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Conserved domains on  [gi|1406955652|gb|AWV90505|]
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tRNA 4-thiouridine(8) synthase ThiI [Bradymonas sediminis]

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 ...
 14-393 1.96e-137

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: 401.39  E-value: 1.96e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  14 YRTIILRLsGELCIKSPQvRRRFQDRLLHNIRMALENAGitEYKLIRHWSRMDVEVND---PRAPEILARVYGIQGVIPA 90
Cdd:COG0301     1 YKVILVRY-GEIALKGKN-RKRFEKRLVKNIRAALKDLG--EVKVKREWGRIYVETDGedaEEAIERLKKVFGIVSFSPA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  91 YAYPWeTLEDIVEIGERLYREKVVGKTFAVRSKRVGNrgNIPFASMDLGRALGSSL--HAQSAGVDLDNPEVVVGVEVRE 168
Cdd:COG0301    77 VEVEK-DLEDIKEAALELAKEELKGKTFKVRAKRAGK--HFPFTSPELEREVGGALleNTPGLKVDLKNPDVTIRVEVRD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 169 NNVFFLDDELVGPGGLPMGSEGKAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNLGG---PAHERGVRDVTKMLcERWSn 245
Cdd:COG0301   154 DKAYVYTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYG- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 246 GYQAKFHIVDLRPIVADMKDNVSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPIL 325
Cdd:COG0301   232 GHRVKLYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVL 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1406955652 326 RPLVGLNKEDIIALARIIGTHDLSADVPEFCA--LDGGRPVTNGSAKRLDREEERVS-RKLLESLVEHRKT 393
Cdd:COG0301   312 RPLIGMDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDlEELLEEAVENAEV 382
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 417-495 3.14e-10

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: 57.28  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 417 EGAVMIDLRTSAARSKWKVPDAVEMDFDTAVGNVAYLPKEATYLLLCDVGLKSAFLADMMRKMGFK-AHSFRRGTRALRR 495
Cdd:COG0607    18 EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTnVYNLAGGIEAWKA 97
 
Name Accession Description Interval E-value
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 14-393 1.96e-137

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: 401.39  E-value: 1.96e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  14 YRTIILRLsGELCIKSPQvRRRFQDRLLHNIRMALENAGitEYKLIRHWSRMDVEVND---PRAPEILARVYGIQGVIPA 90
Cdd:COG0301     1 YKVILVRY-GEIALKGKN-RKRFEKRLVKNIRAALKDLG--EVKVKREWGRIYVETDGedaEEAIERLKKVFGIVSFSPA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  91 YAYPWeTLEDIVEIGERLYREKVVGKTFAVRSKRVGNrgNIPFASMDLGRALGSSL--HAQSAGVDLDNPEVVVGVEVRE 168
Cdd:COG0301    77 VEVEK-DLEDIKEAALELAKEELKGKTFKVRAKRAGK--HFPFTSPELEREVGGALleNTPGLKVDLKNPDVTIRVEVRD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 169 NNVFFLDDELVGPGGLPMGSEGKAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNLGG---PAHERGVRDVTKMLcERWSn 245
Cdd:COG0301   154 DKAYVYTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYG- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 246 GYQAKFHIVDLRPIVADMKDNVSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPIL 325
Cdd:COG0301   232 GHRVKLYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVL 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1406955652 326 RPLVGLNKEDIIALARIIGTHDLSADVPEFCA--LDGGRPVTNGSAKRLDREEERVS-RKLLESLVEHRKT 393
Cdd:COG0301   312 RPLIGMDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDlEELLEEAVENAEV 382
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 18-356 4.75e-81

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: 256.57  E-value: 4.75e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  18 ILRLSGELCIKSpQVRRRFQDRLLHNIRMALENAGITEYkLIRHWSRMDVEVNDPRAPEI----LARVYGIQGVIPAYAY 93
Cdd:TIGR00342   1 ILARYGEIGIKG-KNRLRFEKILKKNIKKALKKYEILRA-VVYHFDRIVVIAIDKEQRDAlldlLTKIPGIVSFSPAFKC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  94 PwETLEDIVEIGERLYREKVVGKTFAVRSKRVGNrgNIPFASMDLGRALGSSLHAQ-SAGVDLDNPEVVVGVEVRENNVF 172
Cdd:TIGR00342  79 D-LPFDEIHILLKALKQLRKEGKTFKVRTKRRGK--DFPLNSVEVNKYVGGGIVEKiGLKVDLTNPDITVHIEIREDEFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 173 FLDDELVGPGGLPMGSEGKAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNLGGPAHERGVRDVTKMLCERWSNGYQAKFH 252
Cdd:TIGR00342 156 IITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 253 IVDLRPIVADMKDNVSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPILRPLVGLN 332
Cdd:TIGR00342 236 VFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMD 315

                         330       340
                  ....*....|....*....|....
gi 1406955652 333 KEDIIALARIIGTHDLSADVPEFC 356
Cdd:TIGR00342 316 KEEIIELAKEIGTYEISIEPHEDC 339
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 186-367 1.52e-65

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: 209.72  E-value: 1.52e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 186 MGSEGKAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNLGGPAHERGVRDVTKMLCERWSNGYQAKFHIVDL-RPIVADMK 264
Cdd:cd01712     1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 265 DNVSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPILRPLVGLNKEDIIALARIIG 344
Cdd:cd01712    81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                         170       180
                  ....*....|....*....|....*
gi 1406955652 345 THDLSADVPE--FCALDGGRPVTNG 367
Cdd:cd01712   161 TYEISILPYEdcCCLFAPKNPVTKP 185
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 187-379 5.53e-54

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 180.32  E-value: 5.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 187 GSEGKAVALMSGGFDSAVAAYMMQKRGIDLDFIFF--NLGGPAHERGVRDVTKMLCERWSNGYQAKFHIVDLRPIVADMK 264
Cdd:pfam02568   1 GTQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 265 DNVSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPILRPLVGLNKEDIIALARIIG 344
Cdd:pfam02568  81 EKAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1406955652 345 THDLSADVPEFCALDGGRPVTNGSAKRLDREEERV 379
Cdd:pfam02568 161 TYEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKL 195
PRK08349 PRK08349
hypothetical protein; Validated
 191-385 2.63e-32

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 122.54  E-value: 2.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 191 KAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNlGGPAHERGVRDVTKMLcERWSNGYQAKFHIVDLR----PIVADMKDN 266
Cdd:PRK08349    2 KAVALLSSGIDSPVAIYLMLRRGVEVYPVHFR-QDEKKEEKVRELVERL-QELHGGKLKDPVVVDAFeeqgPVFEKLREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 267 VSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPILRPLVGLNKEDIIALARIIGTH 346
Cdd:PRK08349   80 KKEKWTCIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTF 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1406955652 347 DLSADVPEFCALDGGRPVTNGSAKRLDREEERVSRKLLE 385
Cdd:PRK08349  160 EISIEPEPPCPFVPKYPVVRASLGEFEKILEEVYVLGPE 198
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 417-495 3.14e-10

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: 57.28  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 417 EGAVMIDLRTSAARSKWKVPDAVEMDFDTAVGNVAYLPKEATYLLLCDVGLKSAFLADMMRKMGFK-AHSFRRGTRALRR 495
Cdd:COG0607    18 EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTnVYNLAGGIEAWKA 97
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 97-158 1.00e-08

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


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 52.28  E-value: 1.00e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1406955652   97 TLEDIVE---IGERLYREKVVGKTFAVRSKRVGNrgNIPFASMDLGRALGSSL--HAQSAGVDLDNP 158
Cdd:smart00981   1 DLEDLYEtalELIRWEKIFKEGKTFAVRAKRRGK--NHEFTSLEVKRAIGDKLleKTGGRKVDLKNP 65
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 417-483 6.04e-04

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 38.79  E-value: 6.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1406955652 417 EGAVMIDLRTSAARSKWKVPDAVEMDFDTAVGNVAYLPKEATYLLLCDVGLKSAFLADMMRKMGFKA 483
Cdd:cd01524    12 DGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFKV 78
 
Name Accession Description Interval E-value
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 14-393 1.96e-137

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: 401.39  E-value: 1.96e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  14 YRTIILRLsGELCIKSPQvRRRFQDRLLHNIRMALENAGitEYKLIRHWSRMDVEVND---PRAPEILARVYGIQGVIPA 90
Cdd:COG0301     1 YKVILVRY-GEIALKGKN-RKRFEKRLVKNIRAALKDLG--EVKVKREWGRIYVETDGedaEEAIERLKKVFGIVSFSPA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  91 YAYPWeTLEDIVEIGERLYREKVVGKTFAVRSKRVGNrgNIPFASMDLGRALGSSL--HAQSAGVDLDNPEVVVGVEVRE 168
Cdd:COG0301    77 VEVEK-DLEDIKEAALELAKEELKGKTFKVRAKRAGK--HFPFTSPELEREVGGALleNTPGLKVDLKNPDVTIRVEVRD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 169 NNVFFLDDELVGPGGLPMGSEGKAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNLGG---PAHERGVRDVTKMLcERWSn 245
Cdd:COG0301   154 DKAYVYTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYG- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 246 GYQAKFHIVDLRPIVADMKDNVSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPIL 325
Cdd:COG0301   232 GHRVKLYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVL 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1406955652 326 RPLVGLNKEDIIALARIIGTHDLSADVPEFCA--LDGGRPVTNGSAKRLDREEERVS-RKLLESLVEHRKT 393
Cdd:COG0301   312 RPLIGMDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDlEELLEEAVENAEV 382
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 18-356 4.75e-81

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: 256.57  E-value: 4.75e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  18 ILRLSGELCIKSpQVRRRFQDRLLHNIRMALENAGITEYkLIRHWSRMDVEVNDPRAPEI----LARVYGIQGVIPAYAY 93
Cdd:TIGR00342   1 ILARYGEIGIKG-KNRLRFEKILKKNIKKALKKYEILRA-VVYHFDRIVVIAIDKEQRDAlldlLTKIPGIVSFSPAFKC 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  94 PwETLEDIVEIGERLYREKVVGKTFAVRSKRVGNrgNIPFASMDLGRALGSSLHAQ-SAGVDLDNPEVVVGVEVRENNVF 172
Cdd:TIGR00342  79 D-LPFDEIHILLKALKQLRKEGKTFKVRTKRRGK--DFPLNSVEVNKYVGGGIVEKiGLKVDLTNPDITVHIEIREDEFL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 173 FLDDELVGPGGLPMGSEGKAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNLGGPAHERGVRDVTKMLCERWSNGYQAKFH 252
Cdd:TIGR00342 156 IITERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 253 IVDLRPIVADMKDNVSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPILRPLVGLN 332
Cdd:TIGR00342 236 VFDFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMD 315

                         330       340
                  ....*....|....*....|....
gi 1406955652 333 KEDIIALARIIGTHDLSADVPEFC 356
Cdd:TIGR00342 316 KEEIIELAKEIGTYEISIEPHEDC 339
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 186-367 1.52e-65

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: 209.72  E-value: 1.52e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 186 MGSEGKAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNLGGPAHERGVRDVTKMLCERWSNGYQAKFHIVDL-RPIVADMK 264
Cdd:cd01712     1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 265 DNVSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPILRPLVGLNKEDIIALARIIG 344
Cdd:cd01712    81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                         170       180
                  ....*....|....*....|....*
gi 1406955652 345 THDLSADVPE--FCALDGGRPVTNG 367
Cdd:cd01712   161 TYEISILPYEdcCCLFAPKNPVTKP 185
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 187-379 5.53e-54

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 180.32  E-value: 5.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 187 GSEGKAVALMSGGFDSAVAAYMMQKRGIDLDFIFF--NLGGPAHERGVRDVTKMLCERWSNGYQAKFHIVDLRPIVADMK 264
Cdd:pfam02568   1 GTQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 265 DNVSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPILRPLVGLNKEDIIALARIIG 344
Cdd:pfam02568  81 EKAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIG 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1406955652 345 THDLSADVPEFCALDGGRPVTNGSAKRLDREEERV 379
Cdd:pfam02568 161 TYEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKL 195
PRK08349 PRK08349
hypothetical protein; Validated
 191-385 2.63e-32

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 122.54  E-value: 2.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 191 KAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNlGGPAHERGVRDVTKMLcERWSNGYQAKFHIVDLR----PIVADMKDN 266
Cdd:PRK08349    2 KAVALLSSGIDSPVAIYLMLRRGVEVYPVHFR-QDEKKEEKVRELVERL-QELHGGKLKDPVVVDAFeeqgPVFEKLREL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 267 VSGSYWQLLLKRLMMRASHMICEEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLTPILRPLVGLNKEDIIALARIIGTH 346
Cdd:PRK08349   80 KKEKWTCIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTF 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1406955652 347 DLSADVPEFCALDGGRPVTNGSAKRLDREEERVSRKLLE 385
Cdd:PRK08349  160 EISIEPEPPCPFVPKYPVVRASLGEFEKILEEVYVLGPE 198
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 17-162 2.58e-31

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: 118.70  E-value: 2.58e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  17 IILRLsGELCIKSpQVRRRFQDRLLHNIRMALEnaGITEYKLIRHWSRMDVEVND---PRAPEILARVYGIQGVIPAYAY 93
Cdd:cd11716     2 ILVRY-GEIALKG-KNRKRFEKRLVKNIRRALK--DLPDVKVEREWGRIYVELNGedlEEVIERLKKVFGIVSFSPAVEV 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1406955652  94 PwETLEDIVEIGERLYREKVV-GKTFAVRSKRVGNRgnIPFASMDLGRALGSSL--HAQSAGVDLDNPEVVV 162
Cdd:cd11716    78 E-KDLEDIKEAALELLKEELKkGKTFKVRAKRADKS--FPFTSMEINREVGAALleNTPDLKVDLKNPDVTI 146
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 191-344 5.82e-11

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: 61.86  E-value: 5.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 191 KAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNLGGPaHERGVRDVTKMLCERwsngYQAKFHIVDLRPI--------VAD 262
Cdd:cd01995     2 KAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQR-HAKEELEAAKLIAKL----LGIEHKVIDLSFLgelggsslTDE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 263 MKDNVSGSYWQLLLKR--------LMMRASHMICEEEGYPAMITGESAGQVSS------------QTLMNLAaiqtsVLT 322
Cdd:cd01995    77 GEEVPDGEYDEESIPStwvpnrnlIFLSIAAAYAESLGASAIVIGVNAEDASGypdcrpefveamNSALNLG-----TAT 151

                         170       180
                  ....*....|....*....|....
gi 1406955652 323 PI--LRPLVGLNKEDIIALARIIG 344
Cdd:cd01995   152 GVkvVAPLIGLSKAEIVKLGVELG 175
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 417-495 3.14e-10

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: 57.28  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 417 EGAVMIDLRTSAARSKWKVPDAVEMDFDTAVGNVAYLPKEATYLLLCDVGLKSAFLADMMRKMGFK-AHSFRRGTRALRR 495
Cdd:COG0607    18 EDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGYTnVYNLAGGIEAWKA 97
Tan1 COG1818
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure ...
 70-158 5.68e-09

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: 55.28  E-value: 5.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  70 NDPRAPEILaRVYGIQGVIPAYaypwetLEDIVEIGERLYREKV-VGKTFAVRSKRvgnRGNIPFASMDLGRALGSSLHa 148
Cdd:COG1818    59 EPWEPRYIL-RVIPVDRVVKTD------LEEIVEAAKELAKKKIpEGETFAVRCEK---RGKSKLSSREVIRAIGEAIK- 127

                          90
                  ....*....|
gi 1406955652 149 QSAGVDLDNP 158
Cdd:COG1818   128 RGAKVDLENP 137
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 97-158 1.00e-08

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


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 52.28  E-value: 1.00e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1406955652   97 TLEDIVE---IGERLYREKVVGKTFAVRSKRVGNrgNIPFASMDLGRALGSSL--HAQSAGVDLDNP 158
Cdd:smart00981   1 DLEDLYEtalELIRWEKIFKEGKTFAVRAKRRGK--NHEFTSLEVKRAIGDKLleKTGGRKVDLKNP 65
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 43-158 3.79e-08

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: 52.44  E-value: 3.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  43 NIRMALENAGITEYKLIRHWSRMDVEVNDP-------RAPEILARVYGIQgVIPAYAYPWETLEDIVEIGERLYREKV-- 113
Cdd:pfam02926   2 EIEELLKKGGINVEVVRSGRGRILVVLKGEnpeedreLLKEALEKAPGIE-RFPVAETCEADLEDILELAKEIIKDKFkk 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1406955652 114 VGKTFAVRSKRVGnrGNIPFASMDLGRALGSSLHAQ-SAGVDLDNP 158
Cdd:pfam02926  81 EGETFAVRVKRRG--KNHEFTSLEINREVGKAIVEKtGLKVDLENP 124
THUMP_SPOUT cd11718
THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are ...
 67-158 6.59e-08

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: 51.51  E-value: 6.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652  67 VEVNDPRAPEILARVYGIQGVIPAYAYPWETLEDIVEIGERLYREKVVGKTFAVRSKRvgnRGNIPFASMDLGRALGSSL 146
Cdd:cd11718    39 VESDEDKKDELALRVPEVERVIPVDAEVKADLDEIVRVAEEIAKHISEGETFAVRTTR---RGKHDFTSIDVNVVLGAAV 115

                          90
                  ....*....|...
gi 1406955652 147 H-AQSAGVDLDNP 158
Cdd:cd11718   116 KeLTGAEVDLNNP 128
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 193-353 2.19e-06

tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 48.09  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 193 VALmSGGFDSAVAAYMMQKRGIDLDFIFFNLG-GPAHERgVRDVTKMLCERwsngYQAKFHIVDLRPIVADMKDNVSG-- 269
Cdd:cd01993    13 VAV-SGGKDSLALLAVLKKLGYNVEALYINLGiGEYSEK-SEEVVKKLAEK----LNLPLHVVDLKEEYGLGIPELAKks 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 270 -----SYWQLLLKRLMMRASHmiceEEGYPAMITGESAGQVSSQTLMNLAAIQTSVLT---PIL-----------RPLVG 330
Cdd:cd01993    87 rrppcSVCGLVKRYIMNKFAV----ENGFDVVATGHNLDDEAAFLLGNILNWNEEYLAkqgPFLlpehgglvtrvKPLYE 162

                         170       180
                  ....*....|....*....|...
gi 1406955652 331 LNKEDIIALARIIGTHDLSADVP 353
Cdd:cd01993   163 ITEEEIALYALLNGIPYLEEECP 185
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 191-340 2.21e-05

7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440368 [Multi-domain]  Cd Length: 223  Bit Score: 45.54  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 191 KAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNLgGPAHERGvRDVTKMLCERwsngYQAK-FHIVDLRPI--------VA 261
Cdd:COG0603     4 KAVVLLSGGLDSTTCLAWALARGYEVYALSFDY-GQRHRKE-LEAARRIAKA----LGVGeHKVIDLDFLgeiggsalTD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 262 DMKDNVSGSYWQ------------LLLkrLMMRAShmICEEEGYPAMITGESAGQVSS------------QTLMNLAaiq 317
Cdd:COG0603    78 DSIEVPEGHYAEegipstyvpgrnLIF--LSIAAA--YAEALGAEDIFIGVNATDYSGypdcrpefieafNAALNLG--- 150

                         170       180
                  ....*....|....*....|...
gi 1406955652 318 TSVLTPILRPLVGLNKEDIIALA 340
Cdd:COG0603   151 TKRPVRIHTPLMHLSKAEIVKLG 173
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 191-340 1.31e-04

Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.


Pssm-ID: 428982 [Multi-domain]  Cd Length: 210  Bit Score: 43.37  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 191 KAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNLgGPAHERGVrDVTKMLCErwsnGYQAKFHIVDLRPI----------- 259
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDY-GQRHRKEL-ECAKKIAK----ALGVEHKILDLDFLkqiggsaltdd 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 260 VADMKDN-----------VSG------SYWQLLLKRLMMRASHM-ICEEE--GYP--------AMitgesagqvssQTLM 311
Cdd:pfam06508  75 SIEVPKAeleseeipntyVPGrnliflSIAASLAEALGAEAIFIgVNEEDysGYPdcrpefvkAF-----------NVAL 143

                         170       180
                  ....*....|....*....|....*....
gi 1406955652 312 NLAAIQTSVltPILRPLVGLNKEDIIALA 340
Cdd:pfam06508 144 NLGTMGKPI--EIHTPLMDLSKAEIVKLG 170
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 191-257 1.74e-04

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family 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: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 43.65  E-value: 1.74e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1406955652 191 KAVALMSGGFDSAVAAYMMQKRGIDLDFIFFNL--------GGPAHERGVRDVtKMLCERwsngYQAKFHIVDLR 257
Cdd:cd01998     1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNwddednekGGCCSEEDIEDA-RRVADQ----LGIPLYVVDFS 70
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 192-341 1.91e-04

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 42.90  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 192 AVALmSGGFDSAVAAYMM----QKRGIDLDFIFFNLGGPAHERGVRDVTKMLCERWsngyQAKFHIVDLRPIVADMKDNV 267
Cdd:COG0037    19 LVAV-SGGKDSLALLHLLaklrRRLGFELVAVHVDHGLREESDEDAEFVAELCEEL----GIPLHVVRVDVPAIAKKEGK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 268 SgsywqlllkrLMMRASHM-------ICEEEGYPAMITG-------ESagqvssqTLMNL---------AAIQTS--VLT 322
Cdd:COG0037    94 S----------PEAAARRArygalyeLARELGADKIATGhhlddqaET-------FLLNLlrgsglaglAGMPPSrgGGV 156

                         170
                  ....*....|....*....
gi 1406955652 323 PILRPLVGLNKEDIIALAR 341
Cdd:COG0037   157 RLIRPLLYVSRKEIEAYAK 175
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 191-257 4.82e-04

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 41.47  E-value: 4.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1406955652 191 KAVALMSGGFDSAVAAYMMQKRGIDLDFIF-------FNLGGPAH---ERGVRDVtKMLCERWSngyqAKFHIVDLR 257
Cdd:pfam03054   2 KVVVAMSGGVDSSVAAYLLKEQGHNVIGVFmknwdeeQSLDEEGKccsEEDLADA-QRVCEQLG----IPLYVVNFE 73
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 417-483 6.04e-04

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 38.79  E-value: 6.04e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1406955652 417 EGAVMIDLRTSAARSKWKVPDAVEMDFDTAVGNVAYLPKEATYLLLCDVGLKSAFLADMMRKMGFKA 483
Cdd:cd01524    12 DGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFKV 78
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 191-267 7.84e-04

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 41.59  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1406955652 191 KAVALMSGGFDSAVAAYMMQKRGIDLDFIF---------FNLGGPAHERGVRDVtKMLCERwsngYQAKFHIVDLRpivA 261
Cdd:PRK00143    2 RVVVGMSGGVDSSVAAALLKEQGYEVIGVFmklwddddeTGKGGCCAEEDIADA-RRVADK----LGIPHYVVDFE---K 73


                  ....*.
gi 1406955652 262 DMKDNV 267
Cdd:PRK00143   74 EFWDRV 79
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 191-213 4.46e-03

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 39.27  E-value: 4.46e-03
                          10        20
                  ....*....|....*....|...
gi 1406955652 191 KAVALMSGGFDSAVAAYMMQKRG 213
Cdd:COG0482     2 RVVVGMSGGVDSSVAAALLKEQG 24
 
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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