|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
11-285 |
1.17e-113 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 328.29 E-value: 1.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 11 LRERMARPGCLVFDVRHDLADhaaGRQAYEAGHIPGALYLAPETQLSGARSGrnGRHPLPDRGEFAALMRAQGLTARTEV 90
Cdd:COG2897 1 LAAHLDDPDVVILDVRWDLPD---GRAAYEAGHIPGAVFLDLDTDLSDPRSP--GRHPLPSPEAFAALLGALGISNDTTV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 91 VVYDGGNAMFAVRLWWMLRWLGHEAVTVLDGGWAAWLAAGGESEAGRRDPALSEAQAIEGTvlsgkpsMPQVDACAVLAN 170
Cdd:COG2897 76 VVYDDGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDP-------ELLADADEVLAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 171 LAEPRFTILDARAADRFSGAAETIDPVGGHIPGALNRSFLDNIGPDGRFKAPARLRAEFETLLGDrLDRGVVHQCGSGIT 250
Cdd:COG2897 149 LGDPDAVLVDARSPERYRGEVEPIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGID-PDKPVITYCGSGVR 227
|
250 260 270
....*....|....*....|....*....|....*
gi 2751072797 251 ACHNLFAMELAGLRGSALYPGSWSEWCSDPARPVA 285
Cdd:COG2897 228 AAHTWLALELLGYPNVRLYDGSWSEWGSDPDLPVE 262
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
5-130 |
6.46e-43 |
|
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: 143.14 E-value: 6.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 5 LIQADALRERMARPGCLVFDVRHDLADhAAGRQAYEAGHIPGALYLAPETQLSGARSGRngrHPLPDRGEFAALMRAQGL 84
Cdd:cd01448 1 LVSPDWLAEHLDDPDVRILDARWYLPD-RDGRKEYLEGHIPGAVFFDLDEDLDDKSPGP---HMLPSPEEFAELLGSLGI 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2751072797 85 TARTEVVVYDGGNAMFAVRLWWMLRWLGHEAVTVLDGGWAAWLAAG 130
Cdd:cd01448 77 SNDDTVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
14-288 |
2.13e-39 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 139.07 E-value: 2.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 14 RMARPGclvfdvrhdlADHAAGRQAYEAGHIPGALYLAPETqLSGARSGRNgrHPLPDRGEFAALMRAQGLTARTEVVVY 93
Cdd:PRK11493 27 RMAPPG----------QEDRDVAAEYRAGHIPGAVFFDIEA-LSDHTSPLP--HMMPRPETFAVAMRELGVNQDKHLVVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 94 DGGNAMFAVRLWWMLRWLGHEAVTVLDGGWAAWLAAGGESEAGRRDPALSE--AQAIEGTVLSgkpsmpqvdACAVLANL 171
Cdd:PRK11493 94 DEGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEfnAAFNPEAVVR---------LTDVLLAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 172 AEPRFTILDARAADRFSGAAETIDPvG---GHIPGALNRSFLDNIGpDGRFKAPARLRAEFETlLGDRLDRGVVHQCGSG 248
Cdd:PRK11493 165 HEKTAQIVDARPAARFNAEVDEPRP-GlrrGHIPGALNVPWTELVR-EGELKTTDELDAIFFG-RGVSFDRPIIASCGSG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2751072797 249 ITACHNLFAMELAGLRGSALYPGSWSEWCSDPARPVAQGA 288
Cdd:PRK11493 242 VTAAVVVLALATLDVPNVKLYDGAWSEWGARADLPVEPAK 281
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
17-132 |
2.57e-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: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 17 RPGCLVFDVRHdladhaagRQAYEAGHIPGALYLAPETQLsgarsgrnGRHPLPDRGEFAALMRAQGLTARTEVVVYDGG 96
Cdd:smart00450 2 DEKVVLLDVRS--------PEEYEGGHIPGAVNIPLSELL--------DRRGELDILEFEELLKRLGLDKDKPVVVYCRS 65
|
90 100 110
....*....|....*....|....*....|....*.
gi 2751072797 97 NaMFAVRLWWMLRWLGHEAVTVLDGGWAAWLAAGGE 132
Cdd:smart00450 66 G-NRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
15-126 |
1.74e-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: 64.81 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 15 MARPGCLVFDVRHDladhaagrQAYEAGHIPGALYLAPETqlsgarsgrNGRHPLPDRGEFAALMraqGLTARTEVVVYD 94
Cdd:pfam00581 1 LEDGKVVLIDVRPP--------EEYAKGHIPGAVNVPLSS---------LSLPPLPLLELLEKLL---ELLKDKPIVVYC 60
|
90 100 110
....*....|....*....|....*....|..
gi 2751072797 95 GGNAMfAVRLWWMLRWLGHEAVTVLDGGWAAW 126
Cdd:pfam00581 61 NSGNR-AAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
11-285 |
1.17e-113 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 328.29 E-value: 1.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 11 LRERMARPGCLVFDVRHDLADhaaGRQAYEAGHIPGALYLAPETQLSGARSGrnGRHPLPDRGEFAALMRAQGLTARTEV 90
Cdd:COG2897 1 LAAHLDDPDVVILDVRWDLPD---GRAAYEAGHIPGAVFLDLDTDLSDPRSP--GRHPLPSPEAFAALLGALGISNDTTV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 91 VVYDGGNAMFAVRLWWMLRWLGHEAVTVLDGGWAAWLAAGGESEAGRRDPALSEAQAIEGTvlsgkpsMPQVDACAVLAN 170
Cdd:COG2897 76 VVYDDGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDP-------ELLADADEVLAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 171 LAEPRFTILDARAADRFSGAAETIDPVGGHIPGALNRSFLDNIGPDGRFKAPARLRAEFETLLGDrLDRGVVHQCGSGIT 250
Cdd:COG2897 149 LGDPDAVLVDARSPERYRGEVEPIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGID-PDKPVITYCGSGVR 227
|
250 260 270
....*....|....*....|....*....|....*
gi 2751072797 251 ACHNLFAMELAGLRGSALYPGSWSEWCSDPARPVA 285
Cdd:COG2897 228 AAHTWLALELLGYPNVRLYDGSWSEWGSDPDLPVE 262
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
5-130 |
6.46e-43 |
|
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: 143.14 E-value: 6.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 5 LIQADALRERMARPGCLVFDVRHDLADhAAGRQAYEAGHIPGALYLAPETQLSGARSGRngrHPLPDRGEFAALMRAQGL 84
Cdd:cd01448 1 LVSPDWLAEHLDDPDVRILDARWYLPD-RDGRKEYLEGHIPGAVFFDLDEDLDDKSPGP---HMLPSPEEFAELLGSLGI 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2751072797 85 TARTEVVVYDGGNAMFAVRLWWMLRWLGHEAVTVLDGGWAAWLAAG 130
Cdd:cd01448 77 SNDDTVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
14-288 |
2.13e-39 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 139.07 E-value: 2.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 14 RMARPGclvfdvrhdlADHAAGRQAYEAGHIPGALYLAPETqLSGARSGRNgrHPLPDRGEFAALMRAQGLTARTEVVVY 93
Cdd:PRK11493 27 RMAPPG----------QEDRDVAAEYRAGHIPGAVFFDIEA-LSDHTSPLP--HMMPRPETFAVAMRELGVNQDKHLVVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 94 DGGNAMFAVRLWWMLRWLGHEAVTVLDGGWAAWLAAGGESEAGRRDPALSE--AQAIEGTVLSgkpsmpqvdACAVLANL 171
Cdd:PRK11493 94 DEGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEfnAAFNPEAVVR---------LTDVLLAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 172 AEPRFTILDARAADRFSGAAETIDPvG---GHIPGALNRSFLDNIGpDGRFKAPARLRAEFETlLGDRLDRGVVHQCGSG 248
Cdd:PRK11493 165 HEKTAQIVDARPAARFNAEVDEPRP-GlrrGHIPGALNVPWTELVR-EGELKTTDELDAIFFG-RGVSFDRPIIASCGSG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2751072797 249 ITACHNLFAMELAGLRGSALYPGSWSEWCSDPARPVAQGA 288
Cdd:PRK11493 242 VTAAVVVLALATLDVPNVKLYDGAWSEWGARADLPVEPAK 281
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
37-285 |
2.00e-38 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 137.63 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 37 QAYEAGHIPGALYLapetQLSG-ARSGRNGRHPLPDRGEFAALMRAQGLTARTEVVVYDGGNAMFAVRLWWMLRWLGHEA 115
Cdd:PLN02723 56 QEYQVAHIPGALFF----DLDGiSDRTTDLPHMLPSEEAFAAAVSALGIENKDGVVVYDGKGIFSAARVWWMFRVFGHEK 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 116 VTVLDGGWAAWLAAGGESEAGRRDPALSEAQA----IEgTVLSGKPSMP-----QVDACAVLA------NLAEPRFTILD 180
Cdd:PLN02723 132 VWVLDGGLPKWRASGYDVESSASGDAILKASAaseaIE-KVYQGQTVSPitfqtKFQPHLVWTleqvkkNIEDKTYQHID 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 181 ARAADRFSGAAEtiDP----VGGHIPGALNRSFLDNIGPDGRFKAPARLRAEFETlLGDRLDRGVVHQCGSGITACHNLF 256
Cdd:PLN02723 211 ARSKARFDGAAP--EPrkgiRSGHIPGSKCVPFPQMLDSSQTLLPAEELKKRFEQ-EGISLDSPIVASCGTGVTACILAL 287
|
250 260
....*....|....*....|....*....
gi 2751072797 257 AMELAGLRGSALYPGSWSEWCSDPARPVA 285
Cdd:PLN02723 288 GLHRLGKTDVPVYDGSWTEWGALPDTPVA 316
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
162-276 |
8.52e-38 |
|
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: 129.68 E-value: 8.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 162 VDACAVLANLAEPRFTILDARAADRFSGAAETI--DPVGGHIPGALNRSFLDNIGPDGRFKAPARLRAEFETLLGDrLDR 239
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPrpGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGIT-PDK 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 2751072797 240 GVVHQCGSGITACHNLFAMELAGLRGSALYPGSWSEW 276
Cdd:cd01449 80 PVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
17-132 |
2.57e-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: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 17 RPGCLVFDVRHdladhaagRQAYEAGHIPGALYLAPETQLsgarsgrnGRHPLPDRGEFAALMRAQGLTARTEVVVYDGG 96
Cdd:smart00450 2 DEKVVLLDVRS--------PEEYEGGHIPGAVNIPLSELL--------DRRGELDILEFEELLKRLGLDKDKPVVVYCRS 65
|
90 100 110
....*....|....*....|....*....|....*.
gi 2751072797 97 NaMFAVRLWWMLRWLGHEAVTVLDGGWAAWLAAGGE 132
Cdd:smart00450 66 G-NRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
3-284 |
7.27e-17 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 80.55 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 3 ALLIQADALRERMARPGCLVFDVrhdladhaAGRQAYEAGHIPGALYLAPE-TQLsgarsgrnGRHP----LPDRGEFAA 77
Cdd:PRK09629 8 SLVIEPNDLLERLDAPELILVDL--------TSSARYEAGHIRGARFVDPKrTQL--------GKPPapglLPDTADLEQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 78 LMRAQGLTARTEVVVYDGGNAMFAVRLWWMLRWLGHEAVTVLDGGWAAWlaaggesEAGRRDPALSEAQAIEGTVLSGKP 157
Cdd:PRK09629 72 LFGELGHNPDAVYVVYDDEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAW-------EAQALPLSTDVPPVAGGPVTLTLH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 158 SMPQVDACAVLANLAEPRFTILDARAADRFSGaAETIDPVGGHIPGALNRSFLDNIGPDGRFkapaRLRAEFETLLGD-- 235
Cdd:PRK09629 145 DEPTATREYLQSRLGAADLAIWDARAPTEYSG-EKVVAAKGGHIPGAVNFEWTAGMDKARNL----RIRQDMPEILRDlg 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2751072797 236 -RLDRGVVHQCGSGITACHNLFAMELAGLRGSALYPGSWSEWCSDPARPV 284
Cdd:PRK09629 220 iTPDKEVITHCQTHHRSGFTYLVAKALGYPRVKAYAGSWGEWGNHPDTPV 269
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
15-126 |
1.74e-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: 64.81 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 15 MARPGCLVFDVRHDladhaagrQAYEAGHIPGALYLAPETqlsgarsgrNGRHPLPDRGEFAALMraqGLTARTEVVVYD 94
Cdd:pfam00581 1 LEDGKVVLIDVRPP--------EEYAKGHIPGAVNVPLSS---------LSLPPLPLLELLEKLL---ELLKDKPIVVYC 60
|
90 100 110
....*....|....*....|....*....|..
gi 2751072797 95 GGNAMfAVRLWWMLRWLGHEAVTVLDGGWAAW 126
Cdd:pfam00581 61 NSGNR-AAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
8-127 |
6.54e-13 |
|
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: 64.81 E-value: 6.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 8 ADALRERMARPGCLVFDVRHDLADHAAGRQAY------------EAGHIPGALYLAPETQLSGARSGRNgrhPLPDRGEF 75
Cdd:cd01445 7 AENLEAGKVGKGFQLLDARAQSPGTREARGEYletqpepdavglDSGHIPGASFFDFEECLDEAGFEES---MEPSEAEF 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2751072797 76 AALMRAQGLTARTEVVVYDGGN--AMFAVRLWWMLRWLGHEAVTVLDGGWAAWL 127
Cdd:cd01445 84 AAMFEAKGIDLDKHLIATDGDDlgGFTACHIALAARLCGHPDVAILDGGFFEWF 137
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
6-137 |
1.31e-12 |
|
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: 62.68 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 6 IQADALRERMARPGCLVFDVRhdladhaaGRQAYEAGHIPGALYLapetqlsgarsgrngrhplpDRGEFAAlmRAQGLT 85
Cdd:COG0607 6 ISPAELAELLESEDAVLLDVR--------EPEEFAAGHIPGAINI--------------------PLGELAE--RLDELP 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2751072797 86 ARTEVVVYD--GGNAMFAVRlwwMLRWLGHEAVTVLDGGWAAWLAAGGESEAGR 137
Cdd:COG0607 56 KDKPIVVYCasGGRSAQAAA---LLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
6-126 |
4.94e-11 |
|
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: 58.80 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 6 IQADALRERMARPGCLVFDVRhDLADHA----AGRQAYEAGHIPGALYLaPETQLSgarsgrNGRHPLPDRGEFAALMRA 81
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDAR-SPERFRgevpEPRPGLRSGHIPGAVNI-PWTSLL------DEDGTFKSPEELRALFAA 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2751072797 82 QGLTARTEVVVYDGGNAMfAVRLWWMLRWLGHEAVTVLDGGWAAW 126
Cdd:cd01449 73 LGITPDKPVIVYCGSGVT-ACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
167-276 |
1.16e-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: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 167 VLANLAEPRFTILDAR--------AADRFSGAAETIDPVG---GHIPGALNRSFLDNIGPDGRFKAPARLRAEFETLLGD 235
Cdd:cd01445 10 LEAGKVGKGFQLLDARaqspgtreARGEYLETQPEPDAVGldsGHIPGASFFDFEECLDEAGFEESMEPSEAEFAAMFEA 89
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2751072797 236 R---LDRGVVHQCG---SGITACHNLFAMELAGLRGSALYPGSWSEW 276
Cdd:cd01445 90 KgidLDKHLIATDGddlGGFTACHIALAARLCGHPDVAILDGGFFEW 136
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|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
171-276 |
4.11e-09 |
|
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.
Pssm-ID: 425764 [Multi-domain] Cd Length: 92 Bit Score: 52.87 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 171 LAEPRFTILDARAADRFSGaaetidpvgGHIPGALNrsfldnIGPDGRFKAPARLRAEFETLLGDRLDRGVVHQCGSGIT 250
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAK---------GHIPGAVN------VPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNR 65
|
90 100
....*....|....*....|....*.
gi 2751072797 251 ACHNLFAMELAGLRGSALYPGSWSEW 276
Cdd:pfam00581 66 AAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
173-280 |
6.80e-09 |
|
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: 52.46 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 173 EPRFTILDARAADRFSGaaetidpvgGHIPGALNRSFLDNIGPDGRFKaPARLRAEFETLLGDRLDRGVVHqCGSGITAC 252
Cdd:smart00450 2 DEKVVLLDVRSPEEYEG---------GHIPGAVNIPLSELLDRRGELD-ILEFEELLKRLGLDKDKPVVVY-CRSGNRSA 70
|
90 100
....*....|....*....|....*...
gi 2751072797 253 HNLFAMELAGLRGSALYPGSWSEWCSDP 280
Cdd:smart00450 71 KAAWLLRELGFKNVYLLDGGYKEWSAAG 98
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
11-126 |
1.09e-04 |
|
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.
Pssm-ID: 238089 [Multi-domain] Cd Length: 89 Bit Score: 40.36 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 11 LRERMARPGCLVFDVRhdladhaaGRQAYEAGHIPGALYLapetqlsgarsgrngrhPLpdrGEFAALMRAQGLTARTEV 90
Cdd:cd00158 2 LKELLDDEDAVLLDVR--------EPEEYAAGHIPGAINI-----------------PL---SELEERAALLELDKDKPI 53
|
90 100 110
....*....|....*....|....*....|....*...
gi 2751072797 91 VVYD--GGNAMFAVRLwwmLRWLGHEAVTVLDGGWAAW 126
Cdd:cd00158 54 VVYCrsGNRSARAAKL---LRKAGGTNVYNLEGGMLAW 88
|
|
| glpE |
PRK00162 |
thiosulfate sulfurtransferase GlpE; |
7-126 |
5.11e-03 |
|
thiosulfate sulfurtransferase GlpE;
Pssm-ID: 178908 [Multi-domain] Cd Length: 108 Bit Score: 35.77 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 7 QADALRERMarpGCLVFDVRHDladhaagrQAYEAGHIPGALYLapetqlsgarsgrngrhplpDRGEFAALMRAQGLTA 86
Cdd:PRK00162 11 QAHQKLQEG---GAVLVDIRDP--------QSFAMGHAPGAFHL--------------------TNDSLGAFMRQADFDT 59
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2751072797 87 RTEVVVYDG----GNAMFAVRlwwmlrwLGHEAVTVLDGGWAAW 126
Cdd:PRK00162 60 PVMVMCYHGnssqGAAQYLLQ-------QGFDVVYSIDGGFEAW 96
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
162-276 |
9.21e-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: 35.29 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2751072797 162 VDACAVLANLAEPRFTILDARAADRFSGAAETIDpvGGHIPGA----LNRSFLDNIGPDGRFKAPARLRAEFETLLGDRL 237
Cdd:cd01448 2 VSPDWLAEHLDDPDVRILDARWYLPDRDGRKEYL--EGHIPGAvffdLDEDLDDKSPGPHMLPSPEEFAELLGSLGISND 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 2751072797 238 DRGVVHQCGSGITACHNLFAMELAGLRGSALYPGSWSEW 276
Cdd:cd01448 80 DTVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAW 118
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