NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|447078925|ref|WP_001156181|]
View 

MULTISPECIES: rhodanese-like domain-containing protein [Enterobacteriaceae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 35-143 3.26e-29

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: 102.35  E-value: 3.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  35 SKVKVITRGEATRLINKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIkANNVGELEKhkDKPVIVVDGSGMQCQEPANAL 114
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGEL-AERLDELPK--DKPIVVYCASGGRSAQAAALL 77

                         90       100
                 ....*....|....*....|....*....
gi 447078925 115 TKAGFAQVFVLKEGVAGWAGENLPLVRGK 143
Cdd:COG0607   78 RRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 35-143 3.26e-29

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: 102.35  E-value: 3.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  35 SKVKVITRGEATRLINKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIkANNVGELEKhkDKPVIVVDGSGMQCQEPANAL 114
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGEL-AERLDELPK--DKPIVVYCASGGRSAQAAALL 77

                         90       100
                 ....*....|....*....|....*....
gi 447078925 115 TKAGFAQVFVLKEGVAGWAGENLPLVRGK 143
Cdd:COG0607   78 RRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 44-133 1.28e-26

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: 95.44  E-value: 1.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  44 EATRLINKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIKANNvGELEKHKDKPVIVVDGSGMQCQEPANALTKAGFAQVF 123
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERA-ALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVY 79

                         90
                 ....*....|
gi 447078925 124 VLKEGVAGWA 133
Cdd:cd00158   80 NLEGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 49-133 4.88e-21

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: 81.38  E-value: 4.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925   49 INKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIKANNVGELE-------KHKDKPVIVVDGSGMQCQEPANALTKAGFAQ 121
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLElleklleLLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|..
gi 447078925  122 VFVLKEGVAGWA 133
Cdd:pfam00581  81 VYVLDGGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 50-138 1.79e-19

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: 77.50  E-value: 1.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925    50 NKEDAVVVDLRQRDDFRKGHIAGSINL-----------LPSEIKANNVGELEKHKDKPVIVVDGSGMQCQEPANALTKAG 118
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIplselldrrgeLDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 447078925   119 FAQVFVLKEGVAGWAGENLP 138
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
38-141 1.05e-07

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 47.32  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  38 KVITRGEATRLINKEDAVVVDLRQRDDFRKGHIAGSINL----LPSEIKANNVgelekhkDKPVIVVDGSGMQCQEPANA 113
Cdd:PRK00162   5 ECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLtndsLGAFMRQADF-------DTPVMVMCYHGNSSQGAAQY 77

                         90       100
                 ....*....|....*....|....*...
gi 447078925 114 LTKAGFAQVFVLKEGVAGWAGENLPLVR 141
Cdd:PRK00162  78 LLQQGFDVVYSIDGGFEAWRRTFPAEVA 105
 
Name Accession Description Interval E-value
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 35-143 3.26e-29

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: 102.35  E-value: 3.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  35 SKVKVITRGEATRLINKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIkANNVGELEKhkDKPVIVVDGSGMQCQEPANAL 114
Cdd:COG0607    1 ASVKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGEL-AERLDELPK--DKPIVVYCASGGRSAQAAALL 77

                         90       100
                 ....*....|....*....|....*....
gi 447078925 115 TKAGFAQVFVLKEGVAGWAGENLPLVRGK 143
Cdd:COG0607   78 RRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 44-133 1.28e-26

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: 95.44  E-value: 1.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  44 EATRLINKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIKANNvGELEKHKDKPVIVVDGSGMQCQEPANALTKAGFAQVF 123
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERA-ALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVY 79

                         90
                 ....*....|
gi 447078925 124 VLKEGVAGWA 133
Cdd:cd00158   80 NLEGGMLAWK 89
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 49-133 4.88e-21

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: 81.38  E-value: 4.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925   49 INKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIKANNVGELE-------KHKDKPVIVVDGSGMQCQEPANALTKAGFAQ 121
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLElleklleLLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                          90
                  ....*....|..
gi 447078925  122 VFVLKEGVAGWA 133
Cdd:pfam00581  81 VYVLDGGFEAWK 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 50-138 1.79e-19

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: 77.50  E-value: 1.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925    50 NKEDAVVVDLRQRDDFRKGHIAGSINL-----------LPSEIKANNVGELEKHKDKPVIVVDGSGMQCQEPANALTKAG 118
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIplselldrrgeLDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 447078925   119 FAQVFVLKEGVAGWAGENLP 138
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 50-139 5.84e-10

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 53.13  E-value: 5.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  50 NKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIKANNVGELEKHKdkpVIVVDGSGMQCqepaNALTKAG--FAQV-FVLK 126
Cdd:cd01521   22 GKPDFVLVDVRSAEAYARGHVPGAINLPHREICENATAKLDKEK---LFVVYCDGPGC----NGATKAAlkLAELgFPVK 94

                         90
                 ....*....|....*.
gi 447078925 127 E---GVAGWAGENLPL 139
Cdd:cd01521   95 EmigGLDWWKREGYAT 110
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 48-142 1.66e-08

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 51.33  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  48 LINKEDAVVVDLR-----QRDDFRKGHIAGSINL----------------LPSEIK-ANNVGELEKHKDKPVIVVDGSGM 105
Cdd:COG2897    4 HLDDPDVVILDVRwdlpdGRAAYEAGHIPGAVFLdldtdlsdprspgrhpLPSPEAfAALLGALGISNDTTVVVYDDGGG 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 447078925 106 qcqepANA------LTKAGFAQVFVLKEGVAGWAGENLPLVRG 142
Cdd:COG2897   84 -----LFAarawwlLRYAGHEDVRVLDGGLAAWKAAGLPLETG 121
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 40-132 2.28e-08

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: 48.41  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  40 ITRGEATRLINK-EDAVVVDLRQRDDFRK--GHIAGSINLLPSeikanNVGELEKH--KDKPVIVVDGSGMQCQEPANAL 114
Cdd:cd01444    2 ISVDELAELLAAgEAPVLLDVRDPASYAAlpDHIPGAIHLDED-----SLDDWLGDldRDRPVVVYCYHGNSSAQLAQAL 76

                         90
                 ....*....|....*...
gi 447078925 115 TKAGFAQVFVLKEGVAGW 132
Cdd:cd01444   77 REAGFTDVRSLAGGFEAW 94
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 47-131 5.60e-08

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: 48.09  E-value: 5.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  47 RLINKEDAVVVDLRQRDDFRK-GHIAGSINL-----LPSEIKANNVGELEKH--KDKPVIVVDGSGMQCQEPANALTKAG 118
Cdd:cd01522    9 LLQADPQAVLVDVRTEAEWKFvGGVPDAVHVawqvyPDMEINPNFLAELEEKvgKDRPVLLLCRSGNRSIAAAEAAAQAG 88

                         90
                 ....*....|...
gi 447078925 119 FAQVFVLKEGVAG 131
Cdd:cd01522   89 FTNVYNVLEGFEG 101
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
38-141 1.05e-07

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 47.32  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  38 KVITRGEATRLINKEDAVVVDLRQRDDFRKGHIAGSINL----LPSEIKANNVgelekhkDKPVIVVDGSGMQCQEPANA 113
Cdd:PRK00162   5 ECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLtndsLGAFMRQADF-------DTPVMVMCYHGNSSQGAAQY 77

                         90       100
                 ....*....|....*....|....*...
gi 447078925 114 LTKAGFAQVFVLKEGVAGWAGENLPLVR 141
Cdd:PRK00162  78 LLQQGFDVVYSIDGGFEAWRRTFPAEVA 105
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
40-141 1.38e-07

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 49.24  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  40 ITRGEATRLInKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIKAnnvgELEKH---KDKPVIVVDGSGMQCQEPANALTK 116
Cdd:PRK08762   5 ISPAEARARA-AQGAVLIDVREAHERASGQAEGALRIPRGFLEL----RIETHlpdRDREIVLICASGTRSAHAAATLRE 79

                         90       100
                 ....*....|....*....|....*
gi 447078925 117 AGFAQVFVLKEGVAGWAGENLPLVR 141
Cdd:PRK08762  80 LGYTRVASVAGGFSAWKDAGLPLER 104
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 37-138 2.68e-06

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, and similar uncharacterized putative rhodanese-related sulfurtransferases.


Pssm-ID: 238785 [Multi-domain]  Cd Length: 99  Bit Score: 43.24  E-value: 2.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  37 VKVITRGEATRLINkEDAVVVDLRQRDDFRKGHIAGSINLLPSEIKANNVGELEKHKdkpVIVVDGSGMQCQEPANALTK 116
Cdd:cd01527    1 LTTISPNDACELLA-QGAVLVDIREPDEYLRERIPGARLVPLSQLESEGLPLVGANA---IIFHCRSGMRTQQNAERLAA 76

                         90       100
                 ....*....|....*....|..
gi 447078925 117 AGFAQVFVLKEGVAGWAGENLP 138
Cdd:cd01527   77 ISAGEAYVLEGGLDAWKAAGLP 98
RHOD_Kc cd01525
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the ...
 51-129 3.41e-06

Member of the Rhodanese Homology Domain superfamily. Included in this CD are the rhodanese-like domains found C-terminal of the serine/threonine protein kinases catalytic (S_TKc) domain and the Tre-2, BUB2p, Cdc16p (TBC) domain. The putative active site Cys residue is not present in this CD.


Pssm-ID: 238783 [Multi-domain]  Cd Length: 105  Bit Score: 43.21  E-value: 3.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  51 KEDAVVVDLRQRDDFRKGHIAGSINL--------LPSEIKANNVGELEKHKDKPVIVVDGSGMQCQEPANALTKAGFAQV 122
Cdd:cd01525   14 PAKLAAVDIRSSPDFRRGHIEGSINIpfssvflkEGELEQLPTVPRLENYKGKIIVIVSHSHKHAALFAAFLVKCGVPRV 93


                 ....*..
gi 447078925 123 FVLKEGV 129
Cdd:cd01525   94 CILDGGI 100
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 49-119 3.42e-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: 42.64  E-value: 3.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447078925  49 INKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIKAnNVGELEkhKDKPVIVVDGSGMQCQEPANALTKAGF 119
Cdd:cd01524    9 YRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRD-RLNELP--KDKEIIVYCAVGLRGYIAARILTQNGF 76
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 52-135 1.20e-05

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: 41.61  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  52 EDAVVVDLRQRDDFRKGHIAGSINLLPSEIkANNVGELEKH-KDKPVIVVDGSGMQCQEPANALTKAGFAQVFVLKEGVA 130
Cdd:cd01528   16 EEPVLIDVREPEELEIAFLPGFLHLPMSEI-PERSKELDSDnPDKDIVVLCHHGGRSMQVAQWLLRQGFENVYNLQGGID 94


                 ....*
gi 447078925 131 GWAGE 135
Cdd:cd01528   95 AWSLE 99
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 44-129 1.67e-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: 41.03  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  44 EATRLINKEDAVVVDLRQRDDFRKGHIAGSINL-------LPSEIKANnvgeLEKHKDKPVIVVDGSGMQCqEPANALTK 116
Cdd:cd01518    8 EWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPdvdtfreFPFWLDEN----LDLLKGKKVLMYCTGGIRC-EKASAYLK 82

                         90
                 ....*....|....
gi 447078925 117 A-GFAQVFVLKEGV 129
Cdd:cd01518   83 ErGFKNVYQLKGGI 96
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 52-132 2.65e-05

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 42.55  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  52 EDAVVVDLRQRDDFRKGHIAGSINLLPSEIKAN-NVGELEKHKDkpVIVVDGSGMQCQEPANALTKAGFAQVFVLKEGVA 130
Cdd:PRK05597 273 DGVTLIDVREPSEFAAYSIPGAHNVPLSAIREGaNPPSVSAGDE--VVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIE 350


                 ..
gi 447078925 131 GW 132
Cdd:PRK05597 351 GW 352
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 40-104 3.49e-05

Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.


Pssm-ID: 238726 [Multi-domain]  Cd Length: 118  Bit Score: 40.69  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  40 ITRGEATRLINKEDAVVVDLRQRDDF-----------RKGHIAGSIN-----LL--------PSEIKAnnvgELEKH--- 92
Cdd:cd01449    1 VTAEEVLANLDSGDVQLVDARSPERFrgevpeprpglRSGHIPGAVNipwtsLLdedgtfksPEELRA----LFAALgit 76

                         90
                 ....*....|..
gi 447078925  93 KDKPVIVVDGSG 104
Cdd:cd01449   77 PDKPVIVYCGSG 88
4RHOD_Repeat_1 cd01532
Member of the Rhodanese Homology Domain superfamily, repeat 1. This CD includes putative ...
 47-132 5.13e-05

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: 39.78  E-value: 5.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  47 RLINKEDAVVVDLRQRDDFRKGHIAGSINLLPSEIkannvgELEKH-----KDKPVIVVDGSGMQCQEP--ANALTKAGF 119
Cdd:cd01532    4 ALLAREEIALIDVREEDPFAQSHPLWAANLPLSRL------ELDAWvriprRDTPIVVYGEGGGEDLAPraARRLSELGY 77

                         90
                 ....*....|...
gi 447078925 120 AQVFVLKEGVAGW 132
Cdd:cd01532   78 TDVALLEGGLQGW 90
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 37-76 5.50e-05

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: 40.08  E-value: 5.50e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 447078925  37 VKVITRGEATRLIN------KEDAVVVDLRqRDDFRKGHIAGSINL 76
Cdd:cd01443    1 LKYISPEELVALLEnsdsnaGKDFVVVDLR-RDDYEGGHIKGSINL 45
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 56-132 1.03e-04

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: 38.81  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  56 VVDLRQRDDFRKGHIAGSINLLPSEIkANNVGELEKHK----DKPVIVVDGSGMQCQEPANALTKAGFAQVFVLKEGVAG 131
Cdd:cd01529   15 LLDVRAEDEYAAGHLPGKRSIPGAAL-VLRSQELQALEapgrATRYVLTCDGSLLARFAAQELLALGGKPVALLDGGTSA 93


                 .
gi 447078925 132 W 132
Cdd:cd01529   94 W 94
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 39-105 2.43e-04

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 39.39  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  39 VITRGEATRLINKEDAVVVDLRQRDDF---------RKGHIAGSINL-------------LPSEIKAnNVGELEKHKDKP 96
Cdd:COG2897  139 LADADEVLAALGDPDAVLVDARSPERYrgevepidpRAGHIPGAVNLpwtdlldedgtfkSAEELRA-LFAALGIDPDKP 217


                 ....*....
gi 447078925  97 VIVVDGSGM 105
Cdd:COG2897  218 VITYCGSGV 226
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 56-142 4.58e-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: 37.87  E-value: 4.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  56 VVDLRQRDDFRKGHIAGSINLLPSEIKAnnvgELEK--HKDKPVIVVDGSGMqCQEPANALTKAGFAQVFVLKEGVAGWA 133
Cdd:cd01535   14 VVDVTASANYVKRHIPGAWWVLRAQLAQ----ALEKlpAAERYVLTCGSSLL-ARFAAADLAALTVKPVFVLEGGTAAWI 88


                 ....*....
gi 447078925 134 GENLPLVRG 142
Cdd:cd01535   89 AAGLPVESG 97
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 47-133 6.85e-04

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: 36.70  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  47 RLINKEDAVVVDLRQRDDFRKGHIAGSINL----LP---SEIKANNVGELEkhKDKPVIVVDGSGMQCQEPANALTKAGF 119
Cdd:cd01523    9 RLLAGQPLFILDVRNESDYERWKIDGENNTpyfdPYfdfLEIEEDILDQLP--DDQEVTVICAKEGSSQFVAELLAERGY 86

                         90
                 ....*....|....
gi 447078925 120 AQVFvLKEGVAGWA 133
Cdd:cd01523   87 DVDY-LAGGMKAWS 99
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 44-133 8.19e-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: 36.64  E-value: 8.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  44 EATRLINKEDAVVVDLRQRDDF-RKGHIAGSIN----LLpsEIKANNVGELEK---HKDKPVIVVDGSGMQCQEPANALT 115
Cdd:cd01447    5 DARALLGSPGVLLVDVRDPRELeRTGMIPGAFHaprgML--EFWADPDSPYHKpafAEDKPFVFYCASGWRSALAGKTLQ 82

                         90
                 ....*....|....*...
gi 447078925 116 KAGFAQVFVLKEGVAGWA 133
Cdd:cd01447   83 DMGLKPVYNIEGGFKDWK 100
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
48-130 8.59e-04

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 37.90  E-value: 8.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  48 LINKEDAVVVDLRQRDDFRKGHIAGSINL-------LPSEIKANnvgeLEKHKDKPVIVVDGSGMQCqEPANALTK-AGF 119
Cdd:PRK00142 122 LLDDPDVVFIDMRNDYEYEIGHFENAIEPdietfreFPPWVEEN----LDPLKDKKVVMYCTGGIRC-EKASAWMKhEGF 196

                         90
                 ....*....|.
gi 447078925 120 AQVFVLKEGVA 130
Cdd:PRK00142 197 KEVYQLEGGII 207
4RHOD_Repeat_2 cd01533
Member of the Rhodanese Homology Domain superfamily, repeat 2. This CD includes putative ...
 40-133 9.46e-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: 36.67  E-value: 9.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  40 ITRGEATRLIN-KEDAVVVDLRQRDDFRKGHIAGSINLLPSEIkANNVGELEKHKDKPVIVVDGSGMQCQEPANALTKAG 118
Cdd:cd01533   12 VSADELAALQArGAPLVVLDGRRFDEYRKMTIPGSVSCPGAEL-VLRVGELAPDPRTPIVVNCAGRTRSIIGAQSLINAG 90

                         90
                 ....*....|....*.
gi 447078925 119 FAQ-VFVLKEGVAGWA 133
Cdd:cd01533   91 LPNpVAALRNGTQGWT 106
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 40-133 1.17e-03

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 37.77  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  40 ITRGEATRLINK-EDAVVVDLRQRDDFRKGHIAGSiNLLP-SEIkanNVGE-LEK-HKDKPVIVVDGSGMQCQEPANALT 115
Cdd:PRK07878 289 ITPRELKEWLDSgKKIALIDVREPVEWDIVHIPGA-QLIPkSEI---LSGEaLAKlPQDRTIVLYCKTGVRSAEALAALK 364

                         90
                 ....*....|....*...
gi 447078925 116 KAGFAQVFVLKEGVAGWA 133
Cdd:PRK07878 365 KAGFSDAVHLQGGVVAWA 382
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 47-134 2.16e-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: 35.71  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  47 RLINKEDAVV-VDLRQRDDFRKGHIAGSINL----LPSEIKANNvGELEKH-------KDKPVIVVDGSGMQCQEPANAL 114
Cdd:cd01519    8 NLPNPHPNKVlIDVREPEELKTGKIPGAINIplssLPDALALSE-EEFEKKygfpkpsKDKELIFYCKAGVRSKAAAELA 86

                         90       100
                 ....*....|....*....|
gi 447078925 115 TKAGFaqvfvlkEGVAGWAG 134
Cdd:cd01519   87 RSLGY-------ENVGNYPG 99
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 37-132 3.32e-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: 35.08  E-value: 3.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447078925  37 VKVITRGEATRLI--NKEDAVVVDLRqRDDFRKGHIAGSINlLPSEIKANNVGELEK---HKDKPVIVVDGSGMQCQEPA 111
Cdd:cd01531    1 VSYISPAQLKGWIrnGRPPFQVVDVR-DEDYAGGHIKGSWH-YPSTRFKAQLNQLVQllsGSKKDTVVFHCALSQVRGPS 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 447078925 112 NAL----------TKAGFAQVFVLKEGVAGW 132
Cdd:cd01531   79 AARkflryldeedLETSKFEVYVLHGGFNAW 109
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH