|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
23-277 |
1.76e-94 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 279.37 E-value: 1.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 23 HRESLVLVDVRWFLDgrSGHEAYLAGHLPGAVWADVDTVLSAPPdeTEGRHPLPDPADFARALGALGIGDGTAVVAYDAD 102
Cdd:COG2897 6 DDPDVVILDVRWDLP--DGRAAYEAGHIPGAVFLDLDTDLSDPR--SPGRHPLPSPEAFAALLGALGISNDTTVVVYDDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 103 GGPYAARLVWLLRRTG-RSAALLDGGLSGWP---HGTETGAVTLPEAWLTpVEWPTEVLRSADEVAA----GDAVVLDAR 174
Cdd:COG2897 82 GGLFAARAWWLLRYAGhEDVRVLDGGLAAWKaagLPLETGPPTPAPGDFT-ARPDPELLADADEVLAalgdPDAVLVDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 175 AADRYSGETVlPTDIRSGHIPGARSAPWSANLTADGTFATPAQLRERYEELGVREGVEVVVYCGSGVTACHDLLALEHAG 254
Cdd:COG2897 161 SPERYRGEVE-PIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALELLG 239
|
250 260
....*....|....*....|...
gi 2207252625 255 ITGAALYPGSWSAWSADLSRPVA 277
Cdd:COG2897 240 YPNVRLYDGSWSEWGSDPDLPVE 262
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
15-280 |
3.85e-42 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 146.01 E-value: 3.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 15 VDAAWVREHR--ESLVLVDVRWF---LDGRSGHEAYLAGHLPGAVWADVDTvLSappDETEGR-HPLPDPADFARALGAL 88
Cdd:PRK11493 7 VAADWLAEHIddPEIQIIDARMAppgQEDRDVAAEYRAGHIPGAVFFDIEA-LS---DHTSPLpHMMPRPETFAVAMREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 89 GIGDGTAVVAYDADGGPYAARLVWLLRRTG-RSAALLDGGLSGWPHGT---ETGAVTLPEAWLTPVEWPTEVLRSADEVA 164
Cdd:PRK11493 83 GVNQDKHLVVYDEGNLFSAPRAWWMLRTFGvEKVSILAGGLAGWQRDDlllEEGAVELPEGEFNAAFNPEAVVRLTDVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 165 A---GDAVVLDARAADRYSGETVLP-TDIRSGHIPGARSAPWSAnLTADGTFATPAQLRERYEELGVREGVEVVVYCGSG 240
Cdd:PRK11493 163 AsheKTAQIVDARPAARFNAEVDEPrPGLRRGHIPGALNVPWTE-LVREGELKTTDELDAIFFGRGVSFDRPIIASCGSG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2207252625 241 VTACHDLLALEHAGITGAALYPGSWSAWSADLSRPVATGQ 280
Cdd:PRK11493 242 VTAAVVVLALATLDVPNVKLYDGAWSEWGARADLPVEPAK 281
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
163-270 |
1.01e-37 |
|
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: 129.29 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 163 VAAGDAVVLDARAADRYSGETVLPT-DIRSGHIPGARSAPWSANLTADGTFATPAQLRERYEELGVREGVEVVVYCGSGV 241
Cdd:cd01449 10 LDSGDVQLVDARSPERFRGEVPEPRpGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKPVIVYCGSGV 89
|
90 100
....*....|....*....|....*....
gi 2207252625 242 TACHDLLALEHAGITGAALYPGSWSAWSA 270
Cdd:cd01449 90 TACVLLLALELLGYKNVRLYDGSWSEWGS 118
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
23-131 |
1.63e-14 |
|
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: 67.87 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 23 HRESLVLVDVRWFldgrsghEAYLAGHLPGAVWADVDTVLsappdeteGRHPLPDPADFARALGALGIGDGTAVVAYDaD 102
Cdd:smart00450 1 NDEKVVLLDVRSP-------EEYEGGHIPGAVNIPLSELL--------DRRGELDILEFEELLKRLGLDKDKPVVVYC-R 64
|
90 100 110
....*....|....*....|....*....|
gi 2207252625 103 GGPYAARLVWLLRRTGRS-AALLDGGLSGW 131
Cdd:smart00450 65 SGNRSAKAAWLLRELGFKnVYLLDGGYKEW 94
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
23-131 |
1.76e-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: 53.64 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 23 HRESLVLVDVRwfldgrsGHEAYLAGHLPGAVWAdvdtvlsapPDETEGRHPLPDPADFARALGalgIGDGTAVVAYDAD 102
Cdd:pfam00581 2 EDGKVVLIDVR-------PPEEYAKGHIPGAVNV---------PLSSLSLPPLPLLELLEKLLE---LLKDKPIVVYCNS 62
|
90 100 110
....*....|....*....|....*....|
gi 2207252625 103 GGPyAARLVWLLRRTG-RSAALLDGGLSGW 131
Cdd:pfam00581 63 GNR-AAAAAALLKALGyKNVYVLDGGFEAW 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
23-277 |
1.76e-94 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 279.37 E-value: 1.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 23 HRESLVLVDVRWFLDgrSGHEAYLAGHLPGAVWADVDTVLSAPPdeTEGRHPLPDPADFARALGALGIGDGTAVVAYDAD 102
Cdd:COG2897 6 DDPDVVILDVRWDLP--DGRAAYEAGHIPGAVFLDLDTDLSDPR--SPGRHPLPSPEAFAALLGALGISNDTTVVVYDDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 103 GGPYAARLVWLLRRTG-RSAALLDGGLSGWP---HGTETGAVTLPEAWLTpVEWPTEVLRSADEVAA----GDAVVLDAR 174
Cdd:COG2897 82 GGLFAARAWWLLRYAGhEDVRVLDGGLAAWKaagLPLETGPPTPAPGDFT-ARPDPELLADADEVLAalgdPDAVLVDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 175 AADRYSGETVlPTDIRSGHIPGARSAPWSANLTADGTFATPAQLRERYEELGVREGVEVVVYCGSGVTACHDLLALEHAG 254
Cdd:COG2897 161 SPERYRGEVE-PIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALELLG 239
|
250 260
....*....|....*....|...
gi 2207252625 255 ITGAALYPGSWSAWSADLSRPVA 277
Cdd:COG2897 240 YPNVRLYDGSWSEWGSDPDLPVE 262
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
15-280 |
3.85e-42 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 146.01 E-value: 3.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 15 VDAAWVREHR--ESLVLVDVRWF---LDGRSGHEAYLAGHLPGAVWADVDTvLSappDETEGR-HPLPDPADFARALGAL 88
Cdd:PRK11493 7 VAADWLAEHIddPEIQIIDARMAppgQEDRDVAAEYRAGHIPGAVFFDIEA-LS---DHTSPLpHMMPRPETFAVAMREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 89 GIGDGTAVVAYDADGGPYAARLVWLLRRTG-RSAALLDGGLSGWPHGT---ETGAVTLPEAWLTPVEWPTEVLRSADEVA 164
Cdd:PRK11493 83 GVNQDKHLVVYDEGNLFSAPRAWWMLRTFGvEKVSILAGGLAGWQRDDlllEEGAVELPEGEFNAAFNPEAVVRLTDVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 165 A---GDAVVLDARAADRYSGETVLP-TDIRSGHIPGARSAPWSAnLTADGTFATPAQLRERYEELGVREGVEVVVYCGSG 240
Cdd:PRK11493 163 AsheKTAQIVDARPAARFNAEVDEPrPGLRRGHIPGALNVPWTE-LVREGELKTTDELDAIFFGRGVSFDRPIIASCGSG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2207252625 241 VTACHDLLALEHAGITGAALYPGSWSAWSADLSRPVATGQ 280
Cdd:PRK11493 242 VTAAVVVLALATLDVPNVKLYDGAWSEWGARADLPVEPAK 281
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
163-270 |
1.01e-37 |
|
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: 129.29 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 163 VAAGDAVVLDARAADRYSGETVLPT-DIRSGHIPGARSAPWSANLTADGTFATPAQLRERYEELGVREGVEVVVYCGSGV 241
Cdd:cd01449 10 LDSGDVQLVDARSPERFRGEVPEPRpGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKPVIVYCGSGV 89
|
90 100
....*....|....*....|....*....
gi 2207252625 242 TACHDLLALEHAGITGAALYPGSWSAWSA 270
Cdd:cd01449 90 TACVLLLALELLGYKNVRLYDGSWSEWGS 118
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
14-131 |
1.06e-37 |
|
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: 129.28 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 14 VVDAAWVREH--RESLVLVDVRWFLDGRSGHEAYLAGHLPGAVWADVDTVLSAPPDeteGRHPLPDPADFARALGALGIG 91
Cdd:cd01448 1 LVSPDWLAEHldDPDVRILDARWYLPDRDGRKEYLEGHIPGAVFFDLDEDLDDKSP---GPHMLPSPEEFAELLGSLGIS 77
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2207252625 92 DGTAVVAYDADGGPYAARLVWLLRRTG-RSAALLDGGLSGW 131
Cdd:cd01448 78 NDDTVVVYDDGGGFFAARAWWTLRYFGhENVRVLDGGLQAW 118
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
13-278 |
2.72e-32 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 121.06 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 13 PVVDAAWVREH-RESLVLV-DVRWFL--DGRSGHEAYLAGHLPGAVWADVDTVLSappDETEGRHPLPDPADFARALGAL 88
Cdd:PLN02723 22 PVVSVDWLHANlREPDVKVlDASWYMpdEQRNPIQEYQVAHIPGALFFDLDGISD---RTTDLPHMLPSEEAFAAAVSAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 89 GIGDGTAVVAYDADGGPYAARLVWLLRRTGRSAA-LLDGGLSGWP-----------------------------HGTETG 138
Cdd:PLN02723 99 GIENKDGVVVYDGKGIFSAARVWWMFRVFGHEKVwVLDGGLPKWRasgydvessasgdailkasaaseaiekvyQGQTVS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 139 AVTLPEAWLTPVEWPTEVLRsaDEVAAGDAVVLDARAADRYSGETVLPTD-IRSGHIPGARSAPWSANLTADGTFATPAQ 217
Cdd:PLN02723 179 PITFQTKFQPHLVWTLEQVK--KNIEDKTYQHIDARSKARFDGAAPEPRKgIRSGHIPGSKCVPFPQMLDSSQTLLPAEE 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2207252625 218 LRERYEELGVREGVEVVVYCGSGVTACHDLLALEHAGITGAALYPGSWSAWSADLSRPVAT 278
Cdd:PLN02723 257 LKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEWGALPDTPVAT 317
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
27-276 |
2.38e-19 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 87.87 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 27 LVLVDVrwfldgrSGHEAYLAGHLPGAVWADVD-TVLSAPPdeteGRHPLPDPADFARALGALGIGDGTAVVAYDADGGP 105
Cdd:PRK09629 25 LILVDL-------TSSARYEAGHIRGARFVDPKrTQLGKPP----APGLLPDTADLEQLFGELGHNPDAVYVVYDDEGGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 106 YAARLVWLLRRTGRSA-ALLDGGLSGW-----PHGTETGAVTLPEAWLTPVEWPT---EVLRSadEVAAGDAVVLDARAA 176
Cdd:PRK09629 94 WAGRFIWLLDVIGHSGyHYLDGGVLAWeaqalPLSTDVPPVAGGPVTLTLHDEPTatrEYLQS--RLGAADLAIWDARAP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 177 DRYSGETVLPTdiRSGHIPGARSAPWSANLTADGTFATPAQLRERYEELGVREGVEVVVYCGSGVTACHDLLALEHAGIT 256
Cdd:PRK09629 172 TEYSGEKVVAA--KGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYP 249
|
250 260
....*....|....*....|
gi 2207252625 257 GAALYPGSWSAWSADLSRPV 276
Cdd:PRK09629 250 RVKAYAGSWGEWGNHPDTPV 269
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
23-131 |
1.63e-14 |
|
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: 67.87 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 23 HRESLVLVDVRWFldgrsghEAYLAGHLPGAVWADVDTVLsappdeteGRHPLPDPADFARALGALGIGDGTAVVAYDaD 102
Cdd:smart00450 1 NDEKVVLLDVRSP-------EEYEGGHIPGAVNIPLSELL--------DRRGELDILEFEELLKRLGLDKDKPVVVYC-R 64
|
90 100 110
....*....|....*....|....*....|
gi 2207252625 103 GGPYAARLVWLLRRTGRS-AALLDGGLSGW 131
Cdd:smart00450 65 SGNRSAKAAWLLRELGFKnVYLLDGGYKEW 94
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
165-271 |
1.78e-12 |
|
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: 62.48 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 165 AGDAVVLDARAADRYSGetvlptdirsGHIPGARSAPWSANLTADGTFaTPAQLRERYEELGVREGVEVVVYCGSGVTAC 244
Cdd:smart00450 2 DEKVVLLDVRSPEEYEG----------GHIPGAVNIPLSELLDRRGEL-DILEFEELLKRLGLDKDKPVVVYCRSGNRSA 70
|
90 100
....*....|....*....|....*..
gi 2207252625 245 HDLLALEHAGITGAALYPGSWSAWSAD 271
Cdd:smart00450 71 KAAWLLRELGFKNVYLLDGGYKEWSAA 97
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
19-133 |
1.35e-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: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 19 WVREHRES------LVLVDVRWFLDG-RSGHEAYL------------AGHLPGAVWADVDTVLS-APPDETegrhPLPDP 78
Cdd:cd01445 5 QLAENLEAgkvgkgFQLLDARAQSPGtREARGEYLetqpepdavgldSGHIPGASFFDFEECLDeAGFEES----MEPSE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2207252625 79 ADFARALGALGIGDGTAVVAYDAD--GGPYAARLVWLLRRTG-RSAALLDGGLSGWPH 133
Cdd:cd01445 81 AEFAAMFEAKGIDLDKHLIATDGDdlGGFTACHIALAARLCGhPDVAILDGGFFEWFH 138
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
23-131 |
1.76e-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: 53.64 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 23 HRESLVLVDVRwfldgrsGHEAYLAGHLPGAVWAdvdtvlsapPDETEGRHPLPDPADFARALGalgIGDGTAVVAYDAD 102
Cdd:pfam00581 2 EDGKVVLIDVR-------PPEEYAKGHIPGAVNV---------PLSSLSLPPLPLLELLEKLLE---LLKDKPIVVYCNS 62
|
90 100 110
....*....|....*....|....*....|
gi 2207252625 103 GGPyAARLVWLLRRTG-RSAALLDGGLSGW 131
Cdd:pfam00581 63 GNR-AAAAAALLKALGyKNVYVLDGGFEAW 91
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
163-269 |
3.85e-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: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 163 VAAGDAVVLDARAADRYSGetvlptdirsGHIPGARSAPWSANLTADGTFAtpaQLRERYEELGVREGVEVvvYCGSGVT 242
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAK----------GHIPGAVNVPLSSLSLPPLPLL---ELLEKLLELLKDKPIVV--YCNSGNR 65
|
90 100
....*....|....*....|....*..
gi 2207252625 243 ACHDLLALEHAGITGAALYPGSWSAWS 269
Cdd:pfam00581 66 AAAAAALLKALGYKNVYVLDGGFEAWK 92
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
24-132 |
8.71e-06 |
|
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: 43.44 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 24 RESLVLVDVRWfldgrsgHEAYLAGHLPGAVWADVDtvlsappdetegrhplpdpaDFARALGALGIGDGTAVVAYDADG 103
Cdd:cd00158 8 DEDAVLLDVRE-------PEEYAAGHIPGAINIPLS--------------------ELEERAALLELDKDKPIVVYCRSG 60
|
90 100 110
....*....|....*....|....*....|.
gi 2207252625 104 G--PYAARLvwLLRRTGRSAALLDGGLSGWP 132
Cdd:cd00158 61 NrsARAAKL--LRKAGGTNVYNLEGGMLAWK 89
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
159-270 |
2.18e-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: 42.65 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 159 SADEVAA----GDAVVLDARAADRYsgetvlptdiRSGHIPGARSAPWSanltadgtfatpaQLRERYEELgvREGVEVV 234
Cdd:COG0607 7 SPAELAEllesEDAVLLDVREPEEF----------AAGHIPGAINIPLG-------------ELAERLDEL--PKDKPIV 61
|
90 100 110
....*....|....*....|....*....|....*.
gi 2207252625 235 VYCGSGVTACHDLLALEHAGITGAALYPGSWSAWSA 270
Cdd:COG0607 62 VYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKA 97
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
160-268 |
2.13e-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: 39.21 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 160 ADEVAAGDAVVLDARAADRYsgetvlptdiRSGHIPGARSAPWSanltadgtfatpaQLRERYEELGVREGVEVVVYCGS 239
Cdd:cd00158 3 KELLDDEDAVLLDVREPEEY----------AAGHIPGAINIPLS-------------ELEERAALLELDKDKPIVVYCRS 59
|
90 100
....*....|....*....|....*....
gi 2207252625 240 GVTACHDLLALEHAGITGAALYPGSWSAW 268
Cdd:cd00158 60 GNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
180-270 |
3.80e-04 |
|
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: 39.18 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 180 SGETVL-----PTDIRSGHIPGARSAPWSanlTADGTFA-TPAQLRERYEELGVREGVEVVVYCGSGVTACHDLLALEHA 253
Cdd:cd01519 13 HPNKVLidvrePEELKTGKIPGAINIPLS---SLPDALAlSEEEFEKKYGFPKPSKDKELIFYCKAGVRSKAAAELARSL 89
|
90
....*....|....*..
gi 2207252625 254 GITGAALYPGSWSAWSA 270
Cdd:cd01519 90 GYENVGNYPGSWLDWAA 106
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
151-268 |
6.09e-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: 39.39 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 151 EWPTEVLRsADEVAAGdAVVLDAR--------AADRYSGETVLPTDI--RSGHIPGARSAPWSANLTADGTFATP----A 216
Cdd:cd01445 4 EQLAENLE-AGKVGKG-FQLLDARaqspgtreARGEYLETQPEPDAVglDSGHIPGASFFDFEECLDEAGFEESMepseA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2207252625 217 QLRERYEELGVREGVEVVVYCG---SGVTACHDLLALEHAGITGAALYPGSWSAW 268
Cdd:cd01445 82 EFAAMFEAKGIDLDKHLIATDGddlGGFTACHIALAARLCGHPDVAILDGGFFEW 136
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
15-131 |
6.17e-04 |
|
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: 38.41 E-value: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2207252625 15 VDAAWVRE--HRESLVLVDVRwfldgrsGHEAYLAGHLPGAVWADVDtvlsappdetegrhplpdpaDFARALGALgiGD 92
Cdd:COG0607 6 ISPAELAEllESEDAVLLDVR-------EPEEFAAGHIPGAINIPLG--------------------ELAERLDEL--PK 56
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2207252625 93 GTAVVAYDADGGpYAARLVWLLRRTGRS-AALLDGGLSGW 131
Cdd:COG0607 57 DKPIVVYCASGG-RSAQAAALLRRAGYTnVYNLAGGIEAW 95
|
|
| |
