
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ...
 8-157 3.54e-03

THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases. 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: 212583  Cd Length: 148  Bit Score: 37.85  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2527967767   8 LFLPCAAGVQDFLADEVHGLtgLAGQDLLIE-----RGGIYARG-RWRDVMRLNLHSRLAQRVLLELAHVPCESEDaLYA 81
Cdd:cd11688     1 VFATTGKGLEEILAAELYEL--LEVRGFDAEiqvvpHGRVHFKTdTDEAVYQLVMWSRLISRIMPPLGECKADLED-LYE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2527967767  82 LARRVPWEDWFGTRHTFRVDVTARGSAFKSLQFAALRVKDAVADRFrersgaRPSVQTQQPDVRIHLHLDGAHASL 157
Cdd:cd11688    78 TALEINEPEMGNEGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAF------NPEVDLDNPDIVVNVEVHKEIASI 147
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
271-322 7.48e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 37.58  E-value: 7.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2527967767 271 GSDVSHRMVDFAQRNAERAGVAqaVQLRGGDAlqRQPPCAG-PGLILMNPPYG 322
Cdd:COG2263    73 GVDIDPEALEIARENAERLGVR--VDFIRADV--TRIPLGGsVDTVVMNPPFG 121
 
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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