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Conserved domains on  [gi|1034632427|ref|XP_016861603|]
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tRNA (guanine(6)-N2)-methyltransferase THUMP3 isoform X2 [Homo sapiens]

Protein Classification

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; ...
 293-341 7.41e-16

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: 75.47  E-value: 7.41e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034632427 293 RNITHF-GPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEQTLLG 341
Cdd:pfam01170   1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMG 50
RlmL super family cl43029
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 42-336 1.72e-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


The actual alignment was detected with superfamily member COG0116:

Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 77.83  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427  42 ATVPTGFEQTAADEVREkLGSScKISRDRGKIYFVISVESLAQVH-CLRSVDNLFVVVQEFQDYQFKqtkeevlkDFEDL 120
Cdd:COG0116     5 ATCARGLEALLADELKE-LGAE-DVKVENGGVSFEGDLEDIYRANlWLRTASRVLLPLAEFKARTFD--------DLYEG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 121 AGKLPWSNPLKVwkiNASFKkkkakrkkINQNSSKEKINNGQEVkidQRNVKKeftshaldshildyyenpAIKEdvstl 200
Cdd:COG0116    75 AKAIPWEEYLPP---DGTFA--------VDATSVKSKLFHSQFA---ALRVKD------------------AIVD----- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 201 igddlaSCKDETDESSK-EETEPqvlkfrvtcnragekhcftsneaardfggavqdyfkwkadmtnfDVEVLLNIHDNEV 279
Cdd:COG0116   118 ------RFREKYGARPSvDEDGP--------------------------------------------DVRIHVHLLKDRA 147

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 280 IVGIALTEESLHRRN---ITHFGPttLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIE 336
Cdd:COG0116   148 TLSLDTSGESLHKRGyreAQGEAP--LKETLAAALLLLSGWDGDRPLVDPMCGSGTILIE 205
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 226-283 1.03e-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: 66.53  E-value: 1.03e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034632427  226 KFRVTCNRAGEKHCFTSNEAARDFGGAVQD-YFKWKADMTNFDVEVLLNIHDNEVIVGI 283
Cdd:smart00981  24 TFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 293-341 7.41e-16

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: 75.47  E-value: 7.41e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034632427 293 RNITHF-GPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEQTLLG 341
Cdd:pfam01170   1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMG 50
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 42-336 1.72e-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: 77.83  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427  42 ATVPTGFEQTAADEVREkLGSScKISRDRGKIYFVISVESLAQVH-CLRSVDNLFVVVQEFQDYQFKqtkeevlkDFEDL 120
Cdd:COG0116     5 ATCARGLEALLADELKE-LGAE-DVKVENGGVSFEGDLEDIYRANlWLRTASRVLLPLAEFKARTFD--------DLYEG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 121 AGKLPWSNPLKVwkiNASFKkkkakrkkINQNSSKEKINNGQEVkidQRNVKKeftshaldshildyyenpAIKEdvstl 200
Cdd:COG0116    75 AKAIPWEEYLPP---DGTFA--------VDATSVKSKLFHSQFA---ALRVKD------------------AIVD----- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 201 igddlaSCKDETDESSK-EETEPqvlkfrvtcnragekhcftsneaardfggavqdyfkwkadmtnfDVEVLLNIHDNEV 279
Cdd:COG0116   118 ------RFREKYGARPSvDEDGP--------------------------------------------DVRIHVHLLKDRA 147

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 280 IVGIALTEESLHRRN---ITHFGPttLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIE 336
Cdd:COG0116   148 TLSLDTSGESLHKRGyreAQGEAP--LKETLAAALLLLSGWDGDRPLVDPMCGSGTILIE 205
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 40-286 6.41e-15

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: 71.84  E-value: 6.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427  40 IGATVPTGFEQTAADEVREKLGSscKISRDRGKIYFVISVESLAQV-HCLRSVDNLFVVVQEFqdyqfkqtKEEVLKDFE 118
Cdd:cd11715     1 FFATCPPGLEELLAAELKALGAE--DVEVGPGGVSFEGDLEDAYRAnLWLRTAHRVLLLLAEF--------EAEDFDDLY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 119 DLAGKLPWSNPLKVwkinasfkkkkakrkkinqnsskekinngqevkidqrnvkkeftshaldshildyyenpaikedvs 198
Cdd:cd11715    71 ELAKAIDWEDYLDP------------------------------------------------------------------ 84

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 199 tligddlasckDETdesskeetepqvlkFRVTCNRAGEkHCFTSNEAARDFGGAVQDYFK-----WKADMTNFDVEVLLN 273
Cdd:cd11715    85 -----------DGT--------------FAVRATRVGS-KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVH 138

                         250
                  ....*....|...
gi 1034632427 274 IHDNEVIVGIALT 286
Cdd:cd11715   139 LSKDRATLSLDLS 151
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 226-283 1.03e-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: 66.53  E-value: 1.03e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034632427  226 KFRVTCNRAGEKHCFTSNEAARDFGGAVQD-YFKWKADMTNFDVEVLLNIHDNEVIVGI 283
Cdd:smart00981  24 TFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 226-283 5.74e-11

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: 60.53  E-value: 5.74e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034632427 226 KFRVTCNRAGEKHCFTSNEAARDFGGAVQDYFKWKADMTNFDVEVLLNIHDNEVIVGI 283
Cdd:pfam02926  84 TFAVRVKRRGKNHEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 227-281 2.22e-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: 53.60  E-value: 2.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034632427 227 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 281
Cdd:cd11716   102 FKVRAKRADKSFPFTSMEINREVGAALLENTPdLKVDLKNPDVTIRVEIREDGAYV 157
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 238-336 2.75e-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: 53.27  E-value: 2.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 238 HCFTSNEAARD--FGG-----AVQDYFKWKA------DMTNFDVEVLLNIHDNEVIVGIALTEESLHRRNI-THFGPTTL 303
Cdd:PRK11783   94 DFSGTNDEIRNtqFGAlkvkdAIVDRFRRKGgprpsvDKEQPDIRINARLNKGEATISLDLSGESLHQRGYrQATGEAPL 173

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034632427 304 RSTLAYGMLRLCD-PLPYDIIVDPMCGTGAIPIE 336
Cdd:PRK11783  174 KENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIE 207
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 227-281 5.67e-07

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: 51.63  E-value: 5.67e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034632427 227 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 281
Cdd:COG0301   103 FKVRAKRAGKHFPFTSPELEREVGGALLENTPgLKVDLKNPDVTIRVEVRDDKAYV 158
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 260-342 1.00e-05

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: 47.43  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 260 KADMTNFDVEVLLNIHDNEVIVGIALT--------EESLHRRniTHFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTG 331
Cdd:TIGR01177 117 KVSLRRPDIVVRVVITEDIFYLGRVLEerdkeqfiERKPDRR--PFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTG 194

                          90
                  ....*....|.
gi 1034632427 332 AIPIEQTLLGL 342
Cdd:TIGR01177 195 GFLIEAGLMGA 205
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 297-342 1.04e-04

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: 43.01  E-value: 1.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034632427 297 HFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEQTLLGL 342
Cdd:COG1041     4 FFYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGR 49
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 293-341 7.41e-16

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: 75.47  E-value: 7.41e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034632427 293 RNITHF-GPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEQTLLG 341
Cdd:pfam01170   1 RGYRPFnGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMG 50
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 42-336 1.72e-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: 77.83  E-value: 1.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427  42 ATVPTGFEQTAADEVREkLGSScKISRDRGKIYFVISVESLAQVH-CLRSVDNLFVVVQEFQDYQFKqtkeevlkDFEDL 120
Cdd:COG0116     5 ATCARGLEALLADELKE-LGAE-DVKVENGGVSFEGDLEDIYRANlWLRTASRVLLPLAEFKARTFD--------DLYEG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 121 AGKLPWSNPLKVwkiNASFKkkkakrkkINQNSSKEKINNGQEVkidQRNVKKeftshaldshildyyenpAIKEdvstl 200
Cdd:COG0116    75 AKAIPWEEYLPP---DGTFA--------VDATSVKSKLFHSQFA---ALRVKD------------------AIVD----- 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 201 igddlaSCKDETDESSK-EETEPqvlkfrvtcnragekhcftsneaardfggavqdyfkwkadmtnfDVEVLLNIHDNEV 279
Cdd:COG0116   118 ------RFREKYGARPSvDEDGP--------------------------------------------DVRIHVHLLKDRA 147

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 280 IVGIALTEESLHRRN---ITHFGPttLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIE 336
Cdd:COG0116   148 TLSLDTSGESLHKRGyreAQGEAP--LKETLAAALLLLSGWDGDRPLVDPMCGSGTILIE 205
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 40-286 6.41e-15

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: 71.84  E-value: 6.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427  40 IGATVPTGFEQTAADEVREKLGSscKISRDRGKIYFVISVESLAQV-HCLRSVDNLFVVVQEFqdyqfkqtKEEVLKDFE 118
Cdd:cd11715     1 FFATCPPGLEELLAAELKALGAE--DVEVGPGGVSFEGDLEDAYRAnLWLRTAHRVLLLLAEF--------EAEDFDDLY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 119 DLAGKLPWSNPLKVwkinasfkkkkakrkkinqnsskekinngqevkidqrnvkkeftshaldshildyyenpaikedvs 198
Cdd:cd11715    71 ELAKAIDWEDYLDP------------------------------------------------------------------ 84

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 199 tligddlasckDETdesskeetepqvlkFRVTCNRAGEkHCFTSNEAARDFGGAVQDYFK-----WKADMTNFDVEVLLN 273
Cdd:cd11715    85 -----------DGT--------------FAVRATRVGS-KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVH 138

                         250
                  ....*....|...
gi 1034632427 274 IHDNEVIVGIALT 286
Cdd:cd11715   139 LSKDRATLSLDLS 151
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 226-283 1.03e-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: 66.53  E-value: 1.03e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034632427  226 KFRVTCNRAGEKHCFTSNEAARDFGGAVQD-YFKWKADMTNFDVEVLLNIHDNEVIVGI 283
Cdd:smart00981  24 TFAVRAKRRGKNHEFTSLEVKRAIGDKLLEkTGGRKVDLKNPDVVIRVELRKDKAYLSI 82
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 226-283 5.74e-11

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: 60.53  E-value: 5.74e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034632427 226 KFRVTCNRAGEKHCFTSNEAARDFGGAVQDYFKWKADMTNFDVEVLLNIHDNEVIVGI 283
Cdd:pfam02926  84 TFAVRVKRRGKNHEFTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEIIKDKAYISI 141
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 227-281 2.22e-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: 53.60  E-value: 2.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034632427 227 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 281
Cdd:cd11716   102 FKVRAKRADKSFPFTSMEINREVGAALLENTPdLKVDLKNPDVTIRVEIREDGAYV 157
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 238-336 2.75e-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: 53.27  E-value: 2.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 238 HCFTSNEAARD--FGG-----AVQDYFKWKA------DMTNFDVEVLLNIHDNEVIVGIALTEESLHRRNI-THFGPTTL 303
Cdd:PRK11783   94 DFSGTNDEIRNtqFGAlkvkdAIVDRFRRKGgprpsvDKEQPDIRINARLNKGEATISLDLSGESLHQRGYrQATGEAPL 173

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034632427 304 RSTLAYGMLRLCD-PLPYDIIVDPMCGTGAIPIE 336
Cdd:PRK11783  174 KENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIE 207
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 227-281 5.67e-07

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: 51.63  E-value: 5.67e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034632427 227 FRVTCNRAGEKHCFTSNEAARDFGGAVQDYFK-WKADMTNFDVEVLLNIHDNEVIV 281
Cdd:COG0301   103 FKVRAKRAGKHFPFTSPELEREVGGALLENTPgLKVDLKNPDVTIRVEVRDDKAYV 158
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 260-342 1.00e-05

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: 47.43  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034632427 260 KADMTNFDVEVLLNIHDNEVIVGIALT--------EESLHRRniTHFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTG 331
Cdd:TIGR01177 117 KVSLRRPDIVVRVVITEDIFYLGRVLEerdkeqfiERKPDRR--PFFKPGSMDPKLARAMVNLARVTEGDRVLDPFCGTG 194

                          90
                  ....*....|.
gi 1034632427 332 AIPIEQTLLGL 342
Cdd:TIGR01177 195 GFLIEAGLMGA 205
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 297-342 1.04e-04

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: 43.01  E-value: 1.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034632427 297 HFGPTTLRSTLAYGMLRLCDPLPYDIIVDPMCGTGAIPIEQTLLGL 342
Cdd:COG1041     4 FFYPGSLDPRLARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGR 49
 
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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