|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
14-274 |
3.86e-115 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 331.37 E-value: 3.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 14 ESNLHAPKVVFVEVDEDT----SAYDRDHIAGAIKLDWRTDLQDPVK---RDFVDAQQFSKLLSERGIANEDTVILYGGN 86
Cdd:COG2897 2 AAHLDDPDVVILDVRWDLpdgrAAYEAGHIPGAVFLDLDTDLSDPRSpgrHPLPSPEAFAALLGALGISNDTTVVVYDDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 87 NNWFAAYAYWYFKLYGHEKVKLLDGGRKKWELDGRPLSSDPVSRPVTSYTASpPDNTIRAFRDEVLAAINVKN--LIDVR 164
Cdd:COG2897 82 GGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTAR-PDPELLADADEVLAALGDPDavLVDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 165 SPDEFSGKILAPAhlpqeqsQRPGHIPGAINVPWSRAANEDGTFKSDEELAKLYADAGLDNSKETIAYCRIGERSSHTWF 244
Cdd:COG2897 161 SPERYRGEVEPID-------PRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWL 233
|
250 260 270
....*....|....*....|....*....|
gi 886455744 245 VLrELLGHQNVKNYDGSWTEYGSLVGAPIE 274
Cdd:COG2897 234 AL-ELLGYPNVRLYDGSWSEWGSDPDLPVE 262
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
146-267 |
4.70e-50 |
|
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: 160.88 E-value: 4.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 146 AFRDEVLAAINVKN--LIDVRSPDEFSGKILAPAhlpqeQSQRPGHIPGAINVPWSRAANEDGTFKSDEELAKLYADAGL 223
Cdd:cd01449 1 VTAEEVLANLDSGDvqLVDARSPERFRGEVPEPR-----PGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGI 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 886455744 224 DNSKETIAYCRIGERSSHTWFVLRElLGHQNVKNYDGSWTEYGS 267
Cdd:cd01449 76 TPDKPVIVYCGSGVTACVLLLALEL-LGYKNVRLYDGSWSEWGS 118
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
8-274 |
1.21e-36 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 131.37 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 8 VSADWAESNLHAPKVVFVEV--------DEDTSA-YDRDHIAGAIKLDWRT--DLQDPVKRDFVDAQQFSKLLSERGIAN 76
Cdd:PRK11493 7 VAADWLAEHIDDPEIQIIDArmappgqeDRDVAAeYRAGHIPGAVFFDIEAlsDHTSPLPHMMPRPETFAVAMRELGVNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 77 EDTVILYGGNNNWFAAYAYWYFKLYGHEKVKLLDGGRKKWELDGRPLSSDPVSRPVTSYTASPPDNTIRAfRDEVLAAIN 156
Cdd:PRK11493 87 DKHLVVYDEGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVR-LTDVLLASH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 157 VKN--LIDVRSPDEFSGKILAPahlpqeqsqRPG----HIPGAINVPWSRAANEdGTFKSDEELAKLYADAGLDNSKETI 230
Cdd:PRK11493 166 EKTaqIVDARPAARFNAEVDEP---------RPGlrrgHIPGALNVPWTELVRE-GELKTTDELDAIFFGRGVSFDRPII 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 886455744 231 AYCRIGERSSHTWFVLrELLGHQNVKNYDGSWTEYGSLVGAPIE 274
Cdd:PRK11493 236 ASCGSGVTAAVVVLAL-ATLDVPNVKLYDGAWSEWGARADLPVE 278
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
160-271 |
3.73e-23 |
|
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: 90.60 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 160 LIDVRSPDEFSGkilapahlpqeqsqrpGHIPGAINVPWSRAANEDGTFKSDEeLAKLYADAGLDNSKETIAYCRIGERS 239
Cdd:smart00450 7 LLDVRSPEEYEG----------------GHIPGAVNIPLSELLDRRGELDILE-FEELLKRLGLDKDKPVVVYCRSGNRS 69
|
90 100 110
....*....|....*....|....*....|..
gi 886455744 240 SHTWFVLRElLGHQNVKNYDGSWTEYGSLVGA 271
Cdd:smart00450 70 AKAAWLLRE-LGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
160-265 |
9.77e-18 |
|
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: 75.98 E-value: 9.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 160 LIDVRSPDEFSGkilapahlpqeqsqrpGHIPGAINVPWSRAANEDGTFKSDEElaklyADAGLDNSKETIAYCRIGERS 239
Cdd:pfam00581 8 LIDVRPPEEYAK----------------GHIPGAVNVPLSSLSLPPLPLLELLE-----KLLELLKDKPIVVYCNSGNRA 66
|
90 100
....*....|....*....|....*.
gi 886455744 240 SHTWFVLRElLGHQNVKNYDGSWTEY 265
Cdd:pfam00581 67 AAAAALLKA-LGYKNVYVLDGGFEAW 91
|
|
| tRNA_sel_U_synt |
TIGR03167 |
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ... |
160-197 |
4.31e-03 |
|
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274463 [Multi-domain] Cd Length: 311 Bit Score: 37.96 E-value: 4.31e-03
10 20 30
....*....|....*....|....*....|....*...
gi 886455744 160 LIDVRSPDEFsgkilapahlpqeqsqRPGHIPGAINVP 197
Cdd:TIGR03167 5 LIDVRSPAEF----------------AEGHLPGAINLP 26
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
14-274 |
3.86e-115 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 331.37 E-value: 3.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 14 ESNLHAPKVVFVEVDEDT----SAYDRDHIAGAIKLDWRTDLQDPVK---RDFVDAQQFSKLLSERGIANEDTVILYGGN 86
Cdd:COG2897 2 AAHLDDPDVVILDVRWDLpdgrAAYEAGHIPGAVFLDLDTDLSDPRSpgrHPLPSPEAFAALLGALGISNDTTVVVYDDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 87 NNWFAAYAYWYFKLYGHEKVKLLDGGRKKWELDGRPLSSDPVSRPVTSYTASpPDNTIRAFRDEVLAAINVKN--LIDVR 164
Cdd:COG2897 82 GGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTAR-PDPELLADADEVLAALGDPDavLVDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 165 SPDEFSGKILAPAhlpqeqsQRPGHIPGAINVPWSRAANEDGTFKSDEELAKLYADAGLDNSKETIAYCRIGERSSHTWF 244
Cdd:COG2897 161 SPERYRGEVEPID-------PRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWL 233
|
250 260 270
....*....|....*....|....*....|
gi 886455744 245 VLrELLGHQNVKNYDGSWTEYGSLVGAPIE 274
Cdd:COG2897 234 AL-ELLGYPNVRLYDGSWSEWGSDPDLPVE 262
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
146-267 |
4.70e-50 |
|
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: 160.88 E-value: 4.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 146 AFRDEVLAAINVKN--LIDVRSPDEFSGKILAPAhlpqeQSQRPGHIPGAINVPWSRAANEDGTFKSDEELAKLYADAGL 223
Cdd:cd01449 1 VTAEEVLANLDSGDvqLVDARSPERFRGEVPEPR-----PGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGI 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 886455744 224 DNSKETIAYCRIGERSSHTWFVLRElLGHQNVKNYDGSWTEYGS 267
Cdd:cd01449 76 TPDKPVIVYCGSGVTACVLLLALEL-LGYKNVRLYDGSWSEWGS 118
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
7-120 |
2.54e-41 |
|
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.
Pssm-ID: 238725 [Multi-domain] Cd Length: 122 Bit Score: 138.52 E-value: 2.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 7 LVSADWAESNLHAPKVVFVEVDED------TSAYDRDHIAGAIKLDWRTDLQD--PVKRDFVDAQQFSKLLSERGIANED 78
Cdd:cd01448 1 LVSPDWLAEHLDDPDVRILDARWYlpdrdgRKEYLEGHIPGAVFFDLDEDLDDksPGPHMLPSPEEFAELLGSLGISNDD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 886455744 79 TVILYGGNNNWFAAYAYWYFKLYGHEKVKLLDGGRKKWELDG 120
Cdd:cd01448 81 TVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
8-274 |
1.21e-36 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 131.37 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 8 VSADWAESNLHAPKVVFVEV--------DEDTSA-YDRDHIAGAIKLDWRT--DLQDPVKRDFVDAQQFSKLLSERGIAN 76
Cdd:PRK11493 7 VAADWLAEHIDDPEIQIIDArmappgqeDRDVAAeYRAGHIPGAVFFDIEAlsDHTSPLPHMMPRPETFAVAMRELGVNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 77 EDTVILYGGNNNWFAAYAYWYFKLYGHEKVKLLDGGRKKWELDGRPLSSDPVSRPVTSYTASPPDNTIRAfRDEVLAAIN 156
Cdd:PRK11493 87 DKHLVVYDEGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVR-LTDVLLASH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 157 VKN--LIDVRSPDEFSGKILAPahlpqeqsqRPG----HIPGAINVPWSRAANEdGTFKSDEELAKLYADAGLDNSKETI 230
Cdd:PRK11493 166 EKTaqIVDARPAARFNAEVDEP---------RPGlrrgHIPGALNVPWTELVRE-GELKTTDELDAIFFGRGVSFDRPII 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 886455744 231 AYCRIGERSSHTWFVLrELLGHQNVKNYDGSWTEYGSLVGAPIE 274
Cdd:PRK11493 236 ASCGSGVTAAVVVLAL-ATLDVPNVKLYDGAWSEWGARADLPVE 278
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
1-274 |
6.02e-29 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 112.20 E-value: 6.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 1 MARCDVLVSADWAESNLHAPKVVFVEV-----DEDTSA---YDRDHIAGAI--KLDWRTDLQDPVKRDFVDAQQFSKLLS 70
Cdd:PLN02723 17 ISTNEPVVSVDWLHANLREPDVKVLDAswympDEQRNPiqeYQVAHIPGALffDLDGISDRTTDLPHMLPSEEAFAAAVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 71 ERGIANEDTVILYGGNNNWFAAYAYWYFKLYGHEKVKLLDGGRKKWELDGRPL----SSDPVSRPVTSYTA--------S 138
Cdd:PLN02723 97 ALGIENKDGVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVessaSGDAILKASAASEAiekvyqgqT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 139 PPDNTIRA-FRDEVLAAI-----NVKN----LIDVRSPDEFSGKILAPahlpqEQSQRPGHIPGAINVPWSRAANEDGTF 208
Cdd:PLN02723 177 VSPITFQTkFQPHLVWTLeqvkkNIEDktyqHIDARSKARFDGAAPEP-----RKGIRSGHIPGSKCVPFPQMLDSSQTL 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 886455744 209 KSDEELAKLYADAGLDNSKETIAYCRIGERSSHTWFVLRElLGHQNVKNYDGSWTEYGSLVGAPIE 274
Cdd:PLN02723 252 LPAEELKKRFEQEGISLDSPIVASCGTGVTACILALGLHR-LGKTDVPVYDGSWTEWGALPDTPVA 316
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
17-275 |
3.88e-28 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 112.90 E-value: 3.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 17 LHAPKVVFVEVdEDTSAYDRDHIAGAIKLD-WRTDLQDPVKRDFV-DAQQFSKLLSERGIANEDTVILYGGNNNWFAAYA 94
Cdd:PRK09629 20 LDAPELILVDL-TSSARYEAGHIRGARFVDpKRTQLGKPPAPGLLpDTADLEQLFGELGHNPDAVYVVYDDEGGGWAGRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 95 YWYFKLYGHEKVKLLDGGRKKWELDGRPLSSD--PVSR-PVTSYTASPPDNTiRAFRDEVLAAINVKnLIDVRSPDEFSG 171
Cdd:PRK09629 99 IWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDvpPVAGgPVTLTLHDEPTAT-REYLQSRLGAADLA-IWDARAPTEYSG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 172 KILAPAhlpqeqsqRPGHIPGAINVPWSRAANEDGTFKSDEELAKLYADAGLDNSKETIAYCRIGERSSHTWFVLRElLG 251
Cdd:PRK09629 177 EKVVAA--------KGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKA-LG 247
|
250 260
....*....|....*....|....
gi 886455744 252 HQNVKNYDGSWTEYGSLVGAPIEL 275
Cdd:PRK09629 248 YPRVKAYAGSWGEWGNHPDTPVEV 271
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
160-271 |
3.73e-23 |
|
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: 90.60 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 160 LIDVRSPDEFSGkilapahlpqeqsqrpGHIPGAINVPWSRAANEDGTFKSDEeLAKLYADAGLDNSKETIAYCRIGERS 239
Cdd:smart00450 7 LLDVRSPEEYEG----------------GHIPGAVNIPLSELLDRRGELDILE-FEELLKRLGLDKDKPVVVYCRSGNRS 69
|
90 100 110
....*....|....*....|....*....|..
gi 886455744 240 SHTWFVLRElLGHQNVKNYDGSWTEYGSLVGA 271
Cdd:smart00450 70 AKAAWLLRE-LGFKNVYLLDGGYKEWSAAGPP 100
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
18-122 |
2.64e-18 |
|
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: 77.88 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 18 HAPKVVFVEVDEdTSAYDRDHIAGAIKLDWRTDLQDPVKRDFvdaQQFSKLLSERGIANEDTVILYGGNNNWfAAYAYWY 97
Cdd:smart00450 1 NDEKVVLLDVRS-PEEYEGGHIPGAVNIPLSELLDRRGELDI---LEFEELLKRLGLDKDKPVVVYCRSGNR-SAKAAWL 75
|
90 100
....*....|....*....|....*
gi 886455744 98 FKLYGHEKVKLLDGGRKKWELDGRP 122
Cdd:smart00450 76 LRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
160-265 |
9.77e-18 |
|
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: 75.98 E-value: 9.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 160 LIDVRSPDEFSGkilapahlpqeqsqrpGHIPGAINVPWSRAANEDGTFKSDEElaklyADAGLDNSKETIAYCRIGERS 239
Cdd:pfam00581 8 LIDVRPPEEYAK----------------GHIPGAVNVPLSSLSLPPLPLLELLE-----KLLELLKDKPIVVYCNSGNRA 66
|
90 100
....*....|....*....|....*.
gi 886455744 240 SHTWFVLRElLGHQNVKNYDGSWTEY 265
Cdd:pfam00581 67 AAAAALLKA-LGYKNVYVLDGGFEAW 91
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
160-265 |
3.38e-14 |
|
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: 66.91 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 160 LIDVRSPDEFsgkilapahlpqeqsqRPGHIPGAINVPWSRAanEDGTFKSDEELAKLYADAGLDNSKETIAYCRIGERS 239
Cdd:cd01519 18 LIDVREPEEL----------------KTGKIPGAINIPLSSL--PDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79
|
90 100
....*....|....*....|....*.
gi 886455744 240 SHTWFVLRELlGHQNVKNYDGSWTEY 265
Cdd:cd01519 80 KAAAELARSL-GYENVGNYPGSWLDW 104
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
150-260 |
2.62e-13 |
|
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: 64.24 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 150 EVLAAINVKN--LIDVRSPDEFSGkilapahlpqeqsqrpGHIPGAINVPWSraanedgtfksdeELAKLYADAGLDNSK 227
Cdd:cd00158 1 ELKELLDDEDavLLDVREPEEYAA----------------GHIPGAINIPLS-------------ELEERAALLELDKDK 51
|
90 100 110
....*....|....*....|....*....|...
gi 886455744 228 ETIAYCRIGERSSHTWFVLRElLGHQNVKNYDG 260
Cdd:cd00158 52 PIVVYCRSGNRSARAAKLLRK-AGGTNVYNLEG 83
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
149-266 |
7.91e-13 |
|
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: 63.45 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 149 DEVLAAINVKN--LIDVRSPDEFsgkilapahlpqeqsqRPGHIPGAINVPWSraanedgtfksdeELAKLYADagLDNS 226
Cdd:COG0607 9 AELAELLESEDavLLDVREPEEF----------------AAGHIPGAINIPLG-------------ELAERLDE--LPKD 57
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 886455744 227 KETIAYCRIGERSSHTWFVLRElLGHQNVKNYDG---SWTEYG 266
Cdd:COG0607 58 KPIVVYCASGGRSAQAAALLRR-AGYTNVYNLAGgieAWKAAG 99
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
17-116 |
1.56e-11 |
|
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: 59.42 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 17 LHAPKVVFVEVDEDtSAYDRDHIAGAIKLDWRTDLQDPVKrdfvDAQQFSKLLSergIANEDTVILYGGNNNWfAAYAYW 96
Cdd:pfam00581 1 LEDGKVVLIDVRPP-EEYAKGHIPGAVNVPLSSLSLPPLP----LLELLEKLLE---LLKDKPIVVYCNSGNR-AAAAAA 71
|
90 100
....*....|....*....|
gi 886455744 97 YFKLYGHEKVKLLDGGRKKW 116
Cdd:pfam00581 72 LLKALGYKNVYVLDGGFEAW 91
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
168-265 |
1.40e-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: 55.18 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 168 EFSGKILAPAHLPQEQSQRPGHIPGAINVPWSRAANEDGTFKSDE----ELAKLYADAGLDNSKETIAYCR---IGERSS 240
Cdd:cd01445 33 EARGEYLETQPEPDAVGLDSGHIPGASFFDFEECLDEAGFEESMEpseaEFAAMFEAKGIDLDKHLIATDGddlGGFTAC 112
|
90 100
....*....|....*....|....*
gi 886455744 241 HTWFVLReLLGHQNVKNYDGSWTEY 265
Cdd:cd01445 113 HIALAAR-LCGHPDVAILDGGFFEW 136
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
8-116 |
4.02e-09 |
|
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: 53.41 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 8 VSADWAESNLHAPKVVFV----------EVDEDTSAYDRDHIAGAIKLDWRTDLQDPVKrdFVDAQQFSKLLSERGIANE 77
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVdarsperfrgEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGT--FKSPEELRALFAALGITPD 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 886455744 78 DTVILYGGNNNWfAAYAYWYFKLYGHEKVKLLDGGRKKW 116
Cdd:cd01449 79 KPVIVYCGSGVT-ACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
160-266 |
1.41e-07 |
|
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: 48.42 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 160 LIDVRSPDEFsgkilapahlpqeqsqRPGHIPGAINVPWsraanedgtfksdEELAKLYADagLDNSKETIAYCRIGERS 239
Cdd:cd01524 16 LIDVRTPQEF----------------EKGHIKGAINIPL-------------DELRDRLNE--LPKDKEIIVYCAVGLRG 64
|
90 100
....*....|....*....|....*...
gi 886455744 240 shtWFVLRELLGHQ-NVKNYDGSWTEYG 266
Cdd:cd01524 65 ---YIAARILTQNGfKVKNLDGGYKTYS 89
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
121-260 |
8.77e-07 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 49.49 E-value: 8.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 121 RPLSSDPVSRPVTSYTASPPDNTIRAFRDEVlaainvkNLIDVRSPDEFSGkilapahlpqeqsqrpGHIPGAINVPWSr 200
Cdd:PRK05597 245 RVRGSTPVHGISGGFGEVLDVPRVSALPDGV-------TLIDVREPSEFAA----------------YSIPGAHNVPLS- 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 201 aanedgtfksdeELAKLYADAGLDNSKETIAYCRIGERSSHTWFVLRElLGHQNVKNYDG 260
Cdd:PRK05597 301 ------------AIREGANPPSVSAGDEVVVYCAAGVRSAQAVAILER-AGYTGMSSLDG 347
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
149-265 |
2.91e-06 |
|
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: 45.30 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 149 DEVLAAINVKNL--IDVRSpdefsgkilAPAHLPQEQSQRPGHIPGAINVPWSRAANEDGTFK----SDEELAKLYADAG 222
Cdd:cd01448 5 DWLAEHLDDPDVriLDARW---------YLPDRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPhmlpSPEEFAELLGSLG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 886455744 223 LDNSKETIAYCRIGERSS-HTWFVLReLLGHQNVKNYDGSWTEY 265
Cdd:cd01448 76 ISNDDTVVVYDDGGGFFAaRAWWTLR-YFGHENVRVLDGGLQAW 118
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
7-116 |
3.67e-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: 42.86 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 7 LVSADWAESNLHAPKVVFVEV--DEDTSAYDRDHIAGAIKLDWRT--DLQDPVKRDFVDAQQFSKLLSERGIANEDTVIL 82
Cdd:cd01445 21 LLDARAQSPGTREARGEYLETqpEPDAVGLDSGHIPGASFFDFEEclDEAGFEESMEPSEAEFAAMFEAKGIDLDKHLIA 100
|
90 100 110
....*....|....*....|....*....|....*.
gi 886455744 83 YGGNN--NWFAAYAYWYFKLYGHEKVKLLDGGRKKW 116
Cdd:cd01445 101 TDGDDlgGFTACHIALAARLCGHPDVAILDGGFFEW 136
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
8-123 |
3.94e-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: 41.88 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 8 VSADWAESNLHAPKVVFVEVDEDtSAYDRDHIAGAIKLDWrtdlqdpvkrdfvdaQQFSKLLSErgIANEDTVILY--GG 85
Cdd:COG0607 6 ISPAELAELLESEDAVLLDVREP-EEFAAGHIPGAINIPL---------------GELAERLDE--LPKDKPIVVYcaSG 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 886455744 86 NNnwfAAYAYWYFKLYGHEKVKLLDGGRKKWELDGRPL 123
Cdd:COG0607 68 GR---SAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPV 102
|
|
| SelU |
COG2603 |
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ... |
149-197 |
8.53e-05 |
|
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442015 [Multi-domain] Cd Length: 341 Bit Score: 43.22 E-value: 8.53e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 886455744 149 DEVLAAINVKNLIDVRSPDEFsgkilapahlpqEQsqrpGHIPGAINVP 197
Cdd:COG2603 8 DDFLELLDDDPLIDVRSPVEF------------AE----GHIPGAINLP 40
|
|
| PRK11784 |
PRK11784 |
tRNA 2-selenouridine synthase; Provisional |
160-197 |
4.15e-04 |
|
tRNA 2-selenouridine synthase; Provisional
Pssm-ID: 236982 [Multi-domain] Cd Length: 345 Bit Score: 41.35 E-value: 4.15e-04
10 20 30
....*....|....*....|....*....|....*...
gi 886455744 160 LIDVRSPDEFsgkilapAHlpqeqsqrpGHIPGAINVP 197
Cdd:PRK11784 18 LIDVRSPIEF-------AE---------GHIPGAINLP 39
|
|
| RHOD_ThiF |
cd01526 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ... |
160-264 |
1.17e-03 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.
Pssm-ID: 238784 [Multi-domain] Cd Length: 122 Bit Score: 38.06 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 160 LIDVRSPDEFsgKIlapahlpqeqsqrpGHIPGAINVPWSRAANedgtfKSDEELAKLYADAGLDNSKETIAYCRIGERS 239
Cdd:cd01526 27 LLDVRPKVHF--EI--------------CRLPEAINIPLSELLS-----KAAELKSLQELPLDNDKDSPIYVVCRRGNDS 85
|
90 100
....*....|....*....|....*...
gi 886455744 240 SHTWFVLRELLGHQNVKNYDG---SWTE 264
Cdd:cd01526 86 QTAVRKLKELGLERFVRDIIGglkAWAD 113
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
160-266 |
1.22e-03 |
|
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.
Pssm-ID: 238724 [Multi-domain] Cd Length: 103 Bit Score: 37.41 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 160 LIDVRSPDEFsgkilapahlpqeqsQRPGHIPGAINVPwsRAANEdgtFKSDEElaKLYADAGLDNSKETIAYCRIGERS 239
Cdd:cd01447 17 LVDVRDPREL---------------ERTGMIPGAFHAP--RGMLE---FWADPD--SPYHKPAFAEDKPFVFYCASGWRS 74
|
90 100 110
....*....|....*....|....*....|
gi 886455744 240 SHTWFVLRElLGHQNVKNYDG---SWTEYG 266
Cdd:cd01447 75 ALAGKTLQD-MGLKPVYNIEGgfkDWKEAG 103
|
|
| RHOD_YbbB |
cd01520 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ... |
160-253 |
1.32e-03 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.
Pssm-ID: 238778 [Multi-domain] Cd Length: 128 Bit Score: 38.04 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 160 LIDVRSPDEFsgkilapahlpQEqsqrpGHIPGAINVPW-----------------SRAANEDG----TFKSDEELAKLY 218
Cdd:cd01520 16 LIDVRSPKEF-----------FE-----GHLPGAINLPLlddeeralvgtlykqqgREAAIELGlelvSGKLKRILNEAW 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 886455744 219 ADAgLDNSKETIAYC-RIGERS-SHTWfvLRELLGHQ 253
Cdd:cd01520 80 EAR-LERDPKLLIYCaRGGMRSqSLAW--LLESLGID 113
|
|
| PRK07411 |
PRK07411 |
molybdopterin-synthase adenylyltransferase MoeB; |
160-264 |
2.06e-03 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 39.33 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 886455744 160 LIDVRSPDEFSgkilapahlpqeqsqrPGHIPGAINVPWSRAANEDGTFKSDEelaklyadagLDNSKETIAYCRIGERS 239
Cdd:PRK07411 302 LIDVRNPNEYE----------------IARIPGSVLVPLPDIENGPGVEKVKE----------LLNGHRLIAHCKMGGRS 355
|
90 100
....*....|....*....|....*.
gi 886455744 240 SHTWFVLREL-LGHQNVKNYDGSWTE 264
Cdd:PRK07411 356 AKALGILKEAgIEGTNVKGGITAWSR 381
|
|
| tRNA_sel_U_synt |
TIGR03167 |
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ... |
160-197 |
4.31e-03 |
|
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274463 [Multi-domain] Cd Length: 311 Bit Score: 37.96 E-value: 4.31e-03
10 20 30
....*....|....*....|....*....|....*...
gi 886455744 160 LIDVRSPDEFsgkilapahlpqeqsqRPGHIPGAINVP 197
Cdd:TIGR03167 5 LIDVRSPAEF----------------AEGHLPGAINLP 26
|
|
| |
