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Conserved domains on  [gi|163965375|ref|NP_001106677|]
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thiosulfate:glutathione sulfurtransferase isoform 2 [Homo sapiens]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 13)

rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 4-71 2.06e-27

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.


The actual alignment was detected with superfamily member cd01519:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 106  Bit Score: 95.03  E-value: 2.06e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163965375   4 VSELESALQMEPAAFQALYSAEKPKLEDEhLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREWLE 71
Cdd:cd01519   40 LSSLPDALALSEEEFEKKYGFPKPSKDKE-LIFYCKAGVRSKAAAELARSLGYENVGNYPGSWLDWAA 106
 
Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 4-71 2.06e-27

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 95.03  E-value: 2.06e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163965375   4 VSELESALQMEPAAFQALYSAEKPKLEDEhLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREWLE 71
Cdd:cd01519   40 LSSLPDALALSEEEFEKKYGFPKPSKDKE-LIFYCKAGVRSKAAAELARSLGYENVGNYPGSWLDWAA 106
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 9-69 5.47e-11

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: 52.87  E-value: 5.47e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163965375   9 SALQMEPAAFQALYSAEKPKLEDEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREW 69
Cdd:pfam00581 31 SSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 5-72 6.65e-09

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 47.84  E-value: 6.65e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163965375     5 SELESALQMEPAAFQALYSAEKPKlEDEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREWLEK 72
Cdd:smart00450  31 ELLDRRGELDILEFEELLKRLGLD-KDKPVVVYCRSGNRSAKAAWLLRELGFKNVYLLDGGYKEWSAA 97
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 30-71 1.41e-07

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: 44.57  E-value: 1.41e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 163965375  30 EDEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREWLE 71
Cdd:COG0607   56 KDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKA 97
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
31-69 1.20e-04

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 38.07  E-value: 1.20e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 163965375  31 DEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREW 69
Cdd:PRK08762  57 DREIVLICASGTRSAHAAATLRELGYTRVASVAGGFSAW 95
 
Name Accession Description Interval E-value
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 4-71 2.06e-27

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 95.03  E-value: 2.06e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163965375   4 VSELESALQMEPAAFQALYSAEKPKLEDEhLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREWLE 71
Cdd:cd01519   40 LSSLPDALALSEEEFEKKYGFPKPSKDKE-LIFYCKAGVRSKAAAELARSLGYENVGNYPGSWLDWAA 106
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 9-69 5.47e-11

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: 52.87  E-value: 5.47e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 163965375   9 SALQMEPAAFQALYSAEKPKLEDEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREW 69
Cdd:pfam00581 31 SSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 5-72 6.65e-09

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 47.84  E-value: 6.65e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 163965375     5 SELESALQMEPAAFQALYSAEKPKlEDEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREWLEK 72
Cdd:smart00450  31 ELLDRRGELDILEFEELLKRLGLD-KDKPVVVYCRSGNRSAKAAWLLRELGFKNVYLLDGGYKEWSAA 97
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 30-71 1.41e-07

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: 44.57  E-value: 1.41e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 163965375  30 EDEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREWLE 71
Cdd:COG0607   56 KDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKA 97
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 24-69 1.79e-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: 43.83  E-value: 1.79e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 163965375 24 AEKPKleDEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREW 69
Cdd:cd00158  45 LELDK--DKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 26-71 6.29e-06

Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.


Pssm-ID: 238724 [Multi-domain]  Cd Length: 103  Bit Score: 40.10  E-value: 6.29e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 163965375  26 KPKL-EDEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREWLE 71
Cdd:cd01447   55 KPAFaEDKPFVFYCASGWRSALAGKTLQDMGLKPVYNIEGGFKDWKE 101
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
31-69 1.20e-04

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 38.07  E-value: 1.20e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 163965375  31 DEHLVFFCQMGKRGLQATQLARSLGYTGARNYAGAYREW 69
Cdd:PRK08762  57 DREIVLICASGTRSAHAAATLRELGYTRVASVAGGFSAW 95
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 14-69 4.44e-04

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: 35.69  E-value: 4.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 163965375  14 EPAAFQALYSAEKPKLEDEhLVFFCQMGKRglqATQL---ARSLGYTGARNYAGAYREW 69
Cdd:cd01449   62 SPEELRALFAALGITPDKP-VIVYCGSGVT---ACVLllaLELLGYKNVRLYDGSWSEW 116
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 15-69 6.87e-04

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 35.92  E-value: 6.87e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 163965375  15 PAAFQALYSAEKPKLeDEHLVFFCQMGKRglqATQL---ARSLGYTGARNYAGAYREW 69
Cdd:COG2897  200 AEELRALFAALGIDP-DKPVITYCGSGVR---AAHTwlaLELLGYPNVRLYDGSWSEW 253
 
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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