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Conserved domains on  [gi|836584568|ref|WP_047741842|]
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MULTISPECIES: rhodanese-like domain-containing protein [Enterobacter]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10107424)

rhodanese-like domain-containing protein similar to Bacillus halodurans Bh2092 protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 18-128 1.46e-57

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: 174.08  E-value: 1.46e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  18 HFLRRLSVETDCADVHHAIANNEQDFVLLHVVgSPEQFARRHVPGALHLPRSQITAERMAEWPEGTLFVVYCAGPHCNGA 97
Cdd:cd01521    1 HFEAKLAFETDCWDVAIALKNGKPDFVLVDVR-SAEAYARGHVPGAINLPHREICENATAKLDKEKLFVVYCDGPGCNGA 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 836584568  98 DRAALKLARLGLPVKIMLGGITGWEDEKFAF 128
Cdd:cd01521   80 TKAALKLAELGFPVKEMIGGLDWWKREGYAT 110
 
Name Accession Description Interval E-value
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 18-128 1.46e-57

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: 174.08  E-value: 1.46e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  18 HFLRRLSVETDCADVHHAIANNEQDFVLLHVVgSPEQFARRHVPGALHLPRSQITAERMAEWPEGTLFVVYCAGPHCNGA 97
Cdd:cd01521    1 HFEAKLAFETDCWDVAIALKNGKPDFVLVDVR-SAEAYARGHVPGAINLPHREICENATAKLDKEKLFVVYCDGPGCNGA 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 836584568  98 DRAALKLARLGLPVKIMLGGITGWEDEKFAF 128
Cdd:cd01521   80 TKAALKLAELGFPVKEMIGGLDWWKREGYAT 110
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 28-126 1.09e-16

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: 70.38  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  28 DCADVHHAIANneQDFVLLHVvGSPEQFARRHVPGALHLPRSQItAERMAEWPEGTLFVVYCAGPHcnGADRAALKLARL 107
Cdd:COG0607    7 SPAELAELLES--EDAVLLDV-REPEEFAAGHIPGAINIPLGEL-AERLDELPKDKPIVVYCASGG--RSAQAAALLRRA 80

                         90       100
                 ....*....|....*....|
gi 836584568 108 GLP-VKIMLGGITGWEDEKF 126
Cdd:COG0607   81 GYTnVYNLAGGIEAWKAAGL 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 51-121 3.22e-11

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 55.95  E-value: 3.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568   51 SPEQFARRHVPGALHLPRSQI--TAERMAEWPE-------GTLFVVYCAGPHCngADRAALKLARLGLP-VKIMLGGITG 120
Cdd:pfam00581  13 PPEEYAKGHIPGAVNVPLSSLslPPLPLLELLEkllellkDKPIVVYCNSGNR--AAAAAALLKALGYKnVYVLDGGFEA 90


                  .
gi 836584568  121 W 121
Cdd:pfam00581  91 W 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 39-124 5.58e-08

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


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 47.45  E-value: 5.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568    39 NEQDFVLLHVvGSPEQFARRHVPGALHLPRSQItAERMAEWPEGTLF--------------VVYCAGPHCNGadRAALKL 104
Cdd:smart00450   1 NDEKVVLLDV-RSPEEYEGGHIPGAVNIPLSEL-LDRRGELDILEFEellkrlgldkdkpvVVYCRSGNRSA--KAAWLL 76

                           90       100
                   ....*....|....*....|.
gi 836584568   105 ARLGLP-VKIMLGGITGWEDE 124
Cdd:smart00450  77 RELGFKnVYLLDGGYKEWSAA 97
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
31-128 1.96e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 45.39  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  31 DVHHAIANNEQDFVLLHVVGSpEQFARRHVPGALHLPRSQITAERMAEWPE-GTLFVVYCAGPhcNGADRAALKLARLGL 109
Cdd:PRK08762   6 SPAEARARAAQGAVLIDVREA-HERASGQAEGALRIPRGFLELRIETHLPDrDREIVLICASG--TRSAHAAATLRELGY 82

                         90       100
                 ....*....|....*....|
gi 836584568 110 P-VKIMLGGITGWEDEKFAF 128
Cdd:PRK08762  83 TrVASVAGGFSAWKDAGLPL 102
 
Name Accession Description Interval E-value
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 18-128 1.46e-57

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: 174.08  E-value: 1.46e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  18 HFLRRLSVETDCADVHHAIANNEQDFVLLHVVgSPEQFARRHVPGALHLPRSQITAERMAEWPEGTLFVVYCAGPHCNGA 97
Cdd:cd01521    1 HFEAKLAFETDCWDVAIALKNGKPDFVLVDVR-SAEAYARGHVPGAINLPHREICENATAKLDKEKLFVVYCDGPGCNGA 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 836584568  98 DRAALKLARLGLPVKIMLGGITGWEDEKFAF 128
Cdd:cd01521   80 TKAALKLAELGFPVKEMIGGLDWWKREGYAT 110
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 28-126 1.09e-16

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: 70.38  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  28 DCADVHHAIANneQDFVLLHVvGSPEQFARRHVPGALHLPRSQItAERMAEWPEGTLFVVYCAGPHcnGADRAALKLARL 107
Cdd:COG0607    7 SPAELAELLES--EDAVLLDV-REPEEFAAGHIPGAINIPLGEL-AERLDELPKDKPIVVYCASGG--RSAQAAALLRRA 80

                         90       100
                 ....*....|....*....|
gi 836584568 108 GLP-VKIMLGGITGWEDEKF 126
Cdd:COG0607   81 GYTnVYNLAGGIEAWKAAGL 100
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 39-122 3.70e-12

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: 58.08  E-value: 3.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  39 NEQDFVLLHVvGSPEQFARRHVPGALHLPRSQITAE-RMAEWPEGTLFVVYCAgpHCNGADRAALKLARLGLP-VKIMLG 116
Cdd:cd00158    7 DDEDAVLLDV-REPEEYAAGHIPGAINIPLSELEERaALLELDKDKPIVVYCR--SGNRSARAAKLLRKAGGTnVYNLEG 83


                 ....*.
gi 836584568 117 GITGWE 122
Cdd:cd00158   84 GMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 51-121 3.22e-11

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 55.95  E-value: 3.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568   51 SPEQFARRHVPGALHLPRSQI--TAERMAEWPE-------GTLFVVYCAGPHCngADRAALKLARLGLP-VKIMLGGITG 120
Cdd:pfam00581  13 PPEEYAKGHIPGAVNVPLSSLslPPLPLLELLEkllellkDKPIVVYCNSGNR--AAAAAALLKALGYKnVYVLDGGFEA 90


                  .
gi 836584568  121 W 121
Cdd:pfam00581  91 W 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 39-124 5.58e-08

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


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 47.45  E-value: 5.58e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568    39 NEQDFVLLHVvGSPEQFARRHVPGALHLPRSQItAERMAEWPEGTLF--------------VVYCAGPHCNGadRAALKL 104
Cdd:smart00450   1 NDEKVVLLDV-RSPEEYEGGHIPGAVNIPLSEL-LDRRGELDILEFEellkrlgldkdkpvVVYCRSGNRSA--KAAWLL 76

                           90       100
                   ....*....|....*....|.
gi 836584568   105 ARLGLP-VKIMLGGITGWEDE 124
Cdd:smart00450  77 RELGFKnVYLLDGGYKEWSAA 97
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
31-128 1.96e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 45.39  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  31 DVHHAIANNEQDFVLLHVVGSpEQFARRHVPGALHLPRSQITAERMAEWPE-GTLFVVYCAGPhcNGADRAALKLARLGL 109
Cdd:PRK08762   6 SPAEARARAAQGAVLIDVREA-HERASGQAEGALRIPRGFLELRIETHLPDrDREIVLICASG--TRSAHAAATLRELGY 82

                         90       100
                 ....*....|....*....|
gi 836584568 110 P-VKIMLGGITGWEDEKFAF 128
Cdd:PRK08762  83 TrVASVAGGFSAWKDAGLPL 102
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 34-90 4.01e-06

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: 42.25  E-value: 4.01e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 836584568  34 HAIANNEQDFVLLHVVGSPEQFARRHVPGALHLPRSQITaERMAEWPEGTLFVVYCA 90
Cdd:cd01524    4 HELDNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELR-DRLNELPKDKEIIVYCA 59
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 40-124 3.35e-04

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: 37.41  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  40 EQDFVLLHVVGSPEQFARRHVPGALHLPRSqitaerMAEW---PEGTL----------FVVYCAgphcnGADRAAL--KL 104
Cdd:cd01447   12 SPGVLLVDVRDPRELERTGMIPGAFHAPRG------MLEFwadPDSPYhkpafaedkpFVFYCA-----SGWRSALagKT 80

                         90       100
                 ....*....|....*....|..
gi 836584568 105 AR-LGL-PVKIMLGGITGWEDE 124
Cdd:cd01447   81 LQdMGLkPVYNIEGGFKDWKEA 102
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 40-121 8.95e-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: 36.31  E-value: 8.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  40 EQDFVLLHVVGSPEQFARRHVPGALHLPRSQITAERMAEWP-EGTLFVVYCAGPHCNGADRAALKLARLGLP-VKIMLGG 117
Cdd:cd01532    7 AREEIALIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPrRDTPIVVYGEGGGEDLAPRAARRLSELGYTdVALLEGG 86


                 ....
gi 836584568 118 ITGW 121
Cdd:cd01532   87 LQGW 90
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 56-123 1.02e-03

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: 36.08  E-value: 1.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 836584568  56 ARRHVPGALHLPRSQItAERMAEWPEGTLFVVYCAgpHCNGADRAALKLARLG-LPVKIMLGGITGWED 123
Cdd:cd01444   31 LPDHIPGAIHLDEDSL-DDWLGDLDRDRPVVVYCY--HGNSSAQLAQALREAGfTDVRSLAGGFEAWRR 96
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 49-123 1.05e-03

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 37.54  E-value: 1.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 836584568  49 VGSPEQFARRHVPGALHLPRSQITAERM-AEWPEGTLFVVYCAGphcnGAD--RAALKLARLGLPVKIML-GGITGWED 123
Cdd:PRK05597 280 VREPSEFAAYSIPGAHNVPLSAIREGANpPSVSAGDEVVVYCAA----GVRsaQAVAILERAGYTGMSSLdGGIEGWLD 354
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 36-122 1.10e-03

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: 36.24  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  36 IANNEQDFVLLHVVGspEQFARRHVPGALHLPrSQITAERMAEWPEGTL------FVVYCAGPHCNGAdRAALKLAR--- 106
Cdd:cd01531   13 IRNGRPPFQVVDVRD--EDYAGGHIKGSWHYP-STRFKAQLNQLVQLLSgskkdtVVFHCALSQVRGP-SAARKFLRyld 88

                         90       100
                 ....*....|....*....|..
gi 836584568 107 -----LGLP-VKIMLGGITGWE 122
Cdd:cd01531   89 eedleTSKFeVYVLHGGFNAWE 110
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 39-136 1.20e-03

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 37.46  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  39 NEQDFVLLHV----VGSPEQFARRHVPGALH-----------------LPRSQITAERMAEW--PEGTLFVVYCAGPHcN 95
Cdd:COG2897    6 DDPDVVILDVrwdlPDGRAAYEAGHIPGAVFldldtdlsdprspgrhpLPSPEAFAALLGALgiSNDTTVVVYDDGGG-L 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 836584568  96 GADRAALKLARLGLP-VKIMLGGITGWEDEKFAFASSETAVA 136
Cdd:COG2897   85 FAARAWWLLRYAGHEdVRVLDGGLAAWKAAGLPLETGPPTPA 126
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
8-124 1.75e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 37.02  E-value: 1.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568   8 PAAEPQEAVThflRRLSVETDCADVHHAIANNEQDFVLLHVvGSPEQFARRHVPGALHLPRSQITA----ERMAEWPEGT 83
Cdd:PRK07411 268 PQAKAAEAAQ---KAEIPEMTVTELKALLDSGADDFVLIDV-RNPNEYEIARIPGSVLVPLPDIENgpgvEKVKELLNGH 343

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 836584568  84 LFVVycagpHCNGADRAALKLARL------GLPVKimlGGITGWEDE 124
Cdd:PRK07411 344 RLIA-----HCKMGGRSAKALGILkeagieGTNVK---GGITAWSRE 382
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 40-136 4.20e-03

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: 35.17  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 836584568  40 EQDFVLLHVVGSPEQFARRHVPGALHLPRSQItAERMAEWPEGTLFVVYCAGP---HCNGADRAALklarLGLPVKIMLG 116
Cdd:cd01535    8 EGGQTAVVDVTASANYVKRHIPGAWWVLRAQL-AQALEKLPAAERYVLTCGSSllaRFAAADLAAL----TVKPVFVLEG 82

                         90       100
                 ....*....|....*....|
gi 836584568 117 GITGWEDEKFAFASSETAVA 136
Cdd:cd01535   83 GTAAWIAAGLPVESGETRLA 102
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 52-121 6.56e-03

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: 34.00  E-value: 6.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 836584568  52 PEQFARRHVPGALHLPRSQITAERMAEwpEGTLFVVYcagpHCNGADRAALKLARLGL----PVKIMLGGITGW 121
Cdd:cd01527   25 PDEYLRERIPGARLVPLSQLESEGLPL--VGANAIIF----HCRSGMRTQQNAERLAAisagEAYVLEGGLDAW 92
 
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.
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