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Conserved domains on  [gi|515672126|ref|WP_017104726|]
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MULTISPECIES: thiosulfate sulfurtransferase GlpE [Vibrio]

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;
1-105 1.96e-68

thiosulfate sulfurtransferase GlpE;


:

Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 200.25  E-value: 1.96e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   1 MDQFKHIDVKGAQALIEQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVN 80
Cdd:PRK00162   1 MDQFECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*
gi 515672126  81 QGFEEVYSVDGGFEAWHRAELPVNA 105
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVA 105
 
Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-105 1.96e-68

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 200.25  E-value: 1.96e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   1 MDQFKHIDVKGAQALIEQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVN 80
Cdd:PRK00162   1 MDQFECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*
gi 515672126  81 QGFEEVYSVDGGFEAWHRAELPVNA 105
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVA 105
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 2-103 2.08e-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: 108.90  E-value: 2.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   2 DQFKHIDVKGAQALIEQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVNQ 81
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                         90       100
                 ....*....|....*....|..
gi 515672126  82 GFEEVYSVDGGFEAWHRAELPV 103
Cdd:COG0607   81 GYTNVYNLAGGIEAWKAAGLPV 102
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 6-98 2.68e-31

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: 105.81  E-value: 2.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   6 HIDVKGAQALIEQGE-ARLVDIRDPQSFAVA--HSKTAYHLTNDTMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVNQG 82
Cdd:cd01444    1 RISVDELAELLAAGEaPVLLDVRDPASYAALpdHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                         90
                 ....*....|....*.
gi 515672126  83 FEEVYSVDGGFEAWHR 98
Cdd:cd01444   81 FTDVRSLAGGFEAWRR 96
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 17-102 3.41e-16

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: 67.87  E-value: 3.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126    17 EQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEF--------------EQPILVMCYHGISSQGAAQYLVNQG 82
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIlefeellkrlgldkDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 515672126    83 FEEVYSVDGGFEAWHRAELP 102
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 16-97 2.23e-15

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: 65.58  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   16 IEQGEARLVDIRDPQSFAVAHSKTAYHL----TNDTMVSFMDEVEF------EQPILVMCYHGISSQGAAQYLVNQGFEE 85
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVplssLSLPPLPLLELLEKllellkDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|..
gi 515672126   86 VYSVDGGFEAWH 97
Cdd:pfam00581  81 VYVLDGGFEAWK 92
 
Name Accession Description Interval E-value
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
1-105 1.96e-68

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 200.25  E-value: 1.96e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   1 MDQFKHIDVKGAQALIEQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVN 80
Cdd:PRK00162   1 MDQFECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAFMRQADFDTPVMVMCYHGNSSQGAAQYLLQ 80

                         90       100
                 ....*....|....*....|....*
gi 515672126  81 QGFEEVYSVDGGFEAWHRAELPVNA 105
Cdd:PRK00162  81 QGFDVVYSIDGGFEAWRRTFPAEVA 105
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 2-103 2.08e-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: 108.90  E-value: 2.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   2 DQFKHIDVKGAQALIEQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVNQ 81
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRA 80

                         90       100
                 ....*....|....*....|..
gi 515672126  82 GFEEVYSVDGGFEAWHRAELPV 103
Cdd:COG0607   81 GYTNVYNLAGGIEAWKAAGLPV 102
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 6-98 2.68e-31

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: 105.81  E-value: 2.68e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   6 HIDVKGAQALIEQGE-ARLVDIRDPQSFAVA--HSKTAYHLTNDTMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVNQG 82
Cdd:cd01444    1 RISVDELAELLAAGEaPVLLDVRDPASYAALpdHIPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSSAQLAQALREAG 80

                         90
                 ....*....|....*.
gi 515672126  83 FEEVYSVDGGFEAWHR 98
Cdd:cd01444   81 FTDVRSLAGGFEAWRR 96
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 12-96 3.98e-21

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: 80.04  E-value: 3.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126  12 AQALIEQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEF--EQPILVMCYHGISSQGAAQYLVNQGFEEVYSV 89
Cdd:cd00158    2 LKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELdkDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNL 81


                 ....*..
gi 515672126  90 DGGFEAW 96
Cdd:cd00158   82 EGGMLAW 88
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 17-102 3.41e-16

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: 67.87  E-value: 3.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126    17 EQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEF--------------EQPILVMCYHGISSQGAAQYLVNQG 82
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIlefeellkrlgldkDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 515672126    83 FEEVYSVDGGFEAWHRAELP 102
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
7-103 7.91e-16

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 71.20  E-value: 7.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   7 IDVKGAQALIEQGeARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEV--EFEQPILVMCYHGISSQGAAQYLVNQGFE 84
Cdd:PRK08762   5 ISPAEARARAAQG-AVLIDVREAHERASGQAEGALRIPRGFLELRIETHlpDRDREIVLICASGTRSAHAAATLRELGYT 83

                         90
                 ....*....|....*....
gi 515672126  85 EVYSVDGGFEAWHRAELPV 103
Cdd:PRK08762  84 RVASVAGGFSAWKDAGLPL 102
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 16-97 2.23e-15

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: 65.58  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   16 IEQGEARLVDIRDPQSFAVAHSKTAYHL----TNDTMVSFMDEVEF------EQPILVMCYHGISSQGAAQYLVNQGFEE 85
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVplssLSLPPLPLLELLEKllellkDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|..
gi 515672126   86 VYSVDGGFEAWH 97
Cdd:pfam00581  81 VYVLDGGFEAWK 92
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 17-96 3.73e-15

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: 65.11  E-value: 3.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126  17 EQGEARLVDIRDPQSFAVAHSKTAYHLTND---TMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVNQGFEEVYSVDGGF 93
Cdd:cd01528   14 EREEPVLIDVREPEELEIAFLPGFLHLPMSeipERSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQGFENVYNLQGGI 93


                 ...
gi 515672126  94 EAW 96
Cdd:cd01528   94 DAW 96
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 7-103 1.49e-10

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: 53.26  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   7 IDVKGAQALIEQGeARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVNQGFEEV 86
Cdd:cd01527    4 ISPNDACELLAQG-AVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIFHCRSGMRTQQNAERLAAISAGEA 82

                         90
                 ....*....|....*..
gi 515672126  87 YSVDGGFEAWHRAELPV 103
Cdd:cd01527   83 YVLEGGLDAWKAAGLPV 99
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 23-98 6.68e-10

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: 51.11  E-value: 6.68e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515672126  23 LVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVNQGFeEVYSVDGGFEAWHR 98
Cdd:cd01524   16 LIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGF-KVKNLDGGYKTYST 90
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 7-99 9.27e-10

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: 51.27  E-value: 9.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   7 IDVKGAQALIEQGEARLVDIRDPQSF-AVAHSKTAYHLTNDtMVSFM---------DEVEFEQPILVMCYHGISSQGAAQ 76
Cdd:cd01447    1 LSPEDARALLGSPGVLLVDVRDPRELeRTGMIPGAFHAPRG-MLEFWadpdspyhkPAFAEDKPFVFYCASGWRSALAGK 79

                         90       100
                 ....*....|....*....|...
gi 515672126  77 YLVNQGFEEVYSVDGGFEAWHRA 99
Cdd:cd01447   80 TLQDMGLKPVYNIEGGFKDWKEA 102
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 7-96 5.48e-07

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 46.02  E-value: 5.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   7 IDVKGAQALIEqgEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFM--DEVEFEQPILVMCYHGISSQGAAQYLVNQGFE 84
Cdd:PRK05597 263 LDVPRVSALPD--GVTLIDVREPSEFAAYSIPGAHNVPLSAIREGAnpPSVSAGDEVVVYCAAGVRSAQAVAILERAGYT 340

                         90
                 ....*....|..
gi 515672126  85 EVYSVDGGFEAW 96
Cdd:PRK05597 341 GMSSLDGGIEGW 352
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 15-94 6.77e-07

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: 44.24  E-value: 6.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126  15 LIEQGEARLVDIR-DPQSFAVAHSKTAYHLTNDTMVS------FMDEVE----FEQPILVMCYHGISSQGAAQYLVNQGF 83
Cdd:cd01522   10 LQADPQAVLVDVRtEAEWKFVGGVPDAVHVAWQVYPDmeinpnFLAELEekvgKDRPVLLLCRSGNRSIAAAEAAAQAGF 89

                         90
                 ....*....|.
gi 515672126  84 EEVYSVDGGFE 94
Cdd:cd01522   90 TNVYNVLEGFE 100
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 20-96 1.68e-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: 42.66  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126  20 EARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQ------PILVMCYHGISSQGAAQYLVNQGFEEVYSVDGGF 93
Cdd:cd01529   12 GTALLDVRAEDEYAAGHLPGKRSIPGAALVLRSQELQALEapgratRYVLTCDGSLLARFAAQELLALGGKPVALLDGGT 91


                 ...
gi 515672126  94 EAW 96
Cdd:cd01529   92 SAW 94
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 5-92 1.08e-05

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: 40.64  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   5 KHIDVKGAQALIEQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVE-----FEQ-PILVMCYHGISSQGAAQYL 78
Cdd:cd01518    2 TYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDenldlLKGkKVLMYCTGGIRCEKASAYL 81

                         90
                 ....*....|....
gi 515672126  79 VNQGFEEVYSVDGG 92
Cdd:cd01518   82 KERGFKNVYQLKGG 95
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 7-96 1.15e-05

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: 41.14  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   7 IDVKGAQALIEQGEAR-LVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQ----------PILVMCYHGISSQGAA 75
Cdd:cd01526   10 VSVKDYKNILQAGKKHvLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLQelpldndkdsPIYVVCRRGNDSQTAV 89

                         90       100
                 ....*....|....*....|..
gi 515672126  76 QYLVNQGFE-EVYSVDGGFEAW 96
Cdd:cd01526   90 RKLKELGLErFVRDIIGGLKAW 111
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
14-92 6.62e-05

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 40.22  E-value: 6.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126  14 ALIEQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVE-----FE-QPILVMCYHGISSQGAAQYLVNQGFEEVY 87
Cdd:PRK00142 121 ELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPPWVEenldpLKdKKVVMYCTGGIRCEKASAWMKHEGFKEVY 200


                 ....*
gi 515672126  88 SVDGG 92
Cdd:PRK00142 201 QLEGG 205
PLN02160 PLN02160
thiosulfate sulfurtransferase
 7-104 1.25e-04

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 38.53  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   7 IDVKGAQALIEQGEARLvDIRDPQSFAVAHSKTAYHLTNDTMVS----------FMDEVE-FEQP---ILVMCYHGISSQ 72
Cdd:PLN02160  17 VDVSQAKTLLQSGHQYL-DVRTQDEFRRGHCEAAKIVNIPYMLNtpqgrvknqeFLEQVSsLLNPaddILVGCQSGARSL 95

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515672126  73 GAAQYLVNQGFEEVYSVDGGFEAWHRAELPVN 104
Cdd:PLN02160  96 KATTELVAAGYKKVRNKGGGYLAWVDHSFPIN 127
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 13-96 1.54e-04

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: 37.47  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126  13 QALIEQGEARLVDIRDPQSFAVAHSKTAYHLTndtmvsfMDEVEFE---------QPILVMCYHGIS--SQGAAQYLVNQ 81
Cdd:cd01532    3 QALLAREEIALIDVREEDPFAQSHPLWAANLP-------LSRLELDawvriprrdTPIVVYGEGGGEdlAPRAARRLSEL 75

                         90
                 ....*....|....*
gi 515672126  82 GFEEVYSVDGGFEAW 96
Cdd:cd01532   76 GYTDVALLEGGLQGW 90
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 12-106 4.96e-04

Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue.


Pssm-ID: 238793 [Multi-domain]  Cd Length: 145  Bit Score: 37.10  E-value: 4.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126  12 AQALIEQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQPILVMCYHGISSQGAAQYLVNQGFEEVYSVDG 91
Cdd:cd01535    3 AAWLGEGGQTAVVDVTASANYVKRHIPGAWWVLRAQLAQALEKLPAAERYVLTCGSSLLARFAAADLAALTVKPVFVLEG 82

                         90
                 ....*....|....*
gi 515672126  92 GFEAWHRAELPVNAG 106
Cdd:cd01535   83 GTAAWIAAGLPVESG 97
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 23-98 5.02e-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: 36.62  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126  23 LVDIRDPQsFAVAHSKTAYHL----TNDTMVSFMDEVEFEQPILVMCYHGISSQGA-------AQYLVNQGFE--EVYSV 89
Cdd:cd01443   26 VVDLRRDD-YEGGHIKGSINLpaqsCYQTLPQVYALFSLAGVKLAIFYCGSSQGRGpraarwfADYLRKVGESlpKSYIL 104


                 ....*....
gi 515672126  90 DGGFEAWHR 98
Cdd:cd01443  105 TGGIKAWYH 113
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 13-103 3.20e-03

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 35.45  E-value: 3.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126  13 QALIEQGEA-RLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQ--PILVMCYHGISSQGAAQYLVNQGFEEVYSV 89
Cdd:PRK07878 295 KEWLDSGKKiALIDVREPVEWDIVHIPGAQLIPKSEILSGEALAKLPQdrTIVLYCKTGVRSAEALAALKKAGFSDAVHL 374

                         90
                 ....*....|....*..
gi 515672126  90 DGGFEAWHR---AELPV 103
Cdd:PRK07878 375 QGGVVAWAKqvdPSLPM 391
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 17-96 3.64e-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: 34.17  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126  17 EQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVS--FMDEVEFE-----------QPILVMCYHGISSQGAAQYLVNQGF 83
Cdd:cd01519   12 PHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDalALSEEEFEkkygfpkpskdKELIFYCKAGVRSKAAAELARSLGY 91

                         90
                 ....*....|...
gi 515672126  84 EEVYSVDGGFEAW 96
Cdd:cd01519   92 ENVGNYPGSWLDW 104
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 50-98 4.24e-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: 34.01  E-value: 4.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 515672126  50 SFMDEVEFEQPILVMCYHGISSQGAAQYLVNQGFeEVYSVDGGFEAWHR 98
Cdd:cd01523   53 DILDQLPDDQEVTVICAKEGSSQFVAELLAERGY-DVDYLAGGMKAWSE 100
PRK01415 PRK01415
hypothetical protein; Validated
 1-92 6.62e-03

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 34.15  E-value: 6.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515672126   1 MDQFK--HIDVKGAQALIEQGEARLVDIRDPQSFAVAHSKTAYHLTNDTMVSFMDEVEFEQPIL------VMCYHGISSQ 72
Cdd:PRK01415 106 VDLFKgeYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFKQFPAWVQQNQELLkgkkiaMVCTGGIRCE 185

                         90       100
                 ....*....|....*....|
gi 515672126  73 GAAQYLVNQGFEEVYSVDGG 92
Cdd:PRK01415 186 KSTSLLKSIGYDEVYHLKGG 205
TrhO COG1054
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
 59-92 6.94e-03

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


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 34.35  E-value: 6.94e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 515672126  59 QPILVMCYHGISSQGAAQYLVNQGFEEVYSVDGG 92
Cdd:COG1054  171 KKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGG 204
 
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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