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Conserved domains on  [gi|1799550684|gb|QHM76375|]
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tRNA sulfurtransferase [Mixta theicola]

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 ...
 3-380 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: 515.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684   3 FIIKlFPEITIKSQSvRLRFIKILTGNIRNVLKDLDEtLAVVRHWDHIEVRSKDDSLRAAfIDELTRIPGIHHVLAVEdR 82
Cdd:COG0301     4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGEDAEEA-IERLKKVFGIVSFSPAV-E 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684  83 SWTDMHDIFEQTLAINRERLEGKTFCVRVKRRGQH-PFSSQDVERYVGGGLNQHIESAQVKLSHPQVTVNLEIENDRLLL 161
Cdd:COG0301    79 VEKDLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 162 ITGRYEGLGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG---AAHEIGVRQVAHYLwNRFGrSHRVR 238
Cdd:COG0301   159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYG-GHRVK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 239 FVAINFEPVVAEILEKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLIS 318
Cdd:COG0301   237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799550684 319 HDKEHIINLARQIGTEDFARTMPEYCG--VISKSPTVKAVKARIEAEEENFDFAVL-DRVVQEAT 380
Cdd:COG0301   317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLEELlEEAVENAE 381
ThiI_C_thiazole TIGR04271
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ...
 382-482 8.91e-57

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: 183.53  E-value: 8.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 382 VDIRTIAEQTQENVTEVETVASFSANDALLDIRSLDEQEVKPLKVEGIEVKSLPFYKLGTQFGDLDQSKTWLLYCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 1799550684 462 SRLQALYLHEQGFKNVKVYRP 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 ...
 3-380 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: 515.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684   3 FIIKlFPEITIKSQSvRLRFIKILTGNIRNVLKDLDEtLAVVRHWDHIEVRSKDDSLRAAfIDELTRIPGIHHVLAVEdR 82
Cdd:COG0301     4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGEDAEEA-IERLKKVFGIVSFSPAV-E 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684  83 SWTDMHDIFEQTLAINRERLEGKTFCVRVKRRGQH-PFSSQDVERYVGGGLNQHIESAQVKLSHPQVTVNLEIENDRLLL 161
Cdd:COG0301    79 VEKDLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 162 ITGRYEGLGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG---AAHEIGVRQVAHYLwNRFGrSHRVR 238
Cdd:COG0301   159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYG-GHRVK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 239 FVAINFEPVVAEILEKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLIS 318
Cdd:COG0301   237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799550684 319 HDKEHIINLARQIGTEDFARTMPEYCG--VISKSPTVKAVKARIEAEEENFDFAVL-DRVVQEAT 380
Cdd:COG0301   317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLEELlEEAVENAE 381
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 4-369 2.31e-158

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: 453.79  E-value: 2.31e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684   4 IIKLFPEITIKSQsVRLRFIKILTGNIRNVLKDLDETLAVVRHWDHIEVRSKDDSLRAAFIDELTRIPGIHH--VLAVED 81
Cdd:TIGR00342   1 ILARYGEIGIKGK-NRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIVSfsPAFKCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684  82 RSWTDMHDIFEqtlAINRERLEGKTFCVRVKRRG-QHPFSSQDVERYVGGGLNQHIEsAQVKLSHPQVTVNLEIENDRLL 160
Cdd:TIGR00342  80 LPFDEIHILLK---ALKQLRKEGKTFKVRTKRRGkDFPLNSVEVNKYVGGGIVEKIG-LKVDLTNPDITVHIEIREDEFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 161 LITGRYEGLGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGRSHRVRFV 240
Cdd:TIGR00342 156 IITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 241 AINFEPVVAEILEKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLISHD 320
Cdd:TIGR00342 236 VFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMD 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1799550684 321 KEHIINLARQIGTEDFARTMPEYCGVISK--SPTVKAVKARIEAEEENFDF 369
Cdd:TIGR00342 316 KEEIIELAKEIGTYEISIEPHEDCCTIFKpkHPTTKAKPEKVEKLEEKLDF 366
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 175-369 8.77e-100

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 297.80  E-value: 8.77e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 175 GTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFF--NLGGAAHEIGVRQVAHYLWNRFGRSHRVRFVAINFEPVVAEIL 252
Cdd:pfam02568   1 GTQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 253 EKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLISHDKEHIINLARQIG 332
Cdd:pfam02568  81 EKAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1799550684 333 TEDFARTMPEYCGVISKSPTVKAVKARIEAEEENFDF 369
Cdd:pfam02568 161 TYEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKLDL 197
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 174-355 2.59e-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: 262.87  E-value: 2.59e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 174 IGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGRSHRVRFVAINF-EPVVAEIL 252
Cdd:cd01712     1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 253 EKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLISHDKEHIINLARQIG 332
Cdd:cd01712    81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                         170       180
                  ....*....|....*....|....*
gi 1799550684 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 8.91e-57

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: 183.53  E-value: 8.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 382 VDIRTIAEQTQENVTEVETVASFSANDALLDIRSLDEQEVKPLKVEGIEVKSLPFYKLGTQFGDLDQSKTWLLYCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 1799550684 462 SRLQALYLHEQGFKNVKVYRP 482
Cdd:TIGR04271  81 SRLQALYLKEQGFTNVKVYRP 101
PRK08349 PRK08349
hypothetical protein; Validated
 180-355 4.70e-28

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 110.60  E-value: 4.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 180 VLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEiGVRQVAHYLWNRFGRSHRVRFVAINFE---PVVAEILEKVD 256
Cdd:PRK08349    3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEE-KVRELVERLQELHGGKLKDPVVVDAFEeqgPVFEKLRELKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 257 DGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLISHDKEHIINLARQIGTEDF 336
Cdd:PRK08349   82 EKWTCIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTFEI 161

                         170
                  ....*....|....*....
gi 1799550684 337 ARTMPEYCGVISKSPTVKA 355
Cdd:PRK08349  162 SIEPEPPCPFVPKYPVVRA 180
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 86-161 3.11e-17

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


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 76.16  E-value: 3.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684   86 DMHDIFEQTLAINRER---LEGKTFCVRVKRRG-QHPFSSQDVERYVGGGLNQHIESAQVKLSHPQVTVNLEIENDRLLL 161
Cdd:smart00981   1 DLEDLYETALELIRWEkifKEGKTFAVRAKRRGkNHEFTSLEVKRAIGDKLLEKTGGRKVDLKNPDVVIRVELRKDKAYL 80
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 410-481 3.10e-09

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: 54.20  E-value: 3.10e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799550684 410 LLDIRSLDEQEVKPLKvegiEVKSLPFYKLGTQFGDLDQSKTWLLYCERGVMSRLQALYLHEQGFKNVKVYR 481
Cdd:COG0607    22 LLDVREPEEFAAGHIP----GAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLA 89
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 410-481 3.70e-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: 39.59  E-value: 3.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799550684 410 LLDIRSLDEQEVKPLKvegiEVKSLPFYKLGTQFG--DLDQSKTWLLYCERGVMSRLQALYLHEQGFKNVKVYR 481
Cdd:cd00158    13 LLDVREPEEYAAGHIP----GAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 410-480 9.67e-04

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The 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 stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 38.59  E-value: 9.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684  410 LLDIRSLDEQE-----------VKPLKVEGIEVKSLPFYKLGTQFGdLDQSKTWLLYCERGVMSRLQALYLHEQGFKNVK 478
Cdd:smart00450   7 LLDVRSPEEYEgghipgavnipLSELLDRRGELDILEFEELLKRLG-LDKDKPVVVYCRSGNRSAKAAWLLRELGFKNVY 85


                   ..
gi 1799550684  479 VY 480
Cdd:smart00450  86 LL 87
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 407-481 6.99e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 35.92  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 407 NDALLDIRSLDE------QEVKPLKVEGIEVKSLPFYKLGTQFGDLDQSKTWLLYCERGVMSRLQALYLHEQGFKNVKVY 480
Cdd:pfam00581   5 KVVLIDVRPPEEyakghiPGAVNVPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVL 84


                  .
gi 1799550684 481 R 481
Cdd:pfam00581  85 D 85
 
Name Accession Description Interval E-value
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 3-380 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: 515.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684   3 FIIKlFPEITIKSQSvRLRFIKILTGNIRNVLKDLDEtLAVVRHWDHIEVRSKDDSLRAAfIDELTRIPGIHHVLAVEdR 82
Cdd:COG0301     4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGEDAEEA-IERLKKVFGIVSFSPAV-E 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684  83 SWTDMHDIFEQTLAINRERLEGKTFCVRVKRRGQH-PFSSQDVERYVGGGLNQHIESAQVKLSHPQVTVNLEIENDRLLL 161
Cdd:COG0301    79 VEKDLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 162 ITGRYEGLGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG---AAHEIGVRQVAHYLwNRFGrSHRVR 238
Cdd:COG0301   159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYG-GHRVK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 239 FVAINFEPVVAEILEKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLIS 318
Cdd:COG0301   237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799550684 319 HDKEHIINLARQIGTEDFARTMPEYCG--VISKSPTVKAVKARIEAEEENFDFAVL-DRVVQEAT 380
Cdd:COG0301   317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLEELlEEAVENAE 381
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 4-369 2.31e-158

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: 453.79  E-value: 2.31e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684   4 IIKLFPEITIKSQsVRLRFIKILTGNIRNVLKDLDETLAVVRHWDHIEVRSKDDSLRAAFIDELTRIPGIHH--VLAVED 81
Cdd:TIGR00342   1 ILARYGEIGIKGK-NRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIVSfsPAFKCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684  82 RSWTDMHDIFEqtlAINRERLEGKTFCVRVKRRG-QHPFSSQDVERYVGGGLNQHIEsAQVKLSHPQVTVNLEIENDRLL 160
Cdd:TIGR00342  80 LPFDEIHILLK---ALKQLRKEGKTFKVRTKRRGkDFPLNSVEVNKYVGGGIVEKIG-LKVDLTNPDITVHIEIREDEFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 161 LITGRYEGLGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGRSHRVRFV 240
Cdd:TIGR00342 156 IITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 241 AINFEPVVAEILEKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLISHD 320
Cdd:TIGR00342 236 VFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMD 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1799550684 321 KEHIINLARQIGTEDFARTMPEYCGVISK--SPTVKAVKARIEAEEENFDF 369
Cdd:TIGR00342 316 KEEIIELAKEIGTYEISIEPHEDCCTIFKpkHPTTKAKPEKVEKLEEKLDF 366
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 175-369 8.77e-100

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 297.80  E-value: 8.77e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 175 GTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFF--NLGGAAHEIGVRQVAHYLWNRFGRSHRVRFVAINFEPVVAEIL 252
Cdd:pfam02568   1 GTQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 253 EKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLISHDKEHIINLARQIG 332
Cdd:pfam02568  81 EKAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1799550684 333 TEDFARTMPEYCGVISKSPTVKAVKARIEAEEENFDF 369
Cdd:pfam02568 161 TYEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKLDL 197
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 174-355 2.59e-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: 262.87  E-value: 2.59e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 174 IGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGRSHRVRFVAINF-EPVVAEIL 252
Cdd:cd01712     1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 253 EKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLISHDKEHIINLARQIG 332
Cdd:cd01712    81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                         170       180
                  ....*....|....*....|....*
gi 1799550684 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 8.91e-57

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: 183.53  E-value: 8.91e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 382 VDIRTIAEQTQENVTEVETVASFSANDALLDIRSLDEQEVKPLKVEGIEVKSLPFYKLGTQFGDLDQSKTWLLYCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 1799550684 462 SRLQALYLHEQGFKNVKVYRP 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 2.20e-47

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: 161.08  E-value: 2.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684   2 KFIIKLFpEITIKSQsVRLRFIKILTGNIRNVLKDLDEtLAVVRHWDHIEVRSKDDSLRAAfIDELTRIPGIHH---VLA 78
Cdd:cd11716     1 KILVRYG-EIALKGK-NRKRFEKRLVKNIRRALKDLPD-VKVEREWGRIYVELNGEDLEEV-IERLKKVFGIVSfspAVE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684  79 VEdrswTDMHDIFEQTLAINRERL-EGKTFCVRVKRRG-QHPFSSQDVERYVGGGLNQHIESAQVKLSHPQVTVNLEIEN 156
Cdd:cd11716    77 VE----KDLEDIKEAALELLKEELkKGKTFKVRAKRADkSFPFTSMEINREVGAALLENTPDLKVDLKNPDVTIRVEIRE 152

                         170
                  ....*....|....
gi 1799550684 157 DRLLLITGRYEGLG 170
Cdd:cd11716   153 DGAYVYTERIPGPG 166
PRK08349 PRK08349
hypothetical protein; Validated
 180-355 4.70e-28

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 110.60  E-value: 4.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 180 VLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEiGVRQVAHYLWNRFGRSHRVRFVAINFE---PVVAEILEKVD 256
Cdd:PRK08349    3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEE-KVRELVERLQELHGGKLKDPVVVDAFEeqgPVFEKLRELKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 257 DGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNASDTLILRPLISHDKEHIINLARQIGTEDF 336
Cdd:PRK08349   82 EKWTCIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTFEI 161

                         170
                  ....*....|....*....
gi 1799550684 337 ARTMPEYCGVISKSPTVKA 355
Cdd:PRK08349  162 SIEPEPPCPFVPKYPVVRA 180
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 86-161 3.11e-17

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


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 76.16  E-value: 3.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684   86 DMHDIFEQTLAINRER---LEGKTFCVRVKRRG-QHPFSSQDVERYVGGGLNQHIESAQVKLSHPQVTVNLEIENDRLLL 161
Cdd:smart00981   1 DLEDLYETALELIRWEkifKEGKTFAVRAKRRGkNHEFTSLEVKRAIGDKLLEKTGGRKVDLKNPDVVIRVELRKDKAYL 80
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 28-165 1.64e-16

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: 76.32  E-value: 1.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684  28 GNIRNVLKDLDETLAVVR-HWDHIEVRSKDDSL---RAAFIDELTRIPGIHHVLAVEDrSWTDMHDIFEQTLAINRERL- 102
Cdd:pfam02926   1 KEIEELLKKGGINVEVVRsGRGRILVVLKGENPeedRELLKEALEKAPGIERFPVAET-CEADLEDILELAKEIIKDKFk 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799550684 103 -EGKTFCVRVKRRG-QHPFSSQDVERYVGGGLNQHIeSAQVKLSHPQVTVNLEIENDRLLLITGR 165
Cdd:pfam02926  80 kEGETFAVRVKRRGkNHEFTSLEINREVGKAIVEKT-GLKVDLENPDIVVHVEIIKDKAYISIDR 143
Tan1 COG1818
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure ...
 1-154 7.83e-13

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: 66.07  E-value: 7.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684   1 MKFIIKLFPeitiksqsvrlRFIKILTGNIRNVLKDLDETL-AVVRHWDH-IEVRSKDDSLRAA--FIDELTRIPGIHHV 76
Cdd:COG1818     1 MNLIVTTPR-----------GRERDAIEELRDILEEGDPNAeVVPTGFSGvLLVKTSLDPYEAVekLKEEPWEPRYILRV 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799550684  77 LAVEDRSWTDMHDIFEQTLAINRERL-EGKTFCVRVKRRGQHPFSSQDVERYVGGGLNqhiESAQVKLSHPQVTVNLEI 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 1.62e-09

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: 56.14  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684  52 VRSKDDSLRAAfideLTRIPGIHHVLAVEDRSWTDMHDIFEQTLAINRERLEGKTFCVRVKRRGQHPFSSQDVERYVGGG 131
Cdd:cd11718    39 VESDEDKKDEL----ALRVPEVERVIPVDAEVKADLDEIVRVAEEIAKHISEGETFAVRTTRRGKHDFTSIDVNVVLGAA 114

                          90       100       110
                  ....*....|....*....|....*....|
gi 1799550684 132 LnQHIESAQVKLSHPQVTVNLEIENDRLLL 161
Cdd:cd11718   115 V-KELTGAEVDLNNPDKVVYVEIIGDRAYI 143
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 410-481 3.10e-09

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: 54.20  E-value: 3.10e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1799550684 410 LLDIRSLDEQEVKPLKvegiEVKSLPFYKLGTQFGDLDQSKTWLLYCERGVMSRLQALYLHEQGFKNVKVYR 481
Cdd:COG0607    22 LLDVREPEEFAAGHIP----GAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLA 89
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 89-161 9.97e-08

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: 51.43  E-value: 9.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1799550684  89 DIFEQTLAINRERL--EGKTFCVRVKRRGQHPFSSQDVERYVGGGLNQHIESAQ----VKLSHPQVTVNLEIENDRLLL 161
Cdd:cd11715    68 DLYELAKAIDWEDYldPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREKGkrpsVDLDNPDVRIRVHLSKDRATL 146
THUMP cd11688
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ...
 86-158 8.01e-05

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: 42.86  E-value: 8.01e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1799550684  86 DMHDIFEQTLAINRERL--EGKTFCVRVKRRGQHPFSSQDVERYVGGGLNQhIESAQVKLSHPQVTVNLEIENDR 158
Cdd:cd11688    71 DLEDLYETALEINEPEMgnEGAKFAVRARRRNKTILNSQEIAMKVGDAIVD-AFNPEVDLDNPDIVVNVEVHKEI 144
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 178-346 1.30e-04

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 42.99  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 178 EDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG-AAHEIGV--RQVAHYLwnrfGRSHRV---RFVAINFEPVVAEI 251
Cdd:cd01995     1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQrHAKEELEaaKLIAKLL----GIEHKVidlSFLGELGGSSLTDE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 252 LEKVDDGQMG-------VVLKR--MMVRAASQIAERYGVQALVTG-----------------EALGQVSSQ-TLTNLRli 304
Cdd:cd01995    77 GEEVPDGEYDeesipstWVPNRnlIFLSIAAAYAESLGASAIVIGvnaedasgypdcrpefvEAMNSALNLgTATGVK-- 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1799550684 305 dnasdtlILRPLISHDKEHIINLARQIGtEDFARTMPEY------CGV 346
Cdd:cd01995   155 -------VVAPLIGLSKAEIVKLGVELG-VPLELTWSCYrggekhCGR 194
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 410-481 3.70e-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: 39.59  E-value: 3.70e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1799550684 410 LLDIRSLDEQEVKPLKvegiEVKSLPFYKLGTQFG--DLDQSKTWLLYCERGVMSRLQALYLHEQGFKNVKVYR 481
Cdd:cd00158    13 LLDVREPEEYAAGHIP----GAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
THUMP_THUMPD1_like cd11717
THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins ...
 103-154 4.65e-04

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: 40.64  E-value: 4.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1799550684 103 EGKTFCVRVKRRGQHPFSSQDVERYVGGGLNQHiesAQVKLSHPQVTVNLEI 154
Cdd:cd11717    99 PPKTFAVECKSRNNNKLSRDEVIKAVAELVPEI---HKVDLKNPDKVILVEV 147
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 410-480 9.67e-04

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The 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 stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 38.59  E-value: 9.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684  410 LLDIRSLDEQE-----------VKPLKVEGIEVKSLPFYKLGTQFGdLDQSKTWLLYCERGVMSRLQALYLHEQGFKNVK 478
Cdd:smart00450   7 LLDVRSPEEYEgghipgavnipLSELLDRRGELDILEFEELLKRLG-LDKDKPVVVYCRSGNRSAKAAWLLRELGFKNVY 85


                   ..
gi 1799550684  479 VY 480
Cdd:smart00450  86 LL 87
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 407-481 6.99e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 35.92  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1799550684 407 NDALLDIRSLDE------QEVKPLKVEGIEVKSLPFYKLGTQFGDLDQSKTWLLYCERGVMSRLQALYLHEQGFKNVKVY 480
Cdd:pfam00581   5 KVVLIDVRPPEEyakghiPGAVNVPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVL 84


                  .
gi 1799550684 481 R 481
Cdd:pfam00581  85 D 85
 
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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