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Conserved domains on  [gi|281604144|ref|NP_001164019|]
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tRNA (guanine(6)-N2)-methyltransferase THUMP3 [Rattus norvegicus]

Protein Classification

THUMP_AdoMetMT and UPF0020 domain-containing protein( domain architecture ID 10659632)

THUMP_AdoMetMT and UPF0020 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 294-479 9.52e-78

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: 241.49  E-value: 9.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  294 RNITHF-GPTTLRSTLAYGMLRLCEPKPTDVIVDPMCGTGAIPIEGATEWSHCYHIAGDNNPLAVNRAANNISSLLTKSQ 372
Cdd:pfam01170   1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRAPLYGSDIDRRMVQGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  373 IKDGKTSWGLPIDAVQWDICNLPLRTASVDIIVTDMPFGKRMGSKKRNWNLYPACLREMSRVCRPRtGRAVLLTQDKKCF 452
Cdd:pfam01170  81 LNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRGG-GWLVLLTAENKDF 159

                         170       180
                  ....*....|....*....|....*..
gi 281604144  453 TKALSGMGhvWRKVHTVWVNIGGLHAA 479
Cdd:pfam01170 160 EKAARERA--WRKKKEFNVHIGGTRVI 184
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 219-284 2.05e-13

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: 65.37  E-value: 2.05e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281604144   219 EEAEPQVQKFRVTCNRAGEKHCFTSNEAARGFGGAVQE-YFKWKADMTNFDVEVLLNIHNNEVIVAI 284
Cdd:smart00981  16 EKIFKEGKTFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 294-479 9.52e-78

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: 241.49  E-value: 9.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  294 RNITHF-GPTTLRSTLAYGMLRLCEPKPTDVIVDPMCGTGAIPIEGATEWSHCYHIAGDNNPLAVNRAANNISSLLTKSQ 372
Cdd:pfam01170   1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRAPLYGSDIDRRMVQGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  373 IKDGKTSWGLPIDAVQWDICNLPLRTASVDIIVTDMPFGKRMGSKKRNWNLYPACLREMSRVCRPRtGRAVLLTQDKKCF 452
Cdd:pfam01170  81 LNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRGG-GWLVLLTAENKDF 159

                         170       180
                  ....*....|....*....|....*..
gi 281604144  453 TKALSGMGhvWRKVHTVWVNIGGLHAA 479
Cdd:pfam01170 160 EKAARERA--WRKKKEFNVHIGGTRVI 184
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 298-449 5.50e-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: 98.48  E-value: 5.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 298 HFGPTTLRSTLAYGMLRLCEPKPTDVIVDPMCGTGAIPIEGAteWSHCYHIAGDNNPLAVNRAANNISSLLTKSqikdgk 377
Cdd:COG1041    4 FFYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAG--LLGRRVIGSDIDPKMVEGARENLEHYGYED------ 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281604144 378 tswglpIDAVQWDICNLPLRTASVDIIVTDMPFGKRMGSKKRNW-NLYPACLREMSRVCRPRtGRAVLLTQDK 449
Cdd:COG1041   76 ------ADVIRGDARDLPLADESVDAIVTDPPYGRSSKISGEELlELYEKALEEAARVLKPG-GRVVIVTPRD 141
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 219-284 2.05e-13

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: 65.37  E-value: 2.05e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281604144   219 EEAEPQVQKFRVTCNRAGEKHCFTSNEAARGFGGAVQE-YFKWKADMTNFDVEVLLNIHNNEVIVAI 284
Cdd:smart00981  16 EKIFKEGKTFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 41-287 8.30e-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: 66.06  E-value: 8.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  41 IGATVPTGFEQTAADEVREKLKSSCRIskDRGKIYFDIAVESLAQV-HCLRSVDNLFVVVEEFKDYQFKatkeevlrDFE 119
Cdd:cd11715    1 FFATCPPGLEELLAAELKALGAEDVEV--GPGGVSFEGDLEDAYRAnLWLRTAHRVLLLLAEFEAEDFD--------DLY 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 120 ELAGKLPWSDPLKVWQinttfkkkkakrrkanqsagrekadcgqgdnagekdgkkklasgaadphildyyenpaikeeis 199
Cdd:cd11715   71 ELAKAIDWEDYLDPDG---------------------------------------------------------------- 86

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 200 tligevlasgedengqslreeaepqvqKFRVTCNRAGEkHCFTSNEAARGFGGAVQEYFK-----WKADMTNFDVEVLLN 274
Cdd:cd11715   87 ---------------------------TFAVRATRVGS-KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVH 138

                        250
                 ....*....|...
gi 281604144 275 IHNNEVIVAIALT 287
Cdd:cd11715  139 LSKDRATLSLDLS 151
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 261-444 9.50e-11

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: 63.23  E-value: 9.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  261 KADMTNFDVEVLLNIHNNEVIVAIALT--------EESLHRRniTHFGPTTLRSTLAYGMLRLCEPKPTDVIVDPMCGTG 332
Cdd:TIGR01177 117 KVSLRRPDIVVRVVITEDIFYLGRVLEerdkeqfiERKPDRR--PFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTG 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  333 AIPIEGATEWSHCyhIAGDNNPLAVNRAANNisslLTKSQIKDGKTSwglpidavQWDICNLPLRTASVDIIVTDMPFGk 412
Cdd:TIGR01177 195 GFLIEAGLMGAKV--IGCDIDWKMVAGARIN----LEHYGIEDFFVK--------RGDATKLPLSSESVDAIATDPPYG- 259

                         170       180       190
                  ....*....|....*....|....*....|....
gi 281604144  413 RMGSKKRNWN--LYPACLREMSRVCRPRTGRAVL 444
Cdd:TIGR01177 260 RSTTAAGDGLesLYERSLEEFHEVLKSEGWIVYA 293
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 218-284 1.11e-10

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: 59.76  E-value: 1.11e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281604144  218 REEAEPQVQKFRVTCNRAGEKHCFTSNEAARGFGGAVQEYFKWKADMTNFDVEVLLNIHNNEVIVAI 284
Cdd:pfam02926  75 KDKFKKEGETFAVRVKRRGKNHEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 268-339 4.91e-09

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: 58.66  E-value: 4.91e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281604144 268 DVEVLLNIHNNEVIVAIALTEESLHRRNI-THFGPTTLRSTLAYGML-RLCEPKPTDVIVDPMCGTGAIPIEGA 339
Cdd:PRK11783 136 DIRINARLNKGEATISLDLSGESLHQRGYrQATGEAPLKENLAAAILlRSGWPQEGTPLLDPMCGSGTLLIEAA 209
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 220-282 4.44e-06

Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440070 [Multi-domain]  Cd Length: 382  Bit Score: 48.93  E-value: 4.44e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281604144 220 EAEPQVQKFRVTCNRAGEKHCFTSNEAARGFGGAVQEYFK-WKADMTNFDVEVLLNIHNNEVIV 282
Cdd:COG0301   95 KEELKGKTFKVRAKRAGKHFPFTSPELEREVGGALLENTPgLKVDLKNPDVTIRVEVRDDKAYV 158
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 294-479 9.52e-78

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: 241.49  E-value: 9.52e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  294 RNITHF-GPTTLRSTLAYGMLRLCEPKPTDVIVDPMCGTGAIPIEGATEWSHCYHIAGDNNPLAVNRAANNISSLLTKSQ 372
Cdd:pfam01170   1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIAPGKFDARVRAPLYGSDIDRRMVQGAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  373 IKDGKTSWGLPIDAVQWDICNLPLRTASVDIIVTDMPFGKRMGSKKRNWNLYPACLREMSRVCRPRtGRAVLLTQDKKCF 452
Cdd:pfam01170  81 LNAENAGVGDLIEFVQADAADLPLLEGSVDVIVTNPPYGIRLGSKGALEALYPEFLREAKRVLRGG-GWLVLLTAENKDF 159

                         170       180
                  ....*....|....*....|....*..
gi 281604144  453 TKALSGMGhvWRKVHTVWVNIGGLHAA 479
Cdd:pfam01170 160 EKAARERA--WRKKKEFNVHIGGTRVI 184
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 298-449 5.50e-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: 98.48  E-value: 5.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 298 HFGPTTLRSTLAYGMLRLCEPKPTDVIVDPMCGTGAIPIEGAteWSHCYHIAGDNNPLAVNRAANNISSLLTKSqikdgk 377
Cdd:COG1041    4 FFYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAG--LLGRRVIGSDIDPKMVEGARENLEHYGYED------ 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 281604144 378 tswglpIDAVQWDICNLPLRTASVDIIVTDMPFGKRMGSKKRNW-NLYPACLREMSRVCRPRtGRAVLLTQDK 449
Cdd:COG1041   76 ------ADVIRGDARDLPLADESVDAIVTDPPYGRSSKISGEELlELYEKALEEAARVLKPG-GRVVIVTPRD 141
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 226-456 1.89e-19

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: 89.77  E-value: 1.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 226 QKFRVTCNRAGEKHcFTSNEAARGFGGAVQEYFKWKA------DMTNFDVEVLLNIHNNEVIVAIALTEESLHRRN---I 296
Cdd:COG0116   88 GTFAVDATSVKSKL-FHSQFAALRVKDAIVDRFREKYgarpsvDEDGPDVRIHVHLLKDRATLSLDTSGESLHKRGyreA 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 297 THFGPttLRSTLAYGMLRLCEPKPTDVIVDPMCGTGAIPIEGA----------------TEWSHC--------------- 345
Cdd:COG0116  167 QGEAP--LKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAAliaaniapglnrdfafEKWPDFdaelwqelreeaear 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 346 ------YHIAG-DNNPLAVNRAANNISSLltksqikdgktswGLP--IDAVQWDICNLPlRTASVDIIVTDMPFGKRMGS 416
Cdd:COG0116  245 ikrdppLPIFGsDIDPRAIEAARENAERA-------------GVAdlIEFEQADFRDLE-PPAEPGLIITNPPYGERLGE 310

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 281604144 417 KKRNWNLYpaclREMSRVCRPR--TGRAVLLTQDKKcFTKAL 456
Cdd:COG0116  311 EEELEALY----RELGDVLKQRfkGWSAYILTSDPE-LEKAI 347
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 219-284 2.05e-13

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: 65.37  E-value: 2.05e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281604144   219 EEAEPQVQKFRVTCNRAGEKHCFTSNEAARGFGGAVQE-YFKWKADMTNFDVEVLLNIHNNEVIVAI 284
Cdd:smart00981  16 EKIFKEGKTFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 41-287 8.30e-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: 66.06  E-value: 8.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  41 IGATVPTGFEQTAADEVREKLKSSCRIskDRGKIYFDIAVESLAQV-HCLRSVDNLFVVVEEFKDYQFKatkeevlrDFE 119
Cdd:cd11715    1 FFATCPPGLEELLAAELKALGAEDVEV--GPGGVSFEGDLEDAYRAnLWLRTAHRVLLLLAEFEAEDFD--------DLY 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 120 ELAGKLPWSDPLKVWQinttfkkkkakrrkanqsagrekadcgqgdnagekdgkkklasgaadphildyyenpaikeeis 199
Cdd:cd11715   71 ELAKAIDWEDYLDPDG---------------------------------------------------------------- 86

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 200 tligevlasgedengqslreeaepqvqKFRVTCNRAGEkHCFTSNEAARGFGGAVQEYFK-----WKADMTNFDVEVLLN 274
Cdd:cd11715   87 ---------------------------TFAVRATRVGS-KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVH 138

                        250
                 ....*....|...
gi 281604144 275 IHNNEVIVAIALT 287
Cdd:cd11715  139 LSKDRATLSLDLS 151
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 261-444 9.50e-11

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: 63.23  E-value: 9.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  261 KADMTNFDVEVLLNIHNNEVIVAIALT--------EESLHRRniTHFGPTTLRSTLAYGMLRLCEPKPTDVIVDPMCGTG 332
Cdd:TIGR01177 117 KVSLRRPDIVVRVVITEDIFYLGRVLEerdkeqfiERKPDRR--PFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTG 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  333 AIPIEGATEWSHCyhIAGDNNPLAVNRAANNisslLTKSQIKDGKTSwglpidavQWDICNLPLRTASVDIIVTDMPFGk 412
Cdd:TIGR01177 195 GFLIEAGLMGAKV--IGCDIDWKMVAGARIN----LEHYGIEDFFVK--------RGDATKLPLSSESVDAIATDPPYG- 259

                         170       180       190
                  ....*....|....*....|....*....|....
gi 281604144  413 RMGSKKRNWN--LYPACLREMSRVCRPRTGRAVL 444
Cdd:TIGR01177 260 RSTTAAGDGLesLYERSLEEFHEVLKSEGWIVYA 293
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 218-284 1.11e-10

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: 59.76  E-value: 1.11e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 281604144  218 REEAEPQVQKFRVTCNRAGEKHCFTSNEAARGFGGAVQEYFKWKADMTNFDVEVLLNIHNNEVIVAI 284
Cdd:pfam02926  75 KDKFKKEGETFAVRVKRRGKNHEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 312-446 3.39e-09

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: 55.39  E-value: 3.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 312 MLRLCEPKPTDVIVDPMCGTGAIPIEGAtewSHCYHIAG-DNNPLAVNRAANNISSLltksqikdgktswGLPIDAVQWD 390
Cdd:COG2226   14 LLAALGLRPGARVLDLGCGTGRLALALA---ERGARVTGvDISPEMLELARERAAEA-------------GLNVEFVVGD 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 281604144 391 ICNLPLRTASVDIIVTDMPFgkrmgskkRNWNLYPACLREMSRVCRPRtGRAVLLT 446
Cdd:COG2226   78 AEDLPFPDGSFDLVISSFVL--------HHLPDPERALAEIARVLKPG-GRLVVVD 124
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 268-339 4.91e-09

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: 58.66  E-value: 4.91e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281604144 268 DVEVLLNIHNNEVIVAIALTEESLHRRNI-THFGPTTLRSTLAYGML-RLCEPKPTDVIVDPMCGTGAIPIEGA 339
Cdd:PRK11783 136 DIRINARLNKGEATISLDLSGESLHQRGYrQATGEAPLKENLAAAILlRSGWPQEGTPLLDPMCGSGTLLIEAA 209
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 219-282 8.98e-08

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: 51.68  E-value: 8.98e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 281604144 219 EEAEPQVQKFRVTCNRAGEKHCFTSNEAARGFGGAVQEYFK-WKADMTNFDVEVLLNIHNNEVIV 282
Cdd:cd11716   93 KEELKKGKTFKVRAKRADKSFPFTSMEINREVGAALLENTPdLKVDLKNPDVTIRVEIREDGAYV 157
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 324-437 4.07e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 45.25  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144  324 IVDPMCGTGAIPIEGATEWSHCYhIAGDNNPLAVNRAANNISSLltksqikdgktswGLPIDAVQWDICNLPLRTASVDI 403
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARV-TGVDLSPEMLERARERAAEA-------------GLNVEFVQGDAEDLPFPDGSFDL 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 281604144  404 IVTDMPFGkrmgskKRNWNLYPACLREMSRVCRP 437
Cdd:pfam13649  67 VVSSGVLH------HLPDPDLEAALREIARVLKP 94
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 220-282 4.44e-06

Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440070 [Multi-domain]  Cd Length: 382  Bit Score: 48.93  E-value: 4.44e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 281604144 220 EAEPQVQKFRVTCNRAGEKHCFTSNEAARGFGGAVQEYFK-WKADMTNFDVEVLLNIHNNEVIV 282
Cdd:COG0301   95 KEELKGKTFKVRAKRAGKHFPFTSPELEREVGGALLENTPgLKVDLKNPDVTIRVEVRDDKAYV 158
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 312-445 5.54e-04

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


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 41.68  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281604144 312 MLRLCEPKPTDVIVDPMCGTGAIpiegATEWSHcyhiagdnnplAVNRAANNI-----SSLLTKSQIKDGKTSWGLPIDA 386
Cdd:PRK00216  43 TIKWLGVRPGDKVLDLACGTGDL----AIALAK-----------AVGKTGEVVgldfsEGMLAVGREKLRDLGLSGNVEF 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 281604144 387 VQWDICNLPLRTASVDIiVTdMPFGKRmgskkrnwNL--YPACLREMSRVCRPRtGRAVLL 445
Cdd:PRK00216 108 VQGDAEALPFPDNSFDA-VT-IAFGLR--------NVpdIDKALREMYRVLKPG-GRLVIL 157
 
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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