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Conserved domains on  [gi|759549475|ref|WP_043269294|]
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MULTISPECIES: thiosulfate sulfurtransferase GlpE [Pseudomonas]

Protein Classification

thiosulfate sulfurtransferase GlpE( domain architecture ID 10791817)

thiosulfate sulfurtransferase GlpE catalyzes the sulfur transfer reaction from thiosulfate to cyanide

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-106 3.82e-65

thiosulfate sulfurtransferase GlpE;


:

Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 192.16  E-value: 3.82e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   1 MSEFKRIAPEQAHQLR-QAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQADLDAPLLVFCYHGNSSQSAAAYFVQ 79
Cdd:PRK00162   1 MDQFECINVEQAHQKLqEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*..
gi 759549475  80 QGFTDVYSVDGGFELWRSVYPADTSSG 106
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVASG 107
 
Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-106 3.82e-65

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 192.16  E-value: 3.82e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   1 MSEFKRIAPEQAHQLR-QAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQADLDAPLLVFCYHGNSSQSAAAYFVQ 79
Cdd:PRK00162   1 MDQFECINVEQAHQKLqEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*..
gi 759549475  80 QGFTDVYSVDGGFELWRSVYPADTSSG 106
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVASG 107
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 6-96 2.03e-34

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: 113.90  E-value: 2.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   6 RIAPEQAHQLRQAG--AQVVDIRDPQSYAM--GHVTGSRHIDNYSVADFIRQADLDAPLLVFCYHGNSSQSAAAYFVQQG 81
Cdd:cd01444    1 RISVDELAELLAAGeaPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                         90
                 ....*....|....*
gi 759549475  82 FTDVYSVDGGFELWR 96
Cdd:cd01444   81 FTDVRSLAGGFEAWR 95
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 2-97 5.13e-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: 108.13  E-value: 5.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   2 SEFKRIAPEQAHQ-LRQAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQADLDAPLLVFCYHGNSSQSAAAYFVQQ 80
Cdd:COG0607    1 ASVKEISPAELAElLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                         90
                 ....*....|....*..
gi 759549475  81 GFTDVYSVDGGFELWRS 97
Cdd:COG0607   81 GYTNVYNLAGGIEAWKA 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 15-95 1.08e-17

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: 71.36  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   15 LRQAGAQVVDIRDPQSYAMGHVTGSRHID----NYSVADF------IRQADLDAPLLVFCYHGNSSQSAAAYFVQQGFTD 84
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPlsslSLPPLPLlellekLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
gi 759549475   85 VYSVDGGFELW 95
Cdd:pfam00581  81 VYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 17-101 2.40e-17

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: 70.95  E-value: 2.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475    17 QAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQ--------------ADLDAPLLVFCYHGNSSQSAAAYFVQQGF 82
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeellkrlgLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....*....
gi 759549475    83 TDVYSVDGGFELWRSVYPA 101
Cdd:smart00450  82 KNVYLLDGGYKEWSAAGPP 100
 
Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-106 3.82e-65

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 192.16  E-value: 3.82e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   1 MSEFKRIAPEQAHQLR-QAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQADLDAPLLVFCYHGNSSQSAAAYFVQ 79
Cdd:PRK00162   1 MDQFECINVEQAHQKLqEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*..
gi 759549475  80 QGFTDVYSVDGGFELWRSVYPADTSSG 106
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVASG 107
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 6-96 2.03e-34

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: 113.90  E-value: 2.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   6 RIAPEQAHQLRQAG--AQVVDIRDPQSYAM--GHVTGSRHIDNYSVADFIRQADLDAPLLVFCYHGNSSQSAAAYFVQQG 81
Cdd:cd01444    1 RISVDELAELLAAGeaPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                         90
                 ....*....|....*
gi 759549475  82 FTDVYSVDGGFELWR 96
Cdd:cd01444   81 FTDVRSLAGGFEAWR 95
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 2-97 5.13e-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: 108.13  E-value: 5.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   2 SEFKRIAPEQAHQ-LRQAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQADLDAPLLVFCYHGNSSQSAAAYFVQQ 80
Cdd:COG0607    1 ASVKEISPAELAElLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                         90
                 ....*....|....*..
gi 759549475  81 GFTDVYSVDGGFELWRS 97
Cdd:COG0607   81 GYTNVYNLAGGIEAWKA 97
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 15-96 1.17e-23

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: 86.58  E-value: 1.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475  15 LRQAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQADL--DAPLLVFCYHGNSSQSAAAYFVQQGFTDVYSVDGGF 92
Cdd:cd00158    6 LDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELdkDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGGM 85


                 ....
gi 759549475  93 ELWR 96
Cdd:cd00158   86 LAWK 89
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
3-97 2.37e-19

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 80.83  E-value: 2.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   3 EFKRIAPEQAHQLRQAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQA--DLDAPLLVFCYHGNSSQSAAAYFVQQ 80
Cdd:PRK08762   1 SIREISPAEARARAAQGAVLIDVREAHERASGQAEGALRIPRGFLELRIETHlpDRDREIVLICASGTRSAHAAATLREL 80

                         90
                 ....*....|....*..
gi 759549475  81 GFTDVYSVDGGFELWRS 97
Cdd:PRK08762  81 GYTRVASVAGGFSAWKD 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 15-95 1.08e-17

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: 71.36  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   15 LRQAGAQVVDIRDPQSYAMGHVTGSRHID----NYSVADF------IRQADLDAPLLVFCYHGNSSQSAAAYFVQQGFTD 84
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPlsslSLPPLPLlellekLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|.
gi 759549475   85 VYSVDGGFELW 95
Cdd:pfam00581  81 VYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 17-101 2.40e-17

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: 70.95  E-value: 2.40e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475    17 QAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQ--------------ADLDAPLLVFCYHGNSSQSAAAYFVQQGF 82
Cdd:smart00450   2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeellkrlgLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81

                           90
                   ....*....|....*....
gi 759549475    83 TDVYSVDGGFELWRSVYPA 101
Cdd:smart00450  82 KNVYLLDGGYKEWSAAGPP 100
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 7-95 7.06e-11

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: 54.32  E-value: 7.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   7 IAPEQAHQLRQ---AGAQVVDIRDPQSYAMGHVTGSRHIDNYSV---ADFIRQADLDAPLLVFCYHGNSSQSAAAYFVQQ 80
Cdd:cd01528    2 ISVAELAEWLAderEEPVLIDVREPEELEIAFLPGFLHLPMSEIperSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQ 81

                         90
                 ....*....|....*
gi 759549475  81 GFTDVYSVDGGFELW 95
Cdd:cd01528   82 GFENVYNLQGGIDAW 96
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 7-95 7.52e-11

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: 53.81  E-value: 7.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   7 IAPEQAHQLRQAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQADLDAPLLVFCYHGNSSQSAAAYFVQQGFtDVY 86
Cdd:cd01524    1 VQWHELDNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGF-KVK 79


                 ....*....
gi 759549475  87 SVDGGFELW 95
Cdd:cd01524   80 NLDGGYKTY 88
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 7-93 2.24e-10

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: 53.49  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   7 IAPEQAHQLRQAG--AQVVDIR-DPQSYAMGHVTGSRHIDNYSVADFIR----------QADLDAPLLVFCYHGNSSQSA 73
Cdd:cd01522    1 LTPAEAWALLQADpqAVLVDVRtEAEWKFVGGVPDAVHVAWQVYPDMEInpnflaeleeKVGKDRPVLLLCRSGNRSIAA 80

                         90       100
                 ....*....|....*....|
gi 759549475  74 AAYFVQQGFTDVYSVDGGFE 93
Cdd:cd01522   81 AEAAAQAGFTNVYNVLEGFE 100
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 18-96 5.44e-10

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: 51.97  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475  18 AGAQVVDIRDPQSYAMGHVTGSRHIDNYSVaDFIRQADLDA--PLLVFCY--HGNSSQSAAAYFVQQGFtDVYSVDGGFE 93
Cdd:cd01521   24 PDFVLVDVRSAEAYARGHVPGAINLPHREI-CENATAKLDKekLFVVYCDgpGCNGATKAALKLAELGF-PVKEMIGGLD 101


                 ...
gi 759549475  94 LWR 96
Cdd:cd01521  102 WWK 104
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 19-96 1.38e-08

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 50.64  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475  19 GAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQADLDAP--LLVFCYHGNSSQSAAAYFVQQGFTDVYSVDGGFELWR 96
Cdd:PRK05597 274 GVTLIDVREPSEFAAYSIPGAHNVPLSAIREGANPPSVSAGdeVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGWL 353
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 7-96 2.29e-07

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: 45.11  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   7 IAPEQA-HQLRQAGAQVVDIRDPQSY-AMGHVTGSRHI-----------DNYSVADFIRQadlDAPLLVFCYHGNSSQSA 73
Cdd:cd01447    1 LSPEDArALLGSPGVLLVDVRDPRELeRTGMIPGAFHAprgmlefwadpDSPYHKPAFAE---DKPFVFYCASGWRSALA 77

                         90       100
                 ....*....|....*....|...
gi 759549475  74 AAYFVQQGFTDVYSVDGGFELWR 96
Cdd:cd01447   78 GKTLQDMGLKPVYNIEGGFKDWK 100
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 5-96 2.09e-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: 42.47  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   5 KRIAPEQAHQLRQAGAQVVDIRDPQSYAMGHVTGSRHIDNYSVADFIRQADlDAPLLVF-CYHGNSSQSAAAYFVQQGFT 83
Cdd:cd01527    2 TTISPNDACELLAQGAVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLV-GANAIIFhCRSGMRTQQNAERLAAISAG 80

                         90
                 ....*....|...
gi 759549475  84 DVYSVDGGFELWR 96
Cdd:cd01527   81 EAYVLEGGLDAWK 93
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 6-96 2.93e-06

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: 42.68  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   6 RIAPEQAHQLRQAGAQ--VVDIRDPQSYAMGHVTGSRHI-------DNYSVADFIR---QADLDAPLLVFCYHGNSSQSA 73
Cdd:cd01526    9 RVSVKDYKNILQAGKKhvLLDVRPKVHFEICRLPEAINIplsellsKAAELKSLQElplDNDKDSPIYVVCRRGNDSQTA 88

                         90       100
                 ....*....|....*....|....
gi 759549475  74 AAYFVQQGFT-DVYSVDGGFELWR 96
Cdd:cd01526   89 VRKLKELGLErFVRDIIGGLKAWA 112
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 19-97 5.56e-06

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: 41.51  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475  19 GAQVVDIRDPQSYAMGHVTGSRHIDNYSVA------DFIRQADLDAPLLVFCYHGNSSQSAAAYFVQQGFTDVYSVDGGF 92
Cdd:cd01529   12 GTALLDVRAEDEYAAGHLPGKRSIPGAALVlrsqelQALEAPGRATRYVLTCDGSLLARFAAQELLALGGKPVALLDGGT 91


                 ....*
gi 759549475  93 ELWRS 97
Cdd:cd01529   92 SAWVA 96
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 5-99 1.79e-05

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: 40.47  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   5 KRIAPEQAHQLRQAGA---QVVDIRDpQSYAMGHVTGSRHIDNYSVADFIRQ-----ADLDAPLLVFcyHGNSSQ----S 72
Cdd:cd01531    2 SYISPAQLKGWIRNGRppfQVVDVRD-EDYAGGHIKGSWHYPSTRFKAQLNQlvqllSGSKKDTVVF--HCALSQvrgpS 78

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 759549475  73 AAAYFV--------QQGFTDVYSVDGGFELWRSVY 99
Cdd:cd01531   79 AARKFLryldeedlETSKFEVYVLHGGFNAWESSY 113
COG5350 COG5350
Predicted protein tyrosine phosphatase [General function prediction only];
24-76 2.48e-05

Predicted protein tyrosine phosphatase [General function prediction only];


Pssm-ID: 444131  Cd Length: 165  Bit Score: 40.61  E-value: 2.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 759549475  24 DIRDPQsyaMGHVT-GSRHIDnySVADFIRQADLDAPLLVFCYHGNSSQSAAAY 76
Cdd:COG5350   52 DIIEPM---PGLILpTEEHVE--ALLAFGRDWDREAPLLVHCHAGISRSTAAAL 100
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 22-97 9.42e-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: 35.52  E-value: 9.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475  22 VVDIRDPQSYAMGHVTGSRHidnYSVADFIRQADLDAP-----LLVFCYHGNSSQSAAAYFVQQGFtDVYSVDGGFELWR 96
Cdd:cd01534   19 RFDVRTPEEYEAGHLPGFRH---TPGGQLVQETDHFAPvrgarIVLADDDGVRADMTASWLAQMGW-EVYVLEGGLAAAL 94


                 .
gi 759549475  97 S 97
Cdd:cd01534   95 A 95
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 7-91 1.47e-03

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: 35.25  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475   7 IAPEQAHQLRQAGAQVV-DIRDPQSYAMGHVTGSRHIDNYSVADFIRQAD--LDA----PLLVFCYHGNSSQSAAAYFVQ 79
Cdd:cd01518    4 LSPAEWNELLEDPEVVLlDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDenLDLlkgkKVLMYCTGGIRCEKASAYLKE 83

                         90
                 ....*....|..
gi 759549475  80 QGFTDVYSVDGG 91
Cdd:cd01518   84 RGFKNVYQLKGG 95
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 11-97 3.07e-03

Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 1st repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238790 [Multi-domain]  Cd Length: 92  Bit Score: 34.00  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475  11 QAHQLRQAGAQVVDIRDPQSYAMGH--VTGSRHIDNYSVADFIRQADLDAPLLVFCYHGNS--SQSAAAYFVQQGFTDVY 86
Cdd:cd01532    2 RQALLAREEIALIDVREEDPFAQSHplWAANLPLSRLELDAWVRIPRRDTPIVVYGEGGGEdlAPRAARRLSELGYTDVA 81

                         90
                 ....*....|.
gi 759549475  87 SVDGGFELWRS 97
Cdd:cd01532   82 LLEGGLQGWRA 92
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 13-97 5.24e-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: 33.76  E-value: 5.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475  13 HQLRQAGAQVVDIRDPQSYA-----------MGHVTGSRHIDNYSV---------ADFIRQA------DLDAPLLVFCYH 66
Cdd:cd01449    8 ANLDSGDVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWTSLldedgtfksPEELRALfaalgiTPDKPVIVYCGS 87

                         90       100       110
                 ....*....|....*....|....*....|.
gi 759549475  67 GNSSQSAAAYFVQQGFTDVYSVDGGFELWRS 97
Cdd:cd01449   88 GVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 23-90 8.07e-03

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 33.28  E-value: 8.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 759549475  23 VDIRDPQSYAMGHVTGSRHIDNYSVADFIRQA--DLDAPLLVFCYHGNSSQSAAAYFVQQGFTDVYSVDG 90
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAvpDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAENAGG 93
 
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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