|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
11-281 |
5.67e-90 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 267.81 E-value: 5.67e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 11 LAAHLSDPKLVILDASMDKVIGREpiVYDEpCFIAGARRLDLERECTDLQSSELHALPSQAQFTELVQRLGIDQDSTVVI 90
Cdd:COG2897 1 LAAHLDDPDVVILDVRWDLPDGRA--AYEA-GHIPGAVFLDLDTDLSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 91 YDNQGIYSSPRGWWCFKVMGFEQVFVLDGGLPKWLKEQRLCADKPATeFPRGNACGQYQAEKVCNALQVLDTLAGKQAMI 170
Cdd:COG2897 78 YDDGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPT-PAPGDFTARPDPELLADADEVLAALGDPDAVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 171 LDARASSRFLGQSpEPReGVRSGHIPGAVNLPFAEVLDGDS-LKPQPALEQIFLHLGAmdarRSGKPLIFSCGSGITACI 249
Cdd:COG2897 157 VDARSPERYRGEV-EPI-DPRAGHIPGAVNLPWTDLLDEDGtFKSAEELRALFAALGI----DPDKPVITYCGSGVRAAH 230
|
250 260 270
....*....|....*....|....*....|..
gi 1372234456 250 LILAAYQVRLDALILYDGSWADWGSKAHLPLA 281
Cdd:COG2897 231 TWLALELLGYPNVRLYDGSWSEWGSDPDLPVE 262
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
1-283 |
4.60e-67 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 211.58 E-value: 4.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 1 MQSALVSSEWLAAHLSDPKLVILDAS--MdKVIGREPIVYDEPCFIAGARRLDLEReCTDLQSSELHALPSQAQFTELVQ 78
Cdd:PLN02723 19 TNEPVVSVDWLHANLREPDVKVLDASwyM-PDEQRNPIQEYQVAHIPGALFFDLDG-ISDRTTDLPHMLPSEEAFAAAVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 79 RLGIDQDSTVVIYDNQGIYSSPRGWWCFKVMGFEQVFVLDGGLPKWLK-----EQRLCAD-----KPATEFPRGNACGQ- 147
Cdd:PLN02723 97 ALGIENKDGVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRAsgydvESSASGDailkaSAASEAIEKVYQGQt 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 148 ---------YQAEKVCNALQVLDTLAGKQAMILDARASSRFLGQSPEPREGVRSGHIPGAVNLPFAEVLDGD-SLKPQPA 217
Cdd:PLN02723 177 vspitfqtkFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSqTLLPAEE 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372234456 218 LEQIFLHLG-AMDarrsgKPLIFSCGSGITACILILAAYQVRLDALILYDGSWADWGSKAHLPLATS 283
Cdd:PLN02723 257 LKKRFEQEGiSLD-----SPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEWGALPDTPVATS 318
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
5-127 |
9.06e-46 |
|
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: 150.08 E-value: 9.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 5 LVSSEWLAAHLSDPKLVILDASMDKVIGREPIVYDEPCfIAGARRLDLErECTDLQSSELHALPSQAQFTELVQRLGIDQ 84
Cdd:cd01448 1 LVSPDWLAEHLDDPDVRILDARWYLPDRDGRKEYLEGH-IPGAVFFDLD-EDLDDKSPGPHMLPSPEEFAELLGSLGISN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1372234456 85 DSTVVIYDNQGIYSSPRGWWCFKVMGFEQVFVLDGGLPKWLKE 127
Cdd:cd01448 79 DDTVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAE 121
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
16-127 |
5.09e-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: 66.33 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 16 SDPKLVILDAsmdkvigREPIVYDEpCFIAGARRLDLEREctdlqsSELHALPSQAQFTELVQRLGIDQDSTVVIYDNQG 95
Cdd:smart00450 1 NDEKVVLLDV-------RSPEEYEG-GHIPGAVNIPLSEL------LDRRGELDILEFEELLKRLGLDKDKPVVVYCRSG 66
|
90 100 110
....*....|....*....|....*....|..
gi 1372234456 96 iYSSPRGWWCFKVMGFEQVFVLDGGLPKWLKE 127
Cdd:smart00450 67 -NRSAKAAWLLRELGFKNVYLLDGGYKEWSAA 97
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
15-124 |
2.07e-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: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 15 LSDPKLVILDAsmdkvigREPIVYDEpCFIAGARRLDLERECtdlqsseLHALPSQAQFTELVQRLGidqDSTVVIYDNQ 94
Cdd:pfam00581 1 LEDGKVVLIDV-------RPPEEYAK-GHIPGAVNVPLSSLS-------LPPLPLLELLEKLLELLK---DKPIVVYCNS 62
|
90 100 110
....*....|....*....|....*....|
gi 1372234456 95 GIySSPRGWWCFKVMGFEQVFVLDGGLPKW 124
Cdd:pfam00581 63 GN-RAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
11-281 |
5.67e-90 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 267.81 E-value: 5.67e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 11 LAAHLSDPKLVILDASMDKVIGREpiVYDEpCFIAGARRLDLERECTDLQSSELHALPSQAQFTELVQRLGIDQDSTVVI 90
Cdd:COG2897 1 LAAHLDDPDVVILDVRWDLPDGRA--AYEA-GHIPGAVFLDLDTDLSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 91 YDNQGIYSSPRGWWCFKVMGFEQVFVLDGGLPKWLKEQRLCADKPATeFPRGNACGQYQAEKVCNALQVLDTLAGKQAMI 170
Cdd:COG2897 78 YDDGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPT-PAPGDFTARPDPELLADADEVLAALGDPDAVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 171 LDARASSRFLGQSpEPReGVRSGHIPGAVNLPFAEVLDGDS-LKPQPALEQIFLHLGAmdarRSGKPLIFSCGSGITACI 249
Cdd:COG2897 157 VDARSPERYRGEV-EPI-DPRAGHIPGAVNLPWTDLLDEDGtFKSAEELRALFAALGI----DPDKPVITYCGSGVRAAH 230
|
250 260 270
....*....|....*....|....*....|..
gi 1372234456 250 LILAAYQVRLDALILYDGSWADWGSKAHLPLA 281
Cdd:COG2897 231 TWLALELLGYPNVRLYDGSWSEWGSDPDLPVE 262
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
1-283 |
4.60e-67 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 211.58 E-value: 4.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 1 MQSALVSSEWLAAHLSDPKLVILDAS--MdKVIGREPIVYDEPCFIAGARRLDLEReCTDLQSSELHALPSQAQFTELVQ 78
Cdd:PLN02723 19 TNEPVVSVDWLHANLREPDVKVLDASwyM-PDEQRNPIQEYQVAHIPGALFFDLDG-ISDRTTDLPHMLPSEEAFAAAVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 79 RLGIDQDSTVVIYDNQGIYSSPRGWWCFKVMGFEQVFVLDGGLPKWLK-----EQRLCAD-----KPATEFPRGNACGQ- 147
Cdd:PLN02723 97 ALGIENKDGVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRAsgydvESSASGDailkaSAASEAIEKVYQGQt 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 148 ---------YQAEKVCNALQVLDTLAGKQAMILDARASSRFLGQSPEPREGVRSGHIPGAVNLPFAEVLDGD-SLKPQPA 217
Cdd:PLN02723 177 vspitfqtkFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSqTLLPAEE 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1372234456 218 LEQIFLHLG-AMDarrsgKPLIFSCGSGITACILILAAYQVRLDALILYDGSWADWGSKAHLPLATS 283
Cdd:PLN02723 257 LKKRFEQEGiSLD-----SPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEWGALPDTPVATS 318
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
3-282 |
3.07e-64 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 203.02 E-value: 3.07e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 3 SALVSSEWLAAHLSDPKLVILDASMDKVIGREPIVYDE--PCFIAGARRLDLErECTDLQSSELHALPSQAQFTELVQRL 80
Cdd:PRK11493 4 TWFVAADWLAEHIDDPEIQIIDARMAPPGQEDRDVAAEyrAGHIPGAVFFDIE-ALSDHTSPLPHMMPRPETFAVAMREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 81 GIDQDSTVVIYDNQGIYSSPRGWWCFKVMGFEQVFVLDGGLPKWlKEQRLCADKPATEFPRGNACGQYQAEKVCNALQVL 160
Cdd:PRK11493 83 GVNQDKHLVVYDEGNLFSAPRAWWMLRTFGVEKVSILAGGLAGW-QRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 161 DTLAGKQAMILDARASSRFLGQSPEPREGVRSGHIPGAVNLPFAEVLDGDSLKPQPALEQIFLHLGAMDARrsgkPLIFS 240
Cdd:PRK11493 162 LASHEKTAQIVDARPAARFNAEVDEPRPGLRRGHIPGALNVPWTELVREGELKTTDELDAIFFGRGVSFDR----PIIAS 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1372234456 241 CGSGITACILILAAYQVRLDALILYDGSWADWGSKAHLPLAT 282
Cdd:PRK11493 238 CGSGVTAAVVVLALATLDVPNVKLYDGAWSEWGARADLPVEP 279
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
5-127 |
9.06e-46 |
|
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: 150.08 E-value: 9.06e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 5 LVSSEWLAAHLSDPKLVILDASMDKVIGREPIVYDEPCfIAGARRLDLErECTDLQSSELHALPSQAQFTELVQRLGIDQ 84
Cdd:cd01448 1 LVSPDWLAEHLDDPDVRILDARWYLPDRDGRKEYLEGH-IPGAVFFDLD-EDLDDKSPGPHMLPSPEEFAELLGSLGISN 78
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1372234456 85 DSTVVIYDNQGIYSSPRGWWCFKVMGFEQVFVLDGGLPKWLKE 127
Cdd:cd01448 79 DDTVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAE 121
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
158-274 |
4.69e-42 |
|
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: 140.46 E-value: 4.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 158 QVLDTLAGKQAMILDARASSRFLGQSPEPREGVRSGHIPGAVNLPFAEVLDGDS-LKPQPALEQIFLHLGAMdarrSGKP 236
Cdd:cd01449 5 EVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGtFKSPEELRALFAALGIT----PDKP 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1372234456 237 LIFSCGSGITACILILAAYQVRLDALILYDGSWADWGS 274
Cdd:cd01449 81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
16-127 |
5.09e-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: 66.33 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 16 SDPKLVILDAsmdkvigREPIVYDEpCFIAGARRLDLEREctdlqsSELHALPSQAQFTELVQRLGIDQDSTVVIYDNQG 95
Cdd:smart00450 1 NDEKVVLLDV-------RSPEEYEG-GHIPGAVNIPLSEL------LDRRGELDILEFEELLKRLGLDKDKPVVVYCRSG 66
|
90 100 110
....*....|....*....|....*....|..
gi 1372234456 96 iYSSPRGWWCFKVMGFEQVFVLDGGLPKWLKE 127
Cdd:smart00450 67 -NRSAKAAWLLRELGFKNVYLLDGGYKEWSAA 97
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
3-280 |
1.20e-13 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 70.53 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 3 SALVSSEWLAAHLSDPKLVILDASMDKVIgrepivydEPCFIAGARRLDLERecTDLQSSELHAL-PSQAQFTELVQRLG 81
Cdd:PRK09629 8 SLVIEPNDLLERLDAPELILVDLTSSARY--------EAGHIRGARFVDPKR--TQLGKPPAPGLlPDTADLEQLFGELG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 82 IDQDSTVVIYDNQGIYSSPRGWWCFKVMGFEQVFVLDGGLPKWlKEQRLCADKPATEFPRGNACGQYQAEKVCNALQVLD 161
Cdd:PRK09629 78 HNPDAVYVVYDDEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAW-EAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 162 TLAGKQAMILDARASSRFLGQSPEPREGvrsGHIPGAVNLPFAEVLD-GDSLKPQPALEQIFLHLGAMdarrSGKPLIFS 240
Cdd:PRK09629 157 RLGAADLAIWDARAPTEYSGEKVVAAKG---GHIPGAVNFEWTAGMDkARNLRIRQDMPEILRDLGIT----PDKEVITH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1372234456 241 CGSGITACILILAAYQVRLDALILYDGSWADWGSKAHLPL 280
Cdd:PRK09629 230 CQTHHRSGFTYLVAKALGYPRVKAYAGSWGEWGNHPDTPV 269
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
165-277 |
4.62e-13 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 64.02 E-value: 4.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 165 GKQAMILDARASSRFLGqspepregvrsGHIPGAVNLPFAEVLDGDSLKPQPALEQIFLHLGamdaRRSGKPLIFSCGSG 244
Cdd:smart00450 2 DEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELLDRRGELDILEFEELLKRLG----LDKDKPVVVYCRSG 66
|
90 100 110
....*....|....*....|....*....|...
gi 1372234456 245 ITACILILAAYQVRLDALILYDGSWADWGSKAH 277
Cdd:smart00450 67 NRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGP 99
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
6-126 |
6.86e-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: 64.43 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 6 VSSEWLAAHLSD----PKLVILDASMDKVIGREP------------IVYDEPCFIAGARRLDLErECTDLQSSELHALPS 69
Cdd:cd01445 1 KSTEQLAENLEAgkvgKGFQLLDARAQSPGTREArgeyletqpepdAVGLDSGHIPGASFFDFE-ECLDEAGFEESMEPS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1372234456 70 QAQFTELVQRLGIDQDSTVVIYD--NQGIYSSPRGWWCFKVMGFEQVFVLDGGLPKWLK 126
Cdd:cd01445 80 EAEFAAMFEAKGIDLDKHLIATDgdDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
149-272 |
9.09e-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: 64.04 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 149 QAEKVCNALQVLDTLAGKQAMildARASSRFLGQSPEPRE-GVRSGHIPGAVNLPFAEVLDGDSLK--PQPALEQIFLHL 225
Cdd:cd01445 11 EAGKVGKGFQLLDARAQSPGT---REARGEYLETQPEPDAvGLDSGHIPGASFFDFEECLDEAGFEesMEPSEAEFAAMF 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1372234456 226 GAMDARRSgKPLIFSCG---SGITACILILAAYQVRLDALILYDGSWADW 272
Cdd:cd01445 88 EAKGIDLD-KHLIATDGddlGGFTACHIALAARLCGHPDVAILDGGFFEW 136
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
15-124 |
2.07e-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: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 15 LSDPKLVILDAsmdkvigREPIVYDEpCFIAGARRLDLERECtdlqsseLHALPSQAQFTELVQRLGidqDSTVVIYDNQ 94
Cdd:pfam00581 1 LEDGKVVLIDV-------RPPEEYAK-GHIPGAVNVPLSSLS-------LPPLPLLELLEKLLELLK---DKPIVVYCNS 62
|
90 100 110
....*....|....*....|....*....|
gi 1372234456 95 GIySSPRGWWCFKVMGFEQVFVLDGGLPKW 124
Cdd:pfam00581 63 GN-RAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
163-272 |
8.72e-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: 51.72 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 163 LAGKQAMILDARASSRFLGqspepregvrsGHIPGAVNLPFAEvLDGDSLKPQPALEQIFlhlgamdARRSGKPLIFSCG 242
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAK-----------GHIPGAVNVPLSS-LSLPPLPLLELLEKLL-------ELLKDKPIVVYCN 61
|
90 100 110
....*....|....*....|....*....|
gi 1372234456 243 SGITACILILAAYQVRLDALILYDGSWADW 272
Cdd:pfam00581 62 SGNRAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
158-283 |
1.01e-07 |
|
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: 49.20 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 158 QVLDTLAGKQAMILDARassrflgqspEPREgVRSGHIPGAVNLPFAEVLDgdslkpqpaleqiflHLGAMDArrsGKPL 237
Cdd:COG0607 10 ELAELLESEDAVLLDVR----------EPEE-FAAGHIPGAINIPLGELAE---------------RLDELPK---DKPI 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1372234456 238 IFSCGSGITACILILAAYQVRLDALILYDGSWADWgSKAHLPLATS 283
Cdd:COG0607 61 VVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAW-KAAGLPVEKG 105
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
11-124 |
1.63e-07 |
|
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.
Pssm-ID: 238089 [Multi-domain] Cd Length: 89 Bit Score: 48.06 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 11 LAAHLSDPKLVILDAsmdkvigREPIVYDEpCFIAGARRLDLErectdlqsselhalpsqaQFTELVQRLGIDQDSTVVI 90
Cdd:cd00158 2 LKELLDDEDAVLLDV-------REPEEYAA-GHIPGAINIPLS------------------ELEERAALLELDKDKPIVV 55
|
90 100 110
....*....|....*....|....*....|....
gi 1372234456 91 YDNQGiYSSPRGWWCFKVMGFEQVFVLDGGLPKW 124
Cdd:cd00158 56 YCRSG-NRSARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
185-272 |
4.14e-07 |
|
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: 47.65 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 185 EPREgVRSGHIPGAVNLPFAEV-----LDGDSLK-----PQPALEqiflhlgamdarrsgKPLIFSCGSGITAciliLAA 254
Cdd:cd01519 23 EPEE-LKTGKIPGAINIPLSSLpdalaLSEEEFEkkygfPKPSKD---------------KELIFYCKAGVRS----KAA 82
|
90 100
....*....|....*....|..
gi 1372234456 255 YQVRLDA----LILYDGSWADW 272
Cdd:cd01519 83 AELARSLgyenVGNYPGSWLDW 104
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
158-272 |
6.22e-07 |
|
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.
Pssm-ID: 238089 [Multi-domain] Cd Length: 89 Bit Score: 46.52 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 158 QVLDTLAGKQAMILDARASSRFlgqspepregvRSGHIPGAVNLPFAEVLDGDSLKPQPaleqiflhlgamdarrSGKPL 237
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEY-----------AAGHIPGAINIPLSELEERAALLELD----------------KDKPI 53
|
90 100 110
....*....|....*....|....*....|....*....
gi 1372234456 238 IFSCGSG----ITACILILAAYQvrldALILYDGSWADW 272
Cdd:cd00158 54 VVYCRSGnrsaRAAKLLRKAGGT----NVYNLEGGMLAW 88
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
6-127 |
6.88e-07 |
|
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: 46.88 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 6 VSSEWLAAHLSDPKLVILDAsmdkvigREPIVYDEpCFIAGARRLDLErectdlqsselhalpsqaqftELVQRLG-IDQ 84
Cdd:COG0607 6 ISPAELAELLESEDAVLLDV-------REPEEFAA-GHIPGAINIPLG---------------------ELAERLDeLPK 56
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1372234456 85 DSTVVIYDNQGiYSSPRGWWCFKVMGFEQVFVLDGGLPKWLKE 127
Cdd:COG0607 57 DKPIVVYCASG-GRSAQAAALLRRAGYTNVYNLAGGIEAWKAA 98
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
6-124 |
2.08e-04 |
|
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: 39.92 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1372234456 6 VSSEWLAAHLSDPKLVILDA-SMDKVIG-REPIVYDEPC-FIAGARRLDLerecTDLQSSElHALPSQAQFTELVQRLGI 82
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDArSPERFRGeVPEPRPGLRSgHIPGAVNIPW----TSLLDED-GTFKSPEELRALFAALGI 75
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1372234456 83 DQDSTVVIYDNQGIYSSPRgWWCFKVMGFEQVFVLDGGLPKW 124
Cdd:cd01449 76 TPDKPVIVYCGSGVTACVL-LLALELLGYKNVRLYDGSWSEW 116
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
159-228 |
1.91e-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: 37.60 E-value: 1.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1372234456 159 VLDTLAGKQAMILDARASSrflgQSPEPREGVRSGHIPGAVNLPFAEVLDGDS--LKPQPALEQIFLHLGAM 228
Cdd:cd01448 7 LAEHLDDPDVRILDARWYL----PDRDGRKEYLEGHIPGAVFFDLDEDLDDKSpgPHMLPSPEEFAELLGSL 74
|
|
| |
