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Conserved domains on  [gi|224466790|gb|ACN44620|]
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thiamine biosynthesis protein ThiI [Salmonella enterica subsp. enterica serovar Paratyphi C str. RKS4594]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 3-379 0e+00

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: 522.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790   3 FIIKlFPEITIKSQSvRLRFIKILTGNIRNVLKHYDEtLAVVRHWDNIEVRAKDENQRLAIrDALTRIPGIHHILEVEDV 82
Cdd:COG0301    4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGEDAEEAI-ERLKKVFGIVSFSPAVEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  83 PFtDMHDIFEKALAQYREQLEGKTFCVRVKRRGKH-EFSSIEVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRLLL 161
Cdd:COG0301   80 EK-DLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 162 IKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG---AVHEIGVRQVAHYLwNRFGSsHRVR 238
Cdd:COG0301  159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYGG-HRVK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 239 FVAINFEPVVGEILEKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLIS 318
Cdd:COG0301  237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224466790 319 YDKEHIINLARQIGTEDFARTMPEYCG--VISKSPTVKAIKAKIEAEEENFDFS-ILDKVVEEA 379
Cdd:COG0301  317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLEeLLEEAVENA 380
ThiI_C_thiazole TIGR04271
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ...
 382-482 2.64e-58

thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein in which most of the length of the protein is responsible for sulfurtransferase activity in 4-thiouridine modification to tRNA (EC 2.8.1.4 - see model TIGR00342). This rhodanese-like C-terminal domain, by itself, is able to synthesize the thiazole moiety during thiamin biosynthesis. Note that the invariant Cys residue in this domain is unusual in being required for both activities of the bifunctional ThiI protein.


:

Pssm-ID: 275094 [Multi-domain]  Cd Length: 101  Bit Score: 187.38  E-value: 2.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  382 VDIREIAQQTQQEVVEVETVSGFGPNDVILDIRSVDEQDDKPLKVEGVDVVSLPFYKLSTKFGDLDQSKTWLLWCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 224466790  462 SRLQALYLREQGFANVKVYRP 482
Cdd:TIGR04271  81 SRLQALYLKEQGFTNVKVYRP 101
 
Name Accession Description Interval E-value
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 3-379 0e+00

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: 522.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790   3 FIIKlFPEITIKSQSvRLRFIKILTGNIRNVLKHYDEtLAVVRHWDNIEVRAKDENQRLAIrDALTRIPGIHHILEVEDV 82
Cdd:COG0301    4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGEDAEEAI-ERLKKVFGIVSFSPAVEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  83 PFtDMHDIFEKALAQYREQLEGKTFCVRVKRRGKH-EFSSIEVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRLLL 161
Cdd:COG0301   80 EK-DLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 162 IKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG---AVHEIGVRQVAHYLwNRFGSsHRVR 238
Cdd:COG0301  159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYGG-HRVK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 239 FVAINFEPVVGEILEKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLIS 318
Cdd:COG0301  237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224466790 319 YDKEHIINLARQIGTEDFARTMPEYCG--VISKSPTVKAIKAKIEAEEENFDFS-ILDKVVEEA 379
Cdd:COG0301  317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLEeLLEEAVENA 380
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 4-376 1.19e-176

tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase involved in 4-thiouridine modification of tRNA. This protein often is bifunctional, with genetically separable activities, where the C-terminal rhodanese-like domain (residues 385 to 482 in E. coli ThiI), a domain not included in this model, is sufficient to synthesize the thiazole moiety of thiamine (see TIGR04271). Note that ThiI, because of its role in tRNA modification, may occur in species (such as Mycoplasma genitalium) that lack de novo thiamine biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine, Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273025 [Multi-domain]  Cd Length: 371  Bit Score: 500.01  E-value: 1.19e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790    4 IIKLFPEITIKSQsVRLRFIKILTGNIRNVLKHYDETLAVVRHWDNIEVRAKDENQRLAIRDALTRIPGIHH--ILEVED 81
Cdd:TIGR00342   1 ILARYGEIGIKGK-NRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIVSfsPAFKCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790   82 VPFTDMHdIFEKALAQYREqlEGKTFCVRVKRRGKH-EFSSIEVERYVGGGLNQHIEsARVKLTNPDVTVHLEVEDDRLL 160
Cdd:TIGR00342  80 LPFDEIH-ILLKALKQLRK--EGKTFKVRTKRRGKDfPLNSVEVNKYVGGGIVEKIG-LKVDLTNPDITVHIEIREDEFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  161 LIKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAVHEIGVRQVAHYLWNRFGSSHRVRFV 240
Cdd:TIGR00342 156 IITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  241 AINFEPVVGEILEKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYD 320
Cdd:TIGR00342 236 VFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMD 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 224466790  321 KEHIINLARQIGTEDFARTMPEYCGVISK--SPTVKAIKAKIEAEEENFDFSilDKVV 376
Cdd:TIGR00342 316 KEEIIELAKEIGTYEISIEPHEDCCTIFKpkHPTTKAKPEKVEKLEEKLDFS--RKLV 371
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 175-369 1.18e-101

Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for thiamine biosynthesis.


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 302.43  E-value: 1.18e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  175 GTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFF--NLGGAVHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEIL 252
Cdd:pfam02568   1 GTQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  253 EKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDKEHIINLARQIG 332
Cdd:pfam02568  81 EKAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 224466790  333 TEDFARTMPEYCGVISKSPTVKAIKAKIEAEEENFDF 369
Cdd:pfam02568 161 TYEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKLDL 197
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 174-355 1.09e-86

pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide.


Pssm-ID: 467485 [Multi-domain]  Cd Length: 185  Bit Score: 263.64  E-value: 1.09e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 174 IGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAVHEIGVRQVAHYLWNRFGSSHRVRFVAINF-EPVVGEIL 252
Cdd:cd01712    1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 253 EKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDKEHIINLARQIG 332
Cdd:cd01712   81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                        170       180
                 ....*....|....*....|....*
gi 224466790 333 TEDFARTMPE--YCGVISKSPTVKA 355
Cdd:cd01712  161 TYEISILPYEdcCCLFAPKNPVTKP 185
ThiI_C_thiazole TIGR04271
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ...
 382-482 2.64e-58

thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein in which most of the length of the protein is responsible for sulfurtransferase activity in 4-thiouridine modification to tRNA (EC 2.8.1.4 - see model TIGR00342). This rhodanese-like C-terminal domain, by itself, is able to synthesize the thiazole moiety during thiamin biosynthesis. Note that the invariant Cys residue in this domain is unusual in being required for both activities of the bifunctional ThiI protein.


Pssm-ID: 275094 [Multi-domain]  Cd Length: 101  Bit Score: 187.38  E-value: 2.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  382 VDIREIAQQTQQEVVEVETVSGFGPNDVILDIRSVDEQDDKPLKVEGVDVVSLPFYKLSTKFGDLDQSKTWLLWCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 224466790  462 SRLQALYLREQGFANVKVYRP 482
Cdd:TIGR04271  81 SRLQALYLKEQGFTNVKVYRP 101
PRK08349 PRK08349
hypothetical protein; Validated
 180-355 7.60e-27

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 107.13  E-value: 7.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 180 VLSLISGGFDSGVSSYMLMRRGCRVHYCFFNlGGAVHEIGVRQVAHYLWNRFGSSHRvRFVAINFEPVVGEILEKVDDGQ 259
Cdd:PRK08349   3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFR-QDEKKEEKVRELVERLQELHGGKLK-DPVVVDAFEEQGPVFEKLRELK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 260 MG----VVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDKEHIINLARQIGTED 335
Cdd:PRK08349  81 KEkwtcIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTFE 160

                        170       180
                 ....*....|....*....|
gi 224466790 336 FARTMPEYCGVISKSPTVKA 355
Cdd:PRK08349 161 ISIEPEPPCPFVPKYPVVRA 180
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 86-161 8.65e-20

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: 83.48  E-value: 8.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790    86 DMHDIFEKALAQYREQ---LEGKTFCVRVKRRGK-HEFSSIEVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRLLL 161
Cdd:smart00981   1 DLEDLYETALELIRWEkifKEGKTFAVRAKRRGKnHEFTSLEVKRAIGDKLLEKTGGRKVDLKNPDVVIRVELRKDKAYL 80
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 406-481 2.90e-08

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 51.51  E-value: 2.90e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224466790 406 PNDVILDIRSVDEQDDKPLKvegvDVVSLPFYKLSTKFGDLDQSKTWLLWCERGVMSRLQALYLREQGFANVKVYR 481
Cdd:COG0607   18 EDAVLLDVREPEEFAAGHIP----GAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLA 89
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 405-481 4.33e-04

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 39.21  E-value: 4.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224466790 405 GPNDVILDIRSVDEQDDKPLKvegvDVVSLPFYKLSTKFG--DLDQSKTWLLWCERGVMSRLQALYLREQGFANVKVYR 481
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHIP----GAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
 
Name Accession Description Interval E-value
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 3-379 0e+00

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: 522.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790   3 FIIKlFPEITIKSQSvRLRFIKILTGNIRNVLKHYDEtLAVVRHWDNIEVRAKDENQRLAIrDALTRIPGIHHILEVEDV 82
Cdd:COG0301    4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGEDAEEAI-ERLKKVFGIVSFSPAVEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  83 PFtDMHDIFEKALAQYREQLEGKTFCVRVKRRGKH-EFSSIEVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRLLL 161
Cdd:COG0301   80 EK-DLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 162 IKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG---AVHEIGVRQVAHYLwNRFGSsHRVR 238
Cdd:COG0301  159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYGG-HRVK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 239 FVAINFEPVVGEILEKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLIS 318
Cdd:COG0301  237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224466790 319 YDKEHIINLARQIGTEDFARTMPEYCG--VISKSPTVKAIKAKIEAEEENFDFS-ILDKVVEEA 379
Cdd:COG0301  317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLEeLLEEAVENA 380
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 4-376 1.19e-176

tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase involved in 4-thiouridine modification of tRNA. This protein often is bifunctional, with genetically separable activities, where the C-terminal rhodanese-like domain (residues 385 to 482 in E. coli ThiI), a domain not included in this model, is sufficient to synthesize the thiazole moiety of thiamine (see TIGR04271). Note that ThiI, because of its role in tRNA modification, may occur in species (such as Mycoplasma genitalium) that lack de novo thiamine biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine, Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273025 [Multi-domain]  Cd Length: 371  Bit Score: 500.01  E-value: 1.19e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790    4 IIKLFPEITIKSQsVRLRFIKILTGNIRNVLKHYDETLAVVRHWDNIEVRAKDENQRLAIRDALTRIPGIHH--ILEVED 81
Cdd:TIGR00342   1 ILARYGEIGIKGK-NRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIVSfsPAFKCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790   82 VPFTDMHdIFEKALAQYREqlEGKTFCVRVKRRGKH-EFSSIEVERYVGGGLNQHIEsARVKLTNPDVTVHLEVEDDRLL 160
Cdd:TIGR00342  80 LPFDEIH-ILLKALKQLRK--EGKTFKVRTKRRGKDfPLNSVEVNKYVGGGIVEKIG-LKVDLTNPDITVHIEIREDEFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  161 LIKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAVHEIGVRQVAHYLWNRFGSSHRVRFV 240
Cdd:TIGR00342 156 IITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  241 AINFEPVVGEILEKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYD 320
Cdd:TIGR00342 236 VFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMD 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 224466790  321 KEHIINLARQIGTEDFARTMPEYCGVISK--SPTVKAIKAKIEAEEENFDFSilDKVV 376
Cdd:TIGR00342 316 KEEIIELAKEIGTYEISIEPHEDCCTIFKpkHPTTKAKPEKVEKLEEKLDFS--RKLV 371
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 175-369 1.18e-101

Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for thiamine biosynthesis.


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 302.43  E-value: 1.18e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  175 GTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFF--NLGGAVHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEIL 252
Cdd:pfam02568   1 GTQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  253 EKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDKEHIINLARQIG 332
Cdd:pfam02568  81 EKAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 224466790  333 TEDFARTMPEYCGVISKSPTVKAIKAKIEAEEENFDF 369
Cdd:pfam02568 161 TYEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKLDL 197
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 174-355 1.09e-86

pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide.


Pssm-ID: 467485 [Multi-domain]  Cd Length: 185  Bit Score: 263.64  E-value: 1.09e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 174 IGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAVHEIGVRQVAHYLWNRFGSSHRVRFVAINF-EPVVGEIL 252
Cdd:cd01712    1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 253 EKVDDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDKEHIINLARQIG 332
Cdd:cd01712   81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                        170       180
                 ....*....|....*....|....*
gi 224466790 333 TEDFARTMPE--YCGVISKSPTVKA 355
Cdd:cd01712  161 TYEISILPYEdcCCLFAPKNPVTKP 185
ThiI_C_thiazole TIGR04271
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ...
 382-482 2.64e-58

thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein in which most of the length of the protein is responsible for sulfurtransferase activity in 4-thiouridine modification to tRNA (EC 2.8.1.4 - see model TIGR00342). This rhodanese-like C-terminal domain, by itself, is able to synthesize the thiazole moiety during thiamin biosynthesis. Note that the invariant Cys residue in this domain is unusual in being required for both activities of the bifunctional ThiI protein.


Pssm-ID: 275094 [Multi-domain]  Cd Length: 101  Bit Score: 187.38  E-value: 2.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  382 VDIREIAQQTQQEVVEVETVSGFGPNDVILDIRSVDEQDDKPLKVEGVDVVSLPFYKLSTKFGDLDQSKTWLLWCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 224466790  462 SRLQALYLREQGFANVKVYRP 482
Cdd:TIGR04271  81 SRLQALYLKEQGFTNVKVYRP 101
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 2-170 1.17e-51

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: 172.63  E-value: 1.17e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790   2 KFIIKLFpEITIKSQsVRLRFIKILTGNIRNVLKHYDEtLAVVRHWDNIEVRAKDENQRlAIRDALTRIPGIHHILEVED 81
Cdd:cd11716    1 KILVRYG-EIALKGK-NRKRFEKRLVKNIRRALKDLPD-VKVEREWGRIYVELNGEDLE-EVIERLKKVFGIVSFSPAVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  82 VPFtDMHDIFEKALAQYREQL-EGKTFCVRVKRRGK-HEFSSIEVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRL 159
Cdd:cd11716   77 VEK-DLEDIKEAALELLKEELkKGKTFKVRAKRADKsFPFTSMEINREVGAALLENTPDLKVDLKNPDVTIRVEIREDGA 155

                        170
                 ....*....|.
gi 224466790 160 LLIKGRYEGIG 170
Cdd:cd11716  156 YVYTERIPGPG 166
PRK08349 PRK08349
hypothetical protein; Validated
 180-355 7.60e-27

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 107.13  E-value: 7.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 180 VLSLISGGFDSGVSSYMLMRRGCRVHYCFFNlGGAVHEIGVRQVAHYLWNRFGSSHRvRFVAINFEPVVGEILEKVDDGQ 259
Cdd:PRK08349   3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFR-QDEKKEEKVRELVERLQELHGGKLK-DPVVVDAFEEQGPVFEKLRELK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 260 MG----VVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISYDKEHIINLARQIGTED 335
Cdd:PRK08349  81 KEkwtcIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTFE 160

                        170       180
                 ....*....|....*....|
gi 224466790 336 FARTMPEYCGVISKSPTVKA 355
Cdd:PRK08349 161 ISIEPEPPCPFVPKYPVVRA 180
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 28-161 2.32e-22

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: 92.89  E-value: 2.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790   28 GNIRNVLKHYDETLAVVR-HWDNIEVRAKDEN---QRLAIRDALTRIPGIHHILeVEDVPFTDMHDIFEKALAQYREQL- 102
Cdd:pfam02926   1 KEIEELLKKGGINVEVVRsGRGRILVVLKGENpeeDRELLKEALEKAPGIERFP-VAETCEADLEDILELAKEIIKDKFk 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224466790  103 -EGKTFCVRVKRRGK-HEFSSIEVERYVGGGLNQHIeSARVKLTNPDVTVHLEVEDDRLLL 161
Cdd:pfam02926  80 kEGETFAVRVKRRGKnHEFTSLEINREVGKAIVEKT-GLKVDLENPDIVVHVEIIKDKAYI 139
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 86-161 8.65e-20

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: 83.48  E-value: 8.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790    86 DMHDIFEKALAQYREQ---LEGKTFCVRVKRRGK-HEFSSIEVERYVGGGLNQHIESARVKLTNPDVTVHLEVEDDRLLL 161
Cdd:smart00981   1 DLEDLYETALELIRWEkifKEGKTFAVRAKRRGKnHEFTSLEVKRAIGDKLLEKTGGRKVDLKNPDVVIRVELRKDKAYL 80
Tan1 COG1818
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure ...
 1-154 3.31e-15

tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure and biogenesis]; tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441423  Cd Length: 162  Bit Score: 73.00  E-value: 3.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790   1 MKFIIKLFPeitiksqsvrlRFIKILTGNIRNVLKHYDETL-AVVRHWDN-IEVRAKDENQRLA--IRDALTRIPGIHHI 76
Cdd:COG1818    1 MNLIVTTPR-----------GRERDAIEELRDILEEGDPNAeVVPTGFSGvLLVKTSLDPYEAVekLKEEPWEPRYILRV 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224466790  77 LEVEDVPFTDMHDIFEKALAQYREQL-EGKTFCVRVKRRGKHEFSSIEVERYVGGGLNqhiESARVKLTNPDVTVHLEV 154
Cdd:COG1818   70 IPVDRVVKTDLEEIVEAAKELAKKKIpEGETFAVRCEKRGKSKLSSREVIRAIGEAIK---RGAKVDLENPDWVVLVEI 145
THUMP_SPOUT cd11718
THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are ...
 52-161 1.59e-10

THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are characterized by containing an N-terminal THUMP domain and a C-terminal SPOUT RNA methyltransferase domain. No functional information is available 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: 212587  Cd Length: 145  Bit Score: 59.22  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  52 VRAKDENQRLAIRdaltRIPGIHHILEVEDVPFTDMHDIFEKALAQYREQLEGKTFCVRVKRRGKHEFSSIEVERYVGGG 131
Cdd:cd11718   39 VESDEDKKDELAL----RVPEVERVIPVDAEVKADLDEIVRVAEEIAKHISEGETFAVRTTRRGKHDFTSIDVNVVLGAA 114

                         90       100       110
                 ....*....|....*....|....*....|
gi 224466790 132 LnQHIESARVKLTNPDVTVHLEVEDDRLLL 161
Cdd:cd11718  115 V-KELTGAEVDLNNPDKVVYVEIIGDRAYI 143
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 406-481 2.90e-08

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 51.51  E-value: 2.90e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224466790 406 PNDVILDIRSVDEQDDKPLKvegvDVVSLPFYKLSTKFGDLDQSKTWLLWCERGVMSRLQALYLREQGFANVKVYR 481
Cdd:COG0607   18 EDAVLLDVREPEEFAAGHIP----GAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLA 89
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 103-161 1.39e-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: 50.66  E-value: 1.39e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 224466790 103 EGKTFCVRVKRRGKHEFSSIEVERYVGGGLNQHIESA----RVKLTNPDVTVHLEVEDDRLLL 161
Cdd:cd11715   84 PDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREKgkrpSVDLDNPDVRIRVHLSKDRATL 146
THUMP_THUMPD1_like cd11717
THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins ...
 73-154 2.01e-06

THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins including THUMP domain-containing protein 1 and Saccharomyces cerevisiae Tan1. Tan1 is non essential and has been shown to be required for the formation of the modified nucleoside N(4)-acetylcytidine (ac(4)C) in tRNA. To date, there is no functional information available about THUMPD1. 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: 212586  Cd Length: 158  Bit Score: 47.58  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790  73 IHHILEVEDVPFTDMHDIFEKA---LAQY-REQLEGKTFCVRVKRRGKHEFSSIEVERYVGGGLNQHiesARVKLTNPDV 148
Cdd:cd11717   65 IQRLIPIDVTCKASLEEIEKLAkelLKKHfPTAEPPKTFAVECKSRNNNKLSRDEVIKAVAELVPEI---HKVDLKNPDK 141


                 ....*.
gi 224466790 149 TVHLEV 154
Cdd:cd11717  142 VILVEV 147
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 405-481 4.33e-04

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 39.21  E-value: 4.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 224466790 405 GPNDVILDIRSVDEQDDKPLKvegvDVVSLPFYKLSTKFG--DLDQSKTWLLWCERGVMSRLQALYLREQGFANVKVYR 481
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHIP----GAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
THUMP cd11688
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ...
 86-158 8.83e-04

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: 39.78  E-value: 8.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 224466790  86 DMHDIFEKALAQYREQL--EGKTFCVRVKRRGKHEFSSIEVERYVGGGLNQhIESARVKLTNPDVTVHLEVEDDR 158
Cdd:cd11688   71 DLEDLYETALEINEPEMgnEGAKFAVRARRRNKTILNSQEIAMKVGDAIVD-AFNPEVDLDNPDIVVNVEVHKEI 144
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 395-477 2.43e-03

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 37.24  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224466790 395 VVEVETVSGFGPNDVILDIRSVDEQDDKPLKVEGVDVVSLPfyKLSTKFGDLDQSKTWLLWCERGVMSRLQALYLREQGF 474
Cdd:cd01444    4 VDELAELLAAGEAPVLLDVRDPASYAALPDHIPGAIHLDED--SLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAGF 81


                 ...
gi 224466790 475 ANV 477
Cdd:cd01444   82 TDV 84
 
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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