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Conserved domains on  [gi|21903488|sp|P71121|]
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RecName: Full=Thiosulfate sulfurtransferase

Protein Classification

sulfurtransferase( domain architecture ID 11458420)

sulfurtransferase such as thiosulfate sulfurtransferase or 3-mercaptopyruvate sulfurtransferase, which catalyzes the transfer of sulfur to cyanide from donor compounds such as thiosulfate or 3-mercaptopyruvate

CATH:  3.40.250.10
EC:  2.8.1.-
Gene Ontology:  GO:0016783|GO:0000098
PubMed:  12151332|17454295

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 26-289 8.75e-101

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


:

Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 295.93  E-value: 8.75e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  26 LSARLGSPGLKVVESNED----SLLYDIGHLPGAVRIDWAKDLNDP---LTRDFIDGEAFAELMNRKGIARDDTVVVYGD 98
Cdd:COG2897   1 LAAHLDDPDVVILDVRWDlpdgRAAYEAGHIPGAVFLDLDTDLSDPrspGRHPLPSPEAFAALLGALGISNDTTVVVYDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  99 KSNWWAAFTLWVFELFGHSDVRLLNGGRDAWMAEERDTSYVVPEYPSANYPVveRVDENQRAFVAEVLGSLtQSGGMTLV 178
Cdd:COG2897  81 GGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTA--RPDPELLADADEVLAAL-GDPDAVLV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 179 DVRTPSEFSGLDEhgnptsnTGVLRGGHIPGAINLDWSDAVLPNGNFRTRAELDKLYADL--NPADDTVVYCQVGDRAAH 256
Cdd:COG2897 158 DARSPERYRGEVE-------PIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALgiDPDKPVITYCGSGVRAAH 230

                       250       260       270
                ....*....|....*....|....*....|...
gi 21903488 257 TWFVLkYLLGFNNVRNYDGSWAEWGNMVRMPIE 289
Cdd:COG2897 231 TWLAL-ELLGYPNVRLYDGSWSEWGSDPDLPVE 262
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 26-289 8.75e-101

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 295.93  E-value: 8.75e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  26 LSARLGSPGLKVVESNED----SLLYDIGHLPGAVRIDWAKDLNDP---LTRDFIDGEAFAELMNRKGIARDDTVVVYGD 98
Cdd:COG2897   1 LAAHLDDPDVVILDVRWDlpdgRAAYEAGHIPGAVFLDLDTDLSDPrspGRHPLPSPEAFAALLGALGISNDTTVVVYDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  99 KSNWWAAFTLWVFELFGHSDVRLLNGGRDAWMAEERDTSYVVPEYPSANYPVveRVDENQRAFVAEVLGSLtQSGGMTLV 178
Cdd:COG2897  81 GGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTA--RPDPELLADADEVLAAL-GDPDAVLV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 179 DVRTPSEFSGLDEhgnptsnTGVLRGGHIPGAINLDWSDAVLPNGNFRTRAELDKLYADL--NPADDTVVYCQVGDRAAH 256
Cdd:COG2897 158 DARSPERYRGEVE-------PIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALgiDPDKPVITYCGSGVRAAH 230

                       250       260       270
                ....*....|....*....|....*....|...
gi 21903488 257 TWFVLkYLLGFNNVRNYDGSWAEWGNMVRMPIE 289
Cdd:COG2897 231 TWLAL-ELLGYPNVRLYDGSWSEWGSDPDLPVE 262
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 20-132 2.74e-40

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 136.60  E-value: 2.74e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  20 IVSASWLSARLGSPGLKVVESNEDS------LLYDIGHLPGAVRIDWAKDLND--PLTRDFIDGEAFAELMNRKGIARDD 91
Cdd:cd01448   1 LVSPDWLAEHLDDPDVRILDARWYLpdrdgrKEYLEGHIPGAVFFDLDEDLDDksPGPHMLPSPEEFAELLGSLGISNDD 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21903488  92 TVVVYGDKSNWWAAFTLWVFELFGHSDVRLLNGGRDAWMAE 132
Cdd:cd01448  81 TVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAE 121
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 20-292 5.46e-32

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 124.85  E-value: 5.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488   20 IVSASWLSARLGSPGLKVVESNEdSLLYDIGHLPGAVRIDWAK-DLNDPLTRDFI-DGEAFAELMNRKGIARDDTVVVYG 97
Cdd:PRK09629  10 VIEPNDLLERLDAPELILVDLTS-SARYEAGHIRGARFVDPKRtQLGKPPAPGLLpDTADLEQLFGELGHNPDAVYVVYD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488   98 DKSNWWAAFTLWVFELFGHSDVRLLNGGRDAWMAEERDTSYVVPeyPSANYPVVERVDENQRAfVAEVLGSLTQSGGMTL 177
Cdd:PRK09629  89 DEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVP--PVAGGPVTLTLHDEPTA-TREYLQSRLGAADLAI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  178 VDVRTPSEFSGldehgnptSNTGVLRGGHIPGAINLDWSDAVLPNGNFRTRAELDKLYADL--NPADDTVVYCQVGDRAA 255
Cdd:PRK09629 166 WDARAPTEYSG--------EKVVAAKGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLgiTPDKEVITHCQTHHRSG 237

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 21903488  256 HTWFVLKyLLGFNNVRNYDGSWAEWGNMVRMPIETGE 292
Cdd:PRK09629 238 FTYLVAK-ALGYPRVKAYAGSWGEWGNHPDTPVEVPT 273
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 171-280 3.09e-21

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: 86.36  E-value: 3.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488    171 QSGGMTLVDVRTPSEFsgldehgnptsntgvlRGGHIPGAINLDWSDAVLPNGNFRTRAELDKL-YADLNPADDTVVYCQ 249
Cdd:smart00450   1 NDEKVVLLDVRSPEEY----------------EGGHIPGAVNIPLSELLDRRGELDILEFEELLkRLGLDKDKPVVVYCR 64

                           90       100       110
                   ....*....|....*....|....*....|.
gi 21903488    250 VGDRAAHTWFVLKyLLGFNNVRNYDGSWAEW 280
Cdd:smart00450  65 SGNRSAKAAWLLR-ELGFKNVYLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 171-280 4.14e-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: 85.61  E-value: 4.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488   171 QSGGMTLVDVRTPSEFSGldehgnptsntgvlrgGHIPGAINLDWSDAVLPNGNFrtrAELDKLYADLNPADDTVVYCQV 250
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAK----------------GHIPGAVNVPLSSLSLPPLPL---LELLEKLLELLKDKPIVVYCNS 62

                          90       100       110
                  ....*....|....*....|....*....|
gi 21903488   251 GDRAAHTWFVLKYlLGFNNVRNYDGSWAEW 280
Cdd:pfam00581  63 GNRAAAAAALLKA-LGYKNVYVLDGGFEAW 91
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 176-213 9.67e-03

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 37.19  E-value: 9.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 21903488   176 TLVDVRTPSEFsglDEhgnptsntgvlrgGHIPGAINL 213
Cdd:TIGR03167   4 PLIDVRSPAEF---AE-------------GHLPGAINL 25
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 26-289 8.75e-101

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 295.93  E-value: 8.75e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  26 LSARLGSPGLKVVESNED----SLLYDIGHLPGAVRIDWAKDLNDP---LTRDFIDGEAFAELMNRKGIARDDTVVVYGD 98
Cdd:COG2897   1 LAAHLDDPDVVILDVRWDlpdgRAAYEAGHIPGAVFLDLDTDLSDPrspGRHPLPSPEAFAALLGALGISNDTTVVVYDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  99 KSNWWAAFTLWVFELFGHSDVRLLNGGRDAWMAEERDTSYVVPEYPSANYPVveRVDENQRAFVAEVLGSLtQSGGMTLV 178
Cdd:COG2897  81 GGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTA--RPDPELLADADEVLAAL-GDPDAVLV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 179 DVRTPSEFSGLDEhgnptsnTGVLRGGHIPGAINLDWSDAVLPNGNFRTRAELDKLYADL--NPADDTVVYCQVGDRAAH 256
Cdd:COG2897 158 DARSPERYRGEVE-------PIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALgiDPDKPVITYCGSGVRAAH 230

                       250       260       270
                ....*....|....*....|....*....|...
gi 21903488 257 TWFVLkYLLGFNNVRNYDGSWAEWGNMVRMPIE 289
Cdd:COG2897 231 TWLAL-ELLGYPNVRLYDGSWSEWGSDPDLPVE 262
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 20-132 2.74e-40

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 136.60  E-value: 2.74e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  20 IVSASWLSARLGSPGLKVVESNEDS------LLYDIGHLPGAVRIDWAKDLND--PLTRDFIDGEAFAELMNRKGIARDD 91
Cdd:cd01448   1 LVSPDWLAEHLDDPDVRILDARWYLpdrdgrKEYLEGHIPGAVFFDLDEDLDDksPGPHMLPSPEEFAELLGSLGISNDD 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21903488  92 TVVVYGDKSNWWAAFTLWVFELFGHSDVRLLNGGRDAWMAE 132
Cdd:cd01448  81 TVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAE 121
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 160-282 7.44e-38

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: 130.06  E-value: 7.44e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 160 AFVAEVLGSLtQSGGMTLVDVRTPSEFSGLDEHGNPTsntgvLRGGHIPGAINLDWSDAVLPNGNFRTRAELDKLYADL- 238
Cdd:cd01449   1 VTAEEVLANL-DSGDVQLVDARSPERFRGEVPEPRPG-----LRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALg 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 21903488 239 -NPADDTVVYCQVGDRAAHTWFVLKyLLGFNNVRNYDGSWAEWGN 282
Cdd:cd01449  75 iTPDKPVIVYCGSGVTACVLLLALE-LLGYKNVRLYDGSWSEWGS 118
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 20-292 5.46e-32

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 124.85  E-value: 5.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488   20 IVSASWLSARLGSPGLKVVESNEdSLLYDIGHLPGAVRIDWAK-DLNDPLTRDFI-DGEAFAELMNRKGIARDDTVVVYG 97
Cdd:PRK09629  10 VIEPNDLLERLDAPELILVDLTS-SARYEAGHIRGARFVDPKRtQLGKPPAPGLLpDTADLEQLFGELGHNPDAVYVVYD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488   98 DKSNWWAAFTLWVFELFGHSDVRLLNGGRDAWMAEERDTSYVVPeyPSANYPVVERVDENQRAfVAEVLGSLTQSGGMTL 177
Cdd:PRK09629  89 DEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVP--PVAGGPVTLTLHDEPTA-TREYLQSRLGAADLAI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  178 VDVRTPSEFSGldehgnptSNTGVLRGGHIPGAINLDWSDAVLPNGNFRTRAELDKLYADL--NPADDTVVYCQVGDRAA 255
Cdd:PRK09629 166 WDARAPTEYSG--------EKVVAAKGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLgiTPDKEVITHCQTHHRSG 237

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 21903488  256 HTWFVLKyLLGFNNVRNYDGSWAEWGNMVRMPIETGE 292
Cdd:PRK09629 238 FTYLVAK-ALGYPRVKAYAGSWGEWGNHPDTPVEVPT 273
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 17-291 4.67e-30

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 114.80  E-value: 4.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488   17 PERIVSASWLSARLGSPGLKVVES------NEDSLL---YDIGHLPGAV--RIDWAKDLNDPLTRDFIDGEAFAELMNRK 85
Cdd:PRK11493   3 TTWFVAADWLAEHIDDPEIQIIDArmappgQEDRDVaaeYRAGHIPGAVffDIEALSDHTSPLPHMMPRPETFAVAMREL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488   86 GIARDDTVVVYgDKSNWWAA-FTLWVFELFGHSDVRLLNGGRDAWMAEERDTSYVVPEYPSANYPVVerVDENQRAFVAE 164
Cdd:PRK11493  83 GVNQDKHLVVY-DEGNLFSApRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAA--FNPEAVVRLTD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  165 VLgSLTQSGGMTLVDVRTPSEFSGLDEHGNPTsntgvLRGGHIPGAINLDWSDAVLpNGNFRTRAELDKLY--ADLNPAD 242
Cdd:PRK11493 160 VL-LASHEKTAQIVDARPAARFNAEVDEPRPG-----LRRGHIPGALNVPWTELVR-EGELKTTDELDAIFfgRGVSFDR 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 21903488  243 DTVVYCQVGDRAAHTWFVLkYLLGFNNVRNYDGSWAEWGNMVRMPIETG 291
Cdd:PRK11493 233 PIIASCGSGVTAAVVVLAL-ATLDVPNVKLYDGAWSEWGARADLPVEPA 280
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 15-290 3.70e-26

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 105.27  E-value: 3.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488   15 AHPERIVSASWLSARLGSPGLKVVES-------NEDSLL-YDIGHLPGAV--RIDWAKDLNDPLTRDFIDGEAFAELMNR 84
Cdd:PLN02723  18 STNEPVVSVDWLHANLREPDVKVLDAswympdeQRNPIQeYQVAHIPGALffDLDGISDRTTDLPHMLPSEEAFAAAVSA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488   85 KGIARDDTVVVYGDKSNWWAAFTLWVFELFGHSDVRLLNGGRDAWMAEERDTSYVVPE----YPSANYPVVERVDENQRA 160
Cdd:PLN02723  98 LGIENKDGVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGdailKASAASEAIEKVYQGQTV 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  161 --------FVAEVLGSLTQ------SGGMTLVDVRTPSEFSGLdehgNPTSNTGVlRGGHIPGAI------NLDWSDAVL 220
Cdd:PLN02723 178 spitfqtkFQPHLVWTLEQvkknieDKTYQHIDARSKARFDGA----APEPRKGI-RSGHIPGSKcvpfpqMLDSSQTLL 252

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  221 PNGNFRTRAEldklYADLNPADDTVVYCQVGDRAAHTWFVLkYLLGFNNVRNYDGSWAEWGNMVRMPIET 290
Cdd:PLN02723 253 PAEELKKRFE----QEGISLDSPIVASCGTGVTACILALGL-HRLGKTDVPVYDGSWTEWGALPDTPVAT 317
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 171-280 3.09e-21

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: 86.36  E-value: 3.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488    171 QSGGMTLVDVRTPSEFsgldehgnptsntgvlRGGHIPGAINLDWSDAVLPNGNFRTRAELDKL-YADLNPADDTVVYCQ 249
Cdd:smart00450   1 NDEKVVLLDVRSPEEY----------------EGGHIPGAVNIPLSELLDRRGELDILEFEELLkRLGLDKDKPVVVYCR 64

                           90       100       110
                   ....*....|....*....|....*....|.
gi 21903488    250 VGDRAAHTWFVLKyLLGFNNVRNYDGSWAEW 280
Cdd:smart00450  65 SGNRSAKAAWLLR-ELGFKNVYLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 171-280 4.14e-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: 85.61  E-value: 4.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488   171 QSGGMTLVDVRTPSEFSGldehgnptsntgvlrgGHIPGAINLDWSDAVLPNGNFrtrAELDKLYADLNPADDTVVYCQV 250
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAK----------------GHIPGAVNVPLSSLSLPPLPL---LELLEKLLELLKDKPIVVYCNS 62

                          90       100       110
                  ....*....|....*....|....*....|
gi 21903488   251 GDRAAHTWFVLKYlLGFNNVRNYDGSWAEW 280
Cdd:pfam00581  63 GNRAAAAAALLKA-LGYKNVYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 47-135 7.06e-17

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: 74.42  E-value: 7.06e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488     47 YDIGHLPGAVRIDWAKDLNDPLTRDFIDgeaFAELMNRKGIARDDTVVVYgDKSNWWAAFTLWVFELFGHSDVRLLNGGR 126
Cdd:smart00450  16 YEGGHIPGAVNIPLSELLDRRGELDILE---FEELLKRLGLDKDKPVVVY-CRSGNRSAKAAWLLRELGFKNVYLLDGGY 91


                   ....*....
gi 21903488    127 DAWMAEERD 135
Cdd:smart00450  92 KEWSAAGPP 100
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 171-292 2.92e-16

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 73.08  E-value: 2.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 171 QSGGMTLVDVRTPSEFsgldehgnptsntgvlRGGHIPGAINLDWSdavlpngnfrtraELDKLYADLNPADDTVVYCQV 250
Cdd:COG0607  16 ESEDAVLLDVREPEEF----------------AAGHIPGAINIPLG-------------ELAERLDELPKDKPIVVYCAS 66

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 21903488 251 GDRAAHtwfVLKYL--LGFNNVRNYDGSWAEWgNMVRMPIETGE 292
Cdd:COG0607  67 GGRSAQ---AAALLrrAGYTNVYNLAGGIEAW-KAAGLPVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 166-280 4.67e-16

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: 71.95  E-value: 4.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 166 LGSLTQSGGMTLVDVRTPSEFsgldehgnptsntgvlRGGHIPGAINldwsdavLPNGNFRTRAELDKlyadLNPADDTV 245
Cdd:cd00158   2 LKELLDDEDAVLLDVREPEEY----------------AAGHIPGAIN-------IPLSELEERAALLE----LDKDKPIV 54

                        90       100       110
                ....*....|....*....|....*....|....*
gi 21903488 246 VYCQVGDRAAHTWFVLKyLLGFNNVRNYDGSWAEW 280
Cdd:cd00158  55 VYCRSGNRSARAAKLLR-KAGGTNVYNLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 47-129 1.47e-11

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


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 59.81  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488    47 YDIGHLPGAVRIDWakdlNDPLTRDFIDGEAFAELMNRkgiARDDTVVVYgDKSNWWAAFTLWVFELFGHSDVRLLNGGR 126
Cdd:pfam00581  17 YAKGHIPGAVNVPL----SSLSLPPLPLLELLEKLLEL---LKDKPIVVY-CNSGNRAAAAAALLKALGYKNVYVLDGGF 88


                  ...
gi 21903488   127 DAW 129
Cdd:pfam00581  89 EAW 91
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 169-280 5.37e-11

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: 58.44  E-value: 5.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 169 LTQSGGMTLVDVRTPSEfsgldehgnptsntgvLRGGHIPGAINLDWSDAV----LPNGNFRTRAELDKlyadlnPADDT 244
Cdd:cd01519  10 PNPHPNKVLIDVREPEE----------------LKTGKIPGAINIPLSSLPdalaLSEEEFEKKYGFPK------PSKDK 67

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 21903488 245 --VVYCQVGDRAAHTWFVLKyLLGFNNVRNYDGSWAEW 280
Cdd:cd01519  68 elIFYCKAGVRSKAAAELAR-SLGYENVGNYPGSWLDW 104
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 21-121 4.34e-10

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: 56.49  E-value: 4.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  21 VSASWLSARLGSPGLKVV--------ESNEDSLLYDI--GHLPGAVRIDWAKDLNDPLTrdFIDGEAFAELMNRKGIARD 90
Cdd:cd01449   1 VTAEEVLANLDSGDVQLVdarsperfRGEVPEPRPGLrsGHIPGAVNIPWTSLLDEDGT--FKSPEELRALFAALGITPD 78

                        90       100       110
                ....*....|....*....|....*....|.
gi 21903488  91 DTVVVYgDKSNWWAAFTLWVFELFGHSDVRL 121
Cdd:cd01449  79 KPVIVY-CGSGVTACVLLLALELLGYKNVRL 108
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 19-130 2.27e-07

Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only the second repeat contains the catalytically active Cys residue. The role of the 1st repeat is uncertain, but believed to be involved in protein interaction. This CD aligns the 1st and 2nd repeats.


Pssm-ID: 238722 [Multi-domain]  Cd Length: 138  Bit Score: 49.02  E-value: 2.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  19 RIVSASWLSARLGSPGLKVVESNE--DSLLYDIGHLPGAVRIDWA--KDLNDPLTRDFIDGEAFAELMNRKGIARDDTVV 94
Cdd:cd01445  20 QLLDARAQSPGTREARGEYLETQPepDAVGLDSGHIPGASFFDFEecLDEAGFEESMEPSEAEFAAMFEAKGIDLDKHLI 99

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 21903488  95 VYG--DKSNWWAAFTLWVFELFGHSDVRLLNGGRDAWM 130
Cdd:cd01445 100 ATDgdDLGGFTACHIALAARLCGHPDVAILDGGFFEWF 137
PLN02160 PLN02160
thiosulfate sulfurtransferase
 168-280 2.95e-07

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 48.93  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  168 SLTQSGGMTLvDVRTPSEFsgldehgnptsntgvlRGGHIPGA--INLDWSDAVlPNGNFRTRAELDKLYADLNPADDTV 245
Cdd:PLN02160  24 TLLQSGHQYL-DVRTQDEF----------------RRGHCEAAkiVNIPYMLNT-PQGRVKNQEFLEQVSSLLNPADDIL 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 21903488  246 VYCQVGDRA--AHTWFVLKyllGFNNVRNYDGSWAEW 280
Cdd:PLN02160  86 VGCQSGARSlkATTELVAA---GYKKVRNKGGGYLAW 119
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 174-275 3.60e-07

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: 47.26  E-value: 3.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 174 GMTLVDVRTPSEFsgldehgnptsntgvlRGGHIPGAINLdwsdavlPNGNFRTR-AELDKlyadlnpADDTVVYCQVGD 252
Cdd:cd01524  13 GVTLIDVRTPQEF----------------EKGHIKGAINI-------PLDELRDRlNELPK-------DKEIIVYCAVGL 62

                        90       100
                ....*....|....*....|....*
gi 21903488 253 R--AAHTWFVLKyllGFnNVRNYDG 275
Cdd:cd01524  63 RgyIAARILTQN---GF-KVKNLDG 83
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 174-280 9.43e-07

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 49.49  E-value: 9.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  174 GMTLVDVRTPSEFSgldehgnptsntgvlrGGHIPGAINLdwsdavlpngnfrtraELDKLYADLNP-----ADDTVVYC 248
Cdd:PRK05597 274 GVTLIDVREPSEFA----------------AYSIPGAHNV----------------PLSAIREGANPpsvsaGDEVVVYC 321

                         90       100       110
                 ....*....|....*....|....*....|..
gi 21903488  249 QVGDRAAHTWFVLKYlLGFNNVRNYDGSWAEW 280
Cdd:PRK05597 322 AAGVRSAQAVAILER-AGYTGMSSLDGGIEGW 352
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 21-132 4.07e-06

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: 44.96  E-value: 4.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  21 VSASWLSARLGSPGLKVV---ESNEdsllYDIGHLPGAVRIDWAKdlndpltrdfidgeaFAELMNRkgIARDDTVVVY- 96
Cdd:COG0607   6 ISPAELAELLESEDAVLLdvrEPEE----FAAGHIPGAINIPLGE---------------LAERLDE--LPKDKPIVVYc 64

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 21903488  97 --GDKSnWWAAFTLwvfELFGHSDVRLLNGGRDAWMAE 132
Cdd:COG0607  65 asGGRS-AQAAALL---RRAGYTNVYNLAGGIEAWKAA 98
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 169-280 1.36e-05

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: 43.18  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 169 LTQSGGMTLVDVRTPSEfsgldehgnptsntgVLRGGHIPGAINLdwsdavlPNGNFRTRAELDKLYAD--LNPADDTVV 246
Cdd:cd01447   9 LLGSPGVLLVDVRDPRE---------------LERTGMIPGAFHA-------PRGMLEFWADPDSPYHKpaFAEDKPFVF 66

                        90       100       110
                ....*....|....*....|....*....|....
gi 21903488 247 YCQVGDRAAHTWFVLKYlLGFNNVRNYDGSWAEW 280
Cdd:cd01447  67 YCASGWRSALAGKTLQD-MGLKPVYNIEGGFKDW 99
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
171-295 1.48e-05

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 46.16  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  171 QSGGMTLVDVRTPSEFSGldehgnptsntgvlrgGHIPGAINLDwsdavlpngnfrtRAELDKLYADLNPADDT--VVYC 248
Cdd:PRK08762  14 AAQGAVLIDVREAHERAS----------------GQAEGALRIP-------------RGFLELRIETHLPDRDReiVLIC 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 21903488  249 QVGDRAAHTWFVLKyLLGFNNVRNYDG---SWAEWGNMVRMPIETGENTK 295
Cdd:PRK08762  65 ASGTRSAHAAATLR-ELGYTRVASVAGgfsAWKDAGLPLERPRLLTDEQD 113
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 162-280 6.23e-05

Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only the second repeat contains the catalytically active Cys residue. The role of the 1st repeat is uncertain, but believed to be involved in protein interaction. This CD aligns the 1st and 2nd repeats.


Pssm-ID: 238722 [Multi-domain]  Cd Length: 138  Bit Score: 42.09  E-value: 6.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 162 VAEVLGSLTQSGGMTLVDVR--TPSEFSGLDEH--GNPTSNTGVLRGGHIPGAINLDWSDAVLPNGNFR----TRAELDK 233
Cdd:cd01445   6 LAENLEAGKVGKGFQLLDARaqSPGTREARGEYleTQPEPDAVGLDSGHIPGASFFDFEECLDEAGFEEsmepSEAEFAA 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 21903488 234 LYADLNPADDTVVYCQVGDR-----AAHTWFVLkYLLGFNNVRNYDGSWAEW 280
Cdd:cd01445  86 MFEAKGIDLDKHLIATDGDDlggftACHIALAA-RLCGHPDVAILDGGFFEW 136
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 205-280 8.12e-05

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 41.45  E-value: 8.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 205 GHIPGAINLDWSDAVLPN----GNFRTRAELDKLYADLNPADDT--VVYCQVGDR-AAHTWFVLKYlLGFNNVRNYDGSW 277
Cdd:cd01448  37 GHIPGAVFFDLDEDLDDKspgpHMLPSPEEFAELLGSLGISNDDtvVVYDDGGGFfAARAWWTLRY-FGHENVRVLDGGL 115


                ...
gi 21903488 278 AEW 280
Cdd:cd01448 116 QAW 118
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 177-280 1.21e-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: 40.46  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488 177 LVDVRTPSEfsgldehgnptsntgvLRGGHIPGAINLdwsdavlPNGNFRTRA-ELDklyaDLNPADDTVVYCQVGDRAA 255
Cdd:cd01528  20 LIDVREPEE----------------LEIAFLPGFLHL-------PMSEIPERSkELD----SDNPDKDIVVLCHHGGRSM 72

                        90       100
                ....*....|....*....|....*..
gi 21903488 256 HTWFvlkYLL--GFNNVRNYDGSWAEW 280
Cdd:cd01528  73 QVAQ---WLLrqGFENVYNLQGGIDAW 96
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 47-129 1.75e-04

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: 39.59  E-value: 1.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  47 YDIGHLPGAVRIdwakdlndPLTRdfidgeaFAELMNRKGIARDDTVVVYgDKSNWWAAFTLWVFELFGHSDVRLLNGGR 126
Cdd:cd00158  22 YAAGHIPGAINI--------PLSE-------LEERAALLELDKDKPIVVY-CRSGNRSARAAKLLRKAGGTNVYNLEGGM 85


                ...
gi 21903488 127 DAW 129
Cdd:cd00158  86 LAW 88
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 177-213 3.88e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 38.27  E-value: 3.88e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 21903488  177 LVDVRTPSEFsglDEhgnptsntgvlrgGHIPGAINL 213
Cdd:PRK11784  18 LIDVRSPIEF---AE-------------GHIPGAINL 38
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 47-131 4.92e-03

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 35.70  E-value: 4.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21903488  47 YDIGHLPGAVRIDwakdlNDPLtrdfidgeafAELMNRkgIARDDTVVVY---GDKSNWWAAFtlwvFELFGHSDVRLLN 123
Cdd:cd01444  30 ALPDHIPGAIHLD-----EDSL----------DDWLGD--LDRDRPVVVYcyhGNSSAQLAQA----LREAGFTDVRSLA 88


                ....*...
gi 21903488 124 GGRDAWMA 131
Cdd:cd01444  89 GGFEAWRR 96
tRNA_sel_U_synt TIGR03167
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ...
 176-213 9.67e-03

tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274463 [Multi-domain]  Cd Length: 311  Bit Score: 37.19  E-value: 9.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 21903488   176 TLVDVRTPSEFsglDEhgnptsntgvlrgGHIPGAINL 213
Cdd:TIGR03167   4 PLIDVRSPAEF---AE-------------GHLPGAINL 25
 
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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