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Conserved domains on  [gi|1785196388|gb|QGX90842|]
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tRNA 4-thiouridine(8) synthase ThiI [Tatumella sp. TA1]

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 5.31e-178

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: 503.85  E-value: 5.31e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388   3 FIVKlFPEITIKSQSvRLRFIKILSSNIRNVLKSVDEdIAVVRLWDHITVRTrKPELSAAVAEALTRIPGIHHVLSVEdR 82
Cdd:COG0301     4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVET-DGEDAEEAIERLKKVFGIVSFSPAV-E 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  83 TFTSLHDIFEQTLALYQSQLEGKTFCVRAKRRGKH-EFTSHEVERYVGGGLNQHIASASVKLQQPDMTVHLEIDQERLLL 161
Cdd:COG0301    79 VEKDLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 162 IKDRYEGLGGFPIGTQEDVISLISGGFDSGVSSYMLMRRGSRVHYCFFNLGG---AAHEIGVRQVAHYLwNTFGrSHRVR 238
Cdd:COG0301   159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYG-GHRVK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 239 FIAIDFEPVVGEILEKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLIS 318
Cdd:COG0301   237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785196388 319 HDKEHIIKVARQIGTEDFAKTMPEYCG--VISKSPTVKAVKEKIEAEENNFDF-AILERVISEAR 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 3.49e-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: 187.00  E-value: 3.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 382 IDIRDIAVETTQEVAEVESVSALTAQDSILDIRSIDEQDDKPLMVEGVEIKSIPFYKLATQFGDLDRSRTWLLYCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 1785196388 462 SRLQALYLHEQGFTNVKVYRP 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 5.31e-178

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: 503.85  E-value: 5.31e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388   3 FIVKlFPEITIKSQSvRLRFIKILSSNIRNVLKSVDEdIAVVRLWDHITVRTrKPELSAAVAEALTRIPGIHHVLSVEdR 82
Cdd:COG0301     4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVET-DGEDAEEAIERLKKVFGIVSFSPAV-E 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  83 TFTSLHDIFEQTLALYQSQLEGKTFCVRAKRRGKH-EFTSHEVERYVGGGLNQHIASASVKLQQPDMTVHLEIDQERLLL 161
Cdd:COG0301    79 VEKDLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 162 IKDRYEGLGGFPIGTQEDVISLISGGFDSGVSSYMLMRRGSRVHYCFFNLGG---AAHEIGVRQVAHYLwNTFGrSHRVR 238
Cdd:COG0301   159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYG-GHRVK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 239 FIAIDFEPVVGEILEKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLIS 318
Cdd:COG0301   237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785196388 319 HDKEHIIKVARQIGTEDFAKTMPEYCG--VISKSPTVKAVKEKIEAEENNFDF-AILERVISEAR 380
Cdd:COG0301   317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLeELLEEAVENAE 381
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 4-369 1.77e-147

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: 426.05  E-value: 1.77e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388   4 IVKLFPEITIKSQsVRLRFIKILSSNIRNVLKSVDEDIAVVRLWDHITVRTRKPELSAAVAEALTRIPGIHH--VLSVED 81
Cdd:TIGR00342   1 ILARYGEIGIKGK-NRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIVSfsPAFKCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  82 RTFTSLHDIFEqtlALYQSQLEGKTFCVRAKRRGKH-EFTSHEVERYVGGGLNQHIaSASVKLQQPDMTVHLEIDQERLL 160
Cdd:TIGR00342  80 LPFDEIHILLK---ALKQLRKEGKTFKVRTKRRGKDfPLNSVEVNKYVGGGIVEKI-GLKVDLTNPDITVHIEIREDEFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 161 LIKDRYEGLGGFPIGTQEDVISLISGGFDSGVSSYMLMRRGSRVHYCFFNLGGAAHEIGVRQVAHYLWNTFGRSHRVRFI 240
Cdd:TIGR00342 156 IITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 241 AIDFEPVVGEILEKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLISHD 320
Cdd:TIGR00342 236 VFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMD 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1785196388 321 KEHIIKVARQIGTEDFAKTMPEYCGVISK--SPTVKAVKEKIEAEENNFDF 369
Cdd:TIGR00342 316 KEEIIELAKEIGTYEISIEPHEDCCTIFKpkHPTTKAKPEKVEKLEEKLDF 366
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 175-369 4.46e-94

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 283.17  E-value: 4.46e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 175 GTQEDVISLISGGFDSGVSSYMLMRRGSRVHYCFF--NLGGAAHEIGVRQVAHYLWNTFGRSHRVRFIAIDFEPVVGEIL 252
Cdd:pfam02568   1 GTQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 253 EKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLISHDKEHIIKVARQIG 332
Cdd:pfam02568  81 EKAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1785196388 333 TEDFAKTMPEYCGVISKSPTVKAVKEKIEAEENNFDF 369
Cdd:pfam02568 161 TYEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKLDL 197
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 174-355 1.71e-82

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: 252.86  E-value: 1.71e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 174 IGTQEDVISLISGGFDSGVSSYMLMRRGSRVHYCFFNLGGAAHEIGVRQVAHYLWNTFGRSHRVRFIAIDF-EPVVGEIL 252
Cdd:cd01712     1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 253 EKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLISHDKEHIIKVARQIG 332
Cdd:cd01712    81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                         170       180
                  ....*....|....*....|....*
gi 1785196388 333 TEDFAKTMPE--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 3.49e-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: 187.00  E-value: 3.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 382 IDIRDIAVETTQEVAEVESVSALTAQDSILDIRSIDEQDDKPLMVEGVEIKSIPFYKLATQFGDLDRSRTWLLYCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 1785196388 462 SRLQALYLHEQGFTNVKVYRP 482
Cdd:TIGR04271  81 SRLQALYLKEQGFTNVKVYRP 101
PRK08349 PRK08349
hypothetical protein; Validated
 180-361 3.51e-29

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 113.68  E-value: 3.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 180 VISLISGGFDSGVSSYMLMRRGSRVHYCFFNLGGAAHEiGVRQVAHYLWNTFGRSHRvRFIAIDFEPVVGEILEKVDDGQ 259
Cdd:PRK08349    3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEE-KVRELVERLQELHGGKLK-DPVVVDAFEEQGPVFEKLRELK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 260 MG----VVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLISHDKEHIIKVARQIGTED 335
Cdd:PRK08349   81 KEkwtcIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTFE 160

                         170       180
                  ....*....|....*....|....*.
gi 1785196388 336 FAKTMPEYCGVISKSPTVKAVKEKIE 361
Cdd:PRK08349  161 ISIEPEPPCPFVPKYPVVRASLGEFE 186
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 86-161 4.51e-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: 75.77  E-value: 4.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388   86 SLHDIFEQTLAL---YQSQLEGKTFCVRAKRRGK-HEFTSHEVERYVGGGLNQHIASASVKLQQPDMTVHLEIDQERLLL 161
Cdd:smart00981   1 DLEDLYETALELirwEKIFKEGKTFAVRAKRRGKnHEFTSLEVKRAIGDKLLEKTGGRKVDLKNPDVVIRVELRKDKAYL 80
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 396-481 7.69e-11

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: 58.83  E-value: 7.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 396 AEVESVSALTAQDS-------ILDIRSIDEQDDKPLmvEGVeiKSIPFYKLATQFGDLDRSRTWLLYCERGVMSRLQALY 468
Cdd:COG0607     1 ASVKEISPAELAELlesedavLLDVREPEEFAAGHI--PGA--INIPLGELAERLDELPKDKPIVVYCASGGRSAQAAAL 76

                          90
                  ....*....|...
gi 1785196388 469 LHEQGFTNVKVYR 481
Cdd:COG0607    77 LRRAGYTNVYNLA 89
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 410-481 2.77e-05

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: 42.67  E-value: 2.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785196388 410 ILDIRSIDEqddkplmVEGVEIK---SIPFYKLATQFG--DLDRSRTWLLYCERGVMSRLQALYLHEQGFTNVKVYR 481
Cdd:cd00158    13 LLDVREPEE-------YAAGHIPgaiNIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 410-480 7.96e-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: 38.98  E-value: 7.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  410 ILDIRSIDEQD----------DKPLMVEGVEIKSIPFYKLATQFGDLDRSRTWLLYCERGVMSRLQALYLHEQGFTNVKV 479
Cdd:smart00450   7 LLDVRSPEEYEgghipgavniPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKNVYL 86


                   .
gi 1785196388  480 Y 480
Cdd:smart00450  87 L 87
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 410-481 1.23e-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: 38.23  E-value: 1.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785196388 410 ILDIRSIDEQDD------KPLMVEGVEIKSIPFYKLATQFGDLDRSRTWLLYCERGVMSRLQALYLHEQGFTNVKVYR 481
Cdd:pfam00581   8 LIDVRPPEEYAKghipgaVNVPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLD 85
 
Name Accession Description Interval E-value
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 3-380 5.31e-178

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: 503.85  E-value: 5.31e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388   3 FIVKlFPEITIKSQSvRLRFIKILSSNIRNVLKSVDEdIAVVRLWDHITVRTrKPELSAAVAEALTRIPGIHHVLSVEdR 82
Cdd:COG0301     4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVET-DGEDAEEAIERLKKVFGIVSFSPAV-E 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  83 TFTSLHDIFEQTLALYQSQLEGKTFCVRAKRRGKH-EFTSHEVERYVGGGLNQHIASASVKLQQPDMTVHLEIDQERLLL 161
Cdd:COG0301    79 VEKDLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 162 IKDRYEGLGGFPIGTQEDVISLISGGFDSGVSSYMLMRRGSRVHYCFFNLGG---AAHEIGVRQVAHYLwNTFGrSHRVR 238
Cdd:COG0301   159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYG-GHRVK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 239 FIAIDFEPVVGEILEKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLIS 318
Cdd:COG0301   237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785196388 319 HDKEHIIKVARQIGTEDFAKTMPEYCG--VISKSPTVKAVKEKIEAEENNFDF-AILERVISEAR 380
Cdd:COG0301   317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLeELLEEAVENAE 381
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 4-369 1.77e-147

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: 426.05  E-value: 1.77e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388   4 IVKLFPEITIKSQsVRLRFIKILSSNIRNVLKSVDEDIAVVRLWDHITVRTRKPELSAAVAEALTRIPGIHH--VLSVED 81
Cdd:TIGR00342   1 ILARYGEIGIKGK-NRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIVSfsPAFKCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  82 RTFTSLHDIFEqtlALYQSQLEGKTFCVRAKRRGKH-EFTSHEVERYVGGGLNQHIaSASVKLQQPDMTVHLEIDQERLL 160
Cdd:TIGR00342  80 LPFDEIHILLK---ALKQLRKEGKTFKVRTKRRGKDfPLNSVEVNKYVGGGIVEKI-GLKVDLTNPDITVHIEIREDEFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 161 LIKDRYEGLGGFPIGTQEDVISLISGGFDSGVSSYMLMRRGSRVHYCFFNLGGAAHEIGVRQVAHYLWNTFGRSHRVRFI 240
Cdd:TIGR00342 156 IITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 241 AIDFEPVVGEILEKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLISHD 320
Cdd:TIGR00342 236 VFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMD 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1785196388 321 KEHIIKVARQIGTEDFAKTMPEYCGVISK--SPTVKAVKEKIEAEENNFDF 369
Cdd:TIGR00342 316 KEEIIELAKEIGTYEISIEPHEDCCTIFKpkHPTTKAKPEKVEKLEEKLDF 366
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 175-369 4.46e-94

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 283.17  E-value: 4.46e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 175 GTQEDVISLISGGFDSGVSSYMLMRRGSRVHYCFF--NLGGAAHEIGVRQVAHYLWNTFGRSHRVRFIAIDFEPVVGEIL 252
Cdd:pfam02568   1 GTQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 253 EKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLISHDKEHIIKVARQIG 332
Cdd:pfam02568  81 EKAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1785196388 333 TEDFAKTMPEYCGVISKSPTVKAVKEKIEAEENNFDF 369
Cdd:pfam02568 161 TYEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKLDL 197
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 174-355 1.71e-82

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: 252.86  E-value: 1.71e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 174 IGTQEDVISLISGGFDSGVSSYMLMRRGSRVHYCFFNLGGAAHEIGVRQVAHYLWNTFGRSHRVRFIAIDF-EPVVGEIL 252
Cdd:cd01712     1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 253 EKVDDGQMGVVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLISHDKEHIIKVARQIG 332
Cdd:cd01712    81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                         170       180
                  ....*....|....*....|....*
gi 1785196388 333 TEDFAKTMPE--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 3.49e-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: 187.00  E-value: 3.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 382 IDIRDIAVETTQEVAEVESVSALTAQDSILDIRSIDEQDDKPLMVEGVEIKSIPFYKLATQFGDLDRSRTWLLYCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 1785196388 462 SRLQALYLHEQGFTNVKVYRP 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 5.13e-45

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: 154.91  E-value: 5.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388   2 KFIVKLFpEITIKSQsVRLRFIKILSSNIRNVLKSVdEDIAVVRLWDHITVRTRKpELSAAVAEALTRIPGIHHVLSVEd 81
Cdd:cd11716     1 KILVRYG-EIALKGK-NRKRFEKRLVKNIRRALKDL-PDVKVEREWGRIYVELNG-EDLEEVIERLKKVFGIVSFSPAV- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  82 RTFTSLHDIFEQTLALYQSQL-EGKTFCVRAKRRGK-HEFTSHEVERYVGGGLNQHIASASVKLQQPDMTVHLEIDQERL 159
Cdd:cd11716    76 EVEKDLEDIKEAALELLKEELkKGKTFKVRAKRADKsFPFTSMEINREVGAALLENTPDLKVDLKNPDVTIRVEIREDGA 155

                         170
                  ....*....|.
gi 1785196388 160 LLIKDRYEGLG 170
Cdd:cd11716   156 YVYTERIPGPG 166
PRK08349 PRK08349
hypothetical protein; Validated
 180-361 3.51e-29

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 113.68  E-value: 3.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 180 VISLISGGFDSGVSSYMLMRRGSRVHYCFFNLGGAAHEiGVRQVAHYLWNTFGRSHRvRFIAIDFEPVVGEILEKVDDGQ 259
Cdd:PRK08349    3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEE-KVRELVERLQELHGGKLK-DPVVVDAFEEQGPVFEKLRELK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 260 MG----VVLKRMMVRAASQIAERYGVQALVTGEALGQVSSQTLTNLRLIDNVTDTLVLRPLISHDKEHIIKVARQIGTED 335
Cdd:PRK08349   81 KEkwtcIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTFE 160

                         170       180
                  ....*....|....*....|....*.
gi 1785196388 336 FAKTMPEYCGVISKSPTVKAVKEKIE 361
Cdd:PRK08349  161 ISIEPEPPCPFVPKYPVVRASLGEFE 186
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 29-165 9.13e-18

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: 79.79  E-value: 9.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  29 NIRNVLKSVDEDIAVVRL-WDHITVRTRKP---ELSAAVAEALTRIPGIHHvLSVEDRTFTSLHDIFEQTLALYQSQL-- 102
Cdd:pfam02926   2 EIEELLKKGGINVEVVRSgRGRILVVLKGEnpeEDRELLKEALEKAPGIER-FPVAETCEADLEDILELAKEIIKDKFkk 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785196388 103 EGKTFCVRAKRRGK-HEFTSHEVERYVGGGLNQHIaSASVKLQQPDMTVHLEIDQERLLLIKDR 165
Cdd:pfam02926  81 EGETFAVRVKRRGKnHEFTSLEINREVGKAIVEKT-GLKVDLENPDIVVHVEIIKDKAYISIDR 143
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 86-161 4.51e-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: 75.77  E-value: 4.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388   86 SLHDIFEQTLAL---YQSQLEGKTFCVRAKRRGK-HEFTSHEVERYVGGGLNQHIASASVKLQQPDMTVHLEIDQERLLL 161
Cdd:smart00981   1 DLEDLYETALELirwEKIFKEGKTFAVRAKRRGKnHEFTSLEVKRAIGDKLLEKTGGRKVDLKNPDVVIRVELRKDKAYL 80
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 396-481 7.69e-11

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: 58.83  E-value: 7.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 396 AEVESVSALTAQDS-------ILDIRSIDEQDDKPLmvEGVeiKSIPFYKLATQFGDLDRSRTWLLYCERGVMSRLQALY 468
Cdd:COG0607     1 ASVKEISPAELAELlesedavLLDVREPEEFAAGHI--PGA--INIPLGELAERLDELPKDKPIVVYCASGGRSAQAAAL 76

                          90
                  ....*....|...
gi 1785196388 469 LHEQGFTNVKVYR 481
Cdd:COG0607    77 LRRAGYTNVYNLA 89
THUMP_SPOUT cd11718
THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are ...
 65-161 3.12e-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: 58.45  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  65 EALTRIPGIHHVLSVEDRTFTSLHDIFEQTLALYQSQLEGKTFCVRAKRRGKHEFTSHEVERYVGGGLnQHIASASVKLQ 144
Cdd:cd11718    48 ELALRVPEVERVIPVDAEVKADLDEIVRVAEEIAKHISEGETFAVRTTRRGKHDFTSIDVNVVLGAAV-KELTGAEVDLN 126

                          90
                  ....*....|....*..
gi 1785196388 145 QPDMTVHLEIDQERLLL 161
Cdd:cd11718   127 NPDKVVYVEIIGDRAYI 143
Tan1 COG1818
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure ...
 1-154 4.93e-10

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: 57.98  E-value: 4.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388   1 MKFIVKLFPeitiksqsvrlRFIKILSSNIRNVLKSVDEDI-AVVRLWDH-ITVRTR--KPELSAAVAEALTRIPGIHHV 76
Cdd:COG1818     1 MNLIVTTPR-----------GRERDAIEELRDILEEGDPNAeVVPTGFSGvLLVKTSldPYEAVEKLKEEPWEPRYILRV 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785196388  77 LSVEDRTFTSLHDIFEQTLALYQSQL-EGKTFCVRAKRRGKHEFTSHEVERYVGGGLNQhiaSASVKLQQPDMTVHLEI 154
Cdd:COG1818    70 IPVDRVVKTDLEEIVEAAKELAKKKIpEGETFAVRCEKRGKSKLSSREVIRAIGEAIKR---GAKVDLENPDWVVLVEI 145
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 103-161 3.10e-06

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: 46.80  E-value: 3.10e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785196388 103 EGKTFCVRAKRRGKHEFTSHEVERYVGGG----LNQHIASASVKLQQPDMTVHLEIDQERLLL 161
Cdd:cd11715    84 PDGTFAVRATRVGSKLFHSQFAALRVKDAivdrFREKGKRPSVDLDNPDVRIRVHLSKDRATL 146
THUMP_THUMPD1_like cd11717
THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins ...
 30-154 1.31e-05

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: 45.27  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  30 IRNVLKSVDEDIAVVrlwdhITVRTRKPELSAAVAEAL-----------TRIpgIHHVLSVEDRTFTSLHDIFEQTLALY 98
Cdd:cd11717    18 LYNLLQSVETGVKNV-----VFIKTRPPVDPVELVEKIfedaastkkkrTRF--IQRLIPIDVTCKASLEEIEKLAKELL 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  99 Q----SQLEGKTFCVRAKRRGKHEFTSHEVERYVGGGLNQHiasASVKLQQPDMTVHLEI 154
Cdd:cd11717    91 KkhfpTAEPPKTFAVECKSRNNNKLSRDEVIKAVAELVPEI---HKVDLKNPDKVILVEV 147
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 410-481 2.77e-05

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: 42.67  E-value: 2.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785196388 410 ILDIRSIDEqddkplmVEGVEIK---SIPFYKLATQFG--DLDRSRTWLLYCERGVMSRLQALYLHEQGFTNVKVYR 481
Cdd:cd00158    13 LLDVREPEE-------YAAGHIPgaiNIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 398-477 5.35e-04

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: 39.17  E-value: 5.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388 398 VESVSALTAQDS---ILDIRSIDEQDDKPLMVEG---VEIKSipfykLATQFGDLDRSRTWLLYCERGVMSRLQALYLHE 471
Cdd:cd01444     4 VDELAELLAAGEapvLLDVRDPASYAALPDHIPGaihLDEDS-----LDDWLGDLDRDRPVVVYCYHGNSSAQLAQALRE 78


                  ....*.
gi 1785196388 472 QGFTNV 477
Cdd:cd01444    79 AGFTDV 84
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 410-480 7.96e-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: 38.98  E-value: 7.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  410 ILDIRSIDEQD----------DKPLMVEGVEIKSIPFYKLATQFGDLDRSRTWLLYCERGVMSRLQALYLHEQGFTNVKV 479
Cdd:smart00450   7 LLDVRSPEEYEgghipgavniPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKNVYL 86


                   .
gi 1785196388  480 Y 480
Cdd:smart00450  87 L 87
THUMP cd11688
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ...
 24-158 1.07e-03

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: 39.39  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785196388  24 KILSSNIRNVLKSVDEDIAV-VRLWDHITVRTRKPElsaAVAEALTRIPGIHHVLSVEDRTFTSLHDIFEQTLALYQSQL 102
Cdd:cd11688    11 EILAAELYELLEVRGFDAEIqVVPHGRVHFKTDTDE---AVYQLVMWSRLISRIMPPLGECKADLEDLYETALEINEPEM 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1785196388 103 --EGKTFCVRAKRRGKHEFTSHEVERYVGGGLNQhIASASVKLQQPDMTVHLEIDQER 158
Cdd:cd11688    88 gnEGAKFAVRARRRNKTILNSQEIAMKVGDAIVD-AFNPEVDLDNPDIVVNVEVHKEI 144
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 410-481 1.23e-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: 38.23  E-value: 1.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785196388 410 ILDIRSIDEQDD------KPLMVEGVEIKSIPFYKLATQFGDLDRSRTWLLYCERGVMSRLQALYLHEQGFTNVKVYR 481
Cdd:pfam00581   8 LIDVRPPEEYAKghipgaVNVPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLD 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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