|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
5-277 |
2.77e-62 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 197.32 E-value: 2.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 5 DNVRIIDASYVETAAlnnakfntnhpeiiisdiksPDLYTDEHIPGAVHFDL--DIGSYSSEYiKHDLYPPEHFQKYLRL 82
Cdd:COG2897 8 PDVVILDVRWDLPDG--------------------RAAYEAGHIPGAVFLDLdtDLSDPRSPG-RHPLPSPEAFAALLGA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 83 LGVNNGDQLVIYSNGpasGMKFASRAYWTFKMYGFTTVSLLNGGMDVWKAAGGPTDNAVVTPKLGNVNVKsLDNTILAKF 162
Cdd:COG2897 67 LGISNDTTVVVYDDG---GGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTAR-PDPELLADA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 163 EEIpFNNFAETNTVYLDTRIRAQFDGEDPlatnfPGTKAKGsHVTGAINFPMAKVIGPDG-FISQQDVDEQISSLGLTSA 241
Cdd:COG2897 143 DEV-LAALGDPDAVLVDARSPERYRGEVE-----PIDPRAG-HIPGAVNLPWTDLLDEDGtFKSAEELRALFAALGIDPD 215
|
250 260 270
....*....|....*....|....*....|....*..
gi 1734337025 242 SQVFVGCNTGMQASVIFVALERSGFK-AKLYNGSMFE 277
Cdd:COG2897 216 KPVITYCGSGVRAAHTWLALELLGYPnVRLYDGSWSE 252
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
5-134 |
2.80e-41 |
|
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: 138.91 E-value: 2.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 5 DNVRIIDAS-YVEtaalnnakfntnhpeiiisDIKSPDLYTDEHIPGAVHFDLDIGSYSSEYIKHDLYPPEHFQKYLRLL 83
Cdd:cd01448 14 PDVRILDARwYLP-------------------DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1734337025 84 GVNNGDQLVIYSNGpasGMKFASRAYWTFKMYGFTTVSLLNGGMDVWKAAG 134
Cdd:cd01448 75 GISNDDTVVVYDDG---GGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
43-282 |
5.14e-24 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 98.24 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 43 YTDEHIPGAVHFDLDIGSYSSEYIKHDLYPPEHFQKYLRLLGVNNGDQLVIYSNGpasGMKFASRAYWTFKMYGFTTVSL 122
Cdd:PRK11493 42 YRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMRELGVNQDKHLVVYDEG---NLFSAPRAWWMLRTFGVEKVSI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 123 LNGGMDVWKAAGGPTDNAVVTP-------KLGNVNVKSLDNTILA---KFEEIpfnnfaetntvyLDTRIRAQFDGE--D 190
Cdd:PRK11493 119 LAGGLAGWQRDDLLLEEGAVELpegefnaAFNPEAVVRLTDVLLAsheKTAQI------------VDARPAARFNAEvdE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 191 PLatnfPGTKaKGsHVTGAINFPMAKVIGPDGFISQQDVDEQISSLGLTSASQVFVGCNTGMQASVIFVALERSGFK-AK 269
Cdd:PRK11493 187 PR----PGLR-RG-HIPGALNVPWTELVREGELKTTDELDAIFFGRGVSFDRPIIASCGSGVTAAVVVLALATLDVPnVK 260
|
250
....*....|...
gi 1734337025 270 LYNGSMFELSYRA 282
Cdd:PRK11493 261 LYDGAWSEWGARA 273
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
28-136 |
1.42e-20 |
|
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: 84.05 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 28 NHPEIIISDIKSPDLYTDEHIPGAVHFDLDIGSYSSEYIKHDlyppeHFQKYLRLLGVNNGDQLVIYSNgpaSGMkFASR 107
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCR---SGN-RSAK 71
|
90 100
....*....|....*....|....*....
gi 1734337025 108 AYWTFKMYGFTTVSLLNGGMDVWKAAGGP 136
Cdd:smart00450 72 AAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
30-131 |
4.41e-13 |
|
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: 63.66 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 30 PEIIISDIKSPDLYTDEHIPGAVHFDLDIgsysseyikHDLYPPEHFQKYLRLLGVNNGDQLVIYSNGpasgMKFASRAY 109
Cdd:pfam00581 4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSS---------LSLPPLPLLELLEKLLELLKDKPIVVYCNS----GNRAAAAA 70
|
90 100
....*....|....*....|..
gi 1734337025 110 WTFKMYGFTTVSLLNGGMDVWK 131
Cdd:pfam00581 71 ALLKALGYKNVYVLDGGFEAWK 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
5-277 |
2.77e-62 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 197.32 E-value: 2.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 5 DNVRIIDASYVETAAlnnakfntnhpeiiisdiksPDLYTDEHIPGAVHFDL--DIGSYSSEYiKHDLYPPEHFQKYLRL 82
Cdd:COG2897 8 PDVVILDVRWDLPDG--------------------RAAYEAGHIPGAVFLDLdtDLSDPRSPG-RHPLPSPEAFAALLGA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 83 LGVNNGDQLVIYSNGpasGMKFASRAYWTFKMYGFTTVSLLNGGMDVWKAAGGPTDNAVVTPKLGNVNVKsLDNTILAKF 162
Cdd:COG2897 67 LGISNDTTVVVYDDG---GGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTAR-PDPELLADA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 163 EEIpFNNFAETNTVYLDTRIRAQFDGEDPlatnfPGTKAKGsHVTGAINFPMAKVIGPDG-FISQQDVDEQISSLGLTSA 241
Cdd:COG2897 143 DEV-LAALGDPDAVLVDARSPERYRGEVE-----PIDPRAG-HIPGAVNLPWTDLLDEDGtFKSAEELRALFAALGIDPD 215
|
250 260 270
....*....|....*....|....*....|....*..
gi 1734337025 242 SQVFVGCNTGMQASVIFVALERSGFK-AKLYNGSMFE 277
Cdd:COG2897 216 KPVITYCGSGVRAAHTWLALELLGYPnVRLYDGSWSE 252
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
5-134 |
2.80e-41 |
|
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: 138.91 E-value: 2.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 5 DNVRIIDAS-YVEtaalnnakfntnhpeiiisDIKSPDLYTDEHIPGAVHFDLDIGSYSSEYIKHDLYPPEHFQKYLRLL 83
Cdd:cd01448 14 PDVRILDARwYLP-------------------DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1734337025 84 GVNNGDQLVIYSNGpasGMKFASRAYWTFKMYGFTTVSLLNGGMDVWKAAG 134
Cdd:cd01448 75 GISNDDTVVVYDDG---GGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
43-282 |
5.14e-24 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 98.24 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 43 YTDEHIPGAVHFDLDIGSYSSEYIKHDLYPPEHFQKYLRLLGVNNGDQLVIYSNGpasGMKFASRAYWTFKMYGFTTVSL 122
Cdd:PRK11493 42 YRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMRELGVNQDKHLVVYDEG---NLFSAPRAWWMLRTFGVEKVSI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 123 LNGGMDVWKAAGGPTDNAVVTP-------KLGNVNVKSLDNTILA---KFEEIpfnnfaetntvyLDTRIRAQFDGE--D 190
Cdd:PRK11493 119 LAGGLAGWQRDDLLLEEGAVELpegefnaAFNPEAVVRLTDVLLAsheKTAQI------------VDARPAARFNAEvdE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 191 PLatnfPGTKaKGsHVTGAINFPMAKVIGPDGFISQQDVDEQISSLGLTSASQVFVGCNTGMQASVIFVALERSGFK-AK 269
Cdd:PRK11493 187 PR----PGLR-RG-HIPGALNVPWTELVREGELKTTDELDAIFFGRGVSFDRPIIASCGSGVTAAVVVLALATLDVPnVK 260
|
250
....*....|...
gi 1734337025 270 LYNGSMFELSYRA 282
Cdd:PRK11493 261 LYDGAWSEWGARA 273
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
28-136 |
1.42e-20 |
|
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: 84.05 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 28 NHPEIIISDIKSPDLYTDEHIPGAVHFDLDIGSYSSEYIKHDlyppeHFQKYLRLLGVNNGDQLVIYSNgpaSGMkFASR 107
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCR---SGN-RSAK 71
|
90 100
....*....|....*....|....*....
gi 1734337025 108 AYWTFKMYGFTTVSLLNGGMDVWKAAGGP 136
Cdd:smart00450 72 AAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
43-277 |
5.12e-20 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 87.94 E-value: 5.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 43 YTDEHIPGAVHFDLDIGSYSSEYIKHDLYPPEHFQKYLRLLGVNNGDQLVIYSngpASGMKFASRAYWTFKMYGFTTVSL 122
Cdd:PLN02723 58 YQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSALGIENKDGVVVYD---GKGIFSAARVWWMFRVFGHEKVWV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 123 LNGGMDVWKAAGGPTDNAVVTPKLGNVNVKS------------LDNTILAKF--------EEIPFNNFAETNTVyLDTRI 182
Cdd:PLN02723 135 LDGGLPKWRASGYDVESSASGDAILKASAASeaiekvyqgqtvSPITFQTKFqphlvwtlEQVKKNIEDKTYQH-IDARS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 183 RAQFDGEDPLatnfPGTKAKGSHVTGAINFPMAKVIGPDG-FISQQDVDEQISSLGLTSASQVFVGCNTGMQASVIFVAL 261
Cdd:PLN02723 214 KARFDGAAPE----PRKGIRSGHIPGSKCVPFPQMLDSSQtLLPAEELKKRFEQEGISLDSPIVASCGTGVTACILALGL 289
|
250
....*....|....*..
gi 1734337025 262 ERSGFK-AKLYNGSMFE 277
Cdd:PLN02723 290 HRLGKTdVPVYDGSWTE 306
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
168-277 |
1.62e-15 |
|
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: 71.12 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 168 NNFAETNTVYLDTRIRAQFDGEDPlatnFPGTKAKGSHVTGAINFPMAKVIGPDG-FISQQDVDEQISSLGLTSASQVFV 246
Cdd:cd01449 8 ANLDSGDVQLVDARSPERFRGEVP----EPRPGLRSGHIPGAVNIPWTSLLDEDGtFKSPEELRALFAALGITPDKPVIV 83
|
90 100 110
....*....|....*....|....*....|..
gi 1734337025 247 GCNTGMQASVIFVALERSGFK-AKLYNGSMFE 277
Cdd:cd01449 84 YCGSGVTACVLLLALELLGYKnVRLYDGSWSE 115
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
30-131 |
4.41e-13 |
|
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: 63.66 E-value: 4.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 30 PEIIISDIKSPDLYTDEHIPGAVHFDLDIgsysseyikHDLYPPEHFQKYLRLLGVNNGDQLVIYSNGpasgMKFASRAY 109
Cdd:pfam00581 4 GKVVLIDVRPPEEYAKGHIPGAVNVPLSS---------LSLPPLPLLELLEKLLELLKDKPIVVYCNS----GNRAAAAA 70
|
90 100
....*....|....*....|..
gi 1734337025 110 WTFKMYGFTTVSLLNGGMDVWK 131
Cdd:pfam00581 71 ALLKALGYKNVYVLDGGFEAWK 92
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
174-284 |
2.51e-11 |
|
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: 59.01 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 174 NTVYLDTRIRAQFDGedplatnfpgtkakgSHVTGAINFPMAKVIGPDGFISQQDVDEQISSLGLTSASQVFVGCNTGMQ 253
Cdd:smart00450 4 KVVLLDVRSPEEYEG---------------GHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNR 68
|
90 100 110
....*....|....*....|....*....|..
gi 1734337025 254 ASVIFVALERSGFK-AKLYNGSMFELSYRAPE 284
Cdd:smart00450 69 SAKAAWLLRELGFKnVYLLDGGYKEWSAAGPP 100
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
30-277 |
9.43e-11 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 62.06 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 30 PEIIISDIKSPDLYTDEHIPGAVHFDLDIGSYSSEYIKHDLYPPEHFQKYLRLLGVNNGDQLVIYSNgpaSGMKFASRAY 109
Cdd:PRK09629 23 PELILVDLTSSARYEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVYDD---EGGGWAGRFI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 110 WTFKMYGFTTVSLLNGGMDVWKAAGGPTDNAvVTPKLGNVNVKSLDNTILAKFEEIPfNNFAETNTVYLDTRIRAQFDGE 189
Cdd:PRK09629 100 WLLDVIGHSGYHYLDGGVLAWEAQALPLSTD-VPPVAGGPVTLTLHDEPTATREYLQ-SRLGAADLAIWDARAPTEYSGE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 190 DPLAtnfpgtkAKGSHVTGAINFP-MAKVIGPDGFISQQDVDEQISSLGLTSASQVFVGCNTGMQASVIFVALERSGF-K 267
Cdd:PRK09629 178 KVVA-------AKGGHIPGAVNFEwTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYpR 250
|
250
....*....|
gi 1734337025 268 AKLYNGSMFE 277
Cdd:PRK09629 251 VKAYAGSWGE 260
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
28-137 |
1.95e-08 |
|
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: 51.12 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 28 NHPEIIISDIKSPDLYTDEHIPGAVHFDLDigsysseyikhdlyppeHFQKylRLLGVNNGDQLVIYSNGPASGMKFASR 107
Cdd:COG0607 16 ESEDAVLLDVREPEEFAAGHIPGAINIPLG-----------------ELAE--RLDELPKDKPIVVYCASGGRSAQAAAL 76
|
90 100 110
....*....|....*....|....*....|
gi 1734337025 108 AywtfKMYGFTTVSLLNGGMDVWKAAGGPT 137
Cdd:COG0607 77 L----RRAGYTNVYNLAGGIEAWKAAGLPV 102
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
28-131 |
5.10e-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: 49.61 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 28 NHPEIIISDIKSPDLYTDEHIPGAVHFdldigsysseyikhdlyPPEHFQKYLRLLGVNNGDQLVIYSngpASGMKfASR 107
Cdd:cd00158 7 DDEDAVLLDVREPEEYAAGHIPGAINI-----------------PLSELEERAALLELDKDKPIVVYC---RSGNR-SAR 65
|
90 100
....*....|....*....|....
gi 1734337025 108 AYWTFKMYGFTTVSLLNGGMDVWK 131
Cdd:cd00158 66 AAKLLRKAGGTNVYNLEGGMLAWK 89
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
47-130 |
5.42e-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: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 47 HIPGAVHFDLDIGSYSSEYIKHDLYPPEHFQKYLRLLGVNNGDQLVIYsNGPASGMKFASRAYWTFKMYGFTTVSLLNGG 126
Cdd:cd01445 54 HIPGASFFDFEECLDEAGFEESMEPSEAEFAAMFEAKGIDLDKHLIAT-DGDDLGGFTACHIALAARLCGHPDVAILDGG 132
|
....
gi 1734337025 127 MDVW 130
Cdd:cd01445 133 FFEW 136
|
|
| RHOD_PspE2 |
cd01521 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ... |
28-137 |
4.33e-06 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.
Pssm-ID: 238779 [Multi-domain] Cd Length: 110 Bit Score: 44.65 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 28 NHPEIIISDIKSPDLYTDEHIPGAVHfdldigsysseyIKHDLYPPEHFQKYLRllgvnnGDQLVIYSNGPasGMKFASR 107
Cdd:cd01521 22 GKPDFVLVDVRSAEAYARGHVPGAIN------------LPHREICENATAKLDK------EKLFVVYCDGP--GCNGATK 81
|
90 100 110
....*....|....*....|....*....|
gi 1734337025 108 AYWTFKMYGFtTVSLLNGGMDVWKAAGGPT 137
Cdd:cd01521 82 AALKLAELGF-PVKEMIGGLDWWKREGYAT 110
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
12-133 |
2.42e-05 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 45.25 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 12 ASYVETAALNNAKFNTNHPEIIISDIKSPDLYTDEHIPGAVHFDLDIgsysseyIKHDLYPPEhfqkylrllgVNNGDQL 91
Cdd:PRK05597 255 ISGGFGEVLDVPRVSALPDGVTLIDVREPSEFAAYSIPGAHNVPLSA-------IREGANPPS----------VSAGDEV 317
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1734337025 92 VIYSngpASGMKFAsRAYWTFKMYGFTTVSLLNGGMDVWKAA 133
Cdd:PRK05597 318 VVYC---AAGVRSA-QAVAILERAGYTGMSSLDGGIEGWLDS 355
|
|
| Acr2p |
cd01531 |
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ... |
13-134 |
8.91e-05 |
|
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.
Pssm-ID: 238789 [Multi-domain] Cd Length: 113 Bit Score: 41.25 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 13 SYVETAALNnAKFNTNHPEIIISDIKSPDlYTDEHIPGAVHfdldigsYSSEYIKHDLypPEHFQkylrLLGVNNGDQLV 92
Cdd:cd01531 2 SYISPAQLK-GWIRNGRPPFQVVDVRDED-YAGGHIKGSWH-------YPSTRFKAQL--NQLVQ----LLSGSKKDTVV 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1734337025 93 I---YSN--GPASGMKFaSRAYWTFKMY-GFTTVSLLNGGMDVWKAAG 134
Cdd:cd01531 67 FhcaLSQvrGPSAARKF-LRYLDEEDLEtSKFEVYVLHGGFNAWESSY 113
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| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
26-130 |
9.30e-05 |
|
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: 41.08 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 26 NTNHPEIIISDIKSPDLYTDE-----------HIPGAVHFDLdigsysSEYIKHD--LYPPEHFQKYLRLLGVNNGDQLV 92
Cdd:cd01449 9 NLDSGDVQLVDARSPERFRGEvpeprpglrsgHIPGAVNIPW------TSLLDEDgtFKSPEELRALFAALGITPDKPVI 82
|
90 100 110
....*....|....*....|....*....|....*...
gi 1734337025 93 IYSNgpaSGMKfASRAYWTFKMYGFTTVSLLNGGMDVW 130
Cdd:cd01449 83 VYCG---SGVT-ACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
30-132 |
5.48e-03 |
|
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.
Pssm-ID: 238721 [Multi-domain] Cd Length: 96 Bit Score: 35.70 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1734337025 30 PEIIISDIKSPDLYTD--EHIPGAVHFDLDigsysseyikhdlyppehfqKYLRLLGVNNGDQ-LVIYSNGPASGMKFAS 106
Cdd:cd01444 15 EAPVLLDVRDPASYAAlpDHIPGAIHLDED--------------------SLDDWLGDLDRDRpVVVYCYHGNSSAQLAQ 74
|
90 100
....*....|....*....|....*.
gi 1734337025 107 RaywtFKMYGFTTVSLLNGGMDVWKA 132
Cdd:cd01444 75 A----LREAGFTDVRSLAGGFEAWRR 96
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|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
202-277 |
5.81e-03 |
|
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: 35.54 E-value: 5.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1734337025 202 KGSHVTGAINFPMAKVIGPDgfISQQDVDEQIssLGLTSASQVFVGCNTGMQASVIFVALERSGF-KAKLYNGSMFE 277
Cdd:pfam00581 18 AKGHIPGAVNVPLSSLSLPP--LPLLELLEKL--LELLKDKPIVVYCNSGNRAAAAAALLKALGYkNVYVLDGGFEA 90
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