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Conserved domains on  [gi|489497208|ref|WP_003402121|]
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MULTISPECIES: sulfur carrier protein ThiS [Mycobacterium]

Protein Classification

sulfur carrier protein ThiS( domain architecture ID 10088150)

ThiS ubiquitin-like sulfur carrier protein is involved in thiamin biosynthesis in bacteria

Gene Symbol:  thiS
Gene Ontology:  GO:0009228
PubMed:  11135670

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Ubl_ThiS cd00565
ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS; ThiS, also termed Thiamine ...
 13-68 8.28e-18

ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS; ThiS, also termed Thiamine biosynthesis protein (ThiaminS), is a sulfur carrier protein involved in thiamin biosynthesis in prokaryotes. It has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub), and is activated in an ATP-dependent manner by sulfurtransferases, similar to the activation mechanism of Ub-activating enzyme E1. ThiS has common evolutionary origin with Ub-related protein modifiers in eukaryotes, a beta-grasp fold as Ub, and is closely related to proteins MoaD and Urm1.


:

Pssm-ID: 340451 [Multi-domain]  Cd Length: 64  Bit Score: 69.07  E-value: 8.28e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 489497208 13 DEQTTIAALLDSLGFGDRGIAVALNFSVLPRSDWATkiCELRKPVRLEVVTAVQGG 68
Cdd:cd00565  11 DEGLTLAELLEELGFTPKGVAVELNGEIVPRSEWAE--TILKDGDRIEIVTFVGGG 64
 
Name Accession Description Interval E-value
Ubl_ThiS cd00565
ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS; ThiS, also termed Thiamine ...
 13-68 8.28e-18

ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS; ThiS, also termed Thiamine biosynthesis protein (ThiaminS), is a sulfur carrier protein involved in thiamin biosynthesis in prokaryotes. It has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub), and is activated in an ATP-dependent manner by sulfurtransferases, similar to the activation mechanism of Ub-activating enzyme E1. ThiS has common evolutionary origin with Ub-related protein modifiers in eukaryotes, a beta-grasp fold as Ub, and is closely related to proteins MoaD and Urm1.


Pssm-ID: 340451 [Multi-domain]  Cd Length: 64  Bit Score: 69.07  E-value: 8.28e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 489497208 13 DEQTTIAALLDSLGFGDRGIAVALNFSVLPRSDWATkiCELRKPVRLEVVTAVQGG 68
Cdd:cd00565  11 DEGLTLAELLEELGFTPKGVAVELNGEIVPRSEWAE--TILKDGDRIEIVTFVGGG 64
thiS TIGR01683
thiamine biosynthesis protein ThiS; This model represents ThiS, a small, ubiquitin-like ...
 13-68 5.30e-17

thiamine biosynthesis protein ThiS; This model represents ThiS, a small, ubiquitin-like thiamine biosynthesis protein related to MoaD, a molybdenum cofactor biosynthesis protein. Both proteins are involved in sulfur transfer. ThiS has a conserved Gly-Gly C-terminus that is modified, in reactions requiring ThiI, ThiF, IscS, and a sulfur atom from Cys, into the thiocarboxylate that provides the sulfur for thiazole biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273754 [Multi-domain]  Cd Length: 64  Bit Score: 67.20  E-value: 5.30e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489497208  13 DEQTTIAALLDSLGFGDRGIAVALNFSVLPRSDWATKICElrKPVRLEVVTAVQGG 68
Cdd:TIGR01683 11 EDGTTLAALLESLGLDPRRVAVAVNGEIVPRSEWDDTILK--EGDRIEIVTFVGGG 64
ThiS COG2104
Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]; ...
 13-68 1.07e-16

Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]; Sulfur carrier protein ThiS (thiamine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 441707 [Multi-domain]  Cd Length: 66  Bit Score: 66.25  E-value: 1.07e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 489497208 13 DEQTTIAALLDSLGFGDRGIAVALNFSVLPRSDWATkiCELRKPVRLEVVTAVQGG 68
Cdd:COG2104  13 PEGTTLADLLEELGLDPKGVAVAVNGEIVPRSQWAS--TVLKEGDRVEIVTAVGGG 66
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 13-68 3.38e-07

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 45.12  E-value: 3.38e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489497208  13 DEQTTIAALLDSLGFGDRGIAVALNFSVLPRSDWATKIceLRKPVRLEVVTAVQGG 68
Cdd:PRK11840  13 PAGLTIAALLAELGLAPKKVAVERNLEIVPRSEYGQVA--LEEGDELEIVHFVGGG 66
ThiS pfam02597
ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in ...
 13-68 1.88e-05

ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalyzed by IscS. MoaD, a protein involved sulphur transfer in molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end.


Pssm-ID: 396932 [Multi-domain]  Cd Length: 74  Bit Score: 38.04  E-value: 1.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497208  13 DEQTTIAALLDSLGFGD----RGIAVALNFSVLPRSDWATKICElrkPVRLEVVTAVQGG 68
Cdd:pfam02597 18 AEGATVAELLEALGLRYpelrERVAVAVNGEIVPRLWLDTPLKD---GDEVAIIPPVGGG 74
 
Name Accession Description Interval E-value
Ubl_ThiS cd00565
ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS; ThiS, also termed Thiamine ...
 13-68 8.28e-18

ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS; ThiS, also termed Thiamine biosynthesis protein (ThiaminS), is a sulfur carrier protein involved in thiamin biosynthesis in prokaryotes. It has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub), and is activated in an ATP-dependent manner by sulfurtransferases, similar to the activation mechanism of Ub-activating enzyme E1. ThiS has common evolutionary origin with Ub-related protein modifiers in eukaryotes, a beta-grasp fold as Ub, and is closely related to proteins MoaD and Urm1.


Pssm-ID: 340451 [Multi-domain]  Cd Length: 64  Bit Score: 69.07  E-value: 8.28e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 489497208 13 DEQTTIAALLDSLGFGDRGIAVALNFSVLPRSDWATkiCELRKPVRLEVVTAVQGG 68
Cdd:cd00565  11 DEGLTLAELLEELGFTPKGVAVELNGEIVPRSEWAE--TILKDGDRIEIVTFVGGG 64
thiS TIGR01683
thiamine biosynthesis protein ThiS; This model represents ThiS, a small, ubiquitin-like ...
 13-68 5.30e-17

thiamine biosynthesis protein ThiS; This model represents ThiS, a small, ubiquitin-like thiamine biosynthesis protein related to MoaD, a molybdenum cofactor biosynthesis protein. Both proteins are involved in sulfur transfer. ThiS has a conserved Gly-Gly C-terminus that is modified, in reactions requiring ThiI, ThiF, IscS, and a sulfur atom from Cys, into the thiocarboxylate that provides the sulfur for thiazole biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273754 [Multi-domain]  Cd Length: 64  Bit Score: 67.20  E-value: 5.30e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489497208  13 DEQTTIAALLDSLGFGDRGIAVALNFSVLPRSDWATKICElrKPVRLEVVTAVQGG 68
Cdd:TIGR01683 11 EDGTTLAALLESLGLDPRRVAVAVNGEIVPRSEWDDTILK--EGDRIEIVTFVGGG 64
ThiS COG2104
Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]; ...
 13-68 1.07e-16

Sulfur carrier protein ThiS (thiamine biosynthesis) [Coenzyme transport and metabolism]; Sulfur carrier protein ThiS (thiamine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 441707 [Multi-domain]  Cd Length: 66  Bit Score: 66.25  E-value: 1.07e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 489497208 13 DEQTTIAALLDSLGFGDRGIAVALNFSVLPRSDWATkiCELRKPVRLEVVTAVQGG 68
Cdd:COG2104  13 PEGTTLADLLEELGLDPKGVAVAVNGEIVPRSQWAS--TVLKEGDRVEIVTAVGGG 66
PRK11840 PRK11840
bifunctional sulfur carrier protein/thiazole synthase protein; Provisional
 13-68 3.38e-07

bifunctional sulfur carrier protein/thiazole synthase protein; Provisional


Pssm-ID: 236998 [Multi-domain]  Cd Length: 326  Bit Score: 45.12  E-value: 3.38e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489497208  13 DEQTTIAALLDSLGFGDRGIAVALNFSVLPRSDWATKIceLRKPVRLEVVTAVQGG 68
Cdd:PRK11840  13 PAGLTIAALLAELGLAPKKVAVERNLEIVPRSEYGQVA--LEEGDELEIVHFVGGG 66
ThiS pfam02597
ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in ...
 13-68 1.88e-05

ThiS family; ThiS (thiaminS) is a 66 aa protein involved in sulphur transfer. ThiS is coded in the thiCEFSGH operon in E. coli. This family of proteins have two conserved Glycines at the COOH terminus. Thiocarboxylate is formed at the last G in the activation process. Sulphur is transferred from ThiI to ThiS in a reaction catalyzed by IscS. MoaD, a protein involved sulphur transfer in molybdopterin synthesis, is about the same length and shows limited sequence similarity to ThiS. Both have the conserved GG at the COOH end.


Pssm-ID: 396932 [Multi-domain]  Cd Length: 74  Bit Score: 38.04  E-value: 1.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489497208  13 DEQTTIAALLDSLGFGD----RGIAVALNFSVLPRSDWATKICElrkPVRLEVVTAVQGG 68
Cdd:pfam02597 18 AEGATVAELLEALGLRYpelrERVAVAVNGEIVPRLWLDTPLKD---GDEVAIIPPVGGG 74
 
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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