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Conserved domains on  [gi|446584465|ref|WP_000661811|]
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MULTISPECIES: rhodanese-like domain-containing protein [Bacillus]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10001806)

rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present

CATH:  3.40.250.10
PubMed:  12151332|17454295

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-94 6.78e-36

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: 117.38  E-value: 6.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465   1 MKEMTTKELEEKLLRKEVVnIVDVREVEEVAEGKIPEACNIPLGLLEFRMHELNKNQEYIIVCRSGGRSARAVQFLESYG 80
Cdd:COG0607    3 VKEISPAELAELLESEDAV-LLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90
                 ....*....|....*
gi 446584465  81 F-QVINVVGGMLAWE 94
Cdd:COG0607   82 YtNVYNLAGGIEAWK 96
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-94 6.78e-36

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: 117.38  E-value: 6.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465   1 MKEMTTKELEEKLLRKEVVnIVDVREVEEVAEGKIPEACNIPLGLLEFRMHELNKNQEYIIVCRSGGRSARAVQFLESYG 80
Cdd:COG0607    3 VKEISPAELAELLESEDAV-LLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90
                 ....*....|....*
gi 446584465  81 F-QVINVVGGMLAWE 94
Cdd:COG0607   82 YtNVYNLAGGIEAWK 96
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 8-94 1.38e-28

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: 98.53  E-value: 1.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  8 ELEEKLLRKEVVnIVDVREVEEVAEGKIPEACNIPLGLLEFRMH--ELNKNQEYIIVCRSGGRSARAVQFLESYGF-QVI 84
Cdd:cd00158   1 ELKELLDDEDAV-LLDVREPEEYAAGHIPGAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVY 79

                        90
                ....*....|
gi 446584465 85 NVVGGMLAWE 94
Cdd:cd00158  80 NLEGGMLAWK 89
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 19-93 5.54e-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: 72.11  E-value: 5.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465    19 VNIVDVREVEEVAEGKIPEACNIPLGLLEFRM--------------HELNKNQEYIIVCRSGGRSARAVQFLESYGFQ-V 83
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRgeldilefeellkrLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKnV 84

                           90
                   ....*....|
gi 446584465    84 INVVGGMLAW 93
Cdd:smart00450  85 YLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 14-93 8.81e-18

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: 8.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  14 LRKEVVNIVDVREVEEVAEGKIPEACNIPLGLLEFRMH----------ELNKNQEYIIVCRSGGRSARAVQFLESYGF-Q 82
Cdd:pfam00581  1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLpllellekllELLKDKPIVVYCNSGNRAAAAAALLKALGYkN 80

                         90
                 ....*....|.
gi 446584465  83 VINVVGGMLAW 93
Cdd:pfam00581 81 VYVLDGGFEAW 91
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
1-98 1.30e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 70.15  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465   1 MKEMTTKELEEKLLR--KEVVnIVDVREVEEVAEGKIPEACNIPLGLLE-----FRMHELNKNQEYIIVCRSGGRSARAV 73
Cdd:PRK07411 281 IPEMTVTELKALLDSgaDDFV-LIDVRNPNEYEIARIPGSVLVPLPDIEngpgvEKVKELLNGHRLIAHCKMGGRSAKAL 359

                         90       100
                 ....*....|....*....|....*
gi 446584465  74 QFLESYGFQVINVVGGMLAWEGKVE 98
Cdd:PRK07411 360 GILKEAGIEGTNVKGGITAWSREVD 384
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 1-94 6.78e-36

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: 117.38  E-value: 6.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465   1 MKEMTTKELEEKLLRKEVVnIVDVREVEEVAEGKIPEACNIPLGLLEFRMHELNKNQEYIIVCRSGGRSARAVQFLESYG 80
Cdd:COG0607    3 VKEISPAELAELLESEDAV-LLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKPIVVYCASGGRSAQAAALLRRAG 81

                         90
                 ....*....|....*
gi 446584465  81 F-QVINVVGGMLAWE 94
Cdd:COG0607   82 YtNVYNLAGGIEAWK 96
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 8-94 1.38e-28

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: 98.53  E-value: 1.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  8 ELEEKLLRKEVVnIVDVREVEEVAEGKIPEACNIPLGLLEFRMH--ELNKNQEYIIVCRSGGRSARAVQFLESYGF-QVI 84
Cdd:cd00158   1 ELKELLDDEDAV-LLDVREPEEYAAGHIPGAINIPLSELEERAAllELDKDKPIVVYCRSGNRSARAAKLLRKAGGtNVY 79

                        90
                ....*....|
gi 446584465 85 NVVGGMLAWE 94
Cdd:cd00158  80 NLEGGMLAWK 89
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 19-93 5.54e-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: 72.11  E-value: 5.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465    19 VNIVDVREVEEVAEGKIPEACNIPLGLLEFRM--------------HELNKNQEYIIVCRSGGRSARAVQFLESYGFQ-V 83
Cdd:smart00450   5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRgeldilefeellkrLGLDKDKPVVVYCRSGNRSAKAAWLLRELGFKnV 84

                           90
                   ....*....|
gi 446584465    84 INVVGGMLAW 93
Cdd:smart00450  85 YLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 14-93 8.81e-18

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: 8.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  14 LRKEVVNIVDVREVEEVAEGKIPEACNIPLGLLEFRMH----------ELNKNQEYIIVCRSGGRSARAVQFLESYGF-Q 82
Cdd:pfam00581  1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLpllellekllELLKDKPIVVYCNSGNRAAAAAALLKALGYkN 80

                         90
                 ....*....|.
gi 446584465  83 VINVVGGMLAW 93
Cdd:pfam00581 81 VYVLDGGFEAW 91
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 12-93 1.23e-16

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: 68.61  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  12 KLLRKEVVNIVDVREVEEV-AEGKIPEACNIPLGLLEFRM------HE--LNKNQEYIIVCRSGGRSARAVQFLESYGFQ 82
Cdd:cd01447    8 ALLGSPGVLLVDVRDPRELeRTGMIPGAFHAPRGMLEFWAdpdspyHKpaFAEDKPFVFYCASGWRSALAGKTLQDMGLK 87

                         90
                 ....*....|..
gi 446584465  83 -VINVVGGMLAW 93
Cdd:cd01447   88 pVYNIEGGFKDW 99
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 3-98 3.64e-16

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: 67.42  E-value: 3.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465   3 EMTTKELEEKLLR-KEVVNIVDVREVEEVAEGKIPEACNIPLGLLEFRMHEL---NKNQEYIIVCRSGGRSARAVQFLES 78
Cdd:cd01528    1 QISVAELAEWLADeREEPVLIDVREPEELEIAFLPGFLHLPMSEIPERSKELdsdNPDKDIVVLCHHGGRSMQVAQWLLR 80

                         90       100
                 ....*....|....*....|.
gi 446584465  79 YGF-QVINVVGGMLAWEGKVE 98
Cdd:cd01528   81 QGFeNVYNLQGGIDAWSLEVD 101
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
1-98 1.30e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 70.15  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465   1 MKEMTTKELEEKLLR--KEVVnIVDVREVEEVAEGKIPEACNIPLGLLE-----FRMHELNKNQEYIIVCRSGGRSARAV 73
Cdd:PRK07411 281 IPEMTVTELKALLDSgaDDFV-LIDVRNPNEYEIARIPGSVLVPLPDIEngpgvEKVKELLNGHRLIAHCKMGGRSAKAL 359

                         90       100
                 ....*....|....*....|....*
gi 446584465  74 QFLESYGFQVINVVGGMLAWEGKVE 98
Cdd:PRK07411 360 GILKEAGIEGTNVKGGITAWSREVD 384
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
1-94 3.53e-15

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 68.88  E-value: 3.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465   1 MKEMTTKELEEKLLRKEVvnIVDVREVEEVAEGKIPEACNIPLGLLEFRM--HELNKNQEYIIVCRSGGRSARAVQFLES 78
Cdd:PRK08762   2 IREISPAEARARAAQGAV--LIDVREAHERASGQAEGALRIPRGFLELRIetHLPDRDREIVLICASGTRSAHAAATLRE 79

                         90
                 ....*....|....*..
gi 446584465  79 YGF-QVINVVGGMLAWE 94
Cdd:PRK08762  80 LGYtRVASVAGGFSAWK 96
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 5-97 5.43e-15

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: 65.02  E-value: 5.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465   5 TTKELEEKLLRKEVVNIVDVREVEEVAEGKIPEACNIPLGLLEFRMHELNKNQEY----------IIVCRSGGRSARAVQ 74
Cdd:cd01526   11 SVKDYKNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLQELpldndkdspiYVVCRRGNDSQTAVR 90

                         90       100
                 ....*....|....*....|....*
gi 446584465  75 FLESYGFQ--VINVVGGMLAWEGKV 97
Cdd:cd01526   91 KLKELGLErfVRDIIGGLKAWADKV 115
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 11-94 8.69e-15

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.


Pssm-ID: 238782 [Multi-domain]  Cd Length: 90  Bit Score: 63.44  E-value: 8.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465 11 EKLLRKEVVnIVDVREVEEVAEGKIPEACNIPLGLLEFRMHELNKNQEYIIVCRSGGRSARAVQFLESYGFQVINVVGGM 90
Cdd:cd01524   7 DNYRADGVT-LIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKEIIVYCAVGLRGYIAARILTQNGFKVKNLDGGY 85


                ....
gi 446584465 91 LAWE 94
Cdd:cd01524  86 KTYS 89
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 16-93 3.19e-14

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: 62.67  E-value: 3.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  16 KEVVnIVDVREVEEVAEGKIPEACNIPLGLLE--FRMHELN-----------KNQEYIIVCRSGGRSARAVQFLESYGFQ 82
Cdd:cd01519   14 PNKV-LIDVREPEELKTGKIPGAINIPLSSLPdaLALSEEEfekkygfpkpsKDKELIFYCKAGVRSKAAAELARSLGYE 92

                         90
                 ....*....|..
gi 446584465  83 -VINVVGGMLAW 93
Cdd:cd01519   93 nVGNYPGSWLDW 104
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 19-93 5.94e-12

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 59.89  E-value: 5.94e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446584465  19 VNIVDVREVEEVAEGKIPEACNIPLGLLE--FRMHELNKNQEYIIVCRSGGRSARAVQFLESYGFQ-VINVVGGMLAW 93
Cdd:PRK05597 275 VTLIDVREPSEFAAYSIPGAHNVPLSAIRegANPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTgMSSLDGGIEGW 352
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 4-98 1.61e-11

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 58.57  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465   4 MTTKELEEKLLRKEVVNIVDVREVEEVAEGKIPEACNIPLGLLEFRMH--ELNKNQEYIIVCRSGGRSARAVQFLESYGF 81
Cdd:PRK07878 289 ITPRELKEWLDSGKKIALIDVREPVEWDIVHIPGAQLIPKSEILSGEAlaKLPQDRTIVLYCKTGVRSAEALAALKKAGF 368

                         90
                 ....*....|....*...
gi 446584465  82 Q-VINVVGGMLAWEGKVE 98
Cdd:PRK07878 369 SdAVHLQGGVVAWAKQVD 386
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 4-93 6.38e-09

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: 48.64  E-value: 6.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465   4 MTTKELEEKLLRKEVVNIVDVREVEEVAEGKIPEACNIPLGLLEFR--------MHELNKNQEYIIVCRSGGRSARAVQF 75
Cdd:cd01523    1 LDPEDLYARLLAGQPLFILDVRNESDYERWKIDGENNTPYFDPYFDfleieediLDQLPDDQEVTVICAKEGSSQFVAEL 80

                         90
                 ....*....|....*...
gi 446584465  76 LESYGFQVINVVGGMLAW 93
Cdd:cd01523   81 LAERGYDVDYLAGGMKAW 98
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 21-93 2.84e-07

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: 44.65  E-value: 2.84e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446584465  21 IVDVREVEEVAEGKIPEACNIPLGLLEFR-MHELNKNQEYIIVCRSGG--RSARAVQFLESYGFQVINVVGGMLAW 93
Cdd:cd01521   28 LVDVRSAEAYARGHVPGAINLPHREICENaTAKLDKEKLFVVYCDGPGcnGATKAALKLAELGFPVKEMIGGLDWW 103
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 1-93 8.89e-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: 43.24  E-value: 8.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  1 MKEMTTKELEEKLLRKEVvnIVDVREVEEVAEGKIPEACNIPLGLLEFRMHELNKNQEYIIVCRSGGRSARAVQFLESYG 80
Cdd:cd01527   1 LTTISPNDACELLAQGAV--LVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANAIIFHCRSGMRTQQNAERLAAIS 78

                        90
                ....*....|....
gi 446584465 81 FQVINVV-GGMLAW 93
Cdd:cd01527  79 AGEAYVLeGGLDAW 92
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 17-93 1.94e-05

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: 39.58  E-value: 1.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465 17 EVVNIVDVREVEEVAEGKIPEACNIPLGLLEFRMHELN------KNQEYIIVCRSGGRSARAVQFLESYGF-QVINVVGG 89
Cdd:cd01529  11 PGTALLDVRAEDEYAAGHLPGKRSIPGAALVLRSQELQaleapgRATRYVLTCDGSLLARFAAQELLALGGkPVALLDGG 90


                ....
gi 446584465 90 MLAW 93
Cdd:cd01529  91 TSAW 94
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 21-89 4.61e-05

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: 39.23  E-value: 4.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  21 IVDVR-EVEEVAEGKIPEACNIP-------------LGLLEfrmHELNKNQEYIIVCRSGGRSARAVQFLESYGF-QVIN 85
Cdd:cd01522   18 LVDVRtEAEWKFVGGVPDAVHVAwqvypdmeinpnfLAELE---EKVGKDRPVLLLCRSGNRSIAAAEAAAQAGFtNVYN 94


                 ....
gi 446584465  86 VVGG 89
Cdd:cd01522   95 VLEG 98
PLN02160 PLN02160
thiosulfate sulfurtransferase
 22-95 6.66e-05

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 38.91  E-value: 6.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  22 VDVREVEEVAEG--------KIPEACNIPLG------LLEFRMHELNKNQEYIIVCRSGGRSARAVQFLESYGF-QVINV 86
Cdd:PLN02160  33 LDVRTQDEFRRGhceaakivNIPYMLNTPQGrvknqeFLEQVSSLLNPADDILVGCQSGARSLKATTELVAAGYkKVRNK 112


                 ....*....
gi 446584465  87 VGGMLAWEG 95
Cdd:PLN02160 113 GGGYLAWVD 121
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 4-69 2.24e-04

Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 2nd repeat which does contain the putative catalytic Cys residue.


Pssm-ID: 238791 [Multi-domain]  Cd Length: 109  Bit Score: 37.05  E-value: 2.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446584465   4 MTTKELEEKLLRKEVVNIVDVREVEEVAEGKIPEACNIPLGLLEFRMHELNKNQEYIIVCRSGGRS 69
Cdd:cd01533   12 VSADELAALQARGAPLVVLDGRRFDEYRKMTIPGSVSCPGAELVLRVGELAPDPRTPIVVNCAGRT 77
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 13-93 2.46e-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: 36.70  E-value: 2.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465 13 LLRKEVVNIVDVREVEEVAEGKIPEACNIPLGLLEFRMHELNKNQEYIIVC--RSGGR--SARAVQFLESYGFQVINVV- 87
Cdd:cd01532   5 LLAREEIALIDVREEDPFAQSHPLWAANLPLSRLELDAWVRIPRRDTPIVVygEGGGEdlAPRAARRLSELGYTDVALLe 84


                ....*.
gi 446584465 88 GGMLAW 93
Cdd:cd01532  85 GGLQGW 90
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 3-94 3.29e-04

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: 36.47  E-value: 3.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  3 EMTTKELEEKLLRKEVVNIVDVREVEEVAE--GKIPEAcnIPLGLLEFR--MHELNKNQEYIIVCRSGGRSARAVQFLES 78
Cdd:cd01444   1 RISVDELAELLAAGEAPVLLDVRDPASYAAlpDHIPGA--IHLDEDSLDdwLGDLDRDRPVVVYCYHGNSSAQLAQALRE 78

                        90
                ....*....|....*..
gi 446584465 79 YGF-QVINVVGGMLAWE 94
Cdd:cd01444  79 AGFtDVRSLAGGFEAWR 95
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
11-93 2.45e-03

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 34.23  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446584465  11 EKLLRKEVVnIVDVREVEEVAEGKIPEA---CNIPLGllEFrMHELNKNQEYIIVCRSGGRSARAVQFLESYGF-QVINV 86
Cdd:PRK00162  14 QKLQEGGAV-LVDIRDPQSFAMGHAPGAfhlTNDSLG--AF-MRQADFDTPVMVMCYHGNSSQGAAQYLLQQGFdVVYSI 89


                 ....*..
gi 446584465  87 VGGMLAW 93
Cdd:PRK00162  90 DGGFEAW 96
PRK10287 PRK10287
thiosulfate:cyanide sulfurtransferase; Provisional
 22-90 2.71e-03

thiosulfate:cyanide sulfurtransferase; Provisional


Pssm-ID: 182356 [Multi-domain]  Cd Length: 104  Bit Score: 34.05  E-value: 2.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446584465  22 VDVREVEEVAEGKIPEACNIPLGLLEFRMHEL--NKNQEYIIVCRSGGRSARAVQFLESYGFQVINVVGGM 90
Cdd:PRK10287  24 IDVRVPEQYQQEHVQGAINIPLKEVKERIATAvpDKNDTVKLYCNAGRQSGQAKEILSEMGYTHAENAGGL 94
 
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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