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Conserved domains on  [gi|15595786|ref|NP_249280|]
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thiosulfate sulfurtransferase [Pseudomonas aeruginosa PAO1]

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 ...
 3-108 5.03e-64

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 PRK00162:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 108  Bit Score: 189.08  E-value: 5.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786    3 DTFQRIAPEQVRQLR-ENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQ 81
Cdd:PRK00162   2 DQFECINVEQAHQKLqEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQQ 81

                         90       100
                 ....*....|....*....|....*..
gi 15595786   82 GFSDVYSLDGGFELWRSVYPADTSSGE 108
Cdd:PRK00162  82 GFDVVYSIDGGFEAWRRTFPAEVASGA 108
 
Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
3-108 5.03e-64

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 189.08  E-value: 5.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786    3 DTFQRIAPEQVRQLR-ENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQ 81
Cdd:PRK00162   2 DQFECINVEQAHQKLqEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQQ 81

                         90       100
                 ....*....|....*....|....*..
gi 15595786   82 GFSDVYSLDGGFELWRSVYPADTSSGE 108
Cdd:PRK00162  82 GFDVVYSIDGGFEAWRRTFPAEVASGA 108
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 7-97 1.94e-33

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: 111.58  E-value: 1.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   7 RIAPEQVRQLRENG--AQVVDIRDPQSFAV--GHISGSRHIDNHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQG 82
Cdd:cd01444   1 RISVDELAELLAAGeaPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                        90
                ....*....|....*
gi 15595786  83 FSDVYSLDGGFELWR 97
Cdd:cd01444  81 FTDVRSLAGGFEAWR 95
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 3-98 1.01e-32

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: 110.06  E-value: 1.01e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   3 DTFQRIAPEQVRQLREN-GAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQ 81
Cdd:COG0607   1 ASVKEISPAELAELLESeDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                        90
                ....*....|....*..
gi 15595786  82 GFSDVYSLDGGFELWRS 98
Cdd:COG0607  81 GYTNVYNLAGGIEAWKA 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 16-96 1.51e-19

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: 76.37  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786    16 LRENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADF----------IAAADLDAPLVVVCYHGNSSQSAAAYFIQQGFSD 85
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPplpllellekLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
gi 15595786    86 VYSLDGGFELW 96
Cdd:pfam00581  81 VYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 18-102 6.29e-19

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: 74.80  E-value: 6.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786     18 ENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADF--------------IAAADLDAPLVVVCYHGNSSQSAAAYFIQQGF 83
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRrgeldilefeellkRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....*....
gi 15595786     84 SDVYSLDGGFELWRSVYPA 102
Cdd:smart00450  82 KNVYLLDGGYKEWSAAGPP 100
 
Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
3-108 5.03e-64

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 189.08  E-value: 5.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786    3 DTFQRIAPEQVRQLR-ENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQ 81
Cdd:PRK00162   2 DQFECINVEQAHQKLqEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQQ 81

                         90       100
                 ....*....|....*....|....*..
gi 15595786   82 GFSDVYSLDGGFELWRSVYPADTSSGE 108
Cdd:PRK00162  82 GFDVVYSIDGGFEAWRRTFPAEVASGA 108
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 7-97 1.94e-33

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: 111.58  E-value: 1.94e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   7 RIAPEQVRQLRENG--AQVVDIRDPQSFAV--GHISGSRHIDNHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQG 82
Cdd:cd01444   1 RISVDELAELLAAGeaPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                        90
                ....*....|....*
gi 15595786  83 FSDVYSLDGGFELWR 97
Cdd:cd01444  81 FTDVRSLAGGFEAWR 95
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 3-98 1.01e-32

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: 110.06  E-value: 1.01e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   3 DTFQRIAPEQVRQLREN-GAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQ 81
Cdd:COG0607   1 ASVKEISPAELAELLESeDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                        90
                ....*....|....*..
gi 15595786  82 GFSDVYSLDGGFELWRS 98
Cdd:COG0607  81 GYTNVYNLAGGIEAWKA 97
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 16-97 9.41e-25

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: 89.28  E-value: 9.41e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786  16 LRENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAADL--DAPLVVVCYHGNSSQSAAAYFIQQGFSDVYSLDGGF 93
Cdd:cd00158   6 LDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELdkDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGGM 85


                ....
gi 15595786  94 ELWR 97
Cdd:cd00158  86 LAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 16-96 1.51e-19

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: 76.37  E-value: 1.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786    16 LRENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADF----------IAAADLDAPLVVVCYHGNSSQSAAAYFIQQGFSD 85
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPplpllellekLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
gi 15595786    86 VYSLDGGFELW 96
Cdd:pfam00581  81 VYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 18-102 6.29e-19

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: 74.80  E-value: 6.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786     18 ENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADF--------------IAAADLDAPLVVVCYHGNSSQSAAAYFIQQGF 83
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRrgeldilefeellkRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....*....
gi 15595786     84 SDVYSLDGGFELWRSVYPA 102
Cdd:smart00450  82 KNVYLLDGGYKEWSAAGPP 100
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
6-98 1.54e-18

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 78.90  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786    6 QRIAPEQVRQLRENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAA--DLDAPLVVVCYHGNSSQSAAAYFIQQGF 83
Cdd:PRK08762   3 REISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIETHlpDRDREIVLICASGTRSAHAAATLRELGY 82

                         90
                 ....*....|....*
gi 15595786   84 SDVYSLDGGFELWRS 98
Cdd:PRK08762  83 TRVASVAGGFSAWKD 97
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 8-96 1.89e-15

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: 65.75  E-value: 1.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   8 IAPEQVRQLRENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQGFsDVY 87
Cdd:cd01524   1 VQWHELDNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGF-KVK 79


                ....*....
gi 15595786  88 SLDGGFELW 96
Cdd:cd01524  80 NLDGGYKTY 88
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 16-97 4.35e-13

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 60.06  E-value: 4.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786  16 LRENGA--QVVDIRDPQSFAVGHISGSRHIDnHSVADFIAAADLDAPLVVVCY----HGNSSQSAAAYFIQQGFsDVYSL 89
Cdd:cd01521  19 LKNGKPdfVLVDVRSAEAYARGHVPGAINLP-HREICENATAKLDKEKLFVVYcdgpGCNGATKAALKLAELGF-PVKEM 96


                ....*...
gi 15595786  90 DGGFELWR 97
Cdd:cd01521  97 IGGLDWWK 104
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 8-96 3.45e-12

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 57.79  E-value: 3.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   8 IAPEQVRQLRENGA---QVVDIRDPQSFAVGHISGSRHIDNHSV---ADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQ 81
Cdd:cd01528   2 ISVAELAEWLADEReepVLIDVREPEELEIAFLPGFLHLPMSEIperSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQ 81

                        90
                ....*....|....*
gi 15595786  82 GFSDVYSLDGGFELW 96
Cdd:cd01528  82 GFENVYNLQGGIDAW 96
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 20-97 2.22e-10

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 56.03  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   20 GAQVVDIRDPQSFAVGHISGSRH-----IDNHSVADFIAAADLdapLVVVCYHGNSSQSAAAYFIQQGFSDVYSLDGGFE 94
Cdd:PRK05597 274 GVTLIDVREPSEFAAYSIPGAHNvplsaIREGANPPSVSAGDE---VVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIE 350


                 ...
gi 15595786   95 LWR 97
Cdd:PRK05597 351 GWL 353
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 6-97 1.10e-09

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 51.54  E-value: 1.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   6 QRIAPEQVRQLRENGAQ--VVDIRDPQSFAVGHISGSRHIDNHSVADFIAA----------ADLDAPLVVVCYHGNSSQS 73
Cdd:cd01526   8 ERVSVKDYKNILQAGKKhvLLDVRPKVHFEICRLPEAINIPLSELLSKAAElkslqelpldNDKDSPIYVVCRRGNDSQT 87

                        90       100
                ....*....|....*....|....*
gi 15595786  74 AAAYFIQQGFS-DVYSLDGGFELWR 97
Cdd:cd01526  88 AVRKLKELGLErFVRDIIGGLKAWA 112
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 5-96 3.81e-09

Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).


Pssm-ID: 238720 [Multi-domain]  Cd Length: 113  Bit Score: 50.10  E-value: 3.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   5 FQRIAPEQVRQLRENGA-------QVVDIRDPQsFAVGHISGSRHIDNHSVADF----IAAADLDAPLVVVCYHGNSSQ- 72
Cdd:cd01443   1 LKYISPEELVALLENSDsnagkdfVVVDLRRDD-YEGGHIKGSINLPAQSCYQTlpqvYALFSLAGVKLAIFYCGSSQGr 79

                        90       100       110
                ....*....|....*....|....*....|..
gi 15595786  73 -SAAA-----YFIQQGFSD--VYSLDGGFELW 96
Cdd:cd01443  80 gPRAArwfadYLRKVGESLpkSYILTGGIKAW 111
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 11-98 4.74e-09

Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 49.60  E-value: 4.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786  11 EQVRQLRENGAQVVDIRDPQSFAVGHISGSRHIDNHSVA------DFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQGFS 84
Cdd:cd01529   3 ADWLGEHEPGTALLDVRAEDEYAAGHLPGKRSIPGAALVlrsqelQALEAPGRATRYVLTCDGSLLARFAAQELLALGGK 82

                        90
                ....*....|....
gi 15595786  85 DVYSLDGGFELWRS 98
Cdd:cd01529  83 PVALLDGGTSAWVA 96
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 8-97 3.01e-08

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: 47.42  E-value: 3.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   8 IAPEQVR-QLRENGAQVVDIRDPQSF-AVGHISGSRHIdNHSVADFIAAAD---------LDAPLVVVCYHGNSSQSAAA 76
Cdd:cd01447   1 LSPEDARaLLGSPGVLLVDVRDPRELeRTGMIPGAFHA-PRGMLEFWADPDspyhkpafaEDKPFVFYCASGWRSALAGK 79

                        90       100
                ....*....|....*....|.
gi 15595786  77 YFIQQGFSDVYSLDGGFELWR 97
Cdd:cd01447  80 TLQDMGLKPVYNIEGGFKDWK 100
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 8-100 4.26e-07

Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.


Pssm-ID: 238789 [Multi-domain]  Cd Length: 113  Bit Score: 44.71  E-value: 4.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   8 IAPEQVRQLRENGA---QVVDIRDpQSFAVGHISGSRHID----NHSVADFIAAADLDAPLVVVcYHGNSSQ----SAAA 76
Cdd:cd01531   4 ISPAQLKGWIRNGRppfQVVDVRD-EDYAGGHIKGSWHYPstrfKAQLNQLVQLLSGSKKDTVV-FHCALSQvrgpSAAR 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 15595786  77 YF--------IQQGFSDVYSLDGGFELWRSVY 100
Cdd:cd01531  82 KFlryldeedLETSKFEVYVLHGGFNAWESSY 113
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 6-97 1.08e-06

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, and similar uncharacterized putative rhodanese-related sulfurtransferases.


Pssm-ID: 238785 [Multi-domain]  Cd Length: 99  Bit Score: 43.24  E-value: 1.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   6 QRIAPEQVRQLRENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFIQQGFSD 85
Cdd:cd01527   2 TTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIFHCRSGMRTQQNAERLAAISAGE 81

                        90
                ....*....|..
gi 15595786  86 VYSLDGGFELWR 97
Cdd:cd01527  82 AYVLEGGLDAWK 93
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 21-94 2.46e-06

Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.


Pssm-ID: 238780 [Multi-domain]  Cd Length: 117  Bit Score: 42.70  E-value: 2.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786  21 AQVVDIR-DPQSFAVGHISGSRHIDNHSVADFI----------AAADLDAPLVVVCYHGNSSQSAAAYFIQQGFSDVYSL 89
Cdd:cd01522  16 AVLVDVRtEAEWKFVGGVPDAVHVAWQVYPDMEinpnflaeleEKVGKDRPVLLLCRSGNRSIAAAEAAAQAGFTNVYNV 95


                ....*
gi 15595786  90 DGGFE 94
Cdd:cd01522  96 LEGFE 100
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 8-96 1.43e-05

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 40.68  E-value: 1.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   8 IAPEQVRQ-LRENGAQVVDIRD-------PQSFAVGHISGSRHIDNHSVADfiAAADLDAPLV----------------- 62
Cdd:cd01448   2 VSPDWLAEhLDDPDVRILDARWylpdrdgRKEYLEGHIPGAVFFDLDEDLD--DKSPGPHMLPspeefaellgslgisnd 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15595786  63 --VVCYhGNSSQSAAAYFIQQ----GFSDVYSLDGGFELW 96
Cdd:cd01448  80 dtVVVY-DDGGGFFAARAWWTlryfGHENVRVLDGGLQAW 118
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 11-96 3.25e-05

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: 39.56  E-value: 3.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786  11 EQVRQLRENGAQV--VDIRDPQSFAVGHISGSRHI--DNHSVADFIAAAD-----------LDAPLVVVCYHGNSSQSAA 75
Cdd:cd01519   4 EEVKNLPNPHPNKvlIDVREPEELKTGKIPGAINIplSSLPDALALSEEEfekkygfpkpsKDKELIFYCKAGVRSKAAA 83

                        90       100
                ....*....|....*....|.
gi 15595786  76 AYFIQQGFSDVYSLDGGFELW 96
Cdd:cd01519  84 ELARSLGYENVGNYPGSWLDW 104
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 23-97 1.20e-04

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 39.39  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786  23 VVDIR-----DPQSFAVGHISGSRHID-NHSVADfiAAADLDAPLV-------------------VVCYhGNSSQSAAAY 77
Cdd:COG2897  12 ILDVRwdlpdGRAAYEAGHIPGAVFLDlDTDLSD--PRSPGRHPLPspeafaallgalgisndttVVVY-DDGGGLFAAR 88

                        90       100
                ....*....|....*....|....
gi 15595786  78 FIQQ----GFSDVYSLDGGFELWR 97
Cdd:COG2897  89 AWWLlryaGHEDVRVLDGGLAAWK 112
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 8-98 2.74e-04

Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 3rd repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238792 [Multi-domain]  Cd Length: 95  Bit Score: 37.06  E-value: 2.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   8 IAPEQVRQLRENGAQVV---DIRDPQSFAVGHISGSRHIDNhsvADFIAAADLDAP-----LVVVCYHGNSSQSAAAYFI 79
Cdd:cd01534   1 IGAAELARWAAEGDRTVyrfDVRTPEEYEAGHLPGFRHTPG---GQLVQETDHFAPvrgarIVLADDDGVRADMTASWLA 77

                        90
                ....*....|....*....
gi 15595786  80 QQGFsDVYSLDGGFELWRS 98
Cdd:cd01534  78 QMGW-EVYVLEGGLAAALA 95
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 8-92 3.30e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 36.79  E-value: 3.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   8 IAPEQVRQLRENGAQVV-DIRDPQSFAVGHISGSRHIDNHSVADFIAAAD--LDA----PLVVVCYHGNSSQSAAAYFIQ 80
Cdd:cd01518   4 LSPAEWNELLEDPEVVLlDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDenLDLlkgkKVLMYCTGGIRCEKASAYLKE 83

                        90
                ....*....|..
gi 15595786  81 QGFSDVYSLDGG 92
Cdd:cd01518  84 RGFKNVYQLKGG 95
RHOD_Kc cd01525
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the ...
 23-94 4.02e-04

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the rhodanese-like domains found C-terminal of the serine/threonine protein kinases catalytic (S_TKc) domain and the Tre-2, BUB2p, Cdc16p (TBC) domain. The putative active site Cys residue is not present in this CD.


Pssm-ID: 238783 [Multi-domain]  Cd Length: 105  Bit Score: 36.66  E-value: 4.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786  23 VVDIRDPQSFAVGHISGSRHIDNHSVadFIAAADLDA-----------PLVVVCYhGNSSQSA---AAYFIQQGFSDVYS 88
Cdd:cd01525  19 AVDIRSSPDFRRGHIEGSINIPFSSV--FLKEGELEQlptvprlenykGKIIVIV-SHSHKHAalfAAFLVKCGVPRVCI 95


                ....*.
gi 15595786  89 LDGGFE 94
Cdd:cd01525  96 LDGGIN 101
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
2-92 4.74e-04

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 37.90  E-value: 4.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786    2 SDTFQRIAPEQVRQ-LRENGAQVVDIRDPQSFAVGHISGSRHIDNHSVADFIAAAD------LDAPLVVVCYHGNSSQSA 74
Cdd:PRK00142 108 ENVGTYLKPKEVNElLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPPWVEenldplKDKKVVMYCTGGIRCEKA 187

                         90
                 ....*....|....*...
gi 15595786   75 AAYFIQQGFSDVYSLDGG 92
Cdd:PRK00142 188 SAWMKHEGFKEVYQLEGG 205
COG5350 COG5350
Predicted protein tyrosine phosphatase [General function prediction only];
25-79 6.62e-04

Predicted protein tyrosine phosphatase [General function prediction only];


Pssm-ID: 444131  Cd Length: 165  Bit Score: 36.76  E-value: 6.62e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15595786  25 DIRDPQSfavGHI-SGSRHIdnHSVADFIAAADLDAPLVVVCYHGNSSQSAAAYFI 79
Cdd:COG5350  52 DIIEPMP---GLIlPTEEHV--EALLAFGRDWDREAPLLVHCHAGISRSTAAALIA 102
TrhO COG1054
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
 74-92 1.56e-03

tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 36.27  E-value: 1.56e-03
                        10
                ....*....|....*....
gi 15595786  74 AAAYFIQQGFSDVYSLDGG 92
Cdd:COG1054 186 ASAYLKEQGFEEVYQLEGG 204
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 8-98 3.02e-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: 34.53  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   8 IAPEQVRQ-LRENGAQVVDIRDPQSFA-----------VGHISGSRHIDNHSVAD-------------FIAAA--DLDAP 60
Cdd:cd01449   1 VTAEEVLAnLDSGDVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWTSLLDedgtfkspeelraLFAALgiTPDKP 80

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15595786  61 LVVVCYHGNSSQSAAAYFIQQGFSDVYSLDGGFELWRS 98
Cdd:cd01449  81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 13-101 3.02e-03

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 34.95  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786  13 VRQLRENGAQ--VVDIRDPQSFAVGHISGSRHI------------DNHSVADFIAAA------DLDAPLVVVCYHGNSSQ 72
Cdd:cd01446   8 AALLREGGERllLLDCRPFLEYSSSHIRGAVNVccptilrrrlqgGKILLQQLLSCPedrdrlRRGESLAVVVYDESSSD 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15595786  73 ------SAAAYFI-------QQGFSDVYSLDGGFELWRSVYP 101
Cdd:cd01446  88 rerlreDSTAESVlgkllrkLQEGCSVYLLKGGFEQFSSEFP 129
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 15-109 4.72e-03

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 34.78  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595786   15 QLRENGAQVVDI--------RDP-QSFAVGHISGSRHIDNHSVAD--------------FIAAA---DLDAPLVVVCYHG 68
Cdd:PLN02723  32 NLREPDVKVLDAswympdeqRNPiQEYQVAHIPGALFFDLDGISDrttdlphmlpseeaFAAAVsalGIENKDGVVVYDG 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15595786   69 NSSQSAAA---YFIQQGFSDVYSLDGGFELWR-SVYPADTS-SGEA 109
Cdd:PLN02723 112 KGIFSAARvwwMFRVFGHEKVWVLDGGLPKWRaSGYDVESSaSGDA 157
 
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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