|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
36-299 |
4.17e-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: 4.17e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 36 VAEALRAPragqPLQLLDASWYLPklgrDARREFEERHIPGAAFFDIDQC-SDRTSPYDHMLPGAEHFAEYAGRLGVGAA 114
Cdd:COG2897 1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 115 THVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLE 194
Cdd:COG2897 73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 195 SRRFQVVDSRATGRFRGtEPEPRDGIePGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTA 274
Cdd:COG2897 151 DPDAVLVDARSPERYRG-EVEPIDPR-AGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228
|
250 260
....*....|....*....|....*
gi 194473668 275 CHVALGAYLCGKPDVPIYDGSWVEW 299
Cdd:COG2897 229 AHTWLALELLGYPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
6-299 |
2.35e-98 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 292.48 E-value: 2.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 6 SRESETRARSPSvAAMASPQlcrALVSAQWVAEALRAPRagqpLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQC 85
Cdd:PLN02723 3 SSGSETKANYST-QSISTNE---PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 86 SDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDAsdQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSG 165
Cdd:PLN02723 75 SDRTTDLPHMLPSEEAFAAAVSALGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 166 KSQPA---------------------PAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGH 224
Cdd:PLN02723 153 ASGDAilkasaaseaiekvyqgqtvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRKGIRSGH 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194473668 225 IPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 299
Cdd:PLN02723 233 IPGSKCVPFPQMLDSSQTLLPAEELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
184-299 |
4.96e-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: 4.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 184 KTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKP 263
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKP 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 194473668 264 LVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 299
Cdd:cd01449 81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
64-161 |
1.38e-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: 79.43 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 64 DARR--EFEERHIPGAAFFDIDQCSDRTSPYDHMlpgaeHFAEYAGRLGVGAATHVVIYDASDqglYSAPRVWWMFRAFG 141
Cdd:smart00450 9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 194473668 142 HHAVSLLDGGLRHWLRQNLP 161
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
64-155 |
3.84e-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: 58.65 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 64 DARR--EFEERHIPGAAFFDIDqcsdrtSPYDHMLPGAEHFAEYAGRLGvgaATHVVIYDASDQglySAPRVWWMFRAFG 141
Cdd:pfam00581 10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77
|
90
....*....|....
gi 194473668 142 HHAVSLLDGGLRHW 155
Cdd:pfam00581 78 YKNVYVLDGGFEAW 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
36-299 |
4.17e-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: 4.17e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 36 VAEALRAPragqPLQLLDASWYLPklgrDARREFEERHIPGAAFFDIDQC-SDRTSPYDHMLPGAEHFAEYAGRLGVGAA 114
Cdd:COG2897 1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 115 THVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLE 194
Cdd:COG2897 73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 195 SRRFQVVDSRATGRFRGtEPEPRDGIePGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTA 274
Cdd:COG2897 151 DPDAVLVDARSPERYRG-EVEPIDPR-AGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228
|
250 260
....*....|....*....|....*
gi 194473668 275 CHVALGAYLCGKPDVPIYDGSWVEW 299
Cdd:COG2897 229 AHTWLALELLGYPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
6-299 |
2.35e-98 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 292.48 E-value: 2.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 6 SRESETRARSPSvAAMASPQlcrALVSAQWVAEALRAPRagqpLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQC 85
Cdd:PLN02723 3 SSGSETKANYST-QSISTNE---PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 86 SDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDAsdQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSG 165
Cdd:PLN02723 75 SDRTTDLPHMLPSEEAFAAAVSALGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 166 KSQPA---------------------PAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGH 224
Cdd:PLN02723 153 ASGDAilkasaaseaiekvyqgqtvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRKGIRSGH 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194473668 225 IPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 299
Cdd:PLN02723 233 IPGSKCVPFPQMLDSSQTLLPAEELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
31-303 |
6.03e-88 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 264.65 E-value: 6.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 31 VSAQWVAEALRAPRagqpLQLLDASWYLPKL-GRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRL 109
Cdd:PRK11493 7 VAADWLAEHIDDPE----IQIIDARMAPPGQeDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 110 GVGAATHVVIYDASDqgLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDI 189
Cdd:PRK11493 83 GVNQDKHLVVYDEGN--LFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 190 KENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDfLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCG 269
Cdd:PRK11493 161 LLASHEKTAQIVDARPAARFNAEVDEPRPGLRRGHIPGALNVPWTE-LVREGELKTTDELDAIFFGRGVSFDRPIIASCG 239
|
250 260 270
....*....|....*....|....*....|....
gi 194473668 270 SGVTACHVALGAYLCGKPDVPIYDGSWVEWYMRA 303
Cdd:PRK11493 240 SGVTAAVVVLALATLDVPNVKLYDGAWSEWGARA 273
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
184-299 |
4.96e-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: 4.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 184 KTYEDIKENLESRRFQVVDSRATGRFRGTEPEPRDGIEPGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKP 263
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKP 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 194473668 264 LVATCGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 299
Cdd:cd01449 81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
30-159 |
6.07e-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: 167.03 E-value: 6.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 30 LVSAQWVAEALRAPRagqpLQLLDASWYLPklGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRL 109
Cdd:cd01448 1 LVSPDWLAEHLDDPD----VRILDARWYLP--DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 194473668 110 GVGAATHVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQN 159
Cdd:cd01448 75 GISNDDTVVVYD--DGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
31-157 |
7.27e-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: 128.76 E-value: 7.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 31 VSAQWVAEALRAPRAGQPLQLLDASWYLPKLgRDARREF------------EERHIPGAAFFDIDQCSDRTSPYDHMLPG 98
Cdd:cd01445 1 KSTEQLAENLEAGKVGKGFQLLDARAQSPGT-REARGEYletqpepdavglDSGHIPGASFFDFEECLDEAGFEESMEPS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 194473668 99 AEHFAEYAGRLGVGAATHVVIYDASDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLR 157
Cdd:cd01445 80 EAEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
184-300 |
1.31e-33 |
|
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: 120.28 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 184 KTYEDIKENLE----SRRFQVVDSR--------ATGRFRGTEPEPRD-GIEPGHIPGTVNIPFTDFLSQEGLEKSPE--- 247
Cdd:cd01445 1 KSTEQLAENLEagkvGKGFQLLDARaqspgtreARGEYLETQPEPDAvGLDSGHIPGASFFDFEECLDEAGFEESMEpse 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 194473668 248 -EIRHLFQEKKVDLSKPLVATCG---SGVTACHVALGAYLCGKPDVPIYDGSWVEWY 300
Cdd:cd01445 81 aEFAAMFEAKGIDLDKHLIATDGddlGGFTACHIALAARLCGHPDVAILDGGFFEWF 137
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
64-161 |
1.38e-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: 79.43 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 64 DARR--EFEERHIPGAAFFDIDQCSDRTSPYDHMlpgaeHFAEYAGRLGVGAATHVVIYDASDqglYSAPRVWWMFRAFG 141
Cdd:smart00450 9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 194473668 142 HHAVSLLDGGLRHWLRQNLP 161
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGPP 100
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
49-299 |
2.13e-18 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 85.55 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 49 LQLLDA-SWYLPKLGRDARreFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDasDQGL 127
Cdd:PRK09629 17 LERLDApELILVDLTSSAR--YEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVYD--DEGG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 128 YSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATG 207
Cdd:PRK09629 93 GWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQSRLGAADLAIWDARAPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 208 RFRGTEPEPRDGiepGHIPGTVNIPFTDFLSQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVTACHVALGAYLCGKP 287
Cdd:PRK09629 173 EYSGEKVVAAKG---GHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYP 249
|
250
....*....|..
gi 194473668 288 DVPIYDGSWVEW 299
Cdd:PRK09629 250 RVKAYAGSWGEW 261
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
194-305 |
6.88e-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: 6.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 194 ESRRFQVVDSRATGRFRGtepeprdgiepGHIPGTVNIPFTDFLsQEGLEKSPEEIRHLFQEKKVDLSKPLVATCGSGVT 273
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELL-DRRGELDILEFEELLKRLGLDKDKPVVVYCRSGNR 68
|
90 100 110
....*....|....*....|....*....|..
gi 194473668 274 ACHVALGAYLCGKPDVPIYDGSWVEWYMRARP 305
Cdd:smart00450 69 SAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
64-155 |
3.84e-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: 58.65 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 64 DARR--EFEERHIPGAAFFDIDqcsdrtSPYDHMLPGAEHFAEYAGRLGvgaATHVVIYDASDQglySAPRVWWMFRAFG 141
Cdd:pfam00581 10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77
|
90
....*....|....
gi 194473668 142 HHAVSLLDGGLRHW 155
Cdd:pfam00581 78 YKNVYVLDGGFEAW 91
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
185-299 |
7.35e-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: 7.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 185 TYEDIKENLE-SRRFQVVDSRatgrfrgtepEPRDgIEPGHIPGTVNIPFTDFlsQEGLEKSPEEIRHLFQEKKVDLSKP 263
Cdd:cd01519 2 SFEEVKNLPNpHPNKVLIDVR----------EPEE-LKTGKIPGAINIPLSSL--PDALALSEEEFEKKYGFPKPSKDKE 68
|
90 100 110
....*....|....*....|....*....|....*....
gi 194473668 264 LVATCGSGV---TACHVALGAylcGKPDVPIYDGSWVEW 299
Cdd:cd01519 69 LIFYCKAGVrskAAAELARSL---GYENVGNYPGSWLDW 104
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
193-299 |
2.10e-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: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 193 LESRRFQVVDSRATGRFrgtepeprdgiEPGHIPGTVNIPFTDF-LSQEGLEKSPEEIRHLFQEKKVdlskplVATCGSG 271
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEY-----------AKGHIPGAVNVPLSSLsLPPLPLLELLEKLLELLKDKPI------VVYCNSG 63
|
90 100
....*....|....*....|....*...
gi 194473668 272 VTACHVALGAYLCGKPDVPIYDGSWVEW 299
Cdd:pfam00581 64 NRAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
188-299 |
1.21e-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: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 188 DIKENLESRRFQVVDSRATGRFRGtepeprdgiepGHIPGTVNIPFtdflsqeglekspEEIRHLFQEKKVDLSKPLVAT 267
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEYAA-----------GHIPGAINIPL-------------SELEERAALLELDKDKPIVVY 56
|
90 100 110
....*....|....*....|....*....|..
gi 194473668 268 CGSGVTACHVALGAYLCGKPDVPIYDGSWVEW 299
Cdd:cd00158 57 CRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
185-305 |
4.31e-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: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 185 TYEDIKENLESRRFQVVDSRatgrfrgtEPEPRDGiepGHIPGTVNIPFTDFLSQEGlekspeeirhlfqekKVDLSKPL 264
Cdd:COG0607 7 SPAELAELLESEDAVLLDVR--------EPEEFAA---GHIPGAINIPLGELAERLD---------------ELPKDKPI 60
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 194473668 265 VATCGSGVTACHVAlgAYLC--GKPDVPIYDGSWVEWYMRARP 305
Cdd:COG0607 61 VVYCASGGRSAQAA--ALLRraGYTNVYNLAGGIEAWKAAGLP 101
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
31-166 |
9.23e-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: 46.50 E-value: 9.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 31 VSAQWVAEALRAPRAgqplQLLDAswylpklgRDARrEFEERHIPGAAFFDIDQCSDRTSPYDhmlpgaehfaeyagrlg 110
Cdd:COG0607 6 ISPAELAELLESEDA----VLLDV--------REPE-EFAAGHIPGAINIPLGELAERLDELP----------------- 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 194473668 111 vgAATHVVIYDASDqglYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGK 166
Cdd:COG0607 56 --KDKPIVVYCASG---GRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
64-155 |
8.62e-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: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 64 DAR--REFEERHIPGAAFFDIDQcsdrtspydhmlpgaehFAEYAGRLGVGAATHVVIYDASDQglySAPRVWWMFRAFG 141
Cdd:cd00158 15 DVRepEEYAAGHIPGAINIPLSE-----------------LEERAALLELDKDKPIVVYCRSGN---RSARAAKLLRKAG 74
|
90
....*....|....
gi 194473668 142 HHAVSLLDGGLRHW 155
Cdd:cd00158 75 GTNVYNLEGGMLAW 88
|
|
| Cdc25_Acr2p |
cd01443 |
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ... |
178-300 |
1.62e-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: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194473668 178 LDPAFIKTYEDIKENLESRRFQVVDSRatgrfrgtepepRDGIEPGHIPGTVNIPFTDFLSQEgleksPEEIRHLFQEKK 257
Cdd:cd01443 4 ISPEELVALLENSDSNAGKDFVVVDLR------------RDDYEGGHIKGSINLPAQSCYQTL-----PQVYALFSLAGV 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 194473668 258 VDlskpLVATCGS----GVTACH------VALGAYlcgKPDVPIYDGSWVEWY 300
Cdd:cd01443 67 KL----AIFYCGSsqgrGPRAARwfadylRKVGES---LPKSYILTGGIKAWY 112
|
|
| |
