|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
27-279 |
5.89e-112 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 324.05 E-value: 5.89e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 27 PGLRVLDASWYSPGtreARKEYLERHVPGASFFDIEEC-RDTASPYEMMLPSEAGFAEYVGRLGISNHTHVVVYDGEhlG 105
Cdd:COG2897 8 PDVVILDVRWDLPD---GRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYDDG--G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 106 SFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLDRSLLKTYEQVLENLESKRFQLVDSRSQ 185
Cdd:COG2897 83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALGDPDAVLVDARSP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 186 GRFLGTEPEPDAVGldsGHIRGAVNMPFMDFLTEDGFEKGPEELRALFQTKKVDLSQPLIATCRKGVTACHVALAAYLCG 265
Cdd:COG2897 163 ERYRGEVEPIDPRA---GHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALELLG 239
|
250
....*....|....
gi 17402865 266 KPDVAVYDGSWSEW 279
Cdd:COG2897 240 YPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
9-279 |
2.22e-88 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 266.28 E-value: 2.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 9 ALVSTKWLAESIRTgklgPGLRVLDASWYSPG-TREARKEYLERHVPGASFFDIEECRDTASPYEMMLPSEAGFAEYVGR 87
Cdd:PLN02723 22 PVVSVDWLHANLRE----PDVKVLDASWYMPDeQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 88 LGISNHTHVVVYDGEhlGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPE------------------ 149
Cdd:PLN02723 98 LGIENKDGVVVYDGK--GIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAilkasaaseaiekvyqgq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 150 ---PAVFKATLDRSLLKTYEQVLENLESKRFQLVDSRSQGRFLGTEPEPDAvGLDSGHIRGAVNMPFMDFLTEDGFEKGP 226
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRK-GIRSGHIPGSKCVPFPQMLDSSQTLLPA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17402865 227 EELRALFQTKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:PLN02723 255 EELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
11-136 |
6.82e-64 |
|
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: 197.71 E-value: 6.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 11 VSTKWLAESIRTGKLGPGLRVLDASWYSPGTREARKEYLE------------RHVPGASFFDIEECRDTASPYEMMLPSE 78
Cdd:cd01445 1 KSTEQLAENLEAGKVGKGFQLLDARAQSPGTREARGEYLEtqpepdavgldsGHIPGASFFDFEECLDEAGFEESMEPSE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 17402865 79 AGFAEYVGRLGISNHTHVVVYDGEHLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLK 136
Cdd:cd01445 81 AEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
173-285 |
6.69e-19 |
|
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: 79.81 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 173 ESKRFQLVDSRSQGRFLGtepepdavgldsGHIRGAVNMPFMDFLTEDGfEKGPEELRALFQTKKVDLSQPLIATCRKGV 252
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG------------GHIPGAVNIPLSELLDRRG-ELDILEFEELLKRLGLDKDKPVVVYCRSGN 67
|
90 100 110
....*....|....*....|....*....|...
gi 17402865 253 TACHVALAAYLCGKPDVAVYDGSWSEWFRRAPP 285
Cdd:smart00450 68 RSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
172-279 |
1.32e-14 |
|
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: 67.89 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 172 LESKRFQLVDSRSQGRFlgtepepdavglDSGHIRGAVNMPFMDF-LTEDGFEKGPEELRALFQTKKVdlsqplIATCRK 250
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEY------------AKGHIPGAVNVPLSSLsLPPLPLLELLEKLLELLKDKPI------VVYCNS 62
|
90 100
....*....|....*....|....*....
gi 17402865 251 GVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:pfam00581 63 GNRAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
27-279 |
5.89e-112 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 324.05 E-value: 5.89e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 27 PGLRVLDASWYSPGtreARKEYLERHVPGASFFDIEEC-RDTASPYEMMLPSEAGFAEYVGRLGISNHTHVVVYDGEhlG 105
Cdd:COG2897 8 PDVVILDVRWDLPD---GRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYDDG--G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 106 SFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLDRSLLKTYEQVLENLESKRFQLVDSRSQ 185
Cdd:COG2897 83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALGDPDAVLVDARSP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 186 GRFLGTEPEPDAVGldsGHIRGAVNMPFMDFLTEDGFEKGPEELRALFQTKKVDLSQPLIATCRKGVTACHVALAAYLCG 265
Cdd:COG2897 163 ERYRGEVEPIDPRA---GHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALELLG 239
|
250
....*....|....
gi 17402865 266 KPDVAVYDGSWSEW 279
Cdd:COG2897 240 YPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
9-279 |
2.22e-88 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 266.28 E-value: 2.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 9 ALVSTKWLAESIRTgklgPGLRVLDASWYSPG-TREARKEYLERHVPGASFFDIEECRDTASPYEMMLPSEAGFAEYVGR 87
Cdd:PLN02723 22 PVVSVDWLHANLRE----PDVKVLDASWYMPDeQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 88 LGISNHTHVVVYDGEhlGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPE------------------ 149
Cdd:PLN02723 98 LGIENKDGVVVYDGK--GIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAilkasaaseaiekvyqgq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 150 ---PAVFKATLDRSLLKTYEQVLENLESKRFQLVDSRSQGRFLGTEPEPDAvGLDSGHIRGAVNMPFMDFLTEDGFEKGP 226
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRK-GIRSGHIPGSKCVPFPQMLDSSQTLLPA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 17402865 227 EELRALFQTKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:PLN02723 255 EELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
11-283 |
2.51e-78 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 239.61 E-value: 2.51e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 11 VSTKWLAESIRTgklgPGLRVLDASWYSPG--TREARKEYLERHVPGASFFDIEECRDTASPYEMMLPSEAGFAEYVGRL 88
Cdd:PRK11493 7 VAADWLAEHIDD----PEIQIIDARMAPPGqeDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 89 GISNHTHVVVYDGEHLgsFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLDRSLLKTYEQV 168
Cdd:PRK11493 83 GVNQDKHLVVYDEGNL--FSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 169 LENLESKRFQLVDSRSQGRFLGT--EPEPdavGLDSGHIRGAVNMPFMDfLTEDGFEKGPEELRALFQTKKVDLSQPLIA 246
Cdd:PRK11493 161 LLASHEKTAQIVDARPAARFNAEvdEPRP---GLRRGHIPGALNVPWTE-LVREGELKTTDELDAIFFGRGVSFDRPIIA 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 17402865 247 TCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFRRA 283
Cdd:PRK11493 237 SCGSGVTAAVVVLALATLDVPNVKLYDGAWSEWGARA 273
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
11-136 |
6.82e-64 |
|
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: 197.71 E-value: 6.82e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 11 VSTKWLAESIRTGKLGPGLRVLDASWYSPGTREARKEYLE------------RHVPGASFFDIEECRDTASPYEMMLPSE 78
Cdd:cd01445 1 KSTEQLAENLEAGKVGKGFQLLDARAQSPGTREARGEYLEtqpepdavgldsGHIPGASFFDFEECLDEAGFEESMEPSE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 17402865 79 AGFAEYVGRLGISNHTHVVVYDGEHLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLK 136
Cdd:cd01445 81 AEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
10-138 |
1.23e-55 |
|
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: 175.89 E-value: 1.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 10 LVSTKWLAESIRTgklgPGLRVLDASWYSPGtREARKEYLERHVPGASFFDIEECRDTASPYEMMLPSEAGFAEYVGRLG 89
Cdd:cd01448 1 LVSPDWLAEHLDD----PDVRILDARWYLPD-RDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSLG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 17402865 90 ISNHTHVVVYDGEhlGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEG 138
Cdd:cd01448 76 ISNDDTVVVYDDG--GGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
163-281 |
1.45e-54 |
|
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: 172.82 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 163 KTYEQVLENLESKRFQLVDSRSQGRFLGTEPEPDAvGLDSGHIRGAVNMPFMDFLTEDGFEKGPEELRALFQTKKVDLSQ 242
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRP-GLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDK 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 17402865 243 PLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFR 281
Cdd:cd01449 80 PVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
163-281 |
2.95e-49 |
|
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: 160.34 E-value: 2.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 163 KTYEQVLENLE----SKRFQLVDSRSQ--------GRFLGTEPEPDAVGLDSGHIRGAVNMPFMDFLTEDGFEKGPE--- 227
Cdd:cd01445 1 KSTEQLAENLEagkvGKGFQLLDARAQspgtrearGEYLETQPEPDAVGLDSGHIPGASFFDFEECLDEAGFEESMEpse 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 17402865 228 -ELRALFQTKKVDLSQPLIATCRK---GVTACHVALAAYLCGKPDVAVYDGSWSEWFR 281
Cdd:cd01445 81 aEFAAMFEAKGIDLDKHLIATDGDdlgGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
173-285 |
6.69e-19 |
|
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: 79.81 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 173 ESKRFQLVDSRSQGRFLGtepepdavgldsGHIRGAVNMPFMDFLTEDGfEKGPEELRALFQTKKVDLSQPLIATCRKGV 252
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG------------GHIPGAVNIPLSELLDRRG-ELDILEFEELLKRLGLDKDKPVVVYCRSGN 67
|
90 100 110
....*....|....*....|....*....|...
gi 17402865 253 TACHVALAAYLCGKPDVAVYDGSWSEWFRRAPP 285
Cdd:smart00450 68 RSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
26-140 |
7.28e-17 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 74.42 E-value: 7.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 26 GPGLRVLDASWyspgtreaRKEYLERHVPGASFFDIEECRDTASPYEMMLpseagFAEYVGRLGISNHTHVVVYDGehlG 105
Cdd:smart00450 2 DEKVVLLDVRS--------PEEYEGGHIPGAVNIPLSELLDRRGELDILE-----FEELLKRLGLDKDKPVVVYCR---S 65
|
90 100 110
....*....|....*....|....*....|....*
gi 17402865 106 SFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHP 140
Cdd:smart00450 66 GNRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
41-279 |
4.54e-16 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 78.24 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 41 TREARkeYLERHVPGASFFDIEECRDTASPYEMMLPSEAGFAEYVGRLGISNHTHVVVYDGEhlGSFYAPRVWWMFRVFG 120
Cdd:PRK09629 31 TSSAR--YEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVYDDE--GGGWAGRFIWLLDVIG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 121 HRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLDRSLLKTYEQVLENLESKRFQLVDSRSQGRFLGTEpepdAVGL 200
Cdd:PRK09629 107 HSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQSRLGAADLAIWDARAPTEYSGEK----VVAA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17402865 201 DSGHIRGAVNMPFMDFLTEDGFEKGPEELRALFQTKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:PRK09629 183 KGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYPRVKAYAGSWGEW 261
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
172-279 |
1.32e-14 |
|
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: 67.89 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 172 LESKRFQLVDSRSQGRFlgtepepdavglDSGHIRGAVNMPFMDF-LTEDGFEKGPEELRALFQTKKVdlsqplIATCRK 250
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEY------------AKGHIPGAVNVPLSSLsLPPLPLLELLEKLLELLKDKPI------VVYCNS 62
|
90 100
....*....|....*....|....*....
gi 17402865 251 GVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:pfam00581 63 GNRAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
47-134 |
6.35e-10 |
|
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: 55.18 E-value: 6.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 47 EYLERHVPGASFFdieecrdtasPYEMMLPSEAGFAEYVGRL-GISNHTHVVVYDGEHLGSfyaPRVWWMFRVFGHRTVS 125
Cdd:pfam00581 16 EYAKGHIPGAVNV----------PLSSLSLPPLPLLELLEKLlELLKDKPIVVYCNSGNRA---AAAAALLKALGYKNVY 82
|
....*....
gi 17402865 126 VLNGGFRNW 134
Cdd:pfam00581 83 VLDGGFEAW 91
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
167-279 |
1.15e-09 |
|
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: 54.23 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 167 QVLENLESKRFQLVDSRSQGRFlgtepepdavglDSGHIRGAVNMPFMDFLTEDGFEKGPEElralfqtkkvdlsQPLIA 246
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEY------------AAGHIPGAINIPLSELEERAALLELDKD-------------KPIVV 55
|
90 100 110
....*....|....*....|....*....|...
gi 17402865 247 TCRKGVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:cd00158 56 YCRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
164-285 |
3.16e-09 |
|
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: 53.43 E-value: 3.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 164 TYEQVLENLESKRFQLVDSRSQGRFlgtepepdavglDSGHIRGAVNMPFMDFltedgfekgPEELRALfqtkkvDLSQP 243
Cdd:COG0607 7 SPAELAELLESEDAVLLDVREPEEF------------AAGHIPGAINIPLGEL---------AERLDEL------PKDKP 59
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 17402865 244 LIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFRRAPP 285
Cdd:COG0607 60 IVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLP 101
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
191-279 |
3.43e-09 |
|
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: 53.43 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 191 TEPEPDAVGLD--------SGHIRGAVNMPFMDFltEDGFEKGPEELRALFQTKKVDLSQPLIATCRKGV---TACHVAL 259
Cdd:cd01519 10 PNPHPNKVLIDvrepeelkTGKIPGAINIPLSSL--PDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVrskAAAELAR 87
|
90 100
....*....|....*....|
gi 17402865 260 AAylcGKPDVAVYDGSWSEW 279
Cdd:cd01519 88 SL---GYENVGNYPGSWLDW 104
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
162-279 |
1.18e-03 |
|
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: 37.98 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 162 LKTYEQVLENLESKRFQLVDSRSqgrflgTEPEPDAVGL-DSGHIRGAVNMPFMDFLTEDGFEKG----PEELRALFQTK 236
Cdd:cd01448 1 LVSPDWLAEHLDDPDVRILDARW------YLPDRDGRKEyLEGHIPGAVFFDLDEDLDDKSPGPHmlpsPEEFAELLGSL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 17402865 237 KVDLSQPLIATCRKGVTAchvalAAYL------CGKPDVAVYDGSWSEW 279
Cdd:cd01448 75 GISNDDTVVVYDDGGGFF-----AARAwwtlryFGHENVRVLDGGLQAW 118
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
26-134 |
5.66e-03 |
|
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: 35.35 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17402865 26 GPGLRVLDAswyspgtREArKEYLERHVPGASFFDIEEcrdtaspyemmLPSEAGFAEyvgrlgISNHTHVVVYDGehlG 105
Cdd:cd00158 8 DEDAVLLDV-------REP-EEYAAGHIPGAINIPLSE-----------LEERAALLE------LDKDKPIVVYCR---S 59
|
90 100
....*....|....*....|....*....
gi 17402865 106 SFYAPRVWWMFRVFGHRTVSVLNGGFRNW 134
Cdd:cd00158 60 GNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| |
