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MULTISPECIES: tRNA uracil 4-sulfurtransferase ThiI [Klebsiella]

Protein Classification

Graphical summary

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List of domain hits

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

Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


:

Pssm-ID: 440070 [Multi-domain]  Cd Length: 382  Bit Score: 520.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884   3 FIIKlFPEITIKSQSvRLRFIKILTGNIRNVLKNYDEtLAVVRHWDHIEVRAKDENQRPVIrDALTRIPGIHHILEVEDV 82
Cdd:COG0301    4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGEDAEEAI-ERLKKVFGIVSFSPAVEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  83 PFTsLHNIFEQTLPLWREQLEGKSFCVRVKRRGKH-EFTSIEVERYVGGGLNQHIESARVKLTDPDVTVNLEIENDRLLL 161
Cdd:COG0301   80 EKD-LEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 162 VKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG---AAHEIGVRQVAHYLwNRFGSsHRVR 238
Cdd:COG0301  159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYGG-HRVK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 239 FVAINFEPVVGEILEKVEDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLIS 318
Cdd:COG0301  237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505180884 319 HDKEHIINLAREIGTEDFARTMPEYCG--VISKSPTIKAVKAKIEAEEENFDFS-ILDKVVEEA 379
Cdd:COG0301  317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLEeLLEEAVENA 380
ThiI_C_thiazole TIGR04271
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ...
 382-482 5.23e-59

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: 189.31  E-value: 5.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  382 IDIRDIAQQTQQDVVEVETVSGFSANDVILDIRSVDEQDDKPLKVEGVDVVSLPFYKLSTQFGNLDQSKTWLLWCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 505180884  462 SRLQALYLREQGFTNVKVYRP 482
Cdd:TIGR04271  81 SRLQALYLKEQGFTNVKVYRP 101
 
Name Accession Description Interval E-value
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 3-379 0e+00

Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440070 [Multi-domain]  Cd Length: 382  Bit Score: 520.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884   3 FIIKlFPEITIKSQSvRLRFIKILTGNIRNVLKNYDEtLAVVRHWDHIEVRAKDENQRPVIrDALTRIPGIHHILEVEDV 82
Cdd:COG0301    4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGEDAEEAI-ERLKKVFGIVSFSPAVEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  83 PFTsLHNIFEQTLPLWREQLEGKSFCVRVKRRGKH-EFTSIEVERYVGGGLNQHIESARVKLTDPDVTVNLEIENDRLLL 161
Cdd:COG0301   80 EKD-LEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 162 VKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG---AAHEIGVRQVAHYLwNRFGSsHRVR 238
Cdd:COG0301  159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYGG-HRVK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 239 FVAINFEPVVGEILEKVEDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLIS 318
Cdd:COG0301  237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505180884 319 HDKEHIINLAREIGTEDFARTMPEYCG--VISKSPTIKAVKAKIEAEEENFDFS-ILDKVVEEA 379
Cdd:COG0301  317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLEeLLEEAVENA 380
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 4-376 2.91e-168

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: 478.83  E-value: 2.91e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884    4 IIKLFPEITIKSQsVRLRFIKILTGNIRNVLKNYDETLAVVRHWDHIEVRAKDENQRPVIRDALTRIPGIHH--ILEVED 81
Cdd:TIGR00342   1 ILARYGEIGIKGK-NRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIVSfsPAFKCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884   82 VPFTSLHnIFEQTLPLWREqlEGKSFCVRVKRRGKH-EFTSIEVERYVGGGLNQHIEsARVKLTDPDVTVNLEIENDRLL 160
Cdd:TIGR00342  80 LPFDEIH-ILLKALKQLRK--EGKTFKVRTKRRGKDfPLNSVEVNKYVGGGIVEKIG-LKVDLTNPDITVHIEIREDEFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  161 LVKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFV 240
Cdd:TIGR00342 156 IITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  241 AINFEPVVGEILEKVEDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISHD 320
Cdd:TIGR00342 236 VFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMD 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 505180884  321 KEHIINLAREIGTEDFARTMPEYCGVISK--SPTIKAVKAKIEAEEENFDFSilDKVV 376
Cdd:TIGR00342 316 KEEIIELAKEIGTYEISIEPHEDCCTIFKpkHPTTKAKPEKVEKLEEKLDFS--RKLV 371
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 175-369 8.91e-102

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 302.81  E-value: 8.91e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  175 GTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFF--NLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEIL 252
Cdd:pfam02568   1 GTQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  253 EKVEDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISHDKEHIINLAREIG 332
Cdd:pfam02568  81 EKAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 505180884  333 TEDFARTMPEYCGVISKSPTIKAVKAKIEAEEENFDF 369
Cdd:pfam02568 161 TYEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKLDL 197
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 174-355 4.17e-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: 262.10  E-value: 4.17e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 174 IGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINF-EPVVGEIL 252
Cdd:cd01712    1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 253 EKVEDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISHDKEHIINLAREIG 332
Cdd:cd01712   81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                        170       180
                 ....*....|....*....|....*
gi 505180884 333 TEDFARTMPE--YCGVISKSPTIKA 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 5.23e-59

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: 189.31  E-value: 5.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  382 IDIRDIAQQTQQDVVEVETVSGFSANDVILDIRSVDEQDDKPLKVEGVDVVSLPFYKLSTQFGNLDQSKTWLLWCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 505180884  462 SRLQALYLREQGFTNVKVYRP 482
Cdd:TIGR04271  81 SRLQALYLKEQGFTNVKVYRP 101
PRK08349 PRK08349
hypothetical protein; Validated
 180-355 7.15e-27

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 107.13  E-value: 7.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 180 VLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEiGVRQVAHYLWNRFGSSHRVRFVAINFE---PVVGEILEKVE 256
Cdd:PRK08349   3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEE-KVRELVERLQELHGGKLKDPVVVDAFEeqgPVFEKLRELKK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 257 DGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISHDKEHIINLAREIGTEDF 336
Cdd:PRK08349  82 EKWTCIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTFEI 161

                        170
                 ....*....|....*....
gi 505180884 337 ARTMPEYCGVISKSPTIKA 355
Cdd:PRK08349 162 SIEPEPPCPFVPKYPVVRA 180
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 86-161 4.26e-18

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: 78.86  E-value: 4.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884    86 SLHNIFEQTLPLWREQ---LEGKSFCVRVKRRGK-HEFTSIEVERYVGGGLNQHIESARVKLTDPDVTVNLEIENDRLLL 161
Cdd:smart00981   1 DLEDLYETALELIRWEkifKEGKTFAVRAKRRGKnHEFTSLEVKRAIGDKLLEKTGGRKVDLKNPDVVIRVELRKDKAYL 80
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 405-481 1.11e-08

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


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 52.66  E-value: 1.11e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505180884 405 SANDVILDIRSVDEQDDKPLKvegvDVVSLPFYKLSTQFGNLDQSKTWLLWCERGVMSRLQALYLREQGFTNVKVYR 481
Cdd:COG0607   17 SEDAVLLDVREPEEFAAGHIP----GAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLA 89
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 409-481 1.02e-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: 41.13  E-value: 1.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505180884 409 VILDIRSVDEQDDKPLKvegvDVVSLPFYKLSTQFG--NLDQSKTWLLWCERGVMSRLQALYLREQGFTNVKVYR 481
Cdd:cd00158   12 VLLDVREPEEYAAGHIP----GAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
 
Name Accession Description Interval E-value
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 3-379 0e+00

Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440070 [Multi-domain]  Cd Length: 382  Bit Score: 520.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884   3 FIIKlFPEITIKSQSvRLRFIKILTGNIRNVLKNYDEtLAVVRHWDHIEVRAKDENQRPVIrDALTRIPGIHHILEVEDV 82
Cdd:COG0301    4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGEDAEEAI-ERLKKVFGIVSFSPAVEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  83 PFTsLHNIFEQTLPLWREQLEGKSFCVRVKRRGKH-EFTSIEVERYVGGGLNQHIESARVKLTDPDVTVNLEIENDRLLL 161
Cdd:COG0301   80 EKD-LEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 162 VKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG---AAHEIGVRQVAHYLwNRFGSsHRVR 238
Cdd:COG0301  159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYGG-HRVK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 239 FVAINFEPVVGEILEKVEDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLIS 318
Cdd:COG0301  237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505180884 319 HDKEHIINLAREIGTEDFARTMPEYCG--VISKSPTIKAVKAKIEAEEENFDFS-ILDKVVEEA 379
Cdd:COG0301  317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLEeLLEEAVENA 380
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 4-376 2.91e-168

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: 478.83  E-value: 2.91e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884    4 IIKLFPEITIKSQsVRLRFIKILTGNIRNVLKNYDETLAVVRHWDHIEVRAKDENQRPVIRDALTRIPGIHH--ILEVED 81
Cdd:TIGR00342   1 ILARYGEIGIKGK-NRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIVSfsPAFKCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884   82 VPFTSLHnIFEQTLPLWREqlEGKSFCVRVKRRGKH-EFTSIEVERYVGGGLNQHIEsARVKLTDPDVTVNLEIENDRLL 160
Cdd:TIGR00342  80 LPFDEIH-ILLKALKQLRK--EGKTFKVRTKRRGKDfPLNSVEVNKYVGGGIVEKIG-LKVDLTNPDITVHIEIREDEFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  161 LVKGRYEGIGGFPIGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFV 240
Cdd:TIGR00342 156 IITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  241 AINFEPVVGEILEKVEDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISHD 320
Cdd:TIGR00342 236 VFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMD 315

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 505180884  321 KEHIINLAREIGTEDFARTMPEYCGVISK--SPTIKAVKAKIEAEEENFDFSilDKVV 376
Cdd:TIGR00342 316 KEEIIELAKEIGTYEISIEPHEDCCTIFKpkHPTTKAKPEKVEKLEEKLDFS--RKLV 371
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 175-369 8.91e-102

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 302.81  E-value: 8.91e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  175 GTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFF--NLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINFEPVVGEIL 252
Cdd:pfam02568   1 GTQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  253 EKVEDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISHDKEHIINLAREIG 332
Cdd:pfam02568  81 EKAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 505180884  333 TEDFARTMPEYCGVISKSPTIKAVKAKIEAEEENFDF 369
Cdd:pfam02568 161 TYEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKLDL 197
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 174-355 4.17e-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: 262.10  E-value: 4.17e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 174 IGTQEDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEIGVRQVAHYLWNRFGSSHRVRFVAINF-EPVVGEIL 252
Cdd:cd01712    1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 253 EKVEDGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISHDKEHIINLAREIG 332
Cdd:cd01712   81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                        170       180
                 ....*....|....*....|....*
gi 505180884 333 TEDFARTMPE--YCGVISKSPTIKA 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 5.23e-59

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: 189.31  E-value: 5.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  382 IDIRDIAQQTQQDVVEVETVSGFSANDVILDIRSVDEQDDKPLKVEGVDVVSLPFYKLSTQFGNLDQSKTWLLWCERGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 505180884  462 SRLQALYLREQGFTNVKVYRP 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 3.88e-49

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: 165.70  E-value: 3.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884   2 KFIIKLFpEITIKSQsVRLRFIKILTGNIRNVLKNYDEtLAVVRHWDHIEVRAKDENQRPVIrDALTRIPGIHHILEVED 81
Cdd:cd11716    1 KILVRYG-EIALKGK-NRKRFEKRLVKNIRRALKDLPD-VKVEREWGRIYVELNGEDLEEVI-ERLKKVFGIVSFSPAVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  82 VPFTsLHNIFEQTLPLWREQL-EGKSFCVRVKRRGK-HEFTSIEVERYVGGGLNQHIESARVKLTDPDVTVNLEIENDRL 159
Cdd:cd11716   77 VEKD-LEDIKEAALELLKEELkKGKTFKVRAKRADKsFPFTSMEINREVGAALLENTPDLKVDLKNPDVTIRVEIREDGA 155

                        170
                 ....*....|.
gi 505180884 160 LLVKGRYEGIG 170
Cdd:cd11716  156 YVYTERIPGPG 166
PRK08349 PRK08349
hypothetical protein; Validated
 180-355 7.15e-27

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 107.13  E-value: 7.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 180 VLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGGAAHEiGVRQVAHYLWNRFGSSHRVRFVAINFE---PVVGEILEKVE 256
Cdd:PRK08349   3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEE-KVRELVERLQELHGGKLKDPVVVDAFEeqgPVFEKLRELKK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 257 DGQMGVVLKRMMVRAASKVAERYGVQALVTGEALGQVSSQTLTNLRLIDNVSDTLILRPLISHDKEHIINLAREIGTEDF 336
Cdd:PRK08349  82 EKWTCIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTFEI 161

                        170
                 ....*....|....*....
gi 505180884 337 ARTMPEYCGVISKSPTIKA 355
Cdd:PRK08349 162 SIEPEPPCPFVPKYPVVRA 180
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 86-161 4.26e-18

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: 78.86  E-value: 4.26e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884    86 SLHNIFEQTLPLWREQ---LEGKSFCVRVKRRGK-HEFTSIEVERYVGGGLNQHIESARVKLTDPDVTVNLEIENDRLLL 161
Cdd:smart00981   1 DLEDLYETALELIRWEkifKEGKTFAVRAKRRGKnHEFTSLEVKRAIGDKLLEKTGGRKVDLKNPDVVIRVELRKDKAYL 80
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 28-161 4.64e-17

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: 77.86  E-value: 4.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884   28 GNIRNVLKNYDETLAVVR-HWDHIEVRAKDENQRPV---IRDALTRIPGIHHILeVEDVPFTSLHNIFEQTLPLWREQL- 102
Cdd:pfam02926   1 KEIEELLKKGGINVEVVRsGRGRILVVLKGENPEEDrelLKEALEKAPGIERFP-VAETCEADLEDILELAKEIIKDKFk 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505180884  103 -EGKSFCVRVKRRGK-HEFTSIEVERYVGGGLNQHIeSARVKLTDPDVTVNLEIENDRLLL 161
Cdd:pfam02926  80 kEGETFAVRVKRRGKnHEFTSLEINREVGKAIVEKT-GLKVDLENPDIVVHVEIIKDKAYI 139
Tan1 COG1818
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure ...
 63-154 1.21e-12

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: 65.68  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  63 IRDALTRIPGIHHILEVEDVPFTSLHNIFEQTLPLWREQL-EGKSFCVRVKRRGKHEFTSIEVERYVGGGLNqhiESARV 141
Cdd:COG1818   56 LKEEPWEPRYILRVIPVDRVVKTDLEEIVEAAKELAKKKIpEGETFAVRCEKRGKSKLSSREVIRAIGEAIK---RGAKV 132

                         90
                 ....*....|...
gi 505180884 142 KLTDPDVTVNLEI 154
Cdd:COG1818  133 DLENPDWVVLVEI 145
THUMP_SPOUT cd11718
THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are ...
 69-161 5.20e-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: 57.68  E-value: 5.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  69 RIPGIHHILEVEDVPFTSLHNIFEQTLPLWREQLEGKSFCVRVKRRGKHEFTSIEVERYVGGGLnQHIESARVKLTDPDV 148
Cdd:cd11718   52 RVPEVERVIPVDAEVKADLDEIVRVAEEIAKHISEGETFAVRTTRRGKHDFTSIDVNVVLGAAV-KELTGAEVDLNNPDK 130

                         90
                 ....*....|...
gi 505180884 149 TVNLEIENDRLLL 161
Cdd:cd11718  131 VVYVEIIGDRAYI 143
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 405-481 1.11e-08

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


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 52.66  E-value: 1.11e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505180884 405 SANDVILDIRSVDEQDDKPLKvegvDVVSLPFYKLSTQFGNLDQSKTWLLWCERGVMSRLQALYLREQGFTNVKVYR 481
Cdd:COG0607   17 SEDAVLLDVREPEEFAAGHIP----GAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLA 89
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 73-161 5.67e-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: 51.81  E-value: 5.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  73 IHHIL-EVEDVPFTSLHNIFEQT--LPLWREQLEGKSFCVRVKRRGKHEFTSIEVERYVGGGLNQHIESA----RVKLTD 145
Cdd:cd11715   51 AHRVLlLLAEFEAEDFDDLYELAkaIDWEDYLDPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREKgkrpSVDLDN 130

                         90
                 ....*....|....*.
gi 505180884 146 PDVTVNLEIENDRLLL 161
Cdd:cd11715  131 PDVRIRVHLSKDRATL 146
THUMP_THUMPD1_like cd11717
THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins ...
 73-154 9.11e-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: 42.96  E-value: 9.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884  73 IHHILEVEDVPFTSLHNIFEQTLPLWRE----QLEGKSFCVRVKRRGKHEFTSIEVERYVGGGLNQHiesARVKLTDPDV 148
Cdd:cd11717   65 IQRLIPIDVTCKASLEEIEKLAKELLKKhfptAEPPKTFAVECKSRNNNKLSRDEVIKAVAELVPEI---HKVDLKNPDK 141


                 ....*.
gi 505180884 149 TVNLEI 154
Cdd:cd11717  142 VILVEV 147
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 409-481 1.02e-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: 41.13  E-value: 1.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505180884 409 VILDIRSVDEQDDKPLKvegvDVVSLPFYKLSTQFG--NLDQSKTWLLWCERGVMSRLQALYLREQGFTNVKVYR 481
Cdd:cd00158   12 VLLDVREPEEYAAGHIP----GAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 178-346 1.45e-03

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: 39.90  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 178 EDVLSLISGGFDSGVSSYMLMRRGCRVHYCFFNLGG-AAHEIGV--RQVAHYLwnrfGSSHRV---RFVAINFEPVVGEI 251
Cdd:cd01995    1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQrHAKEELEaaKLIAKLL----GIEHKVidlSFLGELGGSSLTDE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180884 252 LEKVEDGQMG-------VVLKR--MMVRAASKVAERYGVQALVTG-----------------EALGQVSSQ-TLTNLRli 304
Cdd:cd01995   77 GEEVPDGEYDeesipstWVPNRnlIFLSIAAAYAESLGASAIVIGvnaedasgypdcrpefvEAMNSALNLgTATGVK-- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 505180884 305 dnvsdtlILRPLISHDKEHIINLAREIGtEDFARTMPEY------CGV 346
Cdd:cd01995  155 -------VVAPLIGLSKAEIVKLGVELG-VPLELTWSCYrggekhCGR 194
THUMP cd11688
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ...
 103-158 4.65e-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: 37.47  E-value: 4.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505180884 103 EGKSFCVRVKRRGKHEFTSIEVERYVGGGLNQhIESARVKLTDPDVTVNLEIENDR 158
Cdd:cd11688   90 EGAKFAVRARRRNKTILNSQEIAMKVGDAIVD-AFNPEVDLDNPDIVVNVEVHKEI 144
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 409-477 5.61e-03

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


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 36.08  E-value: 5.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505180884 409 VILDIRSVDEQDDKPLKVEGVDVVSLPfyKLSTQFGNLDQSKTWLLWCERGVMSRLQALYLREQGFTNV 477
Cdd:cd01444   18 VLLDVRDPASYAALPDHIPGAIHLDED--SLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAGFTDV 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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