|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
26-278 |
1.81e-106 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 310.18 E-value: 1.81e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 26 PGLRVLDASWYSPGtreARKEYLERHVPGASFFDIEEC-RDKASPYEVMLPSEAGFADYVGSLGISNDTHVVVYDgdDLG 104
Cdd:COG2897 8 PDVVILDVRWDLPD---GRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYD--DGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 105 SFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAIFKATLNRSLLKTYEQVLENLESKRFQLVDSRAQ 184
Cdd:COG2897 83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALGDPDAVLVDARSP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 185 GRYLGTQPEPDAVGldsGHIRGSVNMPFMNFLTEDGFEKSPEELRAMFEAKKVDLTKPLIAT*RKGVTACHIALAAYLCG 264
Cdd:COG2897 163 ERYRGEVEPIDPRA---GHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALELLG 239
|
250
....*....|....
gi 12084448 265 KPDVAIYDGSWFEW 278
Cdd:COG2897 240 YPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
8-278 |
4.83e-85 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 257.81 E-value: 4.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 8 ALVSTKWLAESVRAgkvgPGLRVLDASWYSPG-TREARKEYLERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGS 86
Cdd:PLN02723 22 PVVSVDWLHANLRE----PDVKVLDASWYMPDeQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 87 LGISNDTHVVVYDGDdlGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPE------------------ 148
Cdd:PLN02723 98 LGIENKDGVVVYDGK--GIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAilkasaaseaiekvyqgq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 149 ---PAIFKATLNRSLLKTYEQVLENLESKRFQLVDSRAQGRYLGTQPEPDAvGLDSGHIRGSVNMPFMNFLTEDGFEKSP 225
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRK-GIRSGHIPGSKCVPFPQMLDSSQTLLPA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 12084448 226 EELRAMFEAKKVDLTKPLIAT*RKGVTACHIALAAYLCGKPDVAIYDGSWFEW 278
Cdd:PLN02723 255 EELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
10-135 |
6.61e-70 |
|
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: 212.73 E-value: 6.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 10 VSTKWLAESVRAGKVGPGLRVLDASWYSPGTREARKEYLE------------RHVPGASFFDIEECRDKASPYEVMLPSE 77
Cdd:cd01445 1 KSTEQLAENLEAGKVGKGFQLLDARAQSPGTREARGEYLEtqpepdavgldsGHIPGASFFDFEECLDEAGFEESMEPSE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 12084448 78 AGFADYVGSLGISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLK 135
Cdd:cd01445 81 AEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
25-139 |
8.90e-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: 76.73 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 25 GPGLRVLDASWyspgtreaRKEYLERHVPGASFFDIEECRDKASPYEVMLpseagFADYVGSLGISNDTHVVVYDGddlG 104
Cdd:smart00450 2 DEKVVLLDVRS--------PEEYEGGHIPGAVNIPLSELLDRRGELDILE-----FEELLKRLGLDKDKPVVVYCR---S 65
|
90 100 110
....*....|....*....|....*....|....*
gi 12084448 105 SFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHP 139
Cdd:smart00450 66 GNRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
171-278 |
2.32e-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: 59.03 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 171 LESKRFQLVDSRAQGRYlgtqpepdavglDSGHIRGSVNMPFMNF-LTEDGFEKSPEELRAMFEAKKVdltkplIAT*RK 249
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEY------------AKGHIPGAVNVPLSSLsLPPLPLLELLEKLLELLKDKPI------VVYCNS 62
|
90 100
....*....|....*....|....*....
gi 12084448 250 GVTACHIALAAYLCGKPDVAIYDGSWFEW 278
Cdd:pfam00581 63 GNRAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
26-278 |
1.81e-106 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 310.18 E-value: 1.81e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 26 PGLRVLDASWYSPGtreARKEYLERHVPGASFFDIEEC-RDKASPYEVMLPSEAGFADYVGSLGISNDTHVVVYDgdDLG 104
Cdd:COG2897 8 PDVVILDVRWDLPD---GRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISNDTTVVVYD--DGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 105 SFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAIFKATLNRSLLKTYEQVLENLESKRFQLVDSRAQ 184
Cdd:COG2897 83 GLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALGDPDAVLVDARSP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 185 GRYLGTQPEPDAVGldsGHIRGSVNMPFMNFLTEDGFEKSPEELRAMFEAKKVDLTKPLIAT*RKGVTACHIALAAYLCG 264
Cdd:COG2897 163 ERYRGEVEPIDPRA---GHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTWLALELLG 239
|
250
....*....|....
gi 12084448 265 KPDVAIYDGSWFEW 278
Cdd:COG2897 240 YPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
8-278 |
4.83e-85 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 257.81 E-value: 4.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 8 ALVSTKWLAESVRAgkvgPGLRVLDASWYSPG-TREARKEYLERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGS 86
Cdd:PLN02723 22 PVVSVDWLHANLRE----PDVKVLDASWYMPDeQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 87 LGISNDTHVVVYDGDdlGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPE------------------ 148
Cdd:PLN02723 98 LGIENKDGVVVYDGK--GIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAilkasaaseaiekvyqgq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 149 ---PAIFKATLNRSLLKTYEQVLENLESKRFQLVDSRAQGRYLGTQPEPDAvGLDSGHIRGSVNMPFMNFLTEDGFEKSP 225
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRK-GIRSGHIPGSKCVPFPQMLDSSQTLLPA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 12084448 226 EELRAMFEAKKVDLTKPLIAT*RKGVTACHIALAAYLCGKPDVAIYDGSWFEW 278
Cdd:PLN02723 255 EELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
10-282 |
1.09e-73 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 227.28 E-value: 1.09e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 10 VSTKWLAESVRagkvGPGLRVLDASWYSPG--TREARKEYLERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGSL 87
Cdd:PRK11493 7 VAADWLAEHID----DPEIQIIDARMAPPGqeDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 88 GISNDTHVVVYDGDDLgsFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAIFKATLNRSLLKTYEQV 167
Cdd:PRK11493 83 GVNQDKHLVVYDEGNL--FSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 168 LENLESKRFQLVDSRAQGRYLGTQPEPDAvGLDSGHIRGSVNMPFmNFLTEDGFEKSPEELRAMFEAKKVDLTKPLIAT* 247
Cdd:PRK11493 161 LLASHEKTAQIVDARPAARFNAEVDEPRP-GLRRGHIPGALNVPW-TELVREGELKTTDELDAIFFGRGVSFDRPIIASC 238
|
250 260 270
....*....|....*....|....*....|....*
gi 12084448 248 RKGVTACHIALAAYLCGKPDVAIYDGSWFEWFHRA 282
Cdd:PRK11493 239 GSGVTAAVVVLALATLDVPNVKLYDGAWSEWGARA 273
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
10-135 |
6.61e-70 |
|
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: 212.73 E-value: 6.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 10 VSTKWLAESVRAGKVGPGLRVLDASWYSPGTREARKEYLE------------RHVPGASFFDIEECRDKASPYEVMLPSE 77
Cdd:cd01445 1 KSTEQLAENLEAGKVGKGFQLLDARAQSPGTREARGEYLEtqpepdavgldsGHIPGASFFDFEECLDEAGFEESMEPSE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 12084448 78 AGFADYVGSLGISNDTHVVVYDGDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLK 135
Cdd:cd01445 81 AEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
162-280 |
8.82e-57 |
|
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: 179.22 E-value: 8.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 162 KTYEQVLENLE----SKRFQLVDSRAQ--------GRYLGTQPEPDAVGLDSGHIRGSVNMPFMNFLTEDGFEKSPE--- 226
Cdd:cd01445 1 KSTEQLAENLEagkvGKGFQLLDARAQspgtrearGEYLETQPEPDAVGLDSGHIPGASFFDFEECLDEAGFEESMEpse 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 12084448 227 -ELRAMFEAKKVDLTKPLIAT*RK---GVTACHIALAAYLCGKPDVAIYDGSWFEWFH 280
Cdd:cd01445 81 aEFAAMFEAKGIDLDKHLIATDGDdlgGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
9-137 |
2.83e-56 |
|
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: 177.43 E-value: 2.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 9 LVSTKWLAESVRAgkvgPGLRVLDASWYSPGtREARKEYLERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGSLG 88
Cdd:cd01448 1 LVSPDWLAEHLDD----PDVRILDARWYLPD-RDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSLG 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 12084448 89 ISNDTHVVVYdgDDLGSFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEG 137
Cdd:cd01448 76 ISNDDTVVVY--DDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
162-280 |
2.86e-51 |
|
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: 164.34 E-value: 2.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 162 KTYEQVLENLESKRFQLVDSRAQGRYLGTQPEPDAvGLDSGHIRGSVNMPFMNFLTEDGFEKSPEELRAMFEAKKVDLTK 241
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRP-GLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDK 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 12084448 242 PLIAT*RKGVTACHIALAAYLCGKPDVAIYDGSWFEWFH 280
Cdd:cd01449 80 PVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
25-139 |
8.90e-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: 76.73 E-value: 8.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 25 GPGLRVLDASWyspgtreaRKEYLERHVPGASFFDIEECRDKASPYEVMLpseagFADYVGSLGISNDTHVVVYDGddlG 104
Cdd:smart00450 2 DEKVVLLDVRS--------PEEYEGGHIPGAVNIPLSELLDRRGELDILE-----FEELLKRLGLDKDKPVVVYCR---S 65
|
90 100 110
....*....|....*....|....*....|....*
gi 12084448 105 SFYAPRVWWMFRVFGHRTVSVLNGGFRNWLKEGHP 139
Cdd:smart00450 66 GNRSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
40-288 |
5.11e-15 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 75.15 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 40 TREARkeYLERHVPGASFFDIEECRDKASPYEVMLPSEAGFADYVGSLGISNDTHVVVYDgdDLGSFYAPRVWWMFRVFG 119
Cdd:PRK09629 31 TSSAR--YEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVYD--DEGGGWAGRFIWLLDVIG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 120 HRTVSVLNGGFRNWLKEGHPVTSEPSRPEPAIFKATLNRSLLKTYEQVLENLESKRFQLVDSRAQGRYLGTQpepdAVGL 199
Cdd:PRK09629 107 HSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQSRLGAADLAIWDARAPTEYSGEK----VVAA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 200 DSGHIRGSVNMPFMNFLTEDGFEKSPEELRAMFEAKKVDLTKPLIAT*RKGVTACHIALAAYLCGKPDVAIYDGSWFEWF 279
Cdd:PRK09629 183 KGGHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYPRVKAYAGSWGEWG 262
|
....*....
gi 12084448 280 HRapPETWV 288
Cdd:PRK09629 263 NH--PDTPV 269
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
172-284 |
1.36e-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: 68.25 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 172 ESKRFQLVDSRAQGRYLGtqpepdavgldsGHIRGSVNMPFMNFLTEDGfEKSPEELRAMFEAKKVDLTKPLIAT*RKGV 251
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG------------GHIPGAVNIPLSELLDRRG-ELDILEFEELLKRLGLDKDKPVVVYCRSGN 67
|
90 100 110
....*....|....*....|....*....|...
gi 12084448 252 TACHIALAAYLCGKPDVAIYDGSWFEWFHRAPP 284
Cdd:smart00450 68 RSAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
171-278 |
2.32e-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: 59.03 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 171 LESKRFQLVDSRAQGRYlgtqpepdavglDSGHIRGSVNMPFMNF-LTEDGFEKSPEELRAMFEAKKVdltkplIAT*RK 249
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEY------------AKGHIPGAVNVPLSSLsLPPLPLLELLEKLLELLKDKPI------VVYCNS 62
|
90 100
....*....|....*....|....*....
gi 12084448 250 GVTACHIALAAYLCGKPDVAIYDGSWFEW 278
Cdd:pfam00581 63 GNRAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
46-133 |
8.76e-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: 54.80 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 46 EYLERHVPGASFFdieecrdkasPYEVMLPSEAGFADYVGSL-GISNDTHVVVYDGDDLGSfyaPRVWWMFRVFGHRTVS 124
Cdd:pfam00581 16 EYAKGHIPGAVNV----------PLSSLSLPPLPLLELLEKLlELLKDKPIVVYCNSGNRA---AAAAALLKALGYKNVY 82
|
....*....
gi 12084448 125 VLNGGFRNW 133
Cdd:pfam00581 83 VLDGGFEAW 91
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
163-278 |
5.56e-08 |
|
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: 49.96 E-value: 5.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 163 TYEQVlENL--ESKRFQLVDSRaqgrylgtqpEPDAVGldSGHIRGSVNMPFMNFltEDGFEKSPEELRAMFEAKKVDLT 240
Cdd:cd01519 2 SFEEV-KNLpnPHPNKVLIDVR----------EPEELK--TGKIPGAINIPLSSL--PDALALSEEEFEKKYGFPKPSKD 66
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 12084448 241 KPLIAT*RKGV---TACHIALAAylcGKPDVAIYDGSWFEW 278
Cdd:cd01519 67 KELIFYCKAGVrskAAAELARSL---GYENVGNYPGSWLDW 104
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
166-278 |
3.21e-06 |
|
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.
Pssm-ID: 238089 [Multi-domain] Cd Length: 89 Bit Score: 44.60 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 166 QVLENLESKRFQLVDSRAQGRYlgtqpepdavglDSGHIRGSVNMPFmnfltedgfekspEELRAMFEAKKVDLTKPLIA 245
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEY------------AAGHIPGAINIPL-------------SELEERAALLELDKDKPIVV 55
|
90 100 110
....*....|....*....|....*....|...
gi 12084448 246 T*RKGVTACHIALAAYLCGKPDVAIYDGSWFEW 278
Cdd:cd00158 56 YCRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
163-278 |
5.26e-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: 41.49 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 163 TYEQVLENLESKRFQLVDSRaqgrylgtqpEPDAVglDSGHIRGSVNMPFMNFLTedgfekspeelramfEAKKVDLTKP 242
Cdd:COG0607 7 SPAELAELLESEDAVLLDVR----------EPEEF--AAGHIPGAINIPLGELAE---------------RLDELPKDKP 59
|
90 100 110
....*....|....*....|....*....|....*....
gi 12084448 243 LIAT*RKGV---TACHIALAAylcGKPDVAIYDGSWFEW 278
Cdd:COG0607 60 IVVYCASGGrsaQAAALLRRA---GYTNVYNLAGGIEAW 95
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
10-142 |
5.93e-04 |
|
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440372 [Multi-domain] Cd Length: 106 Bit Score: 38.41 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 10 VSTKWLAESVRAGKVgpglRVLDaswyspgTREARkEYLERHVPGASFFDIEECRDKASPyevmlpseagfadyvgslgI 89
Cdd:COG0607 6 ISPAELAELLESEDA----VLLD-------VREPE-EFAAGHIPGAINIPLGELAERLDE-------------------L 54
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 12084448 90 SNDTHVVVYDGDDLGSFYAPRvwwMFRVFGHRTVSVLNGGFRNWLKEGHPVTS 142
Cdd:COG0607 55 PKDKPIVVYCASGGRSAQAAA---LLRRAGYTNVYNLAGGIEAWKAAGLPVEK 104
|
|
| Cdc25_Acr2p |
cd01443 |
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ... |
174-280 |
6.35e-04 |
|
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: 38.54 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 174 KRFQLVDSRaqgrylgtqpEPDavgLDSGHIRGSVNMPfmnflTEDGFEKSPEELRAMFEAKKVDLTKPLIAT*RKGVTA 253
Cdd:cd01443 22 KDFVVVDLR----------RDD---YEGGHIKGSINLP-----AQSCYQTLPQVYALFSLAGVKLAIFYCGSSQGRGPRA 83
|
90 100 110
....*....|....*....|....*....|
gi 12084448 254 CH-IALAAYLCGKPDVAIY--DGSWFEWFH 280
Cdd:cd01443 84 ARwFADYLRKVGESLPKSYilTGGIKAWYH 113
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
25-133 |
1.38e-03 |
|
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: 37.28 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12084448 25 GPGLRVLDAswyspgtREArKEYLERHVPGASFFDIEECRDKAspyevmlpseagfadyvGSLGISNDTHVVVYDGDDLG 104
Cdd:cd00158 8 DEDAVLLDV-------REP-EEYAAGHIPGAINIPLSELEERA-----------------ALLELDKDKPIVVYCRSGNR 62
|
90 100
....*....|....*....|....*....
gi 12084448 105 SfyaPRVWWMFRVFGHRTVSVLNGGFRNW 133
Cdd:cd00158 63 S---ARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| |
