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Conserved domains on  [gi|15833522|ref|NP_312295|]
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thiosulfate:cyanide sulfurtransferase [Escherichia coli O157:H7 str. Sakai]

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;
1-108 4.38e-73

thiosulfate sulfurtransferase GlpE;


:

Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 212.19  E-value: 4.38e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522    1 MDQFECINVADAHQKLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQ 80
Cdd:PRK00162   1 MDQFECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*...
gi 15833522   81 QGYDVVYSIDGGFEAWQRQFPAEVAYGA 108
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVASGA 108
 
Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-108 4.38e-73

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 212.19  E-value: 4.38e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522    1 MDQFECINVADAHQKLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQ 80
Cdd:PRK00162   1 MDQFECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*...
gi 15833522   81 QGYDVVYSIDGGFEAWQRQFPAEVAYGA 108
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVASGA 108
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 6-98 3.57e-40

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: 128.53  E-value: 3.57e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522   6 CINVADAHQKLQ-EKEAVLVDIRDPQSFAM--GHAVQAFHLTNDTLGAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQQG 82
Cdd:cd01444   1 RISVDELAELLAaGEAPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                        90
                ....*....|....*.
gi 15833522  83 YDVVYSIDGGFEAWQR 98
Cdd:cd01444  81 FTDVRSLAGGFEAWRR 96
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 2-99 2.13e-30

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: 103.89  E-value: 2.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522   2 DQFECINVADAHQKLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQQ 81
Cdd:COG0607   1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                        90
                ....*....|....*...
gi 15833522  82 GYDVVYSIDGGFEAWQRQ 99
Cdd:COG0607  81 GYTNVYNLAGGIEAWKAA 98
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 17-102 1.54e-18

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: 73.65  E-value: 1.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522     17 QEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRNNDF--------------DTPVMVMCYHGNSSKGAAQYLLQQG 82
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIlefeellkrlgldkDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 15833522     83 YDVVYSIDGGFEAWQRQFPA 102
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 16-97 2.90e-14

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: 62.50  E-value: 2.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522    16 LQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAF----------MRNNDFDTPVMVMCYHGNSSKGAAQYLLQQGYDV 85
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPplpllellekLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|..
gi 15833522    86 VYSIDGGFEAWQ 97
Cdd:pfam00581  81 VYVLDGGFEAWK 92
 
Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-108 4.38e-73

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 212.19  E-value: 4.38e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522    1 MDQFECINVADAHQKLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQ 80
Cdd:PRK00162   1 MDQFECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*...
gi 15833522   81 QGYDVVYSIDGGFEAWQRQFPAEVAYGA 108
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVASGA 108
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 6-98 3.57e-40

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: 128.53  E-value: 3.57e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522   6 CINVADAHQKLQ-EKEAVLVDIRDPQSFAM--GHAVQAFHLTNDTLGAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQQG 82
Cdd:cd01444   1 RISVDELAELLAaGEAPVLLDVRDPASYAAlpDHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                        90
                ....*....|....*.
gi 15833522  83 YDVVYSIDGGFEAWQR 98
Cdd:cd01444  81 FTDVRSLAGGFEAWRR 96
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 2-99 2.13e-30

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: 103.89  E-value: 2.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522   2 DQFECINVADAHQKLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQQ 81
Cdd:COG0607   1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                        90
                ....*....|....*...
gi 15833522  82 GYDVVYSIDGGFEAWQRQ 99
Cdd:COG0607  81 GYTNVYNLAGGIEAWKAA 98
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 11-97 1.33e-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: 86.20  E-value: 1.33e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522  11 DAHQKLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTL--GAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQQGYDVVYS 88
Cdd:cd00158   1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELeeRAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYN 80


                ....*....
gi 15833522  89 IDGGFEAWQ 97
Cdd:cd00158  81 LEGGMLAWK 89
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 17-102 1.54e-18

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: 73.65  E-value: 1.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522     17 QEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRNNDF--------------DTPVMVMCYHGNSSKGAAQYLLQQG 82
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIlefeellkrlgldkDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 15833522     83 YDVVYSIDGGFEAWQRQFPA 102
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
7-104 1.59e-18

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 78.51  E-value: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522    7 INVADAHQKLQEKeAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRNN--DFDTPVMVMCYHGNSSKGAAQYLLQQGYD 84
Cdd:PRK08762   5 ISPAEARARAAQG-AVLIDVREAHERASGQAEGALRIPRGFLELRIETHlpDRDREIVLICASGTRSAHAAATLRELGYT 83

                         90       100
                 ....*....|....*....|.
gi 15833522   85 VVYSIDGGFEAWQRQ-FPAEV 104
Cdd:PRK08762  84 RVASVAGGFSAWKDAgLPLER 104
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 16-97 2.90e-14

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: 62.50  E-value: 2.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522    16 LQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAF----------MRNNDFDTPVMVMCYHGNSSKGAAQYLLQQGYDV 85
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPplpllellekLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|..
gi 15833522    86 VYSIDGGFEAWQ 97
Cdd:pfam00581  81 VYVLDGGFEAWK 92
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 7-99 2.85e-13

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: 60.49  E-value: 2.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522   7 INVADAHQKLQE--KEAVLVDIRDPQSFAMGHAVQAFHLTndtLGAF-MRNNDFDT-----PVMVMCYHGNSSKGAAQYL 78
Cdd:cd01528   2 ISVAELAEWLADerEEPVLIDVREPEELEIAFLPGFLHLP---MSEIpERSKELDSdnpdkDIVVLCHHGGRSMQVAQWL 78

                        90       100
                ....*....|....*....|.
gi 15833522  79 LQQGYDVVYSIDGGFEAWQRQ 99
Cdd:cd01528  79 LRQGFENVYNLQGGIDAWSLE 99
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 7-98 1.22e-11

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: 56.28  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522   7 INVADAHQKLQEKEAVLVDIRDPQSF-AMGHAVQAFHLTNDTL------------GAFMRnndfDTPVMVMCYHGNSSKG 73
Cdd:cd01447   1 LSPEDARALLGSPGVLLVDVRDPRELeRTGMIPGAFHAPRGMLefwadpdspyhkPAFAE----DKPFVFYCASGWRSAL 76

                        90       100
                ....*....|....*....|....*
gi 15833522  74 AAQYLLQQGYDVVYSIDGGFEAWQR 98
Cdd:cd01447  77 AGKTLQDMGLKPVYNIEGGFKDWKE 101
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 10-94 1.04e-09

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: 51.56  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522  10 ADAHQKLQEKE-AVLVDIR-DPQSFAMGHAVQAFHLTNDTLGAFMRNNDF----------DTPVMVMCYHGNSSKGAAQY 77
Cdd:cd01522   4 AEAWALLQADPqAVLVDVRtEAEWKFVGGVPDAVHVAWQVYPDMEINPNFlaeleekvgkDRPVLLLCRSGNRSIAAAEA 83

                        90
                ....*....|....*..
gi 15833522  78 LLQQGYDVVYSIDGGFE 94
Cdd:cd01522  84 AAQAGFTNVYNVLEGFE 100
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 15-98 2.08e-09

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: 49.96  E-value: 2.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522  15 KLQEKEAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQQGYDvVYSIDGGFE 94
Cdd:cd01524   8 NYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFK-VKNLDGGYK 86


                ....
gi 15833522  95 AWQR 98
Cdd:cd01524  87 TYST 90
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 3-98 5.86e-09

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: 49.27  E-value: 5.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522   3 QFEcINVADAHQKLQEKEA--VLVDIRDPQSFAMGHAVQAFHLTNDTLGA-FMRNNDFDTPVMVMCY--HGNSSKGAAQY 77
Cdd:cd01521   7 AFE-TDCWDVAIALKNGKPdfVLVDVRSAEAYARGHVPGAINLPHREICEnATAKLDKEKLFVVYCDgpGCNGATKAALK 85

                        90       100
                ....*....|....*....|.
gi 15833522  78 LLQQGYDVVYSIdGGFEAWQR 98
Cdd:cd01521  86 LAELGFPVKEMI-GGLDWWKR 105
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 16-97 2.83e-08

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: 47.10  E-value: 2.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522  16 LQEKEAVLVDIRDPQSFAMGHAVQA--FHLTNDTLGAFMRNNDFDTPVMVMCYHGNS--SKGAAQYLLQQGYDVVYSIDG 91
Cdd:cd01532   6 LAREEIALIDVREEDPFAQSHPLWAanLPLSRLELDAWVRIPRRDTPIVVYGEGGGEdlAPRAARRLSELGYTDVALLEG 85


                ....*.
gi 15833522  92 GFEAWQ 97
Cdd:cd01532  86 GLQGWR 91
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 5-101 5.62e-08

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: 47.30  E-value: 5.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522   5 ECINVADAHQKLQE-KEAVLVDIRDPQSFAMGHAVQAFHLTndtLGAFMR-------------NNDFDTPVMVMCYHGNS 70
Cdd:cd01526   8 ERVSVKDYKNILQAgKKHVLLDVRPKVHFEICRLPEAINIP---LSELLSkaaelkslqelplDNDKDSPIYVVCRRGND 84

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15833522  71 SKGAAQYLLQQGYDV-VYSIDGGFEAWQRQ----FP 101
Cdd:cd01526  85 SQTAVRKLKELGLERfVRDIIGGLKAWADKvdptFP 120
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 7-96 2.32e-07

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: 45.17  E-value: 2.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522   7 INVADAHQKLQEKeAVLVDIRDPQSFAMGHAVQAFHLTNDTLGAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQQGYDVV 86
Cdd:cd01527   4 ISPNDACELLAQG-AVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIFHCRSGMRTQQNAERLAAISAGEA 82

                        90
                ....*....|
gi 15833522  87 YSIDGGFEAW 96
Cdd:cd01527  83 YVLEGGLDAW 92
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 14-96 7.73e-07

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: 43.82  E-value: 7.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522  14 QKLQEKEAVLVDIRDPQSFAMGHAVQAFH-------LTNDTLGAFMRNnDFDTPVMVMCYHGNSSKGAAQYLLQQGYDVV 86
Cdd:cd01529   6 LGEHEPGTALLDVRAEDEYAAGHLPGKRSipgaalvLRSQELQALEAP-GRATRYVLTCDGSLLARFAAQELLALGGKPV 84

                        90
                ....*....|
gi 15833522  87 YSIDGGFEAW 96
Cdd:cd01529  85 ALLDGGTSAW 94
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 21-97 7.74e-06

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 42.94  E-value: 7.74e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833522   21 AVLVDIRDPQSFAMGHAVQAFHLTNDTL--GAFMRNNDFDTPVMVMCYHGNSSKGAAQYLLQQGYDVVYSIDGGFEAWQ 97
Cdd:PRK05597 275 VTLIDVREPSEFAAYSIPGAHNVPLSAIreGANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGWL 353
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 10-92 3.05e-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: 3.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522  10 ADAHQKLQEKEAVLVDIRDPQSFAMGH-------AVQAFHLTNDTLGAFMrnNDF-DTPVMVMCYHGNSSKGAAQYLLQQ 81
Cdd:cd01518   7 AEWNELLEDPEVVLLDVRNDYEYDIGHfkgavnpDVDTFREFPFWLDENL--DLLkGKKVLMYCTGGIRCEKASAYLKER 84

                        90
                ....*....|.
gi 15833522  82 GYDVVYSIDGG 92
Cdd:cd01518  85 GFKNVYQLKGG 95
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 19-98 6.23e-04

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: 36.23  E-value: 6.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522  19 KEAVLVDIRDPQsFAMGHAVQAFHL----TNDTLGAFMRNNDFDTPVMVMCYHGNSS----KGA---AQYLLQQGYDV-- 85
Cdd:cd01443  22 KDFVVVDLRRDD-YEGGHIKGSINLpaqsCYQTLPQVYALFSLAGVKLAIFYCGSSQgrgpRAArwfADYLRKVGESLpk 100

                        90
                ....*....|...
gi 15833522  86 VYSIDGGFEAWQR 98
Cdd:cd01443 101 SYILTGGIKAWYH 113
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
10-92 1.00e-03

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 36.75  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522   10 ADAHQKLQEKEAVLVDIRDPQSFAMGH---AV----QAFHltnDTLGAFMRNNDF--DTPVMVMCYHGNSSKGAAQYLLQ 80
Cdd:PRK00142 117 KEVNELLDDPDVVFIDMRNDYEYEIGHfenAIepdiETFR---EFPPWVEENLDPlkDKKVVMYCTGGIRCEKASAWMKH 193

                         90
                 ....*....|..
gi 15833522   81 QGYDVVYSIDGG 92
Cdd:PRK00142 194 EGFKEVYQLEGG 205
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 18-97 1.16e-03

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: 35.32  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833522  18 EKEAVLVDIRDPQSFAMGH-----------AVQAFHLTNDtlgAFMRNNDF-----DTPVMVMCYHGNSSKGAAQYLLQQ 81
Cdd:cd01519  13 HPNKVLIDVREPEELKTGKipgainiplssLPDALALSEE---EFEKKYGFpkpskDKELIFYCKAGVRSKAAAELARSL 89

                        90
                ....*....|....*.
gi 15833522  82 GYDVVYSIDGGFEAWQ 97
Cdd:cd01519  90 GYENVGNYPGSWLDWA 105
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 58-98 3.05e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with rhodanese-like domains found N-terminal of the metallo-beta-lactamase domain.


Pssm-ID: 238781 [Multi-domain]  Cd Length: 100  Bit Score: 34.39  E-value: 3.05e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 15833522  58 DTPVMVMCYHGNSSKGAAQYLLQQGYDVVYsIDGGFEAWQR 98
Cdd:cd01523  61 DQEVTVICAKEGSSQFVAELLAERGYDVDY-LAGGMKAWSE 100
 
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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