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Conserved domains on  [gi|1002309679|ref|XP_015618207|]
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thiosulfate sulfurtransferase 18 [Oryza sativa Japonica Group]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 13)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 19-131 2.44e-32

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.


The actual alignment was detected with superfamily member PLN02160:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 136  Bit Score: 111.33  E-value: 2.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  19 SKQEETERVMrSVDAEEACALLSSGrHQYLDVRMWEDFDKGHVAGAR--NVPYYLSvTPRAKEKNPHFVQQVAALYHAHD 96
Cdd:PLN02160    6 SSSTKAEEVV-SVDVSQAKTLLQSG-HQYLDVRTQDEFRRGHCEAAKivNIPYMLN-TPQGRVKNQEFLEQVSSLLNPAD 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002309679  97 HIIVGCRSGVRSKLATADLVAAGFKNVRILEGGYL 131
Cdd:PLN02160   83 DILVGCQSGARSLKATTELVAAGYKKVRNKGGGYL 117
 
Name Accession Description Interval E-value
PLN02160 PLN02160
thiosulfate sulfurtransferase
 19-131 2.44e-32

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 111.33  E-value: 2.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  19 SKQEETERVMrSVDAEEACALLSSGrHQYLDVRMWEDFDKGHVAGAR--NVPYYLSvTPRAKEKNPHFVQQVAALYHAHD 96
Cdd:PLN02160    6 SSSTKAEEVV-SVDVSQAKTLLQSG-HQYLDVRTQDEFRRGHCEAAKivNIPYMLN-TPQGRVKNQEFLEQVSSLLNPAD 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002309679  97 HIIVGCRSGVRSKLATADLVAAGFKNVRILEGGYL 131
Cdd:PLN02160   83 DILVGCQSGARSLKATTELVAAGYKKVRNKGGGYL 117
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 28-136 5.19e-24

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: 89.26  E-value: 5.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  28 MRSVDAEEACALLSSGRHQYLDVRMWEDFDKGHVAGARNVPYYlsvtprakeknpHFVQQVAALyHAHDHIIVGCRSGVR 107
Cdd:COG0607     3 VKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLG------------ELAERLDEL-PKDKPIVVYCASGGR 69

                          90       100
                  ....*....|....*....|....*....
gi 1002309679 108 SKLATADLVAAGFKNVRILEGGYLSLLRA 136
Cdd:COG0607    70 SAQAAALLRRAGYTNVYNLAGGIEAWKAA 98
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 41-137 1.00e-20

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: 80.58  E-value: 1.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679   41 SSGRHQYLDVRMWEDFDKGHVAGARNVPYYLSVTPRAKEKNPHFVQQVAAL-YHAHDHIIVGCRSGVRSKLATADLVAAG 119
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLgLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90
                   ....*....|....*...
gi 1002309679  120 FKNVRILEGGYLSLLRAA 137
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAG 98
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 38-131 2.43e-18

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: 74.26  E-value: 2.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  38 ALLSSGRHQYLDVRMWEDFDKGHVAGARNVPYYlSVTPRAKEKNPHfvqqvaalyhAHDHIIVGCRSGVRSKLATADLVA 117
Cdd:cd00158     4 ELLDDEDAVLLDVREPEEYAAGHIPGAINIPLS-ELEERAALLELD----------KDKPIVVYCRSGNRSARAAKLLRK 72

                          90
                  ....*....|....
gi 1002309679 118 AGFKNVRILEGGYL 131
Cdd:cd00158    73 AGGTNVYNLEGGML 86
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 40-130 5.20e-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: 73.29  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  40 LSSGRHQYLDVRMWEDFDKGHVAGARNVPYYLSVTPRAKEKNphFVQQVAALYHaHDHIIVGCRSGVRSKLATADLVAAG 119
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLE--LLEKLLELLK-DKPIVVYCNSGNRAAAAAALLKALG 77

                          90
                  ....*....|.
gi 1002309679 120 FKNVRILEGGY 130
Cdd:pfam00581  78 YKNVYVLDGGF 88
 
Name Accession Description Interval E-value
PLN02160 PLN02160
thiosulfate sulfurtransferase
 19-131 2.44e-32

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 111.33  E-value: 2.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  19 SKQEETERVMrSVDAEEACALLSSGrHQYLDVRMWEDFDKGHVAGAR--NVPYYLSvTPRAKEKNPHFVQQVAALYHAHD 96
Cdd:PLN02160    6 SSSTKAEEVV-SVDVSQAKTLLQSG-HQYLDVRTQDEFRRGHCEAAKivNIPYMLN-TPQGRVKNQEFLEQVSSLLNPAD 82

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002309679  97 HIIVGCRSGVRSKLATADLVAAGFKNVRILEGGYL 131
Cdd:PLN02160   83 DILVGCQSGARSLKATTELVAAGYKKVRNKGGGYL 117
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 28-136 5.19e-24

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: 89.26  E-value: 5.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  28 MRSVDAEEACALLSSGRHQYLDVRMWEDFDKGHVAGARNVPYYlsvtprakeknpHFVQQVAALyHAHDHIIVGCRSGVR 107
Cdd:COG0607     3 VKEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLG------------ELAERLDEL-PKDKPIVVYCASGGR 69

                          90       100
                  ....*....|....*....|....*....
gi 1002309679 108 SKLATADLVAAGFKNVRILEGGYLSLLRA 136
Cdd:COG0607    70 SAQAAALLRRAGYTNVYNLAGGIEAWKAA 98
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 41-137 1.00e-20

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: 80.58  E-value: 1.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679   41 SSGRHQYLDVRMWEDFDKGHVAGARNVPYYLSVTPRAKEKNPHFVQQVAAL-YHAHDHIIVGCRSGVRSKLATADLVAAG 119
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLgLDKDKPVVVYCRSGNRSAKAAWLLRELG 80

                           90
                   ....*....|....*...
gi 1002309679  120 FKNVRILEGGYLSLLRAA 137
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAG 98
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 38-131 2.43e-18

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: 74.26  E-value: 2.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  38 ALLSSGRHQYLDVRMWEDFDKGHVAGARNVPYYlSVTPRAKEKNPHfvqqvaalyhAHDHIIVGCRSGVRSKLATADLVA 117
Cdd:cd00158     4 ELLDDEDAVLLDVREPEEYAAGHIPGAINIPLS-ELEERAALLELD----------KDKPIVVYCRSGNRSARAAKLLRK 72

                          90
                  ....*....|....
gi 1002309679 118 AGFKNVRILEGGYL 131
Cdd:cd00158    73 AGGTNVYNLEGGML 86
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 40-130 5.20e-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: 73.29  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  40 LSSGRHQYLDVRMWEDFDKGHVAGARNVPYYLSVTPRAKEKNphFVQQVAALYHaHDHIIVGCRSGVRSKLATADLVAAG 119
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLE--LLEKLLELLK-DKPIVVYCNSGNRAAAAAALLKALG 77

                          90
                  ....*....|.
gi 1002309679 120 FKNVRILEGGY 130
Cdd:pfam00581  78 YKNVYVLDGGF 88
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 31-129 4.25e-13

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: 61.49  E-value: 4.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  31 VDAEEACALLSSGRHQYLDVRMWEDFD-----------KGHVAGARNVPYYLSVTPRAKEKNPhfvQQVAALYHAH---- 95
Cdd:cd01449     1 VTAEEVLANLDSGDVQLVDARSPERFRgevpeprpglrSGHIPGAVNIPWTSLLDEDGTFKSP---EELRALFAALgitp 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1002309679  96 -DHIIVGCRSGVRSKLATADLVAAGFKNVRILEGG 129
Cdd:cd01449    78 dKPVIVYCGSGVTACVLLLALELLGYKNVRLYDGS 112
RHOD_1 cd01522
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ...
 31-128 2.24e-12

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: 59.65  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  31 VDAEEACALLSS-GRHQYLDVRMWEDFDK-GHVAGARNVPY--YLSvtpraKEKNPHFVQQVAALYHAHDHIIVGCRSGV 106
Cdd:cd01522     1 LTPAEAWALLQAdPQAVLVDVRTEAEWKFvGGVPDAVHVAWqvYPD-----MEINPNFLAELEEKVGKDRPVLLLCRSGN 75

                          90       100
                  ....*....|....*....|...
gi 1002309679 107 RSKLATADLVAAGFKNV-RILEG 128
Cdd:cd01522    76 RSIAAAEAAAQAGFTNVyNVLEG 98
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 31-129 2.21e-11

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 59.42  E-value: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  31 VDAEEACALLSSGRHQYLDVRMWEDFD---------KGHVAGARNVPYYLSVTPRAKEKNPhfvQQVAALYHAH-----D 96
Cdd:COG2897   140 ADADEVLAALGDPDAVLVDARSPERYRgevepidprAGHIPGAVNLPWTDLLDEDGTFKSA---EELRALFAALgidpdK 216

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002309679  97 HIIVGCRSGVRSKLATADLVAAGFKNVRILEGG 129
Cdd:COG2897   217 PVITYCGSGVRAAHTWLALELLGYPNVRLYDGS 249
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 31-131 8.30e-10

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: 52.66  E-value: 8.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  31 VDAEEACALLSSGRHQYL-DVRMWEDFDKGHVAGARNVPY-----YLSVTPRAKEKNPHFVQQVAAlyhahDHIIVGCRS 104
Cdd:cd01519     1 YSFEEVKNLPNPHPNKVLiDVREPEELKTGKIPGAINIPLsslpdALALSEEEFEKKYGFPKPSKD-----KELIFYCKA 75

                          90       100
                  ....*....|....*....|....*..
gi 1002309679 105 GVRSKLATADLVAAGFKNVRILEGGYL 131
Cdd:cd01519    76 GVRSKAAAELARSLGYENVGNYPGSWL 102
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
28-130 5.84e-08

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 50.01  E-value: 5.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  28 MRSVDAEEACALLSSGRhQYLDVRMWEDFDKGHVAGARNVPY-YLSVtpRAKEKNPHFVQqvaalyhahdHIIVGCRSGV 106
Cdd:PRK08762    2 IREISPAEARARAAQGA-VLIDVREAHERASGQAEGALRIPRgFLEL--RIETHLPDRDR----------EIVLICASGT 68

                          90       100
                  ....*....|....*....|....
gi 1002309679 107 RSKLATADLVAAGFKNVRILEGGY 130
Cdd:PRK08762   69 RSAHAAATLRELGYTRVASVAGGF 92
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 31-136 7.61e-07

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: 44.72  E-value: 7.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  31 VDAEEACALLSSGRHQYLDVRmweDFD----KGHVAGARNVP---YYLSVTPRAKEKNPHFVQQvaalyhahDHIIVGCR 103
Cdd:cd01447     1 LSPEDARALLGSPGVLLVDVR---DPRelerTGMIPGAFHAPrgmLEFWADPDSPYHKPAFAED--------KPFVFYCA 69

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002309679 104 SGVRSKLATADLVAAGFKNVRILEGGYLSLLRA 136
Cdd:cd01447    70 SGWRSALAGKTLQDMGLKPVYNIEGGFKDWKEA 102
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 48-130 9.94e-07

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 46.40  E-value: 9.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  48 LDVRMWEDFDKGHVAGARNVPyyLSVTprakeKNPHFVQQVAAlyhaHDHIIVGCRSGVRSKLATADLVAAGFKNVRILE 127
Cdd:PRK05597  278 IDVREPSEFAAYSIPGAHNVP--LSAI-----REGANPPSVSA----GDEVVVYCAAGVRSAQAVAILERAGYTGMSSLD 346


                  ...
gi 1002309679 128 GGY 130
Cdd:PRK05597  347 GGI 349
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 30-132 1.30e-05

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 43.16  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  30 SVDAEEACALLSSGRHQYL-DVRMWEDFDKGHVAGARNVPYYLSVTPRAKEKNPHfvqqvaalyhaHDHIIVGCRSGVRS 108
Cdd:PRK07878  288 TITPRELKEWLDSGKKIALiDVREPVEWDIVHIPGAQLIPKSEILSGEALAKLPQ-----------DRTIVLYCKTGVRS 356

                          90       100
                  ....*....|....*....|....
gi 1002309679 109 KLATADLVAAGFKNVRILEGGYLS 132
Cdd:PRK07878  357 AEALAALKKAGFSDAVHLQGGVVA 380
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 46-131 1.42e-05

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: 41.10  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  46 QYLDVRMWEDFDKGHVAGARNVPY-----YLSVTPRAKEknphfvqqvaalyhahdhIIVGCRSGVRSKLATADLVAAGF 120
Cdd:cd01524    15 TLIDVRTPQEFEKGHIKGAINIPLdelrdRLNELPKDKE------------------IIVYCAVGLRGYIAARILTQNGF 76

                          90
                  ....*....|.
gi 1002309679 121 KnVRILEGGYL 131
Cdd:cd01524    77 K-VKNLDGGYK 86
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
 41-130 6.42e-05

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: 39.70  E-value: 6.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  41 SSGRHQYLDVRMwEDFDKGHVAGARNVPYylsvtPRAKEKNPHFVQQVAAlyHAHDHIIVGCR-SGVRSKLATADLVAA- 118
Cdd:cd01531    16 GRPPFQVVDVRD-EDYAGGHIKGSWHYPS-----TRFKAQLNQLVQLLSG--SKKDTVVFHCAlSQVRGPSAARKFLRYl 87

                          90
                  ....*....|....*....
gi 1002309679 119 -------GFKNVRILEGGY 130
Cdd:cd01531    88 deedletSKFEVYVLHGGF 106
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 34-130 6.87e-05

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: 39.17  E-value: 6.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  34 EEACALLSSGRH-QYLDVRMWEDF--DKGHVAGARNVpyylsvtprakekNPHFVQQVAALYHAHDHIIVGCRSGVRSKL 110
Cdd:cd01444     5 DELAELLAAGEApVLLDVRDPASYaaLPDHIPGAIHL-------------DEDSLDDWLGDLDRDRPVVVYCYHGNSSAQ 71

                          90       100
                  ....*....|....*....|
gi 1002309679 111 ATADLVAAGFKNVRILEGGY 130
Cdd:cd01444    72 LAQALREAGFTDVRSLAGGF 91
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 46-129 1.19e-04

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: 38.91  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  46 QYLDVRMWEDFDKGHVAGARNVPYYLSVTpRAKEKNPHFVQQvaalyhahdHIIVGCRSGVRSKLATADLVAAGFKNVRI 125
Cdd:cd01528    19 VLIDVREPEELEIAFLPGFLHLPMSEIPE-RSKELDSDNPDK---------DIVVLCHHGGRSMQVAQWLLRQGFENVYN 88


                  ....
gi 1002309679 126 LEGG 129
Cdd:cd01528    89 LQGG 92
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 48-129 1.25e-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: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  48 LDVRMWEDFDKGHVAGARNVPyylsvtprakekNPHFVQQVAALYHAH-----DHIIVGCRSGVRSKLATADLVAAGFKN 122
Cdd:cd01529    16 LDVRAEDEYAAGHLPGKRSIP------------GAALVLRSQELQALEapgraTRYVLTCDGSLLARFAAQELLALGGKP 83


                  ....*..
gi 1002309679 123 VRILEGG 129
Cdd:cd01529    84 VALLDGG 90
RHOD_YgaP cd01527
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YgaP, ...
 28-129 2.38e-04

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: 37.85  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  28 MRSVDAEEACALLSSGRhQYLDVRMWEDFDKGHVAGARNVPyyLSVtprakeknphfVQQVAALYHAHDHIIVGCRSGVR 107
Cdd:cd01527     1 LTTISPNDACELLAQGA-VLVDIREPDEYLRERIPGARLVP--LSQ-----------LESEGLPLVGANAIIFHCRSGMR 66

                          90       100
                  ....*....|....*....|..
gi 1002309679 108 SKLATADLVAAGFKNVRILEGG 129
Cdd:cd01527    67 TQQNAERLAAISAGEAYVLEGG 88
RHOD_Kc cd01525
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the ...
 48-130 3.59e-04

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: 37.43  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  48 LDVRMWEDFDKGHVAGARNVPYylsvtPRAKEKNPHFVQ-QVAALYHAHDHIIVGCRSGVRSKLAT--ADLVAAGFKNVR 124
Cdd:cd01525    20 VDIRSSPDFRRGHIEGSINIPF-----SSVFLKEGELEQlPTVPRLENYKGKIIVIVSHSHKHAALfaAFLVKCGVPRVC 94


                  ....*.
gi 1002309679 125 ILEGGY 130
Cdd:cd01525    95 ILDGGI 100
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 41-132 3.71e-04

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: 37.67  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  41 SSGRHQYLDVRMWEDFDKGHVAGARNVPYYlSVTPRAKEKNPHFVQQVAAlyHAHDHIIVGCRSGVRSKLATADLVAAGF 120
Cdd:cd01526    21 AGKKHVLLDVRPKVHFEICRLPEAINIPLS-ELLSKAAELKSLQELPLDN--DKDSPIYVVCRRGNDSQTAVRKLKELGL 97

                          90
                  ....*....|...
gi 1002309679 121 K-NVRILEGGYLS 132
Cdd:cd01526    98 ErFVRDIIGGLKA 110
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 31-135 6.85e-04

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 36.79  E-value: 6.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  31 VDAEEACALLSSGRHQYLDVRMWEDFDKGHVAGA--------RNVPYYLSVTPRAKEKNPhfvqqvaalyhahdhIIVGC 102
Cdd:cd01518     4 LSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAvnpdvdtfREFPFWLDENLDLLKGKK---------------VLMYC 68

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1002309679 103 RSGVRSKLATADLVAAGFKNVRILEGGYLSLLR 135
Cdd:cd01518    69 TGGIRCEKASAYLKERGFKNVYQLKGGILKYLE 101
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 48-129 1.72e-03

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: 35.79  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  48 LDVRMWEDFDKGHVAGARNVPYYLsVTPRAKEKNPHFVQQVAALYHAHdhiivgCRSGVRSKLATADLvaaGFKnVRILE 127
Cdd:cd01521    29 VDVRSAEAYARGHVPGAINLPHRE-ICENATAKLDKEKLFVVYCDGPG------CNGATKAALKLAEL---GFP-VKEMI 97


                  ..
gi 1002309679 128 GG 129
Cdd:cd01521    98 GG 99
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
84-140 3.93e-03

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 35.98  E-value: 3.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002309679  84 FVQQVAALYHAHDH--IIVGCRSGVRSKLATADLVAAGFKNVRILEGGYLSLLRAANQQ 140
Cdd:PRK00142  158 FPPWVEENLDPLKDkkVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQ 216
glpE PRK00162
thiosulfate sulfurtransferase GlpE;
31-130 4.07e-03

thiosulfate sulfurtransferase GlpE;


Pssm-ID: 178908 [Multi-domain]  Cd Length: 108  Bit Score: 34.61  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  31 VDAEEACALLSSGRHQYLDVRMWEDFDKGHVAGARNVpyylsvtprakeKNphfvQQVAALYHAHDH---IIVGCRSGVR 107
Cdd:PRK00162    7 INVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHL------------TN----DSLGAFMRQADFdtpVMVMCYHGNS 70

                          90       100
                  ....*....|....*....|...
gi 1002309679 108 SKLATADLVAAGFKNVRILEGGY 130
Cdd:PRK00162   71 SQGAAQYLLQQGFDVVYSIDGGF 93
4RHOD_Repeat_3 cd01534
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ...
 31-134 7.69e-03

Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 3rd repeat which does not contain the putative catalytic Cys residue.


Pssm-ID: 238792 [Multi-domain]  Cd Length: 95  Bit Score: 33.98  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  31 VDAEEACALLSSG-RHQYL-DVRMWEDFDKGHVAGARNVPYYLSVtprakEKNPHFVQQVAAlyhahdHIIVGCRSGVRS 108
Cdd:cd01534     1 IGAAELARWAAEGdRTVYRfDVRTPEEYEAGHLPGFRHTPGGQLV-----QETDHFAPVRGA------RIVLADDDGVRA 69

                          90       100
                  ....*....|....*....|....*.
gi 1002309679 109 KLATADLVAAGFkNVRILEGGYLSLL 134
Cdd:cd01534    70 DMTASWLAQMGW-EVYVLEGGLAAAL 94
RHOD_Lact_B cd01523
Member of the Rhodanese Homology Domain superfamily. This CD includes predicted proteins with ...
 31-129 9.71e-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: 33.62  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002309679  31 VDAEEACALLSSGRHQY-LDVRMWEDFDKGHVAGARNVPYYlsvtprakekNPHF-----VQQVAALYHAHDHIIVGCRS 104
Cdd:cd01523     1 LDPEDLYARLLAGQPLFiLDVRNESDYERWKIDGENNTPYF----------DPYFdfleiEEDILDQLPDDQEVTVICAK 70

                          90       100
                  ....*....|....*....|....*
gi 1002309679 105 GVRSKLATADLVAAGFKnVRILEGG 129
Cdd:cd01523    71 EGSSQFVAELLAERGYD-VDYLAGG 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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