|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
1-271 |
5.98e-158 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 452.65 E-value: 5.98e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 1 MSVFSDLPLVIEPSDLAPRLGAPELILVDLTSAARYAEGHIPGARFVDPKRTQWGQPPAPGLLPAKADLEALFGELGHRP 80
Cdd:PRK09629 1 MSAFTGLSLVIEPNDLLERLDAPELILVDLTSSARYEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 81 EATYVVYDDEGGGWAGRFIWLLDVIGHHHYHYLNGGLPAWIADAQALDREVPAPVGGPLPLTLHDEPSATREYLQSRLGA 160
Cdd:PRK09629 81 DAVYVVYDDEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQSRLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 161 ADLAVWDARNPSEYAGTKVLAAKAGHVPGAINFEWTAGMDPARALRIRADIAEVLEDLGITPDKEVITHCQTHHRSGFTY 240
Cdd:PRK09629 161 ADLAIWDARAPTEYSGEKVVAAKGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTY 240
|
250 260 270
....*....|....*....|....*....|.
gi 15600149 241 LVAKALGYPRVKGYAGSWSEWGNHPDTPVEV 271
Cdd:PRK09629 241 LVAKALGYPRVKAYAGSWGEWGNHPDTPVEV 271
|
|
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
16-270 |
1.42e-94 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 278.98 E-value: 1.42e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 16 LAPRLGAPELILVDLT-----SAARYAEGHIPGARFVDPKRT-QWGQPPAPGLLPAKADLEALFGELGHRPEATYVVYDD 89
Cdd:COG2897 1 LAAHLDDPDVVILDVRwdlpdGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 90 EGGGWAGRFIWLLDVIGHHHYHYLNGGLPAWIADAQALDREVPAPVGGPLPLTLHDEPSATREYLQSRLGAADLAVWDAR 169
Cdd:COG2897 81 GGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALGDPDAVLVDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 170 NPSEYAGTKV-LAAKAGHVPGAINFEWTAGMDPARALRIRADIAEVLEDLGITPDKEVITHCQTHHRSGFTYLVAKALGY 248
Cdd:COG2897 161 SPERYRGEVEpIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALELLGY 240
|
250 260
....*....|....*....|..
gi 15600149 249 PRVKGYAGSWSEWGNHPDTPVE 270
Cdd:COG2897 241 PNVRLYDGSWSEWGSDPDLPVE 262
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
149-263 |
2.67e-40 |
|
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: 135.45 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 149 ATREYLQSRLGAADLAVWDARNPSEYAGTKVL---AAKAGHVPGAINFEWTAGMDPARALRIRADIAEVLEDLGITPDKE 225
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEprpGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKP 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 15600149 226 VITHCQTHHRSGFTYLVAKALGYPRVKGYAGSWSEWGN 263
Cdd:cd01449 81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
159-266 |
1.92e-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: 80.97 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 159 GAADLAVWDARNPSEYAGtkvlaakaGHVPGAINFEWTAGMDPARALRIrADIAEVLEDLGITPDKEVITHCQTHHRSGF 238
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG--------GHIPGAVNIPLSELLDRRGELDI-LEFEELLKRLGLDKDKPVVVYCRSGNRSAK 71
|
90 100
....*....|....*....|....*...
gi 15600149 239 TYLVAKALGYPRVKGYAGSWSEWGNHPD 266
Cdd:smart00450 72 AAWLLRELGFKNVYLLDGGYKEWSAAGP 99
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
158-261 |
9.60e-17 |
|
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: 73.29 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 158 LGAADLAVWDARNPSEYAgtkvlaakAGHVPGAINFEWTAGMDPARALrirADIAEVLEDLGitPDKEVITHCQTHHRSG 237
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYA--------KGHIPGAVNVPLSSLSLPPLPL---LELLEKLLELL--KDKPIVVYCNSGNRAA 67
|
90 100
....*....|....*....|....
gi 15600149 238 FTYLVAKALGYPRVKGYAGSWSEW 261
Cdd:pfam00581 68 AAAALLKALGYKNVYVLDGGFEAW 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
1-271 |
5.98e-158 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 452.65 E-value: 5.98e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 1 MSVFSDLPLVIEPSDLAPRLGAPELILVDLTSAARYAEGHIPGARFVDPKRTQWGQPPAPGLLPAKADLEALFGELGHRP 80
Cdd:PRK09629 1 MSAFTGLSLVIEPNDLLERLDAPELILVDLTSSARYEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 81 EATYVVYDDEGGGWAGRFIWLLDVIGHHHYHYLNGGLPAWIADAQALDREVPAPVGGPLPLTLHDEPSATREYLQSRLGA 160
Cdd:PRK09629 81 DAVYVVYDDEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQSRLGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 161 ADLAVWDARNPSEYAGTKVLAAKAGHVPGAINFEWTAGMDPARALRIRADIAEVLEDLGITPDKEVITHCQTHHRSGFTY 240
Cdd:PRK09629 161 ADLAIWDARAPTEYSGEKVVAAKGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTY 240
|
250 260 270
....*....|....*....|....*....|.
gi 15600149 241 LVAKALGYPRVKGYAGSWSEWGNHPDTPVEV 271
Cdd:PRK09629 241 LVAKALGYPRVKAYAGSWGEWGNHPDTPVEV 271
|
|
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
16-270 |
1.42e-94 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 278.98 E-value: 1.42e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 16 LAPRLGAPELILVDLT-----SAARYAEGHIPGARFVDPKRT-QWGQPPAPGLLPAKADLEALFGELGHRPEATYVVYDD 89
Cdd:COG2897 1 LAAHLDDPDVVILDVRwdlpdGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 90 EGGGWAGRFIWLLDVIGHHHYHYLNGGLPAWIADAQALDREVPAPVGGPLPLTLHDEPSATREYLQSRLGAADLAVWDAR 169
Cdd:COG2897 81 GGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALGDPDAVLVDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 170 NPSEYAGTKV-LAAKAGHVPGAINFEWTAGMDPARALRIRADIAEVLEDLGITPDKEVITHCQTHHRSGFTYLVAKALGY 248
Cdd:COG2897 161 SPERYRGEVEpIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALELLGY 240
|
250 260
....*....|....*....|..
gi 15600149 249 PRVKGYAGSWSEWGNHPDTPVE 270
Cdd:COG2897 241 PNVRLYDGSWSEWGSDPDLPVE 262
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
149-263 |
2.67e-40 |
|
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: 135.45 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 149 ATREYLQSRLGAADLAVWDARNPSEYAGTKVL---AAKAGHVPGAINFEWTAGMDPARALRIRADIAEVLEDLGITPDKE 225
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEprpGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKP 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 15600149 226 VITHCQTHHRSGFTYLVAKALGYPRVKGYAGSWSEWGN 263
Cdd:cd01449 81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
10-122 |
2.54e-35 |
|
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: 122.73 E-value: 2.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 10 VIEPSDLAPRLGAPELILVDLTSA-------ARYAEGHIPGARFVDPKRTQWGQPPAPGLLPAKADLEALFGELGHRPEA 82
Cdd:cd01448 1 LVSPDWLAEHLDDPDVRILDARWYlpdrdgrKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSLGISNDD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15600149 83 TYVVYDDEGGGWAGRFIWLLDVIGHHHYHYLNGGLPAWIA 122
Cdd:cd01448 81 TVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKA 120
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
36-271 |
1.67e-21 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 91.79 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 36 YAEGHIPGARFVDPKRTQWGQPPAPGLLPAKADLEALFGELGHRPEATYVVYDDEGGGWAGRFIWLLDVIGHHHYHYLNG 115
Cdd:PLN02723 58 YQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSALGIENKDGVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 116 GLPAWIADAQALDREVPAPV-----------------GGPLPLTLHDE--PSA--TREYLQSRLGAADLAVWDARNPSEY 174
Cdd:PLN02723 138 GLPKWRASGYDVESSASGDAilkasaaseaiekvyqgQTVSPITFQTKfqPHLvwTLEQVKKNIEDKTYQHIDARSKARF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 175 AGTKVLAAK---AGHVPGAINFEWTAGMDPARALRIRADIAEVLEDLGITPDKEVITHCQTHHRSGFTYLVAKALGYPRV 251
Cdd:PLN02723 218 DGAAPEPRKgirSGHIPGSKCVPFPQMLDSSQTLLPAEELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDV 297
|
250 260
....*....|....*....|
gi 15600149 252 KGYAGSWSEWGNHPDTPVEV 271
Cdd:PLN02723 298 PVYDGSWTEWGALPDTPVAT 317
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
33-270 |
3.73e-21 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 90.15 E-value: 3.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 33 AARYAEGHIPGARFVDPKRTQWGQPPAPGLLPAKADLEALFGELGHRPEATYVVYDDEGGGWAGRFIWLLDVIGHHHYHY 112
Cdd:PRK11493 39 AAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMRELGVNQDKHLVVYDEGNLFSAPRAWWMLRTFGVEKVSI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 113 LNGGLPAWIADAQALDREVPAPVGGPLPLTLHDEP--SATREYLQSRLGAADLAvwDARNPSEYAGT---KVLAAKAGHV 187
Cdd:PRK11493 119 LAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAvvRLTDVLLASHEKTAQIV--DARPAARFNAEvdePRPGLRRGHI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 188 PGAINFEWTAGMDPARaLRIRADIAEVLEDLGITPDKEVITHCQTHHRSGFTYLVAKALGYPRVKGYAGSWSEWGNHPDT 267
Cdd:PRK11493 197 PGALNVPWTELVREGE-LKTTDELDAIFFGRGVSFDRPIIASCGSGVTAAVVVLALATLDVPNVKLYDGAWSEWGARADL 275
|
...
gi 15600149 268 PVE 270
Cdd:PRK11493 276 PVE 278
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
159-266 |
1.92e-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: 80.97 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 159 GAADLAVWDARNPSEYAGtkvlaakaGHVPGAINFEWTAGMDPARALRIrADIAEVLEDLGITPDKEVITHCQTHHRSGF 238
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG--------GHIPGAVNIPLSELLDRRGELDI-LEFEELLKRLGLDKDKPVVVYCRSGNRSAK 71
|
90 100
....*....|....*....|....*...
gi 15600149 239 TYLVAKALGYPRVKGYAGSWSEWGNHPD 266
Cdd:smart00450 72 AAWLLRELGFKNVYLLDGGYKEWSAAGP 99
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
158-261 |
9.60e-17 |
|
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: 73.29 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 158 LGAADLAVWDARNPSEYAgtkvlaakAGHVPGAINFEWTAGMDPARALrirADIAEVLEDLGitPDKEVITHCQTHHRSG 237
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYA--------KGHIPGAVNVPLSSLSLPPLPL---LELLEKLLELL--KDKPIVVYCNSGNRAA 67
|
90 100
....*....|....*....|....
gi 15600149 238 FTYLVAKALGYPRVKGYAGSWSEW 261
Cdd:pfam00581 68 AAAALLKALGYKNVYVLDGGFEAW 91
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
21-124 |
8.33e-16 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 70.95 E-value: 8.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 21 GAPELILVDLTSAARYAEGHIPGARFVDpkRTQWGQPPAPGLlpaKADLEALFGELGHRPEATYVVYDDeGGGWAGRFIW 100
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIP--LSELLDRRGELD---ILEFEELLKRLGLDKDKPVVVYCR-SGNRSAKAAW 74
|
90 100
....*....|....*....|....
gi 15600149 101 LLDVIGHHHYHYLNGGLPAWIADA 124
Cdd:smart00450 75 LLRELGFKNVYLLDGGYKEWSAAG 98
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
20-120 |
3.09e-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: 64.04 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 20 LGAPELILVDLTSAARYAEGHIPGARFVDPKRTQWGQPPapgLLPAKADLEALFgelghrPEATYVVYDDeGGGWAGRFI 99
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLP---LLELLEKLLELL------KDKPIVVYCN-SGNRAAAAA 70
|
90 100
....*....|....*....|.
gi 15600149 100 WLLDVIGHHHYHYLNGGLPAW 120
Cdd:pfam00581 71 ALLKALGYKNVYVLDGGFEAW 91
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
154-261 |
6.75e-11 |
|
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: 58.06 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 154 LQSRLGAADLAVWDARNPSEYAgtkvlaakAGHVPGAINFEWtagmdparalrirADIAEVLEDLGitPDKEVITHCQTH 233
Cdd:COG0607 11 LAELLESEDAVLLDVREPEEFA--------AGHIPGAINIPL-------------GELAERLDELP--KDKPIVVYCASG 67
|
90 100
....*....|....*....|....*...
gi 15600149 234 HRSGFTYLVAKALGYPRVKGYAGSWSEW 261
Cdd:COG0607 68 GRSAQAAALLRRAGYTNVYNLAGGIEAW 95
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
154-261 |
1.24e-10 |
|
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: 56.54 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 154 LQSRLGAADLAVWDARNPSEYAgtkvlaakAGHVPGAINFEWTagmdparalriraDIAEVLEDLGITPDKEVITHCQTH 233
Cdd:cd00158 2 LKELLDDEDAVLLDVREPEEYA--------AGHIPGAINIPLS-------------ELEERAALLELDKDKPIVVYCRSG 60
|
90 100
....*....|....*....|....*...
gi 15600149 234 HRSGFTYLVAKALGYPRVKGYAGSWSEW 261
Cdd:cd00158 61 NRSARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
11-122 |
1.14e-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: 54.59 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 11 IEPSDLAPRLGAPELILVDLTSAARYAEGHIPGARFVDPkrtqwgqppapgllpakADLEALFGELghRPEATYVVYDDe 90
Cdd:COG0607 6 ISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPL-----------------GELAERLDEL--PKDKPIVVYCA- 65
|
90 100 110
....*....|....*....|....*....|..
gi 15600149 91 GGGWAGRFIWLLDVIGHHHYHYLNGGLPAWIA 122
Cdd:COG0607 66 SGGRSAQAAALLRRAGYTNVYNLAGGIEAWKA 97
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
167-261 |
1.84e-08 |
|
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: 51.12 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 167 DARNPSEYagtkvlaaKAGHVPGAINFEWTAGMDparALRIRADiaEVLEDLGI---TPDKEVITHCQTHHRSGFTYLVA 243
Cdd:cd01519 20 DVREPEEL--------KTGKIPGAINIPLSSLPD---ALALSEE--EFEKKYGFpkpSKDKELIFYCKAGVRSKAAAELA 86
|
90
....*....|....*...
gi 15600149 244 KALGYPRVKGYAGSWSEW 261
Cdd:cd01519 87 RSLGYENVGNYPGSWLDW 104
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
15-120 |
2.19e-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: 50.38 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 15 DLAPRLGAPELILVDLTSAARYAEGHIPGARfvdpkrtqwgqppapgLLPAKaDLEALFGELGHRPEATYVVYdDEGGGW 94
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAI----------------NIPLS-ELEERAALLELDKDKPIVVY-CRSGNR 62
|
90 100
....*....|....*....|....*.
gi 15600149 95 AGRFIWLLDVIGHHHYHYLNGGLPAW 120
Cdd:cd00158 63 SARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
33-121 |
1.53e-05 |
|
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: 43.63 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 33 AARYAEGHIPGARFVDPKRTQWGQPPAPGLLPAKADLEALFGELGHRPEATYVVY--DDEGGGWAGRFIWLLDVIGHHHY 110
Cdd:cd01445 47 AVGLDSGHIPGASFFDFEECLDEAGFEESMEPSEAEFAAMFEAKGIDLDKHLIATdgDDLGGFTACHIALAARLCGHPDV 126
|
90
....*....|.
gi 15600149 111 HYLNGGLPAWI 121
Cdd:cd01445 127 AILDGGFFEWF 137
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
167-262 |
5.93e-05 |
|
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.
Pssm-ID: 238782 [Multi-domain] Cd Length: 90 Bit Score: 40.71 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 167 DARNPSEYAgtkvlaakAGHVPGAINFewtagmdPARALRIRadIAEvledlgITPDKEVITHCQTHHRSGFTYLVAKAL 246
Cdd:cd01524 18 DVRTPQEFE--------KGHIKGAINI-------PLDELRDR--LNE------LPKDKEIIVYCAVGLRGYIAARILTQN 74
|
90
....*....|....*.
gi 15600149 247 GYpRVKGYAGSWSEWG 262
Cdd:cd01524 75 GF-KVKNLDGGYKTYS 89
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
194-261 |
6.29e-04 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 40.77 E-value: 6.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600149 194 EWTAGMdPARALRI-RADIAEVLEDLGITPDKEVITHCQTHHRSGFTYLVAKALGYPRVKGYAGSWSEW 261
Cdd:PRK08762 28 ERASGQ-AEGALRIpRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYTRVASVAGGFSAW 95
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
173-261 |
6.66e-04 |
|
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: 39.00 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 173 EYAGTK----VLAAKAGHVPGAINFEWTAGMDPAR----ALRIRADIAEVLEDLGITPDKEVITHCQTHhRSGFT----Y 240
Cdd:cd01445 37 EYLETQpepdAVGLDSGHIPGASFFDFEECLDEAGfeesMEPSEAEFAAMFEAKGIDLDKHLIATDGDD-LGGFTachiA 115
|
90 100
....*....|....*....|.
gi 15600149 241 LVAKALGYPRVKGYAGSWSEW 261
Cdd:cd01445 116 LAARLCGHPDVAILDGGFFEW 136
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
152-227 |
1.06e-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: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600149 152 EYLQSRLGAADLAVWDAR-NPSEYAGTKvlAAKAGHVPGAINFEWTAGMD---PARALRIRAD-IAEVLEDLGITPDKEV 226
Cdd:cd01448 5 DWLAEHLDDPDVRILDARwYLPDRDGRK--EYLEGHIPGAVFFDLDEDLDdksPGPHMLPSPEeFAELLGSLGISNDDTV 82
|
.
gi 15600149 227 I 227
Cdd:cd01448 83 V 83
|
|
| RHOD_PspE2 |
cd01521 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ... |
11-45 |
1.13e-03 |
|
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: 37.72 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|....*..
gi 15600149 11 IEPSDLAPRL--GAPELILVDLTSAARYAEGHIPGAR 45
Cdd:cd01521 10 TDCWDVAIALknGKPDFVLVDVRSAEAYARGHVPGAI 46
|
|
| |
