|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
13-276 |
6.71e-110 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 318.27 E-value: 6.71e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 13 LQEHLDDPTIAIVEVDEDT----SAYEKNHIRNAIRIDWTQDLQDP---VRRDFVDQEGFEKLLSEKGIANDHTVILYGG 85
Cdd:COG2897 1 LAAHLDDPDVVILDVRWDLpdgrAAYEAGHIPGAVFLDLDTDLSDPrspGRHPLPSPEAFAALLGALGISNDTTVVVYDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 86 NNNWFASYAYWYFKLYGHDNVKLLDGGRKKWELDARELVagDEVPERPKTDYKAKAqDTSIRAFRDDVVAAIGSQN--LV 163
Cdd:COG2897 81 GGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLE--TGPPTPAPGDFTARP-DPELLADADEVLAALGDPDavLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 164 DVRSPDEFSGKLLAPAhlpqeqsQRPGHVPSARNIPWSKNANDDGTFKSDEELKELYAAESVDLAKDTIAYCRIGERSAL 243
Cdd:COG2897 158 DARSPERYRGEVEPID-------PRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAH 230
|
250 260 270
....*....|....*....|....*....|...
gi 1892868620 244 TWFVLhELLGVENVKNYDGSWTEYGSLVGVPIE 276
Cdd:COG2897 231 TWLAL-ELLGYPNVRLYDGSWSEWGSDPDLPVE 262
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
148-269 |
4.36e-45 |
|
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: 148.16 E-value: 4.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 148 AFRDDVVAAIGSQN--LVDVRSPDEFSGKLLAPAhlpqeQSQRPGHVPSARNIPWSKNANDDGTFKSDEELKELYAAESV 225
Cdd:cd01449 1 VTAEEVLANLDSGDvqLVDARSPERFRGEVPEPR-----PGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGI 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1892868620 226 DLAKDTIAYCRIGERSALTWFVLHElLGVENVKNYDGSWTEYGS 269
Cdd:cd01449 76 TPDKPVIVYCGSGVTACVLLLALEL-LGYKNVRLYDGSWSEWGS 118
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
1-279 |
2.12e-38 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 135.99 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 1 MSRSdVLVDADWLQEHLDDPTIAIVEV--------DEDTSA-YEKNHIRNAI--RIDWTQDLQDPVRRDFVDQEGFEKLL 69
Cdd:PRK11493 1 MSTT-WFVAADWLAEHIDDPEIQIIDArmappgqeDRDVAAeYRAGHIPGAVffDIEALSDHTSPLPHMMPRPETFAVAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 70 SEKGIANDHTVILYGGNNNWFASYAYWYFKLYGHDNVKLLDGGRKKWELDARELVAGDevPERPKTDYKAKAQDTSIRAf 149
Cdd:PRK11493 80 RELGVNQDKHLVVYDEGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGA--VELPEGEFNAAFNPEAVVR- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 150 RDDVVAAI--GSQNLVDVRSPDEFSGKLLAPahlpqeqsqRPG----HVPSARNIPWSKNANDdGTFKSDEELKELYAAE 223
Cdd:PRK11493 157 LTDVLLASheKTAQIVDARPAARFNAEVDEP---------RPGlrrgHIPGALNVPWTELVRE-GELKTTDELDAIFFGR 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1892868620 224 SVDLAKDTIAYCRIGERSALTWFVLhELLGVENVKNYDGSWTEYGSLVGVPIELGA 279
Cdd:PRK11493 227 GVSFDRPIIASCGSGVTAAVVVLAL-ATLDVPNVKLYDGAWSEWGARADLPVEPAK 281
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
162-272 |
7.92e-19 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 79.43 E-value: 7.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 162 LVDVRSPDEFSGkllapahlpqeqsqrpGHVPSARNIPWSKNANDDGTFKSDEeLKELYAAESVDLAKDTIAYCRIGERS 241
Cdd:smart00450 7 LLDVRSPEEYEG----------------GHIPGAVNIPLSELLDRRGELDILE-FEELLKRLGLDKDKPVVVYCRSGNRS 69
|
90 100 110
....*....|....*....|....*....|.
gi 1892868620 242 ALTWFVLHElLGVENVKNYDGSWTEYGSLVG 272
Cdd:smart00450 70 AKAAWLLRE-LGFKNVYLLDGGYKEWSAAGP 99
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
158-267 |
5.80e-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: 63.27 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 158 GSQNLVDVRSPDEFSGkllapahlpqeqsqrpGHVPSARNIPWSknandDGTFKSDEELKELYAAESVDLAKDTIAYCRI 237
Cdd:pfam00581 4 GKVVLIDVRPPEEYAK----------------GHIPGAVNVPLS-----SLSLPPLPLLELLEKLLELLKDKPIVVYCNS 62
|
90 100 110
....*....|....*....|....*....|
gi 1892868620 238 GERSALTWFvLHELLGVENVKNYDGSWTEY 267
Cdd:pfam00581 63 GNRAAAAAA-LLKALGYKNVYVLDGGFEAW 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
13-276 |
6.71e-110 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 318.27 E-value: 6.71e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 13 LQEHLDDPTIAIVEVDEDT----SAYEKNHIRNAIRIDWTQDLQDP---VRRDFVDQEGFEKLLSEKGIANDHTVILYGG 85
Cdd:COG2897 1 LAAHLDDPDVVILDVRWDLpdgrAAYEAGHIPGAVFLDLDTDLSDPrspGRHPLPSPEAFAALLGALGISNDTTVVVYDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 86 NNNWFASYAYWYFKLYGHDNVKLLDGGRKKWELDARELVagDEVPERPKTDYKAKAqDTSIRAFRDDVVAAIGSQN--LV 163
Cdd:COG2897 81 GGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLE--TGPPTPAPGDFTARP-DPELLADADEVLAALGDPDavLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 164 DVRSPDEFSGKLLAPAhlpqeqsQRPGHVPSARNIPWSKNANDDGTFKSDEELKELYAAESVDLAKDTIAYCRIGERSAL 243
Cdd:COG2897 158 DARSPERYRGEVEPID-------PRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAH 230
|
250 260 270
....*....|....*....|....*....|...
gi 1892868620 244 TWFVLhELLGVENVKNYDGSWTEYGSLVGVPIE 276
Cdd:COG2897 231 TWLAL-ELLGYPNVRLYDGSWSEWGSDPDLPVE 262
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
148-269 |
4.36e-45 |
|
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: 148.16 E-value: 4.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 148 AFRDDVVAAIGSQN--LVDVRSPDEFSGKLLAPAhlpqeQSQRPGHVPSARNIPWSKNANDDGTFKSDEELKELYAAESV 225
Cdd:cd01449 1 VTAEEVLANLDSGDvqLVDARSPERFRGEVPEPR-----PGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGI 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1892868620 226 DLAKDTIAYCRIGERSALTWFVLHElLGVENVKNYDGSWTEYGS 269
Cdd:cd01449 76 TPDKPVIVYCGSGVTACVLLLALEL-LGYKNVRLYDGSWSEWGS 118
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
7-117 |
3.07e-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: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 7 LVDADWLQEHLDDPTIAIVEVDED------TSAYEKNHIRNAIRIDWTQDLQD--PVRRDFVDQEGFEKLLSEKGIANDH 78
Cdd:cd01448 1 LVSPDWLAEHLDDPDVRILDARWYlpdrdgRKEYLEGHIPGAVFFDLDEDLDDksPGPHMLPSPEEFAELLGSLGISNDD 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1892868620 79 TVILYGGNNNWFASYAYWYFKLYGHDNVKLLDGGRKKWE 117
Cdd:cd01448 81 TVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWK 119
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
1-279 |
2.12e-38 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 135.99 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 1 MSRSdVLVDADWLQEHLDDPTIAIVEV--------DEDTSA-YEKNHIRNAI--RIDWTQDLQDPVRRDFVDQEGFEKLL 69
Cdd:PRK11493 1 MSTT-WFVAADWLAEHIDDPEIQIIDArmappgqeDRDVAAeYRAGHIPGAVffDIEALSDHTSPLPHMMPRPETFAVAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 70 SEKGIANDHTVILYGGNNNWFASYAYWYFKLYGHDNVKLLDGGRKKWELDARELVAGDevPERPKTDYKAKAQDTSIRAf 149
Cdd:PRK11493 80 RELGVNQDKHLVVYDEGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGA--VELPEGEFNAAFNPEAVVR- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 150 RDDVVAAI--GSQNLVDVRSPDEFSGKLLAPahlpqeqsqRPG----HVPSARNIPWSKNANDdGTFKSDEELKELYAAE 223
Cdd:PRK11493 157 LTDVLLASheKTAQIVDARPAARFNAEVDEP---------RPGlrrgHIPGALNVPWTELVRE-GELKTTDELDAIFFGR 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1892868620 224 SVDLAKDTIAYCRIGERSALTWFVLhELLGVENVKNYDGSWTEYGSLVGVPIELGA 279
Cdd:PRK11493 227 GVSFDRPIIASCGSGVTAAVVVLAL-ATLDVPNVKLYDGAWSEWGARADLPVEPAK 281
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
1-276 |
2.19e-30 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 116.05 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 1 MSRSDVLVDADWLQEHLDDPTIAIVevdeDTSAYEKNHIRNAIR--------------IDWTQDLQDPVRRDFVDQEGFE 66
Cdd:PLN02723 17 ISTNEPVVSVDWLHANLREPDVKVL----DASWYMPDEQRNPIQeyqvahipgalffdLDGISDRTTDLPHMLPSEEAFA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 67 KLLSEKGIANDHTVILYGGNNNWFASYAYWYFKLYGHDNVKLLDGGRKKWE---LDARELVAGD---------EVPER-- 132
Cdd:PLN02723 93 AAVSALGIENKDGVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRasgYDVESSASGDailkasaasEAIEKvy 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 133 -----PKTDYKAKAQDT---SIRAFRDDVVAAigSQNLVDVRSPDEFSGklLAPAhlPQEqSQRPGHVPSARNIPWSKNA 204
Cdd:PLN02723 173 qgqtvSPITFQTKFQPHlvwTLEQVKKNIEDK--TYQHIDARSKARFDG--AAPE--PRK-GIRSGHIPGSKCVPFPQML 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1892868620 205 NDDGTFKSDEELKELYAAESVDLAKDTIAYCRIGERSALTWFVLHElLGVENVKNYDGSWTEYGSLVGVPIE 276
Cdd:PLN02723 246 DSSQTLLPAEELKKRFEQEGISLDSPIVASCGTGVTACILALGLHR-LGKTDVPVYDGSWTEWGALPDTPVA 316
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
6-277 |
8.13e-24 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 100.58 E-value: 8.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 6 VLVDADWLQEHLDDPTIAIVEVdEDTSAYEKNHIRNAIRID--WTQDLQDPVRRDFVDQEGFEKLLSEKGIANDHTVILY 83
Cdd:PRK09629 9 LVIEPNDLLERLDAPELILVDL-TSSARYEAGHIRGARFVDpkRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 84 GGNNNWFASYAYWYFKLYGHDNVKLLDGGRKKWEldARELVAGDEVPERPKTDYKAKAQDTSIrAFRDDVVAAIGSQNLV 163
Cdd:PRK09629 88 DDEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAWE--AQALPLSTDVPPVAGGPVTLTLHDEPT-ATREYLQSRLGAADLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 164 --DVRSPDEFSGKLLAPAhlpqeqsqRPGHVPSARNIPWSKNANDDGTFKSDEELKELYAAESVDLAKDTIAYCRIGERS 241
Cdd:PRK09629 165 iwDARAPTEYSGEKVVAA--------KGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRS 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1892868620 242 ALTWFVLhELLGVENVKNYDGSWTEYGSLVGVPIEL 277
Cdd:PRK09629 237 GFTYLVA-KALGYPRVKAYAGSWGEWGNHPDTPVEV 271
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
162-272 |
7.92e-19 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 79.43 E-value: 7.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 162 LVDVRSPDEFSGkllapahlpqeqsqrpGHVPSARNIPWSKNANDDGTFKSDEeLKELYAAESVDLAKDTIAYCRIGERS 241
Cdd:smart00450 7 LLDVRSPEEYEG----------------GHIPGAVNIPLSELLDRRGELDILE-FEELLKRLGLDKDKPVVVYCRSGNRS 69
|
90 100 110
....*....|....*....|....*....|.
gi 1892868620 242 ALTWFVLHElLGVENVKNYDGSWTEYGSLVG 272
Cdd:smart00450 70 AKAAWLLRE-LGFKNVYLLDGGYKEWSAAGP 99
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
18-122 |
1.06e-16 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 73.65 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 18 DDPTIAIVEVDEdTSAYEKNHIRNAIRIDWTQDLQdpvRRDFVDQEGFEKLLSEKGIANDHTVILYGGNNNWfASYAYWY 97
Cdd:smart00450 1 NDEKVVLLDVRS-PEEYEGGHIPGAVNIPLSELLD---RRGELDILEFEELLKRLGLDKDKPVVVYCRSGNR-SAKAAWL 75
|
90 100
....*....|....*....|....*
gi 1892868620 98 FKLYGHDNVKLLDGGRKKWELDARE 122
Cdd:smart00450 76 LRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
158-267 |
5.80e-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: 63.27 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 158 GSQNLVDVRSPDEFSGkllapahlpqeqsqrpGHVPSARNIPWSknandDGTFKSDEELKELYAAESVDLAKDTIAYCRI 237
Cdd:pfam00581 4 GKVVLIDVRPPEEYAK----------------GHIPGAVNVPLS-----SLSLPPLPLLELLEKLLELLKDKPIVVYCNS 62
|
90 100 110
....*....|....*....|....*....|
gi 1892868620 238 GERSALTWFvLHELLGVENVKNYDGSWTEY 267
Cdd:pfam00581 63 GNRAAAAAA-LLKALGYKNVYVLDGGFEAW 91
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
17-116 |
7.33e-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: 62.89 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 17 LDDPTIAIVEVDEDtSAYEKNHIRNAIRIDWTQDlqdpvrrDFVDQEGFEKLLSEKGIANDHTVILYGGNNNWfASYAYW 96
Cdd:pfam00581 1 LEDGKVVLIDVRPP-EEYAKGHIPGAVNVPLSSL-------SLPPLPLLELLEKLLELLKDKPIVVYCNSGNR-AAAAAA 71
|
90 100
....*....|....*....|
gi 1892868620 97 YFKLYGHDNVKLLDGGRKKW 116
Cdd:pfam00581 72 LLKALGYKNVYVLDGGFEAW 91
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
162-267 |
8.99e-13 |
|
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: 63.06 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 162 LVDVRSPDEFsgkllapahlpqeqsqRPGHVPSARNIPWSKNanDDGTFKSDEELKELYAAESVDLAKDTIAYCRIGERS 241
Cdd:cd01519 18 LIDVREPEEL----------------KTGKIPGAINIPLSSL--PDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVRS 79
|
90 100
....*....|....*....|....*.
gi 1892868620 242 aLTWFVLHELLGVENVKNYDGSWTEY 267
Cdd:cd01519 80 -KAAAELARSLGYENVGNYPGSWLDW 104
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
8-116 |
1.37e-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: 60.34 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 8 VDADWLQEHLDDPTIAIV----------EVDEDTSAYEKNHIRNAIRIDWTQDLQDPVRrdFVDQEGFEKLLSEKGIAND 77
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVdarsperfrgEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGT--FKSPEELRALFAALGITPD 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1892868620 78 HTVILYGGNNNWfASYAYWYFKLYGHDNVKLLDGGRKKW 116
Cdd:cd01449 79 KPVIVYCGSGVT-ACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
162-262 |
7.26e-10 |
|
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.
Pssm-ID: 238089 [Multi-domain] Cd Length: 89 Bit Score: 54.61 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 162 LVDVRSPDEFSGkllapahlpqeqsqrpGHVPSARNIPWSknanddgtfksdeELKELYAAESVDLAKDTIAYCRIGERS 241
Cdd:cd00158 13 LLDVREPEEYAA----------------GHIPGAINIPLS-------------ELEERAALLELDKDKPIVVYCRSGNRS 63
|
90 100
....*....|....*....|.
gi 1892868620 242 ALTWFVLHElLGVENVKNYDG 262
Cdd:cd00158 64 ARAAKLLRK-AGGTNVYNLEG 83
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
151-268 |
8.88e-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: 54.97 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 151 DDVVAAIGSQN--LVDVRSPDEFsgkllapahlpqeqsqRPGHVPSARNIPWSknanddgtfksdeELKElyAAESVDLA 228
Cdd:COG0607 9 AELAELLESEDavLLDVREPEEF----------------AAGHIPGAINIPLG-------------ELAE--RLDELPKD 57
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1892868620 229 KDTIAYCRIGERSALTWFVLHElLGVENVKNYDG---SWTEYG 268
Cdd:COG0607 58 KPIVVYCASGGRSAQAAALLRR-AGYTNVYNLAGgieAWKAAG 99
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
7-116 |
3.39e-06 |
|
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: 45.55 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 7 LVDADWLQEHLDDPTIAIVEV--DEDTSAYEKNHIRNAIRIDWTQ--DLQDPVRRDFVDQEGFEKLLSEKGIANDHTVIL 82
Cdd:cd01445 21 LLDARAQSPGTREARGEYLETqpEPDAVGLDSGHIPGASFFDFEEclDEAGFEESMEPSEAEFAAMFEAKGIDLDKHLIA 100
|
90 100 110
....*....|....*....|....*....|....*.
gi 1892868620 83 YGGNN--NWFASYAYWYFKLYGHDNVKLLDGGRKKW 116
Cdd:cd01445 101 TDGDDlgGFTACHIALAARLCGHPDVAILDGGFFEW 136
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
8-127 |
7.00e-06 |
|
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: 43.80 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 8 VDADWLQEHLDDPTIAIVEVDEDtSAYEKNHIRNAIRIDWTQdlqdpvrrdfvdqegFEKLLSEkgIANDHTVILY--GG 85
Cdd:COG0607 6 ISPAELAELLESEDAVLLDVREP-EEFAAGHIPGAINIPLGE---------------LAERLDE--LPKDKPIVVYcaSG 67
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1892868620 86 NNnwfASYAYWYFKLYGHDNVKLLDGGRKKWELDARELVAGD 127
Cdd:COG0607 68 GR---SAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
119-262 |
1.09e-04 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 42.94 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 119 DARELVAGDEVPERPKTDYKAKAQDTSIRAFRDDVvaaigsqNLVDVRSPDEFSGkllapahlpqeqsqrpGHVPSARNI 198
Cdd:PRK05597 241 AVLERVRGSTPVHGISGGFGEVLDVPRVSALPDGV-------TLIDVREPSEFAA----------------YSIPGAHNV 297
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1892868620 199 PWSknanddgtfksdeELKELYAAESVDLAKDTIAYCRIGERSALTWFVLHElLGVENVKNYDG 262
Cdd:PRK05597 298 PLS-------------AIREGANPPSVSAGDEVVVYCAAGVRSAQAVAILER-AGYTGMSSLDG 347
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
13-117 |
2.48e-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: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 13 LQEHLDDPTIAIVEVDEDtSAYEKNHIRNAIRIDWTQdlqdpvrrdfvdqegFEKLLSEKGIANDHTVILYGgNNNWFAS 92
Cdd:cd00158 2 LKELLDDEDAVLLDVREP-EEYAAGHIPGAINIPLSE---------------LEERAALLELDKDKPIVVYC-RSGNRSA 64
|
90 100
....*....|....*....|....*
gi 1892868620 93 YAYWYFKLYGHDNVKLLDGGRKKWE 117
Cdd:cd00158 65 RAAKLLRKAGGTNVYNLEGGMLAWK 89
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
151-268 |
4.67e-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: 35.86 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892868620 151 DDVVAAIGSQN--LVDVRSPDEFsgkllapahlpqeqsQRPGHVPSARNIPWSKNAnddgtFKSDEElkELYAAESVDLA 228
Cdd:cd01447 4 EDARALLGSPGvlLVDVRDPREL---------------ERTGMIPGAFHAPRGMLE-----FWADPD--SPYHKPAFAED 61
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1892868620 229 KDTIAYCRIGERSALTWFVLHElLGVENVKNYDG---SWTEYG 268
Cdd:cd01447 62 KPFVFYCASGWRSALAGKTLQD-MGLKPVYNIEGgfkDWKEAG 103
|
|
| |
