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Conserved domains on  [gi|1009287569|ref|NP_001308404|]
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THUMP domain-containing protein 2 isoform 6 [Homo sapiens]

Protein Classification

THUMP domain-containing class I SAM-dependent methyltransferase( domain architecture ID 10659626)

THUMP domain-containing class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; may be an RNA methylase

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:1904047|GO:0003723
PubMed:  12504684|12826405|11295541
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 181-260 2.28e-14

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: 70.08  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 181 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 249
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90
                  ....*....|.
gi 1009287569 250 KAAGLEDKIEL 260
Cdd:pfam01170  84 ENAGVGDLIEF 94
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 93-171 1.13e-08

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


:

Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 51.51  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569   93 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 169
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 1009287569  170 GI 171
Cdd:smart00981  81 SI 82
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 181-260 2.28e-14

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: 70.08  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 181 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 249
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90
                  ....*....|.
gi 1009287569 250 KAAGLEDKIEL 260
Cdd:pfam01170  84 ENAGVGDLIEF 94
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 193-256 1.52e-12

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: 64.97  E-value: 1.52e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1009287569 193 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLED 256
Cdd:COG1041    14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI--GSDIDPKMVEGARENLEHYGYED 75
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 135-256 3.33e-09

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: 57.06  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 135 KVIGiAIMKHFGWKADLRNPQLEIFI-HLNDIYSVVGIPVFRV-------SLASRAYIKTAGLRSTIAWAMASLADIKAG 206
Cdd:TIGR01177 105 RKIG-AILKKKGFKVSLRRPDIVVRVvITEDIFYLGRVLEERDkeqfierKPDRRPFFKPGSMDPKLARAMVNLARVTEG 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287569 207 AFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLED 256
Cdd:TIGR01177 184 DRVLDPFCGTGGFLIEAGLMGAKVI--GCDIDWKMVAGARINLEHYGIED 231
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
128-261 7.61e-09

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


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 56.22  E-value: 7.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 128 FTAQEVGKVIGIAIMKHFG------WKADLRNPQLEIFIHLNDIYSVVGIPVF-RVSLASR---AYIKTAGLRSTIAWAM 197
Cdd:NF040721  104 FTSIDIGRVAGEAVIDSYLrdkgvrLKVNLDEPDVIVRVELIFDELLVGIDTTgDEGLHKRgyrVYQHPAHLNPTIASSL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 198 ASLADIKAGAFVLDPMCGLGTILLEAA---------------------------KEWPDVYY--VGADVSDSQLLGTWDN 248
Cdd:NF040721  184 IYLSGWKDEESLLDPMCGSGTILIEAAlikrnippgkfredfafkkifghelleKIKKDVELkiYGIEKFRKHLEGAKKN 263

                         170
                  ....*....|...
gi 1009287569 249 LKAAGLEDKIELL 261
Cdd:NF040721  264 AENAGVDDTIKFI 276
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 93-171 1.13e-08

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 51.51  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569   93 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 169
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 1009287569  170 GI 171
Cdd:smart00981  81 SI 82
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 111-171 5.29e-07

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 48.35  E-value: 5.29e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009287569 111 DLTFRVSCRCSGTigKAFTAQEVGKVIGIAIMKHFG-----WKADLRNPQLEIFIHLNDIYSVVGI 171
Cdd:cd11715    85 DGTFAVRATRVGS--KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSL 148
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 150-224 5.74e-06

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: 47.87  E-value: 5.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1009287569 150 DLRNPQLEIFIHLNDIYSVVGIPVFRVSLASRAYIKTAG---LRSTIAWAMASLAD-IKAGAFVLDPMCGLGTILLEAA 224
Cdd:PRK11783  131 DKEQPDIRINARLNKGEATISLDLSGESLHQRGYRQATGeapLKENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAA 209
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 113-162 2.78e-05

THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 460749  Cd Length: 143  Bit Score: 43.20  E-value: 2.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287569 113 TFRVSCRCSGTIGKaFTAQEVGKVIGIAIMKHFGWKADLRNPQLEIFIHL 162
Cdd:pfam02926  84 TFAVRVKRRGKNHE-FTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEI 132
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 181-260 2.28e-14

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: 70.08  E-value: 2.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 181 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVY-----------YVGADVSDSQLLGTWDNL 249
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANIApgkfdarvrapLYGSDIDRRMVQGARLNA 83

                          90
                  ....*....|.
gi 1009287569 250 KAAGLEDKIEL 260
Cdd:pfam01170  84 ENAGVGDLIEF 94
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 193-256 1.52e-12

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: 64.97  E-value: 1.52e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1009287569 193 IAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLED 256
Cdd:COG1041    14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAGLLGRRVI--GSDIDPKMVEGARENLEHYGYED 75
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 111-260 3.10e-12

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: 66.66  E-value: 3.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 111 DLTFRVSCRCSGTIGKA--FTAQEVGKVIGIAIMKHFGW--KADLRNPQLEIFIHL-NDIYSV----VGIPVFRvslasR 181
Cdd:COG0116    87 DGTFAVDATSVKSKLFHsqFAALRVKDAIVDRFREKYGArpSVDEDGPDVRIHVHLlKDRATLsldtSGESLHK-----R 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 182 AYIKTAG---LRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAA----------------KEWPD------------- 229
Cdd:COG0116   162 GYREAQGeapLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAAliaaniapglnrdfafEKWPDfdaelwqelreea 241

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1009287569 230 ---------VYYVGADVSDSQLLGTWDNLKAAGLEDKIEL 260
Cdd:COG0116   242 earikrdppLPIFGSDIDPRAIEAARENAERAGVADLIEF 281
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 135-256 3.33e-09

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: 57.06  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 135 KVIGiAIMKHFGWKADLRNPQLEIFI-HLNDIYSVVGIPVFRV-------SLASRAYIKTAGLRSTIAWAMASLADIKAG 206
Cdd:TIGR01177 105 RKIG-AILKKKGFKVSLRRPDIVVRVvITEDIFYLGRVLEERDkeqfierKPDRRPFFKPGSMDPKLARAMVNLARVTEG 183

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287569 207 AFVLDPMCGLGTILLEAAKEWPDVYyvGADVSDSQLLGTWDNLKAAGLED 256
Cdd:TIGR01177 184 DRVLDPFCGTGGFLIEAGLMGAKVI--GCDIDWKMVAGARINLEHYGIED 231
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
128-261 7.61e-09

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


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 56.22  E-value: 7.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 128 FTAQEVGKVIGIAIMKHFG------WKADLRNPQLEIFIHLNDIYSVVGIPVF-RVSLASR---AYIKTAGLRSTIAWAM 197
Cdd:NF040721  104 FTSIDIGRVAGEAVIDSYLrdkgvrLKVNLDEPDVIVRVELIFDELLVGIDTTgDEGLHKRgyrVYQHPAHLNPTIASSL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569 198 ASLADIKAGAFVLDPMCGLGTILLEAA---------------------------KEWPDVYY--VGADVSDSQLLGTWDN 248
Cdd:NF040721  184 IYLSGWKDEESLLDPMCGSGTILIEAAlikrnippgkfredfafkkifghelleKIKKDVELkiYGIEKFRKHLEGAKKN 263

                         170
                  ....*....|...
gi 1009287569 249 LKAAGLEDKIELL 261
Cdd:NF040721  264 AENAGVDDTIKFI 276
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 93-171 1.13e-08

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 51.51  E-value: 1.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287569   93 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 169
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 1009287569  170 GI 171
Cdd:smart00981  81 SI 82
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 111-171 5.29e-07

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 48.35  E-value: 5.29e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009287569 111 DLTFRVSCRCSGTigKAFTAQEVGKVIGIAIMKHFG-----WKADLRNPQLEIFIHLNDIYSVVGI 171
Cdd:cd11715    85 DGTFAVRATRVGS--KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSL 148
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 150-224 5.74e-06

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: 47.87  E-value: 5.74e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1009287569 150 DLRNPQLEIFIHLNDIYSVVGIPVFRVSLASRAYIKTAG---LRSTIAWAMASLAD-IKAGAFVLDPMCGLGTILLEAA 224
Cdd:PRK11783  131 DKEQPDIRINARLNKGEATISLDLSGESLHQRGYRQATGeapLKENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAA 209
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 113-162 2.78e-05

THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 460749  Cd Length: 143  Bit Score: 43.20  E-value: 2.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287569 113 TFRVSCRCSGTIGKaFTAQEVGKVIGIAIMKHFGWKADLRNPQLEIFIHL 162
Cdd:pfam02926  84 TFAVRVKRRGKNHE-FTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEI 132
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 197-261 9.70e-05

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 42.22  E-value: 9.70e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1009287569 197 MASLADIKAGAFVLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELL 261
Cdd:COG2230    43 ILRKLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTLSPEQLEYARERAAEAGLADRVEVR 106
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 98-160 6.85e-04

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: 39.74  E-value: 6.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1009287569  98 NDIEKA----IDTHNQNDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFI 160
Cdd:cd11716    82 EDIKEAalelLKEELKKGKTFKVRAKRADK-SFPFTSMEINREVGAALLENTPdLKVDLKNPDVTIRV 148
CMAS pfam02353
Mycolic acid cyclopropane synthetase; This family consist of ...
 201-262 6.90e-03

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


Pssm-ID: 396777 [Multi-domain]  Cd Length: 272  Bit Score: 37.69  E-value: 6.90e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1009287569 201 ADIKAGAFVLDPMCGLGTILLEAAKEWpDVYYVGADVSDSQLLGTWDNLKAAGLEDKIELLK 262
Cdd:pfam02353  57 LGLKPGMTLLDIGCGWGGLMRRAAERY-DVNVVGLTLSKNQYKLARKRVAAEGLARKVEVLL 117
 
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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