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Conserved domains on  [gi|115534702|ref|NP_506242|]
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Rhodanese domain-containing protein [Caenorhabditis elegans]

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 ...
 155-404 7.49e-55

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


:

Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 182.68  E-value: 7.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 155 LITKRKICILEAaSGDEAKSRDAFSVDHIESARLI-FHSNLS-HAGVPVHPL----QFQRFARSQGIDNDCHVIVYDRGQ 228
Cdd:COG2897    4 HLDDPDVVILDV-RWDLPDGRAAYEAGHIPGAVFLdLDTDLSdPRSPGRHPLpspeAFAALLGALGISNDTTVVVYDDGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 229 MIWSSYTVWIFKLFGHQKVSLLSGGYLGWKTHqarsgQYKTEQGDAPRKPrqGDFLASWNDSVIITYDDVLLNSEIDNFD 308
Cdd:COG2897   83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAA-----GLPLETGPPTPAP--GDFTARPDPELLADADEVLAALGDPDAV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 309 VVDAQTKDEFLGTA--QGALYGHIKGARNIPVDAVYDwAVGQWKDADHLKGLFNNNALSLRKPVIIYCSTSLRSAMVWWA 386
Cdd:COG2897  156 LVDARSPERYRGEVepIDPRAGHIPGAVNLPWTDLLD-EDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLA 234

                        250
                 ....*....|....*....
gi 115534702 387 LTRSGY-NGKIYFGGWPEW 404
Cdd:COG2897  235 LELLGYpNVRLYDGSWSEW 253
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 155-404 7.49e-55

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 182.68  E-value: 7.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 155 LITKRKICILEAaSGDEAKSRDAFSVDHIESARLI-FHSNLS-HAGVPVHPL----QFQRFARSQGIDNDCHVIVYDRGQ 228
Cdd:COG2897    4 HLDDPDVVILDV-RWDLPDGRAAYEAGHIPGAVFLdLDTDLSdPRSPGRHPLpspeAFAALLGALGISNDTTVVVYDDGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 229 MIWSSYTVWIFKLFGHQKVSLLSGGYLGWKTHqarsgQYKTEQGDAPRKPrqGDFLASWNDSVIITYDDVLLNSEIDNFD 308
Cdd:COG2897   83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAA-----GLPLETGPPTPAP--GDFTARPDPELLADADEVLAALGDPDAV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 309 VVDAQTKDEFLGTA--QGALYGHIKGARNIPVDAVYDwAVGQWKDADHLKGLFNNNALSLRKPVIIYCSTSLRSAMVWWA 386
Cdd:COG2897  156 LVDARSPERYRGEVepIDPRAGHIPGAVNLPWTDLLD-EDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLA 234

                        250
                 ....*....|....*....
gi 115534702 387 LTRSGY-NGKIYFGGWPEW 404
Cdd:COG2897  235 LELLGYpNVRLYDGSWSEW 253
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 191-408 2.02e-31

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 120.97  E-value: 2.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 191 HSNLSHAgVPvHPLQFQRFARSQGIDNDCHVIVYDRGQMIWSSYTVWIFKLFGHQKVSLLSGGYLGWKtHQarsgQYKTE 270
Cdd:PRK11493  62 TSPLPHM-MP-RPETFAVAMRELGVNQDKHLVVYDEGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQ-RD----DLLLE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 271 QGDAPRKPrqGDFLASWNDSVIITYDDVLLNSEIDNFDVVDAQTKDEFLGTAQ----GALYGHIKGARNIP-VDAVYDwa 345
Cdd:PRK11493 135 EGAVELPE--GEFNAAFNPEAVVRLTDVLLASHEKTAQIVDARPAARFNAEVDeprpGLRRGHIPGALNVPwTELVRE-- 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115534702 346 vGQWKDADHLKGLFNNNALSLRKPVIIYCSTSLRSAMVWWALTRSGYNG-KIYFGGWPEWVVRA 408
Cdd:PRK11493 211 -GELKTTDELDAIFFGRGVSFDRPIIASCGSGVTAAVVVLALATLDVPNvKLYDGAWSEWGARA 273
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 146-260 5.53e-29

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: 109.63  E-value: 5.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 146 MTPNHLLTLLITKRkICILEAASGDEA-KSRDAFSVDHIESARLI-FHSNLSHAGVPVHPL----QFQRFARSQGIDNDC 219
Cdd:cd01448    2 VSPDWLAEHLDDPD-VRILDARWYLPDrDGRKEYLEGHIPGAVFFdLDEDLDDKSPGPHMLpspeEFAELLGSLGISNDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 115534702 220 HVIVYDRGQMIWSSYTVWIFKLFGHQKVSLLSGGYLGWKTH 260
Cdd:cd01448   81 TVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAE 121
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 174-260 2.51e-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: 76.73  E-value: 2.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702   174 SRDAFSVDHIESARLIFHSNLSHAGVPVHPLQFQRFARSQGIDNDCHVIVYDRGQMiWSSYTVWIFKLFGHQKVSLLSGG 253
Cdd:smart00450  12 SPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGN-RSAKAAWLLRELGFKNVYLLDGG 90


                   ....*..
gi 115534702   254 YLGWKTH 260
Cdd:smart00450  91 YKEWSAA 97
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 303-405 3.53e-15

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: 70.59  E-value: 3.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702  303 EIDNFDVVDAQTKDEFLGtaqgalyGHIKGARNIPVDAVYDWAVGQWKDADHLKGLFNNnalslrKPVIIYCSTSLRSAM 382
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAK-------GHIPGAVNVPLSSLSLPPLPLLELLEKLLELLKD------KPIVVYCNSGNRAAA 68

                          90       100
                  ....*....|....*....|....
gi 115534702  383 VWWALTRSGY-NGKIYFGGWPEWV 405
Cdd:pfam00581  69 AAALLKALGYkNVYVLDGGFEAWK 92
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 155-404 7.49e-55

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 182.68  E-value: 7.49e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 155 LITKRKICILEAaSGDEAKSRDAFSVDHIESARLI-FHSNLS-HAGVPVHPL----QFQRFARSQGIDNDCHVIVYDRGQ 228
Cdd:COG2897    4 HLDDPDVVILDV-RWDLPDGRAAYEAGHIPGAVFLdLDTDLSdPRSPGRHPLpspeAFAALLGALGISNDTTVVVYDDGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 229 MIWSSYTVWIFKLFGHQKVSLLSGGYLGWKTHqarsgQYKTEQGDAPRKPrqGDFLASWNDSVIITYDDVLLNSEIDNFD 308
Cdd:COG2897   83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAA-----GLPLETGPPTPAP--GDFTARPDPELLADADEVLAALGDPDAV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 309 VVDAQTKDEFLGTA--QGALYGHIKGARNIPVDAVYDwAVGQWKDADHLKGLFNNNALSLRKPVIIYCSTSLRSAMVWWA 386
Cdd:COG2897  156 LVDARSPERYRGEVepIDPRAGHIPGAVNLPWTDLLD-EDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLA 234

                        250
                 ....*....|....*....
gi 115534702 387 LTRSGY-NGKIYFGGWPEW 404
Cdd:COG2897  235 LELLGYpNVRLYDGSWSEW 253
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 191-408 2.02e-31

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 120.97  E-value: 2.02e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 191 HSNLSHAgVPvHPLQFQRFARSQGIDNDCHVIVYDRGQMIWSSYTVWIFKLFGHQKVSLLSGGYLGWKtHQarsgQYKTE 270
Cdd:PRK11493  62 TSPLPHM-MP-RPETFAVAMRELGVNQDKHLVVYDEGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQ-RD----DLLLE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 271 QGDAPRKPrqGDFLASWNDSVIITYDDVLLNSEIDNFDVVDAQTKDEFLGTAQ----GALYGHIKGARNIP-VDAVYDwa 345
Cdd:PRK11493 135 EGAVELPE--GEFNAAFNPEAVVRLTDVLLASHEKTAQIVDARPAARFNAEVDeprpGLRRGHIPGALNVPwTELVRE-- 210

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115534702 346 vGQWKDADHLKGLFNNNALSLRKPVIIYCSTSLRSAMVWWALTRSGYNG-KIYFGGWPEWVVRA 408
Cdd:PRK11493 211 -GELKTTDELDAIFFGRGVSFDRPIIASCGSGVTAAVVVLALATLDVPNvKLYDGAWSEWGARA 273
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 146-260 5.53e-29

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: 109.63  E-value: 5.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 146 MTPNHLLTLLITKRkICILEAASGDEA-KSRDAFSVDHIESARLI-FHSNLSHAGVPVHPL----QFQRFARSQGIDNDC 219
Cdd:cd01448    2 VSPDWLAEHLDDPD-VRILDARWYLPDrDGRKEYLEGHIPGAVFFdLDEDLDDKSPGPHMLpspeEFAELLGSLGISNDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 115534702 220 HVIVYDRGQMIWSSYTVWIFKLFGHQKVSLLSGGYLGWKTH 260
Cdd:cd01448   81 TVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAE 121
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 293-404 4.90e-24

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: 96.16  E-value: 4.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 293 ITYDDVLLNSEIDNFDVVDAQTKDEFLGTA----QGALYGHIKGARNIPVDAVYDwAVGQWKDADHLKGLFNNNALSLRK 368
Cdd:cd01449    1 VTAEEVLANLDSGDVQLVDARSPERFRGEVpeprPGLRSGHIPGAVNIPWTSLLD-EDGTFKSPEELRALFAALGITPDK 79

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 115534702 369 PVIIYCSTSLRSAMVWWALTRSGY-NGKIYFGGWPEW 404
Cdd:cd01449   80 PVIVYCGSGVTACVLLLALELLGYkNVRLYDGSWSEW 116
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 178-404 1.02e-21

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 94.87  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 178 FSVDHIESArLIFH--------SNLSHAgVPVHPlQFQRFARSQGIDNDCHVIVYDrGQMIWSSYTVW-IFKLFGHQKVS 248
Cdd:PLN02723  58 YQVAHIPGA-LFFDldgisdrtTDLPHM-LPSEE-AFAAAVSALGIENKDGVVVYD-GKGIFSAARVWwMFRVFGHEKVW 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 249 LLSGGYLGWKThqarSGqYKTE---QGDA----------PRKPRQGD------FLASWNDSVIITYDDVLLNSEIDNFDV 309
Cdd:PLN02723 134 VLDGGLPKWRA----SG-YDVEssaSGDAilkasaaseaIEKVYQGQtvspitFQTKFQPHLVWTLEQVKKNIEDKTYQH 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 310 VDAQTKDEFLGTA----QGALYGHIKGARNIPVDAVYDwAVGQWKDADHLKGLFNNNALSLRKPVIIYCSTSLRSAMVWW 385
Cdd:PLN02723 209 IDARSKARFDGAApeprKGIRSGHIPGSKCVPFPQMLD-SSQTLLPAEELKKRFEQEGISLDSPIVASCGTGVTACILAL 287

                        250       260
                 ....*....|....*....|
gi 115534702 386 ALTRSG-YNGKIYFGGWPEW 404
Cdd:PLN02723 288 GLHRLGkTDVPVYDGSWTEW 307
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 174-260 2.51e-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: 76.73  E-value: 2.51e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702   174 SRDAFSVDHIESARLIFHSNLSHAGVPVHPLQFQRFARSQGIDNDCHVIVYDRGQMiWSSYTVWIFKLFGHQKVSLLSGG 253
Cdd:smart00450  12 SPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGN-RSAKAAWLLRELGFKNVYLLDGG 90


                   ....*..
gi 115534702   254 YLGWKTH 260
Cdd:smart00450  91 YKEWSAA 97
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 309-404 1.01e-16

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: 75.19  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702   309 VVDAQTKDEFLGtaqgalyGHIKGARNIPVDAVYDWAvgQWKDADHLKGLFNNNALSLRKPVIIYCSTSLRSAMVWWALT 388
Cdd:smart00450   7 LLDVRSPEEYEG-------GHIPGAVNIPLSELLDRR--GELDILEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLR 77

                           90
                   ....*....|....*..
gi 115534702   389 RSGY-NGKIYFGGWPEW 404
Cdd:smart00450  78 ELGFkNVYLLDGGYKEW 94
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 303-405 3.53e-15

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: 70.59  E-value: 3.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702  303 EIDNFDVVDAQTKDEFLGtaqgalyGHIKGARNIPVDAVYDWAVGQWKDADHLKGLFNNnalslrKPVIIYCSTSLRSAM 382
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAK-------GHIPGAVNVPLSSLSLPPLPLLELLEKLLELLKD------KPIVVYCNSGNRAAA 68

                          90       100
                  ....*....|....*....|....
gi 115534702  383 VWWALTRSGY-NGKIYFGGWPEWV 405
Cdd:pfam00581  69 AAALLKALGYkNVYVLDGGFEAWK 92
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 305-405 2.51e-11

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: 59.62  E-value: 2.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 305 DNFDVVDAQTKDEFLGtaqgalyGHIKGARNIPVDavydwavgQWKDADHLKGLFNNnalslrKPVIIYCSTSLRSAMVW 384
Cdd:cd00158    9 EDAVLLDVREPEEYAA-------GHIPGAINIPLS--------ELEERAALLELDKD------KPIVVYCRSGNRSARAA 67

                         90       100
                 ....*....|....*....|...
gi 115534702 385 WALTRSGYNgKIYF--GGWPEWV 405
Cdd:cd00158   68 KLLRKAGGT-NVYNleGGMLAWK 89
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 293-404 3.31e-10

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: 56.90  E-value: 3.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 293 ITYDDVLLNSEIDNFDVVDAQTKDEFLGtaqgalyGHIKGARNIPVDAVYDWAvgqwkdadhlkglfnnNALSLRKPVII 372
Cdd:COG0607    6 ISPAELAELLESEDAVLLDVREPEEFAA-------GHIPGAINIPLGELAERL----------------DELPKDKPIVV 62

                         90       100       110
                 ....*....|....*....|....*....|...
gi 115534702 373 YCSTSLRSAMVWWALTRSGY-NGKIYFGGWPEW 404
Cdd:COG0607   63 YCASGGRSAQAAALLRRAGYtNVYNLAGGIEAW 95
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 146-404 7.89e-09

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 57.44  E-value: 7.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 146 MTPNHLLTLLITKRKICIleaasgdEAKSRDAFSVDHIESARLIfHSNLSHAGVPVHP------LQFQRFARSQGIDNDC 219
Cdd:PRK09629  11 IEPNDLLERLDAPELILV-------DLTSSARYEAGHIRGARFV-DPKRTQLGKPPAPgllpdtADLEQLFGELGHNPDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 220 HVIVYDRGQMIWSSYTVWIFKLFGHQKVSLLSGGYLGWkthQARSGQYKTEQGDAPRKPrqgdFLASWNDSVIITYDDVL 299
Cdd:PRK09629  83 VYVVYDDEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAW---EAQALPLSTDVPPVAGGP----VTLTLHDEPTATREYLQ 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 300 LNSEIDNFDVVDAQTKDEFLG-TAQGALYGHIKGARNipvdavYDWAVGQWKDAD-----HLKGLFNNNALSLRKPVIIY 373
Cdd:PRK09629 156 SRLGAADLAIWDARAPTEYSGeKVVAAKGGHIPGAVN------FEWTAGMDKARNlrirqDMPEILRDLGITPDKEVITH 229

                        250       260       270
                 ....*....|....*....|....*....|..
gi 115534702 374 CSTSLRSAMVWWALTRSGY-NGKIYFGGWPEW 404
Cdd:PRK09629 230 CQTHHRSGFTYLVAKALGYpRVKAYAGSWGEW 261
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 174-258 8.65e-09

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: 52.49  E-value: 8.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702  174 SRDAFSVDHIESARLIFHSNLSHAGVPVHPLqfqrFARSQGIDNDCHVIVYDRGqMIWSSYTVWIFKLFGHQKVSLLSGG 253
Cdd:pfam00581  13 PPEEYAKGHIPGAVNVPLSSLSLPPLPLLEL----LEKLLELLKDKPIVVYCNS-GNRAAAAAALLKALGYKNVYVLDGG 87


                  ....*
gi 115534702  254 YLGWK 258
Cdd:pfam00581  88 FEAWK 92
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 205-257 7.90e-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: 48.25  E-value: 7.90e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 115534702 205 QFQRFARSQGIDNDCHVIVYDRGQM--IWSSYTVWIFKLFGHQKVSLLSGGYLGW 257
Cdd:cd01445   82 EFAAMFEAKGIDLDKHLIATDGDDLggFTACHIALAARLCGHPDVAILDGGFFEW 136
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 292-405 6.87e-06

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: 44.92  E-value: 6.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 292 IITYDDVLLNSEIDNFDVVDAQTKDEFLGTAQGALYGHIKGARNIPVDAVYDWAVGQWK---DADHLKGLFNNNALSLRK 368
Cdd:cd01448    1 LVSPDWLAEHLDDPDVRILDARWYLPDRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHmlpSPEEFAELLGSLGISNDD 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 115534702 369 PVIIYCSTSLRSA-MVWWALTRSGY-NGKIYFGGWPEWV 405
Cdd:cd01448   81 TVVVYDDGGGFFAaRAWWTLRYFGHeNVRVLDGGLQAWK 119
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 303-400 1.76e-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: 43.02  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 303 EIDNFD-----VVDAQTKDEFLGtaqgalyGHIKGARNIPVDAVydwavgqwkdADHLkglfnnNALSLRKPVIIYCSTS 377
Cdd:cd01524    5 ELDNYRadgvtLIDVRTPQEFEK-------GHIKGAINIPLDEL----------RDRL------NELPKDKEIIVYCAVG 61

                         90       100
                 ....*....|....*....|...
gi 115534702 378 LRSAMVWWALTRSGYNGKIYFGG 400
Cdd:cd01524   62 LRGYIAARILTQNGFKVKNLDGG 84
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 294-405 1.42e-04

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: 40.72  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 294 TYDDV--LLNSEiDNFDVVDAQTKDEFLgtaqgalYGHIKGARNIPVDAVYD-WAVgqwkDADHLKGLFNNNALSLRKPV 370
Cdd:cd01519    2 SFEEVknLPNPH-PNKVLIDVREPEELK-------TGKIPGAINIPLSSLPDaLAL----SEEEFEKKYGFPKPSKDKEL 69

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 115534702 371 IIYCSTSLRSAMVWWALTRSGY-NGKIYFGGWPEWV 405
Cdd:cd01519   70 IFYCKAGVRSKAAAELARSLGYeNVGNYPGSWLDWA 105
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 152-258 4.00e-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: 39.21  E-value: 4.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 152 LTLLITKRKICILeaasgDeAKSRDAFSVDHIESARLIfhsnlshagvpvhPL-QFQRFARSQGIDNDCHVIVYDR-GQM 229
Cdd:cd00158    2 LKELLDDEDAVLL-----D-VREPEEYAAGHIPGAINI-------------PLsELEERAALLELDKDKPIVVYCRsGNR 62

                         90       100
                 ....*....|....*....|....*....
gi 115534702 230 iwSSYTVWIFKLFGHQKVSLLSGGYLGWK 258
Cdd:cd00158   63 --SARAAKLLRKAGGTNVYNLEGGMLAWK 89
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 272-404 7.52e-04

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 41.40  E-value: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 272 GDAPRKPRQGDFLASWNDSVIITYDDVLLNSEIDNFDVVDAQTKDEFLgtaqgalYGHIKGARNIPVDAVydwavgqwkd 351
Cdd:PRK05597 240 PAVLERVRGSTPVHGISGGFGEVLDVPRVSALPDGVTLIDVREPSEFA-------AYSIPGAHNVPLSAI---------- 302

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 115534702 352 adhLKGLfNNNALSLRKPVIIYCSTSLRSAMVWWALTRSGYNGKIYF-GGWPEW 404
Cdd:PRK05597 303 ---REGA-NPPSVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLdGGIEGW 352
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 182-257 1.29e-03

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: 38.38  E-value: 1.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115534702 182 HIESARLI-FHSNLSHAGVPVHPLQFQRFARSQGIDNDCHVIVYDrGQMIWSSYTVWIFKLFGHQKVSLLSGGYLGW 257
Cdd:cd01449   41 HIPGAVNIpWTSLLDEDGTFKSPEELRALFAALGITPDKPVIVYC-GSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 305-405 2.86e-03

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: 37.39  E-value: 2.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115534702 305 DNFDVVDAQtKDEFLGtaqgalyGHIKGARNIPVDAVYdwavgqwkdaDHLKGLFNNNALSLRKPVIIYCSTSLR--SAM 382
Cdd:cd01443   22 KDFVVVDLR-RDDYEG-------GHIKGSINLPAQSCY----------QTLPQVYALFSLAGVKLAIFYCGSSQGrgPRA 83

                         90       100
                 ....*....|....*....|....*....
gi 115534702 383 VWW---ALTRSGYNGK---IYFGGWPEWV 405
Cdd:cd01443   84 ARWfadYLRKVGESLPksyILTGGIKAWY 112
 
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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