NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|194473681|ref|NP_001123989|]
View 

3-mercaptopyruvate sulfurtransferase isoform 2 [Homo sapiens]

Protein Classification

sulfurtransferase( domain architecture ID 11458420)

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

EC:  2.8.1.-
Gene Ontology:  GO:0016783

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 16-279 2.01e-104

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


:

Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 305.18  E-value: 2.01e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  16 VAEALRAPragqPLQLLDASWYLPklgrDARREFEERHIPGAAFFDIDQC-SDRTSPYDHMLPGAEHFAEYAGRLGVGAA 94
Cdd:COG2897    1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  95 THVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLE 174
Cdd:COG2897   73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 175 SRRFQVVDSRATGRFRGtEPEPRDGIePGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTA 254
Cdd:COG2897  151 DPDAVLVDARSPERYRG-EVEPIDPR-AGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228

                        250       260
                 ....*....|....*....|....*
gi 194473681 255 CHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:COG2897  229 AHTWLALELLGYPNVRLYDGSWSEW 253
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 16-279 2.01e-104

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 305.18  E-value: 2.01e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  16 VAEALRAPragqPLQLLDASWYLPklgrDARREFEERHIPGAAFFDIDQC-SDRTSPYDHMLPGAEHFAEYAGRLGVGAA 94
Cdd:COG2897    1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  95 THVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLE 174
Cdd:COG2897   73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 175 SRRFQVVDSRATGRFRGtEPEPRDGIePGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTA 254
Cdd:COG2897  151 DPDAVLVDARSPERYRG-EVEPIDPR-AGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228

                        250       260
                 ....*....|....*....|....*
gi 194473681 255 CHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:COG2897  229 AHTWLALELLGYPNVRLYDGSWSEW 253
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 9-279 1.99e-98

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 292.09  E-value: 1.99e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681   9 ALVSAQWVAEALRAPRagqpLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGR 88
Cdd:PLN02723  22 PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  89 LGVGAATHVVIYDAsdQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPA------------------ 150
Cdd:PLN02723  98 LGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAilkasaaseaiekvyqgq 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 151 ---PAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPE 227
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLPAE 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194473681 228 EIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:PLN02723 256 ELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 164-279 2.28e-53

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: 169.74  E-value: 2.28e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 164 KTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKP 243
Cdd:cd01449    1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKP 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194473681 244 LVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:cd01449   81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 44-141 1.73e-18

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: 78.66  E-value: 1.73e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681    44 DARR--EFEERHIPGAAFFDIDQCSDRTSPYDHMlpgaeHFAEYAGRLGVGAATHVVIYDASDqglYSAPRVWWMFRAFG 121
Cdd:smart00450   9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 194473681   122 HHAVSLLDGGLRHWLRQNLP 141
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 44-135 5.59e-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: 57.88  E-value: 5.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681   44 DARR--EFEERHIPGAAFFDIDqcsdrtSPYDHMLPGAEHFAEYAGRLGvgaATHVVIYDASDQglySAPRVWWMFRAFG 121
Cdd:pfam00581  10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77

                          90
                  ....*....|....
gi 194473681  122 HHAVSLLDGGLRHW 135
Cdd:pfam00581  78 YKNVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 16-279 2.01e-104

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 305.18  E-value: 2.01e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  16 VAEALRAPragqPLQLLDASWYLPklgrDARREFEERHIPGAAFFDIDQC-SDRTSPYDHMLPGAEHFAEYAGRLGVGAA 94
Cdd:COG2897    1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  95 THVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLE 174
Cdd:COG2897   73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 175 SRRFQVVDSRATGRFRGtEPEPRDGIePGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTA 254
Cdd:COG2897  151 DPDAVLVDARSPERYRG-EVEPIDPR-AGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228

                        250       260
                 ....*....|....*....|....*
gi 194473681 255 CHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:COG2897  229 AHTWLALELLGYPNVRLYDGSWSEW 253
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 9-279 1.99e-98

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 292.09  E-value: 1.99e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681   9 ALVSAQWVAEALRAPRagqpLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGR 88
Cdd:PLN02723  22 PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  89 LGVGAATHVVIYDAsdQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPA------------------ 150
Cdd:PLN02723  98 LGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAilkasaaseaiekvyqgq 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 151 ---PAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPE 227
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLPAE 255

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194473681 228 EIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:PLN02723 256 ELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 11-283 1.20e-88

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 265.80  E-value: 1.20e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  11 VSAQWVAEALRAPRagqpLQLLDASWYLPKL-GRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRL 89
Cdd:PRK11493   7 VAADWLAEHIDDPE----IQIIDARMAPPGQeDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMREL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  90 GVGAATHVVIYDASDqgLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDI 169
Cdd:PRK11493  83 GVNQDKHLVVYDEGN--LFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 170 KENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDfLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCG 249
Cdd:PRK11493 161 LLASHEKTAQIVDARPAARFNAEVDEPRPGLRRGHIPGALNVPWTE-LVREGELKTTDELDAIFFGRGVSFDRPIIASCG 239

                        250       260       270
                 ....*....|....*....|....*....|....
gi 194473681 250 SGVTACHVALGAYLCGKPDVPIYDGSWVEWYMRA 283
Cdd:PRK11493 240 SGVTAAVVVLALATLDVPNVKLYDGAWSEWGARA 273
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 164-279 2.28e-53

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: 169.74  E-value: 2.28e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 164 KTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKP 243
Cdd:cd01449    1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKP 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 194473681 244 LVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:cd01449   81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 10-139 9.33e-52

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: 165.87  E-value: 9.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  10 LVSAQWVAEALRAPRagqpLQLLDASWYLPklGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRL 89
Cdd:cd01448    1 LVSPDWLAEHLDDPD----VRILDARWYLP--DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 194473681  90 GVGAATHVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQN 139
Cdd:cd01448   75 GISNDDTVVVYD--DGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 11-137 3.07e-37

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: 129.14  E-value: 3.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  11 VSAQWVAEALRAPRAGQPLQLLDASWYLPKlGRDARREF------------EERHIPGAAFFDIDQCSDRTSPYDHMLPG 78
Cdd:cd01445    1 KSTEQLAENLEAGKVGKGFQLLDARAQSPG-TREARGEYletqpepdavglDSGHIPGASFFDFEECLDEAGFEESMEPS 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 194473681  79 AEHFAEYAGRLGVGAATHVVIYDASDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLR 137
Cdd:cd01445   80 EAEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 164-280 5.08e-34

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: 121.05  E-value: 5.08e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 164 KTYEDIKENLE----SRRFQVVDSR--------ATGRFRGTEPEPRD-GIEPGHIPGTVNIPFTDFLSQEGLEKSPE--- 227
Cdd:cd01445    1 KSTEQLAENLEagkvGKGFQLLDARaqspgtreARGEYLETQPEPDAvGLDSGHIPGASFFDFEECLDEAGFEESMEpse 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194473681 228 -EIRHLFQEKKVDLSKPLVATCG---SGVTACHVALGAYLCGKPDVPIYDGSWVEWY 280
Cdd:cd01445   81 aEFAAMFEAKGIDLDKHLIATDGddlGGFTACHIALAARLCGHPDVAILDGGFFEWF 137
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 29-279 8.48e-19

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 86.33  E-value: 8.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  29 LQLLDA-SWYLPKLGRDARreFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDasDQGL 107
Cdd:PRK09629  17 LERLDApELILVDLTSSAR--YEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVYD--DEGG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 108 YSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATG 187
Cdd:PRK09629  93 GWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQSRLGAADLAIWDARAPT 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 188 RFRGTEPEPRDGiepGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKP 267
Cdd:PRK09629 173 EYSGEKVVAAKG---GHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYP 249

                        250
                 ....*....|..
gi 194473681 268 DVPIYDGSWVEW 279
Cdd:PRK09629 250 RVKAYAGSWGEW 261
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 44-141 1.73e-18

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: 78.66  E-value: 1.73e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681    44 DARR--EFEERHIPGAAFFDIDQCSDRTSPYDHMlpgaeHFAEYAGRLGVGAATHVVIYDASDqglYSAPRVWWMFRAFG 121
Cdd:smart00450   9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 194473681   122 HHAVSLLDGGLRHWLRQNLP 141
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 174-285 8.41e-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: 8.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681   174 ESRRFQVVDSRATGRFRGtepeprdgiepGHIPGTVNIPFTDFLsQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVT 253
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELL-DRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNR 68

                           90       100       110
                   ....*....|....*....|....*....|..
gi 194473681   254 ACHVALGAYLCGKPDVPIYDGSWVEWYMRARP 285
Cdd:smart00450  69 SAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 165-279 4.96e-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: 4.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 165 TYEDIKENLE-SRRFQVVDSRatgrfrgtepEPRDgIEPGHIPGTVNIPFTDFlsQEGLEKSPEEIRHLFQEKKVDLSKP 243
Cdd:cd01519    2 SFEEVKNLPNpHPNKVLIDVR----------EPEE-LKTGKIPGAINIPLSSL--PDALALSEEEFEKKYGFPKPSKDKE 68

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 194473681 244 LVATCGSGV---TACHVALGAylcGKPDVPIYDGSWVEW 279
Cdd:cd01519   69 LIFYCKAGVrskAAAELARSL---GYENVGNYPGSWLDW 104
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 44-135 5.59e-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: 57.88  E-value: 5.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681   44 DARR--EFEERHIPGAAFFDIDqcsdrtSPYDHMLPGAEHFAEYAGRLGvgaATHVVIYDASDQglySAPRVWWMFRAFG 121
Cdd:pfam00581  10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77

                          90
                  ....*....|....
gi 194473681  122 HHAVSLLDGGLRHW 135
Cdd:pfam00581  78 YKNVYVLDGGFEAW 91
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 173-279 2.98e-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: 53.26  E-value: 2.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  173 LESRRFQVVDSRATGRFrgtepeprdgiEPGHIPGTVNIPFTDF-LSQEGLEKSPEEIRHLFQEKKVdlskplVATCGSG 251
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEY-----------AKGHIPGAVNVPLSSLsLPPLPLLELLEKLLELLKDKPI------VVYCNSG 63

                          90       100
                  ....*....|....*....|....*...
gi 194473681  252 VTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:pfam00581  64 NRAAAAAALLKALGYKNVYVLDGGFEAW 91
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 168-279 1.27e-08

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: 51.53  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 168 DIKENLESRRFQVVDSRATGRFRGtepeprdgiepGHIPGTVNIPFtdflsqeglekspEEIRHLFQEKKVDLSKPLVAT 247
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAA-----------GHIPGAINIPL-------------SELEERAALLELDKDKPIVVY 56

                         90       100       110
                 ....*....|....*....|....*....|..
gi 194473681 248 CGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:cd00158   57 CRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 165-285 3.58e-07

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: 47.65  E-value: 3.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 165 TYEDIKENLESRRFQVVDSRatgrfrgtEPEPRDGiepGHIPGTVNIPFTDFLSQEGlekspeeirhlfqekKVDLSKPL 244
Cdd:COG0607    7 SPAELAELLESEDAVLLDVR--------EPEEFAA---GHIPGAINIPLGELAERLD---------------ELPKDKPI 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 194473681 245 VATCGSGVTACHVAlgAYLC--GKPDVPIYDGSWVEWYMRARP 285
Cdd:COG0607   61 VVYCASGGRSAQAA--ALLRraGYTNVYNLAGGIEAWKAAGLP 101
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 11-146 7.52e-07

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: 46.88  E-value: 7.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  11 VSAQWVAEALRAPRAgqplQLLDAswylpklgRDARrEFEERHIPGAAFFDIDQCSDRTSPYDhmlpgaehfaeyagrlg 90
Cdd:COG0607    6 ISPAELAELLESEDA----VLLDV--------REPE-EFAAGHIPGAINIPLGELAERLDELP----------------- 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 194473681  91 vgAATHVVIYDASDqglYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGK 146
Cdd:COG0607   56 --KDKPIVVYCASG---GRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 44-135 9.08e-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: 37.66  E-value: 9.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681  44 DAR--REFEERHIPGAAFFDIDQcsdrtspydhmlpgaehFAEYAGRLGVGAATHVVIYDASDQglySAPRVWWMFRAFG 121
Cdd:cd00158   15 DVRepEEYAAGHIPGAINIPLSE-----------------LEERAALLELDKDKPIVVYCRSGN---RSARAAKLLRKAG 74

                         90
                 ....*....|....
gi 194473681 122 HHAVSLLDGGLRHW 135
Cdd:cd00158   75 GTNVYNLEGGMLAW 88
Cdc25_Acr2p cd01443
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ...
 158-280 1.50e-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: 37.77  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473681 158 LDPAFIKTYEDIKENLESRRFQVVDSRatgrfrgtepepRDGIEPGHIPGTVNIPFTDFLSQEgleksPEEIRHLFQEKK 237
Cdd:cd01443    4 ISPEELVALLENSDSNAGKDFVVVDLR------------RDDYEGGHIKGSINLPAQSCYQTL-----PQVYALFSLAGV 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 194473681 238 VDlskpLVATCGS----GVTACH------VALGAYlcgKPDVPIYDGSWVEWY 280
Cdd:cd01443   67 KL----AIFYCGSsqgrGPRAARwfadylRKVGES---LPKSYILTGGIKAWY 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH