|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
16-279 |
2.01e-104 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 305.18 E-value: 2.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 16 VAEALRAPragqPLQLLDASWYLPklgrDARREFEERHIPGAAFFDIDQC-SDRTSPYDHMLPGAEHFAEYAGRLGVGAA 94
Cdd:COG2897 1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 95 THVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLE 174
Cdd:COG2897 73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 175 SRRFQVVDSRATGRFRGtEPEPRDGIePGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTA 254
Cdd:COG2897 151 DPDAVLVDARSPERYRG-EVEPIDPR-AGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228
|
250 260
....*....|....*....|....*
gi 61835204 255 CHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:COG2897 229 AHTWLALELLGYPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
9-279 |
1.99e-98 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 292.09 E-value: 1.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 9 ALVSAQWVAEALRAPRagqpLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGR 88
Cdd:PLN02723 22 PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 89 LGVGAATHVVIYDAsdQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPA------------------ 150
Cdd:PLN02723 98 LGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAilkasaaseaiekvyqgq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 151 ---PAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPE 227
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLPAE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 61835204 228 EIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:PLN02723 256 ELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
164-279 |
2.28e-53 |
|
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: 169.74 E-value: 2.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 164 KTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKP 243
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKP 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 61835204 244 LVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:cd01449 81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
44-141 |
1.73e-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: 78.66 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 44 DARR--EFEERHIPGAAFFDIDQCSDRTSPYDHMlpgaeHFAEYAGRLGVGAATHVVIYDASDqglYSAPRVWWMFRAFG 121
Cdd:smart00450 9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 61835204 122 HHAVSLLDGGLRHWLRQNLP 141
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
44-135 |
5.59e-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: 57.88 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 44 DARR--EFEERHIPGAAFFDIDqcsdrtSPYDHMLPGAEHFAEYAGRLGvgaATHVVIYDASDQglySAPRVWWMFRAFG 121
Cdd:pfam00581 10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77
|
90
....*....|....
gi 61835204 122 HHAVSLLDGGLRHW 135
Cdd:pfam00581 78 YKNVYVLDGGFEAW 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
16-279 |
2.01e-104 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 305.18 E-value: 2.01e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 16 VAEALRAPragqPLQLLDASWYLPklgrDARREFEERHIPGAAFFDIDQC-SDRTSPYDHMLPGAEHFAEYAGRLGVGAA 94
Cdd:COG2897 1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 95 THVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLE 174
Cdd:COG2897 73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 175 SRRFQVVDSRATGRFRGtEPEPRDGIePGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTA 254
Cdd:COG2897 151 DPDAVLVDARSPERYRG-EVEPIDPR-AGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228
|
250 260
....*....|....*....|....*
gi 61835204 255 CHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:COG2897 229 AHTWLALELLGYPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
9-279 |
1.99e-98 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 292.09 E-value: 1.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 9 ALVSAQWVAEALRAPRagqpLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGR 88
Cdd:PLN02723 22 PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 89 LGVGAATHVVIYDAsdQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPA------------------ 150
Cdd:PLN02723 98 LGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAilkasaaseaiekvyqgq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 151 ---PAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPE 227
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLPAE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 61835204 228 EIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:PLN02723 256 ELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
11-283 |
1.20e-88 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 265.80 E-value: 1.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 11 VSAQWVAEALRAPRagqpLQLLDASWYLPKL-GRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRL 89
Cdd:PRK11493 7 VAADWLAEHIDDPE----IQIIDARMAPPGQeDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 90 GVGAATHVVIYDASDqgLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDI 169
Cdd:PRK11493 83 GVNQDKHLVVYDEGN--LFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 170 KENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDfLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCG 249
Cdd:PRK11493 161 LLASHEKTAQIVDARPAARFNAEVDEPRPGLRRGHIPGALNVPWTE-LVREGELKTTDELDAIFFGRGVSFDRPIIASCG 239
|
250 260 270
....*....|....*....|....*....|....
gi 61835204 250 SGVTACHVALGAYLCGKPDVPIYDGSWVEWYMRA 283
Cdd:PRK11493 240 SGVTAAVVVLALATLDVPNVKLYDGAWSEWGARA 273
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
164-279 |
2.28e-53 |
|
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: 169.74 E-value: 2.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 164 KTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKP 243
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKP 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 61835204 244 LVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:cd01449 81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
10-139 |
9.33e-52 |
|
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: 165.87 E-value: 9.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 10 LVSAQWVAEALRAPRagqpLQLLDASWYLPklGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRL 89
Cdd:cd01448 1 LVSPDWLAEHLDDPD----VRILDARWYLP--DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 61835204 90 GVGAATHVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQN 139
Cdd:cd01448 75 GISNDDTVVVYD--DGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
11-137 |
3.07e-37 |
|
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: 129.14 E-value: 3.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 11 VSAQWVAEALRAPRAGQPLQLLDASWYLPKlGRDARREF------------EERHIPGAAFFDIDQCSDRTSPYDHMLPG 78
Cdd:cd01445 1 KSTEQLAENLEAGKVGKGFQLLDARAQSPG-TREARGEYletqpepdavglDSGHIPGASFFDFEECLDEAGFEESMEPS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 61835204 79 AEHFAEYAGRLGVGAATHVVIYDASDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLR 137
Cdd:cd01445 80 EAEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
164-280 |
5.08e-34 |
|
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: 121.05 E-value: 5.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 164 KTYEDIKENLE----SRRFQVVDSR--------ATGRFRGTEPEPRD-GIEPGHIPGTVNIPFTDFLSQEGLEKSPE--- 227
Cdd:cd01445 1 KSTEQLAENLEagkvGKGFQLLDARaqspgtreARGEYLETQPEPDAvGLDSGHIPGASFFDFEECLDEAGFEESMEpse 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 61835204 228 -EIRHLFQEKKVDLSKPLVATCG---SGVTACHVALGAYLCGKPDVPIYDGSWVEWY 280
Cdd:cd01445 81 aEFAAMFEAKGIDLDKHLIATDGddlGGFTACHIALAARLCGHPDVAILDGGFFEWF 137
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
29-279 |
8.48e-19 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 86.33 E-value: 8.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 29 LQLLDA-SWYLPKLGRDARreFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDasDQGL 107
Cdd:PRK09629 17 LERLDApELILVDLTSSAR--YEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVYD--DEGG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 108 YSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATG 187
Cdd:PRK09629 93 GWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQSRLGAADLAIWDARAPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 188 RFRGTEPEPRDGiepGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKP 267
Cdd:PRK09629 173 EYSGEKVVAAKG---GHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYP 249
|
250
....*....|..
gi 61835204 268 DVPIYDGSWVEW 279
Cdd:PRK09629 250 RVKAYAGSWGEW 261
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
44-141 |
1.73e-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: 78.66 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 44 DARR--EFEERHIPGAAFFDIDQCSDRTSPYDHMlpgaeHFAEYAGRLGVGAATHVVIYDASDqglYSAPRVWWMFRAFG 121
Cdd:smart00450 9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 61835204 122 HHAVSLLDGGLRHWLRQNLP 141
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGPP 100
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
174-285 |
8.41e-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: 74.42 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 174 ESRRFQVVDSRATGRFRGtepeprdgiepGHIPGTVNIPFTDFLsQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVT 253
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELL-DRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNR 68
|
90 100 110
....*....|....*....|....*....|..
gi 61835204 254 ACHVALGAYLCGKPDVPIYDGSWVEWYMRARP 285
Cdd:smart00450 69 SAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
165-279 |
4.96e-11 |
|
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: 58.44 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 165 TYEDIKENLE-SRRFQVVDSRatgrfrgtepEPRDgIEPGHIPGTVNIPFTDFlsQEGLEKSPEEIRHLFQEKKVDLSKP 243
Cdd:cd01519 2 SFEEVKNLPNpHPNKVLIDVR----------EPEE-LKTGKIPGAINIPLSSL--PDALALSEEEFEKKYGFPKPSKDKE 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 61835204 244 LVATCGSGV---TACHVALGAylcGKPDVPIYDGSWVEW 279
Cdd:cd01519 69 LIFYCKAGVrskAAAELARSL---GYENVGNYPGSWLDW 104
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
44-135 |
5.59e-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: 57.88 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 44 DARR--EFEERHIPGAAFFDIDqcsdrtSPYDHMLPGAEHFAEYAGRLGvgaATHVVIYDASDQglySAPRVWWMFRAFG 121
Cdd:pfam00581 10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77
|
90
....*....|....
gi 61835204 122 HHAVSLLDGGLRHW 135
Cdd:pfam00581 78 YKNVYVLDGGFEAW 91
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| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
173-279 |
2.98e-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: 53.26 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 173 LESRRFQVVDSRATGRFrgtepeprdgiEPGHIPGTVNIPFTDF-LSQEGLEKSPEEIRHLFQEKKVdlskplVATCGSG 251
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEY-----------AKGHIPGAVNVPLSSLsLPPLPLLELLEKLLELLKDKPI------VVYCNSG 63
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90 100
....*....|....*....|....*...
gi 61835204 252 VTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:pfam00581 64 NRAAAAAALLKALGYKNVYVLDGGFEAW 91
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| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
168-279 |
1.27e-08 |
|
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: 51.53 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 168 DIKENLESRRFQVVDSRATGRFRGtepeprdgiepGHIPGTVNIPFtdflsqeglekspEEIRHLFQEKKVDLSKPLVAT 247
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEYAA-----------GHIPGAINIPL-------------SELEERAALLELDKDKPIVVY 56
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90 100 110
....*....|....*....|....*....|..
gi 61835204 248 CGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 279
Cdd:cd00158 57 CRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
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| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
165-285 |
3.58e-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: 47.65 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 165 TYEDIKENLESRRFQVVDSRatgrfrgtEPEPRDGiepGHIPGTVNIPFTDFLSQEGlekspeeirhlfqekKVDLSKPL 244
Cdd:COG0607 7 SPAELAELLESEDAVLLDVR--------EPEEFAA---GHIPGAINIPLGELAERLD---------------ELPKDKPI 60
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90 100 110 120
....*....|....*....|....*....|....*....|...
gi 61835204 245 VATCGSGVTACHVAlgAYLC--GKPDVPIYDGSWVEWYMRARP 285
Cdd:COG0607 61 VVYCASGGRSAQAA--ALLRraGYTNVYNLAGGIEAWKAAGLP 101
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| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
11-146 |
7.52e-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: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 11 VSAQWVAEALRAPRAgqplQLLDAswylpklgRDARrEFEERHIPGAAFFDIDQCSDRTSPYDhmlpgaehfaeyagrlg 90
Cdd:COG0607 6 ISPAELAELLESEDA----VLLDV--------REPE-EFAAGHIPGAINIPLGELAERLDELP----------------- 55
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 61835204 91 vgAATHVVIYDASDqglYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGK 146
Cdd:COG0607 56 --KDKPIVVYCASG---GRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
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| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
44-135 |
9.08e-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: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 44 DAR--REFEERHIPGAAFFDIDQcsdrtspydhmlpgaehFAEYAGRLGVGAATHVVIYDASDQglySAPRVWWMFRAFG 121
Cdd:cd00158 15 DVRepEEYAAGHIPGAINIPLSE-----------------LEERAALLELDKDKPIVVYCRSGN---RSARAAKLLRKAG 74
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90
....*....|....
gi 61835204 122 HHAVSLLDGGLRHW 135
Cdd:cd00158 75 GTNVYNLEGGMLAW 88
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| Cdc25_Acr2p |
cd01443 |
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ... |
158-280 |
1.50e-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: 37.77 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61835204 158 LDPAFIKTYEDIKENLESRRFQVVDSRatgrfrgtepepRDGIEPGHIPGTVNIPFTDFLSQEgleksPEEIRHLFQEKK 237
Cdd:cd01443 4 ISPEELVALLENSDSNAGKDFVVVDLR------------RDDYEGGHIKGSINLPAQSCYQTL-----PQVYALFSLAGV 66
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 61835204 238 VDlskpLVATCGS----GVTACH------VALGAYlcgKPDVPIYDGSWVEWY 280
Cdd:cd01443 67 KL----AIFYCGSsqgrGPRAARwfadylRKVGES---LPKSYILTGGIKAWY 112
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