|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
28-346 |
5.40e-71 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 221.97 E-value: 5.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 28 ARLGSPRLKVVESDED----SLLYDIGHIPTATRIDLRRDLNDPVQ---RDFIDGEAFARLMDSRGISRDDTVVVYGDRS 100
Cdd:COG2897 3 AHLDDPDVVILDVRWDlpdgRAAYEAGHIPGAVFLDLDTDLSDPRSpgrHPLPSPEAFAALLGALGISNDTTVVVYDDGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 101 NLWAAHTLWVLELFGHPDVRLLDGGRDAWMQEEKETSYVVPDLTTSGYPVvgRDDRTARVGVDEIRAALGTGagaeagag 180
Cdd:COG2897 83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTA--RPDPELLADADEVLAALGDP-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 181 agaeagagaggegvdgdddaaraatgtGLQLLDVRDPLSYSGQPAPADgpggdgardagrdagrdaarhpghaairgtaS 260
Cdd:COG2897 153 ---------------------------DAVLVDARSPERYRGEVEPID-------------------------------P 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 261 RWGHIPGAVNVPVDVSTYPNSRFRTRADLEQAFAHL--DPARPTVTYCHTGERSSHLWFVLhHLLGWPSVRSYDGSWVEW 338
Cdd:COG2897 175 RAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALgiDPDKPVITYCGSGVRAAHTWLAL-ELLGYPNVRLYDGSWSEW 253
|
....*...
gi 1533948052 339 GNMVRVPI 346
Cdd:COG2897 254 GSDPDLPV 261
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
20-132 |
6.87e-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: 123.88 E-value: 6.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 20 LVTSSWLGARLGSPRLKVVESDEDS------LLYDIGHIPTATRIDLRRDLND--PVQRDFIDGEAFARLMDSRGISRDD 91
Cdd:cd01448 1 LVSPDWLAEHLDDPDVRILDARWYLpdrdgrKEYLEGHIPGAVFFDLDEDLDDksPGPHMLPSPEEFAELLGSLGISNDD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1533948052 92 TVVVYGDRSNLWAAHTLWVLELFGHPDVRLLDGGRDAWMQE 132
Cdd:cd01448 81 TVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAE 121
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
29-350 |
3.72e-19 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 88.64 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 29 RLGSPRLKVVESdEDSLLYDIGHIPTATRIDLRR-DLNDPVQRDFI-DGEAFARLMDSRGISRDDTVVVYGDRSNLWAAH 106
Cdd:PRK09629 19 RLDAPELILVDL-TSSARYEAGHIRGARFVDPKRtQLGKPPAPGLLpDTADLEQLFGELGHNPDAVYVVYDDEGGGWAGR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 107 TLWVLELFGHPDVRLLDGGRDAWMQEEKETSYVVP-------DLTTSGYPVVGRDDRTARVGVDEiraalgtgagaeaga 179
Cdd:PRK09629 98 FIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPpvaggpvTLTLHDEPTATREYLQSRLGAAD--------------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 180 gagaeagagaggegvdgdddaaraatgtgLQLLDVRDPLSYSGQpapadgpggdgardagrdagrdaarhpghaaiRGTA 259
Cdd:PRK09629 163 -----------------------------LAIWDARAPTEYSGE--------------------------------KVVA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 260 SRWGHIPGAVNVPVDVSTYPNSRFRTRADLEQAFAHL--DPARPTVTYCHTGERSSHLWFVLHhLLGWPSVRSYDGSWVE 337
Cdd:PRK09629 182 AKGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLgiTPDKEVITHCQTHHRSGFTYLVAK-ALGYPRVKAYAGSWGE 260
|
330
....*....|...
gi 1533948052 338 WGNMVRVPIRVGT 350
Cdd:PRK09629 261 WGNHPDTPVEVPT 273
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
263-338 |
2.84e-15 |
|
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: 70.59 E-value: 2.84e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533948052 263 GHIPGAVNVPVDVSTYPNSRFrtrADLEQAFAHLDPARPTVTYCHTGERSSHLWFVLHHlLGWPSVRSYDGSWVEW 338
Cdd:pfam00581 20 GHIPGAVNVPLSSLSLPPLPL---LELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKA-LGYKNVYVLDGGFEAW 91
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
47-135 |
3.90e-15 |
|
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: 70.18 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 47 YDIGHIPTATRIDLRRDLNDPVQRDFIDgeaFARLMDSRGISRDDTVVVYgDRSNLWAAHTLWVLELFGHPDVRLLDGGR 126
Cdd:smart00450 16 YEGGHIPGAVNIPLSELLDRRGELDILE---FEELLKRLGLDKDKPVVVY-CRSGNRSAKAAWLLRELGFKNVYLLDGGY 91
|
....*....
gi 1533948052 127 DAWMQEEKE 135
Cdd:smart00450 92 KEWSAAGPP 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
28-346 |
5.40e-71 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 221.97 E-value: 5.40e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 28 ARLGSPRLKVVESDED----SLLYDIGHIPTATRIDLRRDLNDPVQ---RDFIDGEAFARLMDSRGISRDDTVVVYGDRS 100
Cdd:COG2897 3 AHLDDPDVVILDVRWDlpdgRAAYEAGHIPGAVFLDLDTDLSDPRSpgrHPLPSPEAFAALLGALGISNDTTVVVYDDGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 101 NLWAAHTLWVLELFGHPDVRLLDGGRDAWMQEEKETSYVVPDLTTSGYPVvgRDDRTARVGVDEIRAALGTGagaeagag 180
Cdd:COG2897 83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTA--RPDPELLADADEVLAALGDP-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 181 agaeagagaggegvdgdddaaraatgtGLQLLDVRDPLSYSGQPAPADgpggdgardagrdagrdaarhpghaairgtaS 260
Cdd:COG2897 153 ---------------------------DAVLVDARSPERYRGEVEPID-------------------------------P 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 261 RWGHIPGAVNVPVDVSTYPNSRFRTRADLEQAFAHL--DPARPTVTYCHTGERSSHLWFVLhHLLGWPSVRSYDGSWVEW 338
Cdd:COG2897 175 RAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALgiDPDKPVITYCGSGVRAAHTWLAL-ELLGYPNVRLYDGSWSEW 253
|
....*...
gi 1533948052 339 GNMVRVPI 346
Cdd:COG2897 254 GSDPDLPV 261
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
20-132 |
6.87e-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: 123.88 E-value: 6.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 20 LVTSSWLGARLGSPRLKVVESDEDS------LLYDIGHIPTATRIDLRRDLND--PVQRDFIDGEAFARLMDSRGISRDD 91
Cdd:cd01448 1 LVSPDWLAEHLDDPDVRILDARWYLpdrdgrKEYLEGHIPGAVFFDLDEDLDDksPGPHMLPSPEEFAELLGSLGISNDD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1533948052 92 TVVVYGDRSNLWAAHTLWVLELFGHPDVRLLDGGRDAWMQE 132
Cdd:cd01448 81 TVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAE 121
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
235-340 |
5.96e-26 |
|
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: 100.40 E-value: 5.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 235 ARDAGRDAGRDAARHPGHAAirgtasrwGHIPGAVNVPVDVSTYPNSRFRTRADLEQAFAHL--DPARPTVTYCHTGERS 312
Cdd:cd01449 20 ARSPERFRGEVPEPRPGLRS--------GHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALgiTPDKPVIVYCGSGVTA 91
|
90 100
....*....|....*....|....*...
gi 1533948052 313 SHLWFVLHHlLGWPSVRSYDGSWVEWGN 340
Cdd:cd01449 92 CVLLLALEL-LGYKNVRLYDGSWSEWGS 118
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
29-350 |
3.72e-19 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 88.64 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 29 RLGSPRLKVVESdEDSLLYDIGHIPTATRIDLRR-DLNDPVQRDFI-DGEAFARLMDSRGISRDDTVVVYGDRSNLWAAH 106
Cdd:PRK09629 19 RLDAPELILVDL-TSSARYEAGHIRGARFVDPKRtQLGKPPAPGLLpDTADLEQLFGELGHNPDAVYVVYDDEGGGWAGR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 107 TLWVLELFGHPDVRLLDGGRDAWMQEEKETSYVVP-------DLTTSGYPVVGRDDRTARVGVDEiraalgtgagaeaga 179
Cdd:PRK09629 98 FIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPpvaggpvTLTLHDEPTATREYLQSRLGAAD--------------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 180 gagaeagagaggegvdgdddaaraatgtgLQLLDVRDPLSYSGQpapadgpggdgardagrdagrdaarhpghaaiRGTA 259
Cdd:PRK09629 163 -----------------------------LAIWDARAPTEYSGE--------------------------------KVVA 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 260 SRWGHIPGAVNVPVDVSTYPNSRFRTRADLEQAFAHL--DPARPTVTYCHTGERSSHLWFVLHhLLGWPSVRSYDGSWVE 337
Cdd:PRK09629 182 AKGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLgiTPDKEVITHCQTHHRSGFTYLVAK-ALGYPRVKAYAGSWGE 260
|
330
....*....|...
gi 1533948052 338 WGNMVRVPIRVGT 350
Cdd:PRK09629 261 WGNHPDTPVEVPT 273
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
263-338 |
2.84e-15 |
|
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: 70.59 E-value: 2.84e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533948052 263 GHIPGAVNVPVDVSTYPNSRFrtrADLEQAFAHLDPARPTVTYCHTGERSSHLWFVLHHlLGWPSVRSYDGSWVEW 338
Cdd:pfam00581 20 GHIPGAVNVPLSSLSLPPLPL---LELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKA-LGYKNVYVLDGGFEAW 91
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
47-135 |
3.90e-15 |
|
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: 70.18 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 47 YDIGHIPTATRIDLRRDLNDPVQRDFIDgeaFARLMDSRGISRDDTVVVYgDRSNLWAAHTLWVLELFGHPDVRLLDGGR 126
Cdd:smart00450 16 YEGGHIPGAVNIPLSELLDRRGELDILE---FEELLKRLGLDKDKPVVVY-CRSGNRSAKAAWLLRELGFKNVYLLDGGY 91
|
....*....
gi 1533948052 127 DAWMQEEKE 135
Cdd:smart00450 92 KEWSAAGPP 100
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
17-349 |
7.26e-14 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 70.89 E-value: 7.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 17 PEKLVTSSWLGARLGSPRLKVVES------DEDSLL---YDIGHIPTATRIDLR--RDLNDPVQRDFIDGEAFARLMDSR 85
Cdd:PRK11493 3 TTWFVAADWLAEHIDDPEIQIIDArmappgQEDRDVaaeYRAGHIPGAVFFDIEalSDHTSPLPHMMPRPETFAVAMREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 86 GISRDDTVVVYgDRSNLWAA-HTLWVLELFGHPDVRLLDGGRDAWMQEEKetsyvvpdLTTSGYPVVGRDDRTARVGVDE 164
Cdd:PRK11493 83 GVNQDKHLVVY-DEGNLFSApRAWWMLRTFGVEKVSILAGGLAGWQRDDL--------LLEEGAVELPEGEFNAAFNPEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 165 IRAalgtgagaeagagagaeagagaggegvdgdddaaraatgtglqlldVRDPLSYSGQpapadgpGGDGARDAgrdagR 244
Cdd:PRK11493 154 VVR----------------------------------------------LTDVLLASHE-------KTAQIVDA-----R 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 245 DAARHPGHAAIRGTASRWGHIPGAVNVPVDVSTYpNSRFRTRADLEQAFAH--LDPARPTVTYCHTGERSSHLWFVLHhL 322
Cdd:PRK11493 176 PAARFNAEVDEPRPGLRRGHIPGALNVPWTELVR-EGELKTTDELDAIFFGrgVSFDRPIIASCGSGVTAAVVVLALA-T 253
|
330 340
....*....|....*....|....*..
gi 1533948052 323 LGWPSVRSYDGSWVEWGNMVRVPIRVG 349
Cdd:PRK11493 254 LDVPNVKLYDGAWSEWGARADLPVEPA 280
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
263-338 |
3.16e-13 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 65.17 E-value: 3.16e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1533948052 263 GHIPGAVNVPVDVSTYPNSRFRTRADLEQ-AFAHLDPARPTVTYCHTGERSSHLWFVLHHlLGWPSVRSYDGSWVEW 338
Cdd:smart00450 19 GHIPGAVNIPLSELLDRRGELDILEFEELlKRLGLDKDKPVVVYCRSGNRSAKAAWLLRE-LGFKNVYLLDGGYKEW 94
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
12-350 |
1.71e-11 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 64.44 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 12 QQYAHPEKLVTSSWLGARLGSPRLKVVES-----DE--DSLL-YDIGHIPTATRIDLRR--DLNDPVQRDFIDGEAFARL 81
Cdd:PLN02723 15 QSISTNEPVVSVDWLHANLREPDVKVLDAswympDEqrNPIQeYQVAHIPGALFFDLDGisDRTTDLPHMLPSEEAFAAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 82 MDSRGISRDDTVVVYGDRSNLWAAHTLWVLELFGHPDVRLLDGGRDAWMqeeketsyvvpdltTSGYPVvgrddrTARVG 161
Cdd:PLN02723 95 VSALGIENKDGVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPKWR--------------ASGYDV------ESSAS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 162 VDEIRAALGTGAGAEAGAGAGAEAGAGAGGEGVD----GDDDAARAATGTGLQLLDVRDPLSYSG-QPAPADGpggdgar 236
Cdd:PLN02723 155 GDAILKASAASEAIEKVYQGQTVSPITFQTKFQPhlvwTLEQVKKNIEDKTYQHIDARSKARFDGaAPEPRKG------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 237 dagrdagrdaarhpghaaIRGtasrwGHIPGAVNVP----VDVST--YPNSRFRTRadLEQAFAHLDpaRPTVTYCHTGE 310
Cdd:PLN02723 228 ------------------IRS-----GHIPGSKCVPfpqmLDSSQtlLPAEELKKR--FEQEGISLD--SPIVASCGTGV 280
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1533948052 311 RSSHLWFVLHHlLGWPSVRSYDGSWVEWGNMVRVPIRVGT 350
Cdd:PLN02723 281 TACILALGLHR-LGKTDVPVYDGSWTEWGALPDTPVATST 319
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
47-129 |
3.05e-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: 56.34 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 47 YDIGHIPTATRIDLRRDLNDPVQrdfiDGEAFARLMDsrgISRDDTVVVYgDRSNLWAAHTLWVLELFGHPDVRLLDGGR 126
Cdd:pfam00581 17 YAKGHIPGAVNVPLSSLSLPPLP----LLELLEKLLE---LLKDKPIVVY-CNSGNRAAAAAALLKALGYKNVYVLDGGF 88
|
...
gi 1533948052 127 DAW 129
Cdd:pfam00581 89 EAW 91
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
21-129 |
5.62e-10 |
|
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: 56.49 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 21 VTSSWLGARLGSPRLKVV--------ESDEDSLLYDI--GHIPTATRIDLRRDLNDPVQrdFIDGEAFARLMDSRGISRD 90
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVdarsperfRGEVPEPRPGLrsGHIPGAVNIPWTSLLDEDGT--FKSPEELRALFAALGITPD 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1533948052 91 DTVVVYgDRSNLWAAHTLWVLELFGHPDVRLLDGGRDAW 129
Cdd:cd01449 79 KPVIVY-CGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
263-338 |
5.75e-10 |
|
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: 56.13 E-value: 5.75e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1533948052 263 GHIPGAVNVPVDvstypnsrfrtraDLEQAFAHLDPARPTVTYCHTGERSSHlwfVLHHL--LGWPSVRSYDGSWVEW 338
Cdd:COG0607 34 GHIPGAINIPLG-------------ELAERLDELPKDKPIVVYCASGGRSAQ---AAALLrrAGYTNVYNLAGGIEAW 95
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
19-131 |
1.69e-09 |
|
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: 55.57 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 19 KLVTSSW--LGARLGSPRLKVVESDEDSLLYDIGHIPTATRIDLR--RDLNDPVQRDFIDGEAFARLMDSRGISRDDTVV 94
Cdd:cd01445 20 QLLDARAqsPGTREARGEYLETQPEPDAVGLDSGHIPGASFFDFEecLDEAGFEESMEPSEAEFAAMFEAKGIDLDKHLI 99
|
90 100 110
....*....|....*....|....*....|....*....
gi 1533948052 95 VYG--DRSNLWAAHTLWVLELFGHPDVRLLDGGRDAWMQ 131
Cdd:cd01445 100 ATDgdDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
263-338 |
3.13e-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: 3.13e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1533948052 263 GHIPGAVNVPVdvSTYPNSRFRTRADLEQAFAHLDPA--RPTVTYCHTGERSSHLWFVLHHLlGWPSVRSYDGSWVEW 338
Cdd:cd01519 30 GKIPGAINIPL--SSLPDALALSEEEFEKKYGFPKPSkdKELIFYCKAGVRSKAAAELARSL-GYENVGNYPGSWLDW 104
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
263-338 |
1.10e-07 |
|
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: 48.84 E-value: 1.10e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1533948052 263 GHIPGAVNVPVdvstypnSRFRTRADLEQafahLDPARPTVTYCHTGERSSHLWFVLHHLLGWPsVRSYDGSWVEW 338
Cdd:cd00158 25 GHIPGAINIPL-------SELEERAALLE----LDKDKPIVVYCRSGNRSARAAKLLRKAGGTN-VYNLEGGMLAW 88
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
19-132 |
4.11e-05 |
|
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440372 [Multi-domain] Cd Length: 106 Bit Score: 42.26 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 19 KLVTSSWLGARLGSPRLKVV---ESDEdsllYDIGHIPTATRIDLRRdlndpvqrdfidgeaFARLMDSrgISRDDTVVV 95
Cdd:COG0607 4 KEISPAELAELLESEDAVLLdvrEPEE----FAAGHIPGAINIPLGE---------------LAERLDE--LPKDKPIVV 62
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1533948052 96 Y---GDRSNLwAAHTLwvlELFGHPDVRLLDGGRDAWMQE 132
Cdd:COG0607 63 YcasGGRSAQ-AAALL---RRAGYTNVYNLAGGIEAWKAA 98
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
263-312 |
7.84e-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: 41.10 E-value: 7.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1533948052 263 GHIPGAVNVPVDvstypnsrfrtraDLEQAFAHLDPARPTVTYCHTGERS 312
Cdd:cd01524 28 GHIKGAINIPLD-------------ELRDRLNELPKDKEIIVYCAVGLRG 64
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
47-129 |
9.56e-05 |
|
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: 40.75 E-value: 9.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 47 YDIGHIPTATRIDLRRdlndpvqrdfidgeaFARLMDSRGISRDDTVVVYgDRSNLWAAHTLWVLELFGHPDVRLLDGGR 126
Cdd:cd00158 22 YAAGHIPGAINIPLSE---------------LEERAALLELDKDKPIVVY-CRSGNRSARAAKLLRKAGGTNVYNLEGGM 85
|
...
gi 1533948052 127 DAW 129
Cdd:cd00158 86 LAW 88
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
263-347 |
2.51e-04 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 42.69 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 263 GHIPGAVNVPvdvstypnsrfrtRADLEQAFA-HL-DPARPTVTYCHTGERSSHLWFVLhHLLGWPSVRSYDGSWVEW-- 338
Cdd:PRK08762 32 GQAEGALRIP-------------RGFLELRIEtHLpDRDREIVLICASGTRSAHAAATL-RELGYTRVASVAGGFSAWkd 97
|
90
....*....|
gi 1533948052 339 -GNMVRVPIR 347
Cdd:PRK08762 98 aGLPLERPRL 107
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
206-338 |
6.33e-03 |
|
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: 36.69 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 206 GTGLQLLDVRdplsysgqpapADGPGGDGARdagrdaGRDAARHPGHAAIRGTAsrwGHIPGAVNVPV----DVSTYPNS 281
Cdd:cd01445 16 GKGFQLLDAR-----------AQSPGTREAR------GEYLETQPEPDAVGLDS---GHIPGASFFDFeeclDEAGFEES 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1533948052 282 RFRTRADLEQAFAHL--DPARPTVTY---CHTGERSSHLWFVLHhLLGWPSVRSYDGSWVEW 338
Cdd:cd01445 76 MEPSEAEFAAMFEAKgiDLDKHLIATdgdDLGGFTACHIALAAR-LCGHPDVAILDGGFFEW 136
|
|
| COG3453 |
COG3453 |
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ... |
214-317 |
9.25e-03 |
|
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only];
Pssm-ID: 442676 [Multi-domain] Cd Length: 125 Bit Score: 35.96 E-value: 9.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533948052 214 VRDPLSYSGQPAPADGPGgdgARDAG-------RDAGrDAARHPGHAAIRGTASRWGHipGAVNVPVDVSTYpnsrfrTR 286
Cdd:COG3453 4 ITDRLSVSGQPTPEDLAA---LAAAGfktvinlRPDG-EEPDQPAAADEAAAAEAAGL--EYVHIPVTGGAI------TD 71
|
90 100 110
....*....|....*....|....*....|..
gi 1533948052 287 ADLEQAFAHLDPA-RPTVTYCHTGERSSHLWF 317
Cdd:COG3453 72 EDVEAFAAALAAApGPVLAHCRSGTRSSALWA 103
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