|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
27-279 |
1.43e-111 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 323.28 E-value: 1.43e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 27 PSLRVLDASWYSPGtrqARKEYQERHVPGASFFDIEEC-RDTTSPYEMMLPSEAHFGDYVGNLGISNDTHVVVYDgdDLG 105
Cdd:COG2897 8 PDVVILDVRWDLPD---GRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYD--DGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 106 SFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLNLSLLKTYEQVLENLQSKRFQLVDSRAQ 185
Cdd:COG2897 83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALGDPDAVLVDARSP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 186 GRYLGTQPEPDIVGldsGHIRGSVNMPFMDFLTKDGFEKSPEELRAIFQDKKVDLSQPLIATCRKGVTACHVALAAYLCG 265
Cdd:COG2897 163 ERYRGEVEPIDPRA---GHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALELLG 239
|
250
....*....|....
gi 1729962 266 KPDVAVYDGSWSEW 279
Cdd:COG2897 240 YPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
9-279 |
8.54e-89 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 267.44 E-value: 8.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 9 ALVSTKWLAESIRSgrlgPSLRVLDASWYSPG-TRQARKEYQERHVPGASFFDIEECRDTTSPYEMMLPSEAHFGDYVGN 87
Cdd:PLN02723 22 PVVSVDWLHANLRE----PDVKVLDASWYMPDeQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 88 LGISNDTHVVVYDGDdlGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPE------------------ 149
Cdd:PLN02723 98 LGIENKDGVVVYDGK--GIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAilkasaaseaiekvyqgq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 150 ---PAVFKATLNLSLLKTYEQVLENLQSKRFQLVDSRAQGRYLGTQPEPDiVGLDSGHIRGSVNMPFMDFLTKDGFEKSP 226
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPR-KGIRSGHIPGSKCVPFPQMLDSSQTLLPA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1729962 227 EELRAIFQDKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:PLN02723 255 EELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
11-136 |
2.60e-63 |
|
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: 196.17 E-value: 2.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 11 VSTKWLAESIRSGRLGPSLRVLDASWYSPGTRQARKEYQE------------RHVPGASFFDIEECRDTTSPYEMMLPSE 78
Cdd:cd01445 1 KSTEQLAENLEAGKVGKGFQLLDARAQSPGTREARGEYLEtqpepdavgldsGHIPGASFFDFEECLDEAGFEESMEPSE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729962 79 AHFGDYVGNLGISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLK 136
Cdd:cd01445 81 AEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
173-285 |
6.36e-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: 77.11 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 173 QSKRFQLVDSRAQGRYLGtqpepdivgldsGHIRGSVNMPFMDFLTKDGfEKSPEELRAIFQDKKVDLSQPLIATCRKGV 252
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG------------GHIPGAVNIPLSELLDRRG-ELDILEFEELLKRLGLDKDKPVVVYCRSGN 67
|
90 100 110
....*....|....*....|....*....|...
gi 1729962 253 TACHVALAAYLCGKPDVAVYDGSWSEWFRRAPP 285
Cdd:smart00450 68 RSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
172-279 |
1.43e-14 |
|
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: 67.89 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 172 LQSKRFQLVDSRAQGRYlgtqpepdivglDSGHIRGSVNMPFMDF-LTKDGFEKSPEELRAIFQDKKVdlsqplIATCRK 250
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEY------------AKGHIPGAVNVPLSSLsLPPLPLLELLEKLLELLKDKPI------VVYCNS 62
|
90 100
....*....|....*....|....*....
gi 1729962 251 GVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:pfam00581 63 GNRAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
27-279 |
1.43e-111 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 323.28 E-value: 1.43e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 27 PSLRVLDASWYSPGtrqARKEYQERHVPGASFFDIEEC-RDTTSPYEMMLPSEAHFGDYVGNLGISNDTHVVVYDgdDLG 105
Cdd:COG2897 8 PDVVILDVRWDLPD---GRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYD--DGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 106 SFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLNLSLLKTYEQVLENLQSKRFQLVDSRAQ 185
Cdd:COG2897 83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALGDPDAVLVDARSP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 186 GRYLGTQPEPDIVGldsGHIRGSVNMPFMDFLTKDGFEKSPEELRAIFQDKKVDLSQPLIATCRKGVTACHVALAAYLCG 265
Cdd:COG2897 163 ERYRGEVEPIDPRA---GHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALELLG 239
|
250
....*....|....
gi 1729962 266 KPDVAVYDGSWSEW 279
Cdd:COG2897 240 YPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
9-279 |
8.54e-89 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 267.44 E-value: 8.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 9 ALVSTKWLAESIRSgrlgPSLRVLDASWYSPG-TRQARKEYQERHVPGASFFDIEECRDTTSPYEMMLPSEAHFGDYVGN 87
Cdd:PLN02723 22 PVVSVDWLHANLRE----PDVKVLDASWYMPDeQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 88 LGISNDTHVVVYDGDdlGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPE------------------ 149
Cdd:PLN02723 98 LGIENKDGVVVYDGK--GIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAilkasaaseaiekvyqgq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 150 ---PAVFKATLNLSLLKTYEQVLENLQSKRFQLVDSRAQGRYLGTQPEPDiVGLDSGHIRGSVNMPFMDFLTKDGFEKSP 226
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPR-KGIRSGHIPGSKCVPFPQMLDSSQTLLPA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1729962 227 EELRAIFQDKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:PLN02723 255 EELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
11-283 |
1.36e-79 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 242.69 E-value: 1.36e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 11 VSTKWLAESIRSgrlgPSLRVLDASWYSPG--TRQARKEYQERHVPGASFFDIEECRDTTSPYEMMLPSEAHFGDYVGNL 88
Cdd:PRK11493 7 VAADWLAEHIDD----PEIQIIDARMAPPGqeDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 89 GISNDTHVVVYDGDDLgsFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLNLSLLKTYEQV 168
Cdd:PRK11493 83 GVNQDKHLVVYDEGNL--FSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 169 LENLQSKRFQLVDSRAQGRYLGTQPEPDiVGLDSGHIRGSVNMPFMDfLTKDGFEKSPEELRAIFQDKKVDLSQPLIATC 248
Cdd:PRK11493 161 LLASHEKTAQIVDARPAARFNAEVDEPR-PGLRRGHIPGALNVPWTE-LVREGELKTTDELDAIFFGRGVSFDRPIIASC 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1729962 249 RKGVTACHVALAAYLCGKPDVAVYDGSWSEWFRRA 283
Cdd:PRK11493 239 GSGVTAAVVVLALATLDVPNVKLYDGAWSEWGARA 273
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
11-136 |
2.60e-63 |
|
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: 196.17 E-value: 2.60e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 11 VSTKWLAESIRSGRLGPSLRVLDASWYSPGTRQARKEYQE------------RHVPGASFFDIEECRDTTSPYEMMLPSE 78
Cdd:cd01445 1 KSTEQLAENLEAGKVGKGFQLLDARAQSPGTREARGEYLEtqpepdavgldsGHIPGASFFDFEECLDEAGFEESMEPSE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729962 79 AHFGDYVGNLGISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLK 136
Cdd:cd01445 81 AEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
10-138 |
1.54e-54 |
|
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: 173.19 E-value: 1.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 10 LVSTKWLAESIRsgrlGPSLRVLDASWYSPGtRQARKEYQERHVPGASFFDIEECRDTTSPYEMMLPSEAHFGDYVGNLG 89
Cdd:cd01448 1 LVSPDWLAEHLD----DPDVRILDARWYLPD-RDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSLG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1729962 90 ISNDTHVVVYdgDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEG 138
Cdd:cd01448 76 ISNDDTVVVY--DDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
163-281 |
2.44e-54 |
|
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: 172.43 E-value: 2.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 163 KTYEQVLENLQSKRFQLVDSRAQGRYLGTQPEPDiVGLDSGHIRGSVNMPFMDFLTKDGFEKSPEELRAIFQDKKVDLSQ 242
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPR-PGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDK 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1729962 243 PLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFR 281
Cdd:cd01449 80 PVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
163-281 |
4.34e-51 |
|
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: 164.96 E-value: 4.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 163 KTYEQVLENLQ----SKRFQLVDSRAQ--------GRYLGTQPEPDIVGLDSGHIRGSVNMPFMDFLTKDGFEKSPE--- 227
Cdd:cd01445 1 KSTEQLAENLEagkvGKGFQLLDARAQspgtrearGEYLETQPEPDAVGLDSGHIPGASFFDFEECLDEAGFEESMEpse 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1729962 228 -ELRAIFQDKKVDLSQPLIATCRK---GVTACHVALAAYLCGKPDVAVYDGSWSEWFR 281
Cdd:cd01445 81 aEFAAMFEAKGIDLDKHLIATDGDdlgGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
41-289 |
1.56e-20 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 91.33 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 41 TRQARkeYQERHVPGASFFDIEECRDTTSPYEMMLPSEAHFGDYVGNLGISNDTHVVVYDgdDLGSFYAPRVWWMFRVFG 120
Cdd:PRK09629 31 TSSAR--YEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVYD--DEGGGWAGRFIWLLDVIG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 121 HRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAVFKATLNLSLLKTYEQVLENLQSKRFQLVDSRAQGRYLGTQpepdIVGL 200
Cdd:PRK09629 107 HSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQSRLGAADLAIWDARAPTEYSGEK----VVAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 201 DSGHIRGSVNMPFMDFLTKDGFEKSPEELRAIFQDKKVDLSQPLIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWF 280
Cdd:PRK09629 183 KGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYPRVKAYAGSWGEWG 262
|
....*....
gi 1729962 281 RRapPETRV 289
Cdd:PRK09629 263 NH--PDTPV 269
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
173-285 |
6.36e-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: 77.11 E-value: 6.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 173 QSKRFQLVDSRAQGRYLGtqpepdivgldsGHIRGSVNMPFMDFLTKDGfEKSPEELRAIFQDKKVDLSQPLIATCRKGV 252
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG------------GHIPGAVNIPLSELLDRRG-ELDILEFEELLKRLGLDKDKPVVVYCRSGN 67
|
90 100 110
....*....|....*....|....*....|...
gi 1729962 253 TACHVALAAYLCGKPDVAVYDGSWSEWFRRAPP 285
Cdd:smart00450 68 RSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
26-140 |
4.88e-17 |
|
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: 74.80 E-value: 4.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 26 GPSLRVLDASWyspgtrqaRKEYQERHVPGASFFDIEECRDTTSPYEMMlpseaHFGDYVGNLGISNDTHVVVYDGddlG 105
Cdd:smart00450 2 DEKVVLLDVRS--------PEEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCR---S 65
|
90 100 110
....*....|....*....|....*....|....*
gi 1729962 106 SFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHP 140
Cdd:smart00450 66 GNRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
172-279 |
1.43e-14 |
|
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: 67.89 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 172 LQSKRFQLVDSRAQGRYlgtqpepdivglDSGHIRGSVNMPFMDF-LTKDGFEKSPEELRAIFQDKKVdlsqplIATCRK 250
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEY------------AKGHIPGAVNVPLSSLsLPPLPLLELLEKLLELLKDKPI------VVYCNS 62
|
90 100
....*....|....*....|....*....
gi 1729962 251 GVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:pfam00581 63 GNRAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
47-134 |
1.76e-10 |
|
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: 56.72 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 47 EYQERHVPGASFFDIEECRDTTSPyemMLPSEAHFgdyvgnLGISNDTHVVVYDGDDLGSfyaPRVWWMFRVFGHRTVSV 126
Cdd:pfam00581 16 EYAKGHIPGAVNVPLSSLSLPPLP---LLELLEKL------LELLKDKPIVVYCNSGNRA---AAAAALLKALGYKNVYV 83
|
....*...
gi 1729962 127 LNGGFRNW 134
Cdd:pfam00581 84 LDGGFEAW 91
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
193-279 |
3.11e-09 |
|
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: 53.43 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 193 PEPDIVGLD--------SGHIRGSVNMPFMDFltKDGFEKSPEELRAIFQDKKVDLSQPLIATCRKGV---TACHVALAA 261
Cdd:cd01519 12 PHPNKVLIDvrepeelkTGKIPGAINIPLSSL--PDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVrskAAAELARSL 89
|
90
....*....|....*...
gi 1729962 262 ylcGKPDVAVYDGSWSEW 279
Cdd:cd01519 90 ---GYENVGNYPGSWLDW 104
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
167-279 |
3.96e-09 |
|
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: 52.69 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 167 QVLENLQSKRFQLVDSRAQGRYlgtqpepdivglDSGHIRGSVNMPFMDFLTKDGFEKSPeelraifQDKKVdlsqplIA 246
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEY------------AAGHIPGAINIPLSELEERAALLELD-------KDKPI------VV 55
|
90 100 110
....*....|....*....|....*....|...
gi 1729962 247 TCRKGVTACHVALAAYLCGKPDVAVYDGSWSEW 279
Cdd:cd00158 56 YCRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
164-288 |
1.79e-08 |
|
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: 51.51 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 164 TYEQVLENLQSKRFQLVDSRAQGRYlgtqpepdivglDSGHIRGSVNMPFMDFltkdgfeksPEELRAIFQDKkvdlsqP 243
Cdd:COG0607 7 SPAELAELLESEDAVLLDVREPEEF------------AAGHIPGAINIPLGEL---------AERLDELPKDK------P 59
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1729962 244 LIATCRKGVTACHVALAAYLCGKPDVAVYDGSWSEWFRRAPPETR 288
Cdd:COG0607 60 IVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEK 104
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
45-134 |
8.65e-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: 37.66 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 45 RKEYQERHVPGASFFDIEEcrdttspyemmLPSEAHFgdyvgnLGISNDTHVVVYDGDDLGSfyaPRVWWMFRVFGHRTV 124
Cdd:cd00158 19 PEEYAAGHIPGAINIPLSE-----------LEERAAL------LELDKDKPIVVYCRSGNRS---ARAAKLLRKAGGTNV 78
|
90
....*....|
gi 1729962 125 SVLNGGFRNW 134
Cdd:cd00158 79 YNLEGGMLAW 88
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
47-143 |
2.40e-03 |
|
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: 36.87 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 47 EYQERHVPGASFFDIEEcrdttspyemmLPSEAHfgdyvgnlGISNDTHVVVYDGDDLGSFYAPRvwwMFRVFGHRTVSV 126
Cdd:COG0607 30 EFAAGHIPGAINIPLGE-----------LAERLD--------ELPKDKPIVVYCASGGRSAQAAA---LLRRAGYTNVYN 87
|
90
....*....|....*..
gi 1729962 127 LNGGFRNWLKEGHPVTS 143
Cdd:COG0607 88 LAGGIEAWKAAGLPVEK 104
|
|
| Cdc25_Acr2p |
cd01443 |
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ... |
175-281 |
2.46e-03 |
|
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).
Pssm-ID: 238720 [Multi-domain] Cd Length: 113 Bit Score: 37.00 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729962 175 KRFQLVDSRaqgrylgtqpEPDivgLDSGHIRGSVNMPFMDFLtkdgfEKSPEELRAIFQDKKVDlsqpLIATC----RK 250
Cdd:cd01443 22 KDFVVVDLR----------RDD---YEGGHIKGSINLPAQSCY-----QTLPQVYALFSLAGVKL----AIFYCgssqGR 79
|
90 100 110
....*....|....*....|....*....|....*
gi 1729962 251 GVTACHvALAAYL--CGKPDVAVY--DGSWSEWFR 281
Cdd:cd01443 80 GPRAAR-WFADYLrkVGESLPKSYilTGGIKAWYH 113
|
|
| |
