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Conserved domains on  [gi|117561619|gb|ABK38567|]
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thiamine biosynthesis/tRNA modification protein ThiI [Aeromonas hydrophila subsp. hydrophila ATCC 7966]

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 ...
 3-381 8.85e-179

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: 505.78  E-value: 8.85e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619   3 FIIKlFPEITIKSKSvRQRFIKILQGNIRNVLRRFDDdARVRMDWDKLIVSSRNDQfREQAIEALACIPGIQAFLEVQAS 82
Cdd:COG0301    4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGED-AEEAIERLKKVFGIVSFSPAVEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  83 KFtDLHDIFEQVKAVWGDQLEGKTFCVRAKRHGKH-EFSSLEVERYVGGGLNQHCVSNGVRLKNPDVKINLEIDGEELFI 161
Cdd:COG0301   80 EK-DLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 162 VSAIHQGLSGMPIATQEDVLSLISGGFDSGVASFQFIKRGCRVHYCFFNLGG---AAHEIGVKQVAYHLwNRFGSsHRVR 238
Cdd:COG0301  159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYGG-HRVK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 239 FTAVDFEPVVAEILEKIDNGQMGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLIT 318
Cdd:COG0301  237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117561619 319 WDKPDIISEARRIGTLEFAETMPEYCG--VISKKPTVKAELSRIEAEEENFDF-AILDKVVAEARY 381
Cdd:COG0301  317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLeELLEEAVENAEV 382
ThiI_C_thiazole TIGR04271
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ...
 382-482 8.31e-54

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: 175.83  E-value: 8.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  382 LDIRRIGEETAAEVQEVETTAESGDNEVILDIRSMDEHNEKPLLVEGREVMHIPFFKLTTAFGDLPKEKTYLLYCDRGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 117561619  462 SKLQALYLKEKGFANVKVYRP 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 ...
 3-381 8.85e-179

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: 505.78  E-value: 8.85e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619   3 FIIKlFPEITIKSKSvRQRFIKILQGNIRNVLRRFDDdARVRMDWDKLIVSSRNDQfREQAIEALACIPGIQAFLEVQAS 82
Cdd:COG0301    4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGED-AEEAIERLKKVFGIVSFSPAVEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  83 KFtDLHDIFEQVKAVWGDQLEGKTFCVRAKRHGKH-EFSSLEVERYVGGGLNQHCVSNGVRLKNPDVKINLEIDGEELFI 161
Cdd:COG0301   80 EK-DLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 162 VSAIHQGLSGMPIATQEDVLSLISGGFDSGVASFQFIKRGCRVHYCFFNLGG---AAHEIGVKQVAYHLwNRFGSsHRVR 238
Cdd:COG0301  159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYGG-HRVK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 239 FTAVDFEPVVAEILEKIDNGQMGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLIT 318
Cdd:COG0301  237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117561619 319 WDKPDIISEARRIGTLEFAETMPEYCG--VISKKPTVKAELSRIEAEEENFDF-AILDKVVAEARY 381
Cdd:COG0301  317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLeELLEEAVENAEV 382
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 4-376 2.72e-121

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: 359.42  E-value: 2.72e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619    4 IIKLFPEITIKSKsVRQRFIKILQGNIRNVLRRFDDDARVRMDWDKLIVSSRNDQFREQAIEALACIPGIQAFLEVQASK 83
Cdd:TIGR00342   1 ILARYGEIGIKGK-NRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIVSFSPAFKCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619   84 fTDLHDIFEQVKAVWGDQLEGKTFCVRAKRHGKH-EFSSLEVERYVGGGLNQHcVSNGVRLKNPDVKINLEIDGEELFIV 162
Cdd:TIGR00342  80 -LPFDEIHILLKALKQLRKEGKTFKVRTKRRGKDfPLNSVEVNKYVGGGIVEK-IGLKVDLTNPDITVHIEIREDEFLII 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  163 SAIHQGLSGMPIATQEDVLSLISGGFDSGVASFQFIKRGCRVHYCFFNLGGAAHEIGVKQVAYHLWNRFGSSHRVRFTAV 242
Cdd:TIGR00342 158 TERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLYVF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  243 DFEPVVAEILEKIDNGQMGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLITWDKP 322
Cdd:TIGR00342 238 DFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMDKE 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 117561619  323 DIISEARRIGTLEFAETMPEYCGVISK--KPTVKAELSRIEAEEENFDFaiLDKVV 376
Cdd:TIGR00342 318 EIIELAKEIGTYEISIEPHEDCCTIFKpkHPTTKAKPEKVEKLEEKLDF--SRKLV 371
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 176-369 5.30e-83

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 254.66  E-value: 5.30e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  176 TQEDVLSLISGGFDSGVASFQFIKRGCRVHYCFF--NLGGAAHEIGVKQVAYHLWNRFGSSHRVRFTAVDFEPVVAEILE 253
Cdd:pfam02568   2 TQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEILE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  254 KIDNGQMGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLITWDKPDIISEARRIGT 333
Cdd:pfam02568  82 KAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIGT 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 117561619  334 LEFAETMPEYCGVISKKPTVKAELSRIEAEEENFDF 369
Cdd:pfam02568 162 YEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKLDL 197
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 174-355 3.55e-75

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: 233.98  E-value: 3.55e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 174 IATQEDVLSLISGGFDSGVASFQFIKRGCRVHYCFFNLGGAAHEIGVKQVAYHLWNRFGSSHRVRFTAVDF-EPVVAEIL 252
Cdd:cd01712    1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 253 EKIDNGQMGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLITWDKPDIISEARRIG 332
Cdd:cd01712   81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                        170       180
                 ....*....|....*....|....*
gi 117561619 333 TLEFAETMPE--YCGVISKKPTVKA 355
Cdd:cd01712  161 TYEISILPYEdcCCLFAPKNPVTKP 185
ThiI_C_thiazole TIGR04271
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ...
 382-482 8.31e-54

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: 175.83  E-value: 8.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  382 LDIRRIGEETAAEVQEVETTAESGDNEVILDIRSMDEHNEKPLLVEGREVMHIPFFKLTTAFGDLPKEKTYLLYCDRGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 117561619  462 SKLQALYLKEKGFANVKVYRP 482
Cdd:TIGR04271  81 SRLQALYLKEQGFTNVKVYRP 101
PRK08349 PRK08349
hypothetical protein; Validated
 180-361 1.11e-25

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 103.66  E-value: 1.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 180 VLSLISGGFDSGVASFQFIKRGCRVHYCFFNLGGAAHEiGVKQVAYHLWNRFGSSHRvRFTAVDFEPVVAEILEKI-DNG 258
Cdd:PRK08349   3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEE-KVRELVERLQELHGGKLK-DPVVVDAFEEQGPVFEKLrELK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 259 Q---MGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLITWDKPDIISEARRIGTLE 335
Cdd:PRK08349  81 KekwTCIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTFE 160

                        170       180
                 ....*....|....*....|....*.
gi 117561619 336 FAETMPEYCGVISKKPTVKAELSRIE 361
Cdd:PRK08349 161 ISIEPEPPCPFVPKYPVVRASLGEFE 186
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 86-161 2.41e-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: 79.63  E-value: 2.41e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619    86 DLHDIFEQVKAVWGDQ---LEGKTFCVRAKRHGK-HEFSSLEVERYVGGGLNQHCVSNGVRLKNPDVKINLEIDGEELFI 161
Cdd:smart00981   1 DLEDLYETALELIRWEkifKEGKTFAVRAKRRGKnHEFTSLEVKRAIGDKLLEKTGGRKVDLKNPDVVIRVELRKDKAYL 80
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 395-481 4.34e-13

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: 65.37  E-value: 4.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 395 VQEVETTAESGDnEVILDIRSMDEHNEKPLlvegREVMHIPFFKLTTAFGDLPKEKTYLLYCDRGVMSKLQALYLKEKGF 474
Cdd:COG0607    8 PAELAELLESED-AVLLDVREPEEFAAGHI----PGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGY 82


                 ....*..
gi 117561619 475 ANVKVYR 481
Cdd:COG0607   83 TNVYNLA 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 405-481 1.02e-07

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


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 49.79  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  405 GDNEVILDIRSMDEHNE------KPLLVEGREVMHIPFFKLTTAFGDLPKEKTYLLYCDRGVMSKLQALYLKEKGFANVK 478
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKghipgaVNVPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82


                  ...
gi 117561619  479 VYR 481
Cdd:pfam00581  83 VLD 85
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 405-481 1.20e-07

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: 49.22  E-value: 1.20e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117561619 405 GDNEVILDIRSMDEHNEKPLlvEGreVMHIPFFKLTTAFG--DLPKEKTYLLYCDRGVMSKLQALYLKEKGFANVKVYR 481
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHI--PG--AINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
 
Name Accession Description Interval E-value
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 3-381 8.85e-179

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: 505.78  E-value: 8.85e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619   3 FIIKlFPEITIKSKSvRQRFIKILQGNIRNVLRRFDDdARVRMDWDKLIVSSRNDQfREQAIEALACIPGIQAFLEVQAS 82
Cdd:COG0301    4 ILVR-YGEIALKGKN-RKRFEKRLVKNIRAALKDLGE-VKVKREWGRIYVETDGED-AEEAIERLKKVFGIVSFSPAVEV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  83 KFtDLHDIFEQVKAVWGDQLEGKTFCVRAKRHGKH-EFSSLEVERYVGGGLNQHCVSNGVRLKNPDVKINLEIDGEELFI 161
Cdd:COG0301   80 EK-DLEDIKEAALELAKEELKGKTFKVRAKRAGKHfPFTSPELEREVGGALLENTPGLKVDLKNPDVTIRVEVRDDKAYV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 162 VSAIHQGLSGMPIATQEDVLSLISGGFDSGVASFQFIKRGCRVHYCFFNLGG---AAHEIGVKQVAYHLwNRFGSsHRVR 238
Cdd:COG0301  159 YTERIPGPGGLPVGTQGKVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHSGPytsERAEEKVKDLARKL-SRYGG-HRVK 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 239 FTAVDFEPVVAEILEKIDNGQMGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLIT 318
Cdd:COG0301  237 LYVVPFTEVQEEILEKVPERYRTVLLRRMMMRIAERIAEKEGALALVTGESLGQVASQTLENLAVIDAVTDLPVLRPLIG 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117561619 319 WDKPDIISEARRIGTLEFAETMPEYCG--VISKKPTVKAELSRIEAEEENFDF-AILDKVVAEARY 381
Cdd:COG0301  317 MDKEEIIEIARKIGTYEISILPYEDCCtvFVPKHPETKPKLEKVEKEEEKLDLeELLEEAVENAEV 382
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 4-376 2.72e-121

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: 359.42  E-value: 2.72e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619    4 IIKLFPEITIKSKsVRQRFIKILQGNIRNVLRRFDDDARVRMDWDKLIVSSRNDQFREQAIEALACIPGIQAFLEVQASK 83
Cdd:TIGR00342   1 ILARYGEIGIKGK-NRLRFEKILKKNIKKALKKYEILRAVVYHFDRIVVIAIDKEQRDALLDLLTKIPGIVSFSPAFKCD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619   84 fTDLHDIFEQVKAVWGDQLEGKTFCVRAKRHGKH-EFSSLEVERYVGGGLNQHcVSNGVRLKNPDVKINLEIDGEELFIV 162
Cdd:TIGR00342  80 -LPFDEIHILLKALKQLRKEGKTFKVRTKRRGKDfPLNSVEVNKYVGGGIVEK-IGLKVDLTNPDITVHIEIREDEFLII 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  163 SAIHQGLSGMPIATQEDVLSLISGGFDSGVASFQFIKRGCRVHYCFFNLGGAAHEIGVKQVAYHLWNRFGSSHRVRFTAV 242
Cdd:TIGR00342 158 TERYEGIGGLPVGTQGKVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFNEPAASEKAREKVERLANSLNETGGSVKLYVF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  243 DFEPVVAEILEKIDNGQMGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLITWDKP 322
Cdd:TIGR00342 238 DFTDVQEEIIHIIPEGYTCVLCRRMMYKAASKVAEKEGCLAIVTGESLGQVASQTLENLRVIQAVSNTPILRPLIGMDKE 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 117561619  323 DIISEARRIGTLEFAETMPEYCGVISK--KPTVKAELSRIEAEEENFDFaiLDKVV 376
Cdd:TIGR00342 318 EIIELAKEIGTYEISIEPHEDCCTIFKpkHPTTKAKPEKVEKLEEKLDF--SRKLV 371
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 176-369 5.30e-83

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


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 254.66  E-value: 5.30e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  176 TQEDVLSLISGGFDSGVASFQFIKRGCRVHYCFF--NLGGAAHEIGVKQVAYHLWNRFGSSHRVRFTAVDFEPVVAEILE 253
Cdd:pfam02568   2 TQGKVLALISGGIDSPVAAYMMMRRGCRVVALHFinNPGTSAEAIGKVQKLAELLARYGTSHEVRLVVFDFTDVQKEILE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  254 KIDNGQMGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLITWDKPDIISEARRIGT 333
Cdd:pfam02568  82 KAPEGYRCVLLKRCMYRIAEKVAEEEGADALVTGESLGQVASQTLDNLRVISAVSNTPILRPLIGLDKEDIINLAKEIGT 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 117561619  334 LEFAETMPEYCGVISKKPTVKAELSRIEAEEENFDF 369
Cdd:pfam02568 162 YEISIEPYDCCTVFAKHPTTKAKPEEVEKEEEKLDL 197
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 174-355 3.55e-75

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: 233.98  E-value: 3.55e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 174 IATQEDVLSLISGGFDSGVASFQFIKRGCRVHYCFFNLGGAAHEIGVKQVAYHLWNRFGSSHRVRFTAVDF-EPVVAEIL 252
Cdd:cd01712    1 VGTSGKVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGPYTSEKAVEKVKDLARVLSEYQGGVKLYLVPFtDKIQKEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 253 EKIDNGQMGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLITWDKPDIISEARRIG 332
Cdd:cd01712   81 EKVPESYRIVLMRRMMYRIAEKIAERLGADALVTGESLGQVASQTLENLKVIDSVTDLPVLRPLIGMDKEEIIDIARRIG 160

                        170       180
                 ....*....|....*....|....*
gi 117561619 333 TLEFAETMPE--YCGVISKKPTVKA 355
Cdd:cd01712  161 TYEISILPYEdcCCLFAPKNPVTKP 185
ThiI_C_thiazole TIGR04271
thiazole biosynthesis domain; The ThiI protein of Escherichia coli is a bifunctional protein ...
 382-482 8.31e-54

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: 175.83  E-value: 8.31e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  382 LDIRRIGEETAAEVQEVETTAESGDNEVILDIRSMDEHNEKPLLVEGREVMHIPFFKLTTAFGDLPKEKTYLLYCDRGVM 461
Cdd:TIGR04271   1 IDIDEIADDTNEEVAEVETVSELSSGDVIIDIRHPDEQEKAPLELEGVEVIKIPFYKLATQFAELDQDKTYLLYCDKGVM 80

                          90       100
                  ....*....|....*....|.
gi 117561619  462 SKLQALYLKEKGFANVKVYRP 482
Cdd:TIGR04271  81 SRLQALYLKEQGFTNVKVYRP 101
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 2-169 1.03e-51

THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the formation of the modified base S(4)U (4-thiouridine) found at position 8 in some prokaryotic tRNAs. This modification acts as a signal for UV exposure, triggering a response that provides protection against its damaging effects. ThiI consists of an N-terminal THUMP domain, followed by an NFLD domain, and a C-terminal PP-loop pyrophosphatase domain. The N-terminal THUMP domain has been implicated in the recognition of the acceptor-stem region. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212585  Cd Length: 166  Bit Score: 172.63  E-value: 1.03e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619   2 KFIIKLFpEITIKSKsVRQRFIKILQGNIRNVLRRFDDdARVRMDWDKLIVSSrNDQFREQAIEALACIPGIQAFLEVQA 81
Cdd:cd11716    1 KILVRYG-EIALKGK-NRKRFEKRLVKNIRRALKDLPD-VKVEREWGRIYVEL-NGEDLEEVIERLKKVFGIVSFSPAVE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  82 SKFtDLHDIFEQVKAVWGDQL-EGKTFCVRAKRHGK-HEFSSLEVERYVGGGLNQHCVSNGVRLKNPDVKINLEIDGEEL 159
Cdd:cd11716   77 VEK-DLEDIKEAALELLKEELkKGKTFKVRAKRADKsFPFTSMEINREVGAALLENTPDLKVDLKNPDVTIRVEIREDGA 155

                        170
                 ....*....|
gi 117561619 160 FIVSAIHQGL 169
Cdd:cd11716  156 YVYTERIPGP 165
PRK08349 PRK08349
hypothetical protein; Validated
 180-361 1.11e-25

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 103.66  E-value: 1.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 180 VLSLISGGFDSGVASFQFIKRGCRVHYCFFNLGGAAHEiGVKQVAYHLWNRFGSSHRvRFTAVDFEPVVAEILEKI-DNG 258
Cdd:PRK08349   3 AVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEE-KVRELVERLQELHGGKLK-DPVVVDAFEEQGPVFEKLrELK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 259 Q---MGVVLKRMMMRAAAKVADEFQIPALVTGECVGQVSSQTLTNLNVIDRVTDKVILRPLITWDKPDIISEARRIGTLE 335
Cdd:PRK08349  81 KekwTCIFCKYTMYRKAERIAHEIGASAIITGDSLGQVASQTLDNLMVISTATDLPVLRPLIGLDKEEIVKIAKEIGTFE 160

                        170       180
                 ....*....|....*....|....*.
gi 117561619 336 FAETMPEYCGVISKKPTVKAELSRIE 361
Cdd:PRK08349 161 ISIEPEPPCPFVPKYPVVRASLGEFE 186
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 86-161 2.41e-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: 79.63  E-value: 2.41e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619    86 DLHDIFEQVKAVWGDQ---LEGKTFCVRAKRHGK-HEFSSLEVERYVGGGLNQHCVSNGVRLKNPDVKINLEIDGEELFI 161
Cdd:smart00981   1 DLEDLYETALELIRWEkifKEGKTFAVRAKRRGKnHEFTSLEVKRAIGDKLLEKTGGRKVDLKNPDVVIRVELRKDKAYL 80
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 28-161 4.50e-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: 4.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619   28 GNIRNVLRRFDDDA-RVRMDWDKLIVSSRNDQF---REQAIEALACIPGIQAFLEVQAsKFTDLHDIFEQVKAVWGDQL- 102
Cdd:pfam02926   1 KEIEELLKKGGINVeVVRSGRGRILVVLKGENPeedRELLKEALEKAPGIERFPVAET-CEADLEDILELAKEIIKDKFk 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117561619  103 -EGKTFCVRAKRHGK-HEFSSLEVERYVGGGLNQHcVSNGVRLKNPDVKINLEIDGEELFI 161
Cdd:pfam02926  80 kEGETFAVRVKRRGKnHEFTSLEINREVGKAIVEK-TGLKVDLENPDIVVHVEIIKDKAYI 139
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 395-481 4.34e-13

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: 65.37  E-value: 4.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 395 VQEVETTAESGDnEVILDIRSMDEHNEKPLlvegREVMHIPFFKLTTAFGDLPKEKTYLLYCDRGVMSKLQALYLKEKGF 474
Cdd:COG0607    8 PAELAELLESED-AVLLDVREPEEFAAGHI----PGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAGY 82


                 ....*..
gi 117561619 475 ANVKVYR 481
Cdd:COG0607   83 TNVYNLA 89
Tan1 COG1818
tRNA(Ser,Leu) C12 N-acetylase TAN1, contains THUMP domain [Translation, ribosomal structure ...
 1-161 7.36e-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: 63.37  E-value: 7.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619   1 MKFIIKLFPeitiksksvrqRFIKILQGNIRNVLRRFDDDARV-RMDWDKLI---VSSRNDQFREQAIEALACIPGIQAF 76
Cdd:COG1818    1 MNLIVTTPR-----------GRERDAIEELRDILEEGDPNAEVvPTGFSGVLlvkTSLDPYEAVEKLKEEPWEPRYILRV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  77 LEVQASKFTDLHDIFEQVKAVWGDQL-EGKTFCVRAKRHGKHEFSSLEVERYVGGGLNQhcvSNGVRLKNPDVKINLEID 155
Cdd:COG1818   70 IPVDRVVKTDLEEIVEAAKELAKKKIpEGETFAVRCEKRGKSKLSSREVIRAIGEAIKR---GAKVDLENPDWVVLVEIL 146


                 ....*.
gi 117561619 156 GEELFI 161
Cdd:COG1818  147 GDKAGI 152
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 76-161 1.77e-11

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: 62.21  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  76 FLEVQASKFTDLHDIFEQVKAV-WGDQL-EGKTFCVRAKRHGKHEFSSLEVERYVGGGLNQHCVSNGVR----LKNPDVK 149
Cdd:cd11715   55 LLLLAEFEAEDFDDLYELAKAIdWEDYLdPDGTFAVRATRVGSKLFHSQFAALRVKDAIVDRFREKGKRpsvdLDNPDVR 134

                         90
                 ....*....|..
gi 117561619 150 INLEIDGEELFI 161
Cdd:cd11715  135 IRVHLSKDRATL 146
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 405-481 1.02e-07

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


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 49.79  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  405 GDNEVILDIRSMDEHNE------KPLLVEGREVMHIPFFKLTTAFGDLPKEKTYLLYCDRGVMSKLQALYLKEKGFANVK 478
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKghipgaVNVPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVY 82


                  ...
gi 117561619  479 VYR 481
Cdd:pfam00581  83 VLD 85
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 405-481 1.20e-07

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: 49.22  E-value: 1.20e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 117561619 405 GDNEVILDIRSMDEHNEKPLlvEGreVMHIPFFKLTTAFG--DLPKEKTYLLYCDRGVMSKLQALYLKEKGFANVKVYR 481
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHI--PG--AINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLE 82
THUMP_SPOUT cd11718
THUMP domain associated with SPOUT RNA Methylases; Members of this archaeal protein family are ...
 32-161 2.15e-06

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: 47.28  E-value: 2.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  32 NVLRRFDDDARVR---MDWDKLIVSSRNDQFREQAIEAlacIPGIQAFLEVQASKFTDLHDIFEQVKAVWGDQLEGKTFC 108
Cdd:cd11718   15 SYIKEIDPDAKVEpapMGFLGLVLVESDEDKKDELALR---VPEVERVIPVDAEVKADLDEIVRVAEEIAKHISEGETFA 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 117561619 109 VRAKRHGKHEFSSLEVERYVGGGLnQHCVSNGVRLKNPDVKINLEIDGEELFI 161
Cdd:cd11718   92 VRTTRRGKHDFTSIDVNVVLGAAV-KELTGAEVDLNNPDKVVYVEIIGDRAYI 143
THUMP_THUMPD1_like cd11717
THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins ...
 73-157 5.16e-06

THUMP domain-containing protein 1-like; This family contains THUMP domain-only proteins including THUMP domain-containing protein 1 and Saccharomyces cerevisiae Tan1. Tan1 is non essential and has been shown to be required for the formation of the modified nucleoside N(4)-acetylcytidine (ac(4)C) in tRNA. To date, there is no functional information available about THUMPD1. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212586  Cd Length: 158  Bit Score: 46.42  E-value: 5.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619  73 IQAFLEVQASKFTDLHDIFEQVKAVWG----DQLEGKTFCVRAKRHGKHEFSSLEVERYVGGGLNQHcvsNGVRLKNPDV 148
Cdd:cd11717   65 IQRLIPIDVTCKASLEEIEKLAKELLKkhfpTAEPPKTFAVECKSRNNNKLSRDEVIKAVAELVPEI---HKVDLKNPDK 141


                 ....*....
gi 117561619 149 KINLEIDGE 157
Cdd:cd11717  142 VILVEVIKN 150
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 395-477 1.07e-04

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


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 41.09  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 395 VQEVETTAESGDNEVILDIRSMDEHNEKPLLVEGreVMHIPFFKLTTAFGDLPKEKTYLLYCDRGVMSKLQALYLKEKGF 474
Cdd:cd01444    4 VDELAELLAAGEAPVLLDVRDPASYAALPDHIPG--AIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAGF 81


                 ...
gi 117561619 475 ANV 477
Cdd:cd01444   82 TDV 84
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 395-478 6.25e-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: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 395 VQEVETTAESGDNEVILDIRSMDEHNEKplLVEGreVMHIPFFKLTTAFGDLPKEKTYLLYCDRGVMSKLQALYLKEKGF 474
Cdd:cd01524    1 VQWHELDNYRADGVTLIDVRTPQEFEKG--HIKG--AINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGF 76


                 ....
gi 117561619 475 aNVK 478
Cdd:cd01524   77 -KVK 79
THUMP cd11688
THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, ...
 103-161 1.09e-03

THUMP domain, predicted to bind RNA; The THUMP domain is named after THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212583  Cd Length: 148  Bit Score: 39.39  E-value: 1.09e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 117561619 103 EGKTFCVRAKRHGKHEFSSLEVERYVGGGLNQHCVSNgVRLKNPDVKINLEIDGEELFI 161
Cdd:cd11688   90 EGAKFAVRARRRNKTILNSQEIAMKVGDAIVDAFNPE-VDLDNPDIVVNVEVHKEIASI 147
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 393-480 2.45e-03

Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.


Pssm-ID: 238726 [Multi-domain]  Cd Length: 118  Bit Score: 38.00  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117561619 393 AEVQEVETTAESGDnEVILDIRSMDEHN-EKPLLVEGREVMHIP----------------------FFKLTTAFGDLPkE 449
Cdd:cd01449    1 VTAEEVLANLDSGD-VQLVDARSPERFRgEVPEPRPGLRSGHIPgavnipwtslldedgtfkspeeLRALFAALGITP-D 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 117561619 450 KTYLLYCDRGVMSKLQALYLKEKGFANVKVY 480
Cdd:cd01449   79 KPVIVYCGSGVTACVLLLALELLGYKNVRLY 109
 
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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