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Conserved domains on  [gi|3122964|sp|Q08686|]
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RecName: Full=Thiosulfate sulfurtransferase TUM1; AltName: Full=Thiouridine modification protein 1; AltName: Full=tRNA-thiouridine modification protein 1

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 ...
 23-290 9.27e-67

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


:

Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 209.26  E-value: 9.27e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   23 RIVPVDATWYLPswklDNKVDFLtKPRIPNSIFFDID-AISDKKSPYPHMFPTKKVFDDAMSNLGVQKDDILVVYDRVGN 101
Cdd:COG2897   9 DVVILDVRWDLP----DGRAAYE-AGHIPGAVFLDLDtDLSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYDDGGG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  102 FSSPRCAWTLGVMGHPKVYLLN-NFNQYREFKYPLDSSKVaafsPYPKSHYESseSFQDKEIVDYEEMFQLVKSGELAKk 180
Cdd:COG2897  84 LFAARAWWLLRYAGHEDVRVLDgGLAAWKAAGLPLETGPP----TPAPGDFTA--RPDPELLADADEVLAALGDPDAVL- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  181 fnaFDARSLGRFEGtEPEPRsDIPSGHIPGTQPLPYGSLLDpETKTYPEAgEAIHATLEKALkdfhctLDPSKPTICSCG 260
Cdd:COG2897 157 ---VDARSPERYRG-EVEPI-DPRAGHIPGAVNLPWTDLLD-EDGTFKSA-EELRALFAALG------IDPDKPVITYCG 223

                       250       260       270
                ....*....|....*....|....*....|
gi 3122964  261 TGVSGVIIKTALELAGVPNVRLYDGSWTEW 290
Cdd:COG2897 224 SGVRAAHTWLALELLGYPNVRLYDGSWSEW 253
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 23-290 9.27e-67

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 209.26  E-value: 9.27e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   23 RIVPVDATWYLPswklDNKVDFLtKPRIPNSIFFDID-AISDKKSPYPHMFPTKKVFDDAMSNLGVQKDDILVVYDRVGN 101
Cdd:COG2897   9 DVVILDVRWDLP----DGRAAYE-AGHIPGAVFLDLDtDLSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYDDGGG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  102 FSSPRCAWTLGVMGHPKVYLLN-NFNQYREFKYPLDSSKVaafsPYPKSHYESseSFQDKEIVDYEEMFQLVKSGELAKk 180
Cdd:COG2897  84 LFAARAWWLLRYAGHEDVRVLDgGLAAWKAAGLPLETGPP----TPAPGDFTA--RPDPELLADADEVLAALGDPDAVL- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  181 fnaFDARSLGRFEGtEPEPRsDIPSGHIPGTQPLPYGSLLDpETKTYPEAgEAIHATLEKALkdfhctLDPSKPTICSCG 260
Cdd:COG2897 157 ---VDARSPERYRG-EVEPI-DPRAGHIPGAVNLPWTDLLD-EDGTFKSA-EELRALFAALG------IDPDKPVITYCG 223

                       250       260       270
                ....*....|....*....|....*....|
gi 3122964  261 TGVSGVIIKTALELAGVPNVRLYDGSWTEW 290
Cdd:COG2897 224 SGVRAAHTWLALELLGYPNVRLYDGSWSEW 253
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 27-290 1.56e-59

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 192.71  E-value: 1.56e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964    27 VDATWYLPSWKLDNKVDFlTKPRIPNSIFFDIDAISDKKSPYPHMFPTKKVFDDAMSNLGVQKDDILVVYDRVGNFSSPR 106
Cdd:PLN02723  41 LDASWYMPDEQRNPIQEY-QVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSALGIENKDGVVVYDGKGIFSAAR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   107 CAWTLGVMGHPKVYLLN-NFNQYREFKYPLDSSKVAAFSPYPKSHYESSESFQDKEIVD---YEEMFQL--------VKS 174
Cdd:PLN02723 120 VWWMFRVFGHEKVWVLDgGLPKWRASGYDVESSASGDAILKASAASEAIEKVYQGQTVSpitFQTKFQPhlvwtleqVKK 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   175 GELAKKFNAFDARSLGRFEGTEPEPRSDIPSGHIPGTQPLPYGSLLDPETKTYPeAGEaihatLEKALKDFHCTLDpsKP 254
Cdd:PLN02723 200 NIEDKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLP-AEE-----LKKRFEQEGISLD--SP 271

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 3122964   255 TICSCGTGVSGVIIKTALELAGVPNVRLYDGSWTEW 290
Cdd:PLN02723 272 IVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 163-290 7.17e-43

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: 143.16  E-value: 7.17e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  163 VDYEEMFQLVKSGELAKkfnaFDARSLGRFEGTEPEPRSDIPSGHIPGTQPLPYGSLLDPETKTYPEagEAIHATLEKAL 242
Cdd:cd01449   1 VTAEEVLANLDSGDVQL----VDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSP--EELRALFAALG 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3122964  243 kdfhctLDPSKPTICSCGTGVSGVIIKTALELAGVPNVRLYDGSWTEW 290
Cdd:cd01449  75 ------ITPDKPVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 178-296 1.94e-13

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: 65.17  E-value: 1.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964     178 AKKFNAFDARSLGRFEGtepeprsdipsGHIPGTQPLPYGSLLDPETKTYPEAGEAIHATLEkalkdfhctLDPSKPTIC 257
Cdd:smart00450   2 DEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELLDRRGELDILEFEELLKRLG---------LDKDKPVVV 61

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 3122964     258 SCGTGVSGVIIKTALELAGVPNVRLYDGSWTEWVLKSGP 296
Cdd:smart00450  62 YCRSGNRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 184-291 2.05e-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: 53.64  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964    184 FDARSLGRFEGtepeprsdipsGHIPGTQPLPYGSLLDPEtktypeageAIHATLEKALKDfhctLDPSKPTICSCGTGV 263
Cdd:pfam00581   9 IDVRPPEEYAK-----------GHIPGAVNVPLSSLSLPP---------LPLLELLEKLLE----LLKDKPIVVYCNSGN 64

                          90       100
                  ....*....|....*....|....*...
gi 3122964    264 SGVIIKTALELAGVPNVRLYDGSWTEWV 291
Cdd:pfam00581  65 RAAAAAALLKALGYKNVYVLDGGFEAWK 92
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 23-290 9.27e-67

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 209.26  E-value: 9.27e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   23 RIVPVDATWYLPswklDNKVDFLtKPRIPNSIFFDID-AISDKKSPYPHMFPTKKVFDDAMSNLGVQKDDILVVYDRVGN 101
Cdd:COG2897   9 DVVILDVRWDLP----DGRAAYE-AGHIPGAVFLDLDtDLSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYDDGGG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  102 FSSPRCAWTLGVMGHPKVYLLN-NFNQYREFKYPLDSSKVaafsPYPKSHYESseSFQDKEIVDYEEMFQLVKSGELAKk 180
Cdd:COG2897  84 LFAARAWWLLRYAGHEDVRVLDgGLAAWKAAGLPLETGPP----TPAPGDFTA--RPDPELLADADEVLAALGDPDAVL- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  181 fnaFDARSLGRFEGtEPEPRsDIPSGHIPGTQPLPYGSLLDpETKTYPEAgEAIHATLEKALkdfhctLDPSKPTICSCG 260
Cdd:COG2897 157 ---VDARSPERYRG-EVEPI-DPRAGHIPGAVNLPWTDLLD-EDGTFKSA-EELRALFAALG------IDPDKPVITYCG 223

                       250       260       270
                ....*....|....*....|....*....|
gi 3122964  261 TGVSGVIIKTALELAGVPNVRLYDGSWTEW 290
Cdd:COG2897 224 SGVRAAHTWLALELLGYPNVRLYDGSWSEW 253
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 27-290 1.56e-59

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 192.71  E-value: 1.56e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964    27 VDATWYLPSWKLDNKVDFlTKPRIPNSIFFDIDAISDKKSPYPHMFPTKKVFDDAMSNLGVQKDDILVVYDRVGNFSSPR 106
Cdd:PLN02723  41 LDASWYMPDEQRNPIQEY-QVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSALGIENKDGVVVYDGKGIFSAAR 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   107 CAWTLGVMGHPKVYLLN-NFNQYREFKYPLDSSKVAAFSPYPKSHYESSESFQDKEIVD---YEEMFQL--------VKS 174
Cdd:PLN02723 120 VWWMFRVFGHEKVWVLDgGLPKWRASGYDVESSASGDAILKASAASEAIEKVYQGQTVSpitFQTKFQPhlvwtleqVKK 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   175 GELAKKFNAFDARSLGRFEGTEPEPRSDIPSGHIPGTQPLPYGSLLDPETKTYPeAGEaihatLEKALKDFHCTLDpsKP 254
Cdd:PLN02723 200 NIEDKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLP-AEE-----LKKRFEQEGISLD--SP 271

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 3122964   255 TICSCGTGVSGVIIKTALELAGVPNVRLYDGSWTEW 290
Cdd:PLN02723 272 IVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 50-290 1.02e-47

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 161.03  E-value: 1.02e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964    50 IPNSIFFDIDAISDKKSPYPHMFPTKKVFDDAMSNLGVQKDDILVVYDRvGN-FSSPRCAWTLGVMGHPKVYLL-NNFNQ 127
Cdd:PRK11493  47 IPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMRELGVNQDKHLVVYDE-GNlFSAPRAWWMLRTFGVEKVSILaGGLAG 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   128 YREFKYPLDSSKVAAfspyPKSHYESseSFQDKEIVDYEEMfqLVKSGElaKKFNAFDARSLGRFEGTEPEPRSDIPSGH 207
Cdd:PRK11493 126 WQRDDLLLEEGAVEL----PEGEFNA--AFNPEAVVRLTDV--LLASHE--KTAQIVDARPAARFNAEVDEPRPGLRRGH 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   208 IPGTQPLPYGSLLDP-ETKTYPEageaIHATLEKALKDFHctldpsKPTICSCGTGVSGVIIKTALELAGVPNVRLYDGS 286
Cdd:PRK11493 196 IPGALNVPWTELVREgELKTTDE----LDAIFFGRGVSFD------RPIIASCGSGVTAAVVVLALATLDVPNVKLYDGA 265


                 ....
gi 3122964   287 WTEW 290
Cdd:PRK11493 266 WSEW 269
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 163-290 7.17e-43

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: 143.16  E-value: 7.17e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  163 VDYEEMFQLVKSGELAKkfnaFDARSLGRFEGTEPEPRSDIPSGHIPGTQPLPYGSLLDPETKTYPEagEAIHATLEKAL 242
Cdd:cd01449   1 VTAEEVLANLDSGDVQL----VDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSP--EELRALFAALG 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3122964  243 kdfhctLDPSKPTICSCGTGVSGVIIKTALELAGVPNVRLYDGSWTEW 290
Cdd:cd01449  75 ------ITPDKPVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 6-128 2.40e-37

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: 129.28  E-value: 2.40e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964    6 LISPKAFVKLVASEKVhriVPVDATWYLPSWklDNKVDFLtKPRIPNSIFFDIDAISDKKSPYPHMFPTKKVFDDAMSNL 85
Cdd:cd01448   1 LVSPDWLAEHLDDPDV---RILDARWYLPDR--DGRKEYL-EGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 3122964   86 GVQKDDILVVYDRVGNFSSPRCAWTLGVMGHPKVYLLNNFNQY 128
Cdd:cd01448  75 GISNDDTVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQA 117
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 178-296 1.94e-13

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: 65.17  E-value: 1.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964     178 AKKFNAFDARSLGRFEGtepeprsdipsGHIPGTQPLPYGSLLDPETKTYPEAGEAIHATLEkalkdfhctLDPSKPTIC 257
Cdd:smart00450   2 DEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELLDRRGELDILEFEELLKRLG---------LDKDKPVVV 61

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 3122964     258 SCGTGVSGVIIKTALELAGVPNVRLYDGSWTEWVLKSGP 296
Cdd:smart00450  62 YCRSGNRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 27-123 2.73e-12

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: 63.27  E-value: 2.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   27 VDATWYLPSWKLDNKVDFLTKPR----------IPNSIFFDIDAISDKKSPYPHMFPTKKVFDDAMSNLGVQKDDILVVY 96
Cdd:cd01445  22 LDARAQSPGTREARGEYLETQPEpdavgldsghIPGASFFDFEECLDEAGFEESMEPSEAEFAAMFEAKGIDLDKHLIAT 101

                        90       100
                ....*....|....*....|....*....
gi 3122964   97 DR--VGNFSSPRCAWTLGVMGHPKVYLLN 123
Cdd:cd01445 102 DGddLGGFTACHIALAARLCGHPDVAILD 130
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 49-134 9.71e-12

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: 60.55  E-value: 9.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964      49 RIPNSIFFDIDAISDKKSPYPHMfptkkVFDDAMSNLGVQKDDILVVYDRVGNFSsPRCAWTLGVMGHPKVYLLNN-FNQ 127
Cdd:smart00450  20 HIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSGNRS-AKAAWLLRELGFKNVYLLDGgYKE 93


                   ....*..
gi 3122964     128 YREFKYP 134
Cdd:smart00450  94 WSAAGPP 100
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 163-290 1.88e-10

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: 57.88  E-value: 1.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  163 VDYEEMFQLVKSGELAKKFNAFDAR--------SLGRFEGTEPEPRS-DIPSGHIPGTQPLPYGSLLDPET-KTYPEAGE 232
Cdd:cd01445   1 KSTEQLAENLEAGKVGKGFQLLDARaqspgtreARGEYLETQPEPDAvGLDSGHIPGASFFDFEECLDEAGfEESMEPSE 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3122964  233 AIHATLEKALKdfhctLDPSKPTICSCGTGVSGVI---IKTALELAGVPNVRLYDGSWTEW 290
Cdd:cd01445  81 AEFAAMFEAKG-----IDLDKHLIATDGDDLGGFTachIALAARLCGHPDVAILDGGFFEW 136
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 184-291 2.05e-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: 53.64  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964    184 FDARSLGRFEGtepeprsdipsGHIPGTQPLPYGSLLDPEtktypeageAIHATLEKALKDfhctLDPSKPTICSCGTGV 263
Cdd:pfam00581   9 IDVRPPEEYAK-----------GHIPGAVNVPLSSLSLPP---------LPLLELLEKLLE----LLKDKPIVVYCNSGN 64

                          90       100
                  ....*....|....*....|....*...
gi 3122964    264 SGVIIKTALELAGVPNVRLYDGSWTEWV 291
Cdd:pfam00581  65 RAAAAAALLKALGYKNVYVLDGGFEAWK 92
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 65-290 1.46e-08

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 55.51  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964    65 KSPYPHMFPTKKVFDDAMSNLGVQKDDILVVYDRVGNFSSPRCAWTLGVMGHPKV-YLLNNFNQYREFKYPLdSSKVAAF 143
Cdd:PRK09629  56 KPPAPGLLPDTADLEQLFGELGHNPDAVYVVYDDEGGGWAGRFIWLLDVIGHSGYhYLDGGVLAWEAQALPL-STDVPPV 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964   144 SPYPkshyeSSESFQDKEIVDYEEMFQLVKSGELAkkfnAFDARSLGRFEGtepEPRSDIPSGHIPGTQPLPYGSLLDPE 223
Cdd:PRK09629 135 AGGP-----VTLTLHDEPTATREYLQSRLGAADLA----IWDARAPTEYSG---EKVVAAKGGHIPGAVNFEWTAGMDKA 202

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3122964   224 TKTypeageAIHATLEKALKDFHCTldPSKPTICSCGTGVSGVIIKTALELAGVPNVRLYDGSWTEW 290
Cdd:PRK09629 203 RNL------RIRQDMPEILRDLGIT--PDKEVITHCQTHHRSGFTYLVAKALGYPRVKAYAGSWGEW 261
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 49-123 7.23e-05

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: 40.93  E-value: 7.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3122964     49 RIPNSIFFDIDAISDkkspypHMFPTKKVFDDAMSNLgvqKDDILVVYDRVGNfSSPRCAWTLGVMGHPKVYLLN 123
Cdd:pfam00581  21 HIPGAVNVPLSSLSL------PPLPLLELLEKLLELL---KDKPIVVYCNSGN-RAAAAAALLKALGYKNVYVLD 85
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 168-290 7.89e-05

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: 41.11  E-value: 7.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  168 MFQLVKSGELAKKFNA-----FDARSLGRFEgtepeprsdipSGHIPGTQPLPYGSLLDpetktypEAGEaihatlekal 242
Cdd:COG0607   2 SVKEISPAELAELLESedavlLDVREPEEFA-----------AGHIPGAINIPLGELAE-------RLDE---------- 53

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 3122964  243 kdfhctLDPSKPTICSCGTGVSGVIIKTALELAGVPNVRLYDGSWTEW 290
Cdd:COG0607  54 ------LPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAW 95
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 206-291 1.06e-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: 1.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3122964  206 GHIPGTQPLPYGSLldpetktypeaGEAIHATLEkalkDFHCTL-----DPSKPTICSCGTGVSGviiKTALELA---GV 277
Cdd:cd01519  30 GKIPGAINIPLSSL-----------PDALALSEE----EFEKKYgfpkpSKDKELIFYCKAGVRS---KAAAELArslGY 91

                        90
                ....*....|....
gi 3122964  278 PNVRLYDGSWTEWV 291
Cdd:cd01519  92 ENVGNYPGSWLDWA 105
 
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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