|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
16-279 |
1.97e-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: 1.97e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 16 VAEALKSPrasqPLKLLDASWYLPklgrDARREFEERHIPGAAFFDIDRC-SDHTSPYDHMLPSATHFADYAGSLGVSAA 94
Cdd:COG2897 1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 95 THVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISSGKSPSEPAEFCAQLDPSFIKTHEDILENLD 174
Cdd:COG2897 73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 175 ARRFQVVDARAAGRFQGTQpEPRDGIePGHIPGSVNIPFTEFLTSEGLEKSPEEIQRLFQEKKVDLSKPLVATCGSGVTA 254
Cdd:COG2897 151 DPDAVLVDARSPERYRGEV-EPIDPR-AGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228
|
250 260
....*....|....*....|....*
gi 20304123 255 CHVVLGAFLCGKPDVPVYDGSWVEW 279
Cdd:COG2897 229 AHTWLALELLGYPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
9-287 |
3.47e-96 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 286.31 E-value: 3.47e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 9 ALVSAQWVAEALKSPRasqpLKLLDASWYLPKLGRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGS 88
Cdd:PLN02723 22 PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 89 LGVSAATHVVIYDGsdQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISS---------GKSPSE--------- 150
Cdd:PLN02723 98 LGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESsasgdailkASAASEaiekvyqgq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 151 ---PAEFCAQLDPSFIKTHEDILENLDARRFQVVDARAAGRFQGTQPEPRDGIEPGHIPGSVNIPFTEFLTSEGLEKSPE 227
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLPAE 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 228 EIQRLFQEKKVDLSKPLVATCGSGVTACHVVLGAFLCGKPDVPVYDGSWVEWymRAQPEH 287
Cdd:PLN02723 256 ELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW--GALPDT 313
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
164-279 |
3.05e-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: 3.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 164 KTHEDILENLDARRFQVVDARAAGRFQGTQPEPRDGIEPGHIPGSVNIPFTEFLTSEGLEKSPEEIQRLFQEKKVDLSKP 243
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKP 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 20304123 244 LVATCGSGVTACHVVLGAFLCGKPDVPVYDGSWVEW 279
Cdd:cd01449 81 VIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
174-285 |
3.53e-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: 77.88 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 174 DARRFQVVDARAAGRFQGtqpeprdgiepGHIPGSVNIPFTEFLTSEGlEKSPEEIQRLFQEKKVDLSKPLVATCGSGVT 253
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELLDRRG-ELDILEFEELLKRLGLDKDKPVVVYCRSGNR 68
|
90 100 110
....*....|....*....|....*....|..
gi 20304123 254 ACHVVLGAFLCGKPDVPVYDGSWVEWYMRAQP 285
Cdd:smart00450 69 SAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
44-135 |
1.01e-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: 60.19 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 44 DARR--EFEERHIPGAAFFDIDrcsdhtSPYDHMLPSATHFADYAGSLGvsaATHVVIYDGSDQglySAPRVWWMFRAFG 121
Cdd:pfam00581 10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77
|
90
....*....|....
gi 20304123 122 HHSVSLLDGGFRYW 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 |
1.97e-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: 1.97e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 16 VAEALKSPrasqPLKLLDASWYLPklgrDARREFEERHIPGAAFFDIDRC-SDHTSPYDHMLPSATHFADYAGSLGVSAA 94
Cdd:COG2897 1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 95 THVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISSGKSPSEPAEFCAQLDPSFIKTHEDILENLD 174
Cdd:COG2897 73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 175 ARRFQVVDARAAGRFQGTQpEPRDGIePGHIPGSVNIPFTEFLTSEGLEKSPEEIQRLFQEKKVDLSKPLVATCGSGVTA 254
Cdd:COG2897 151 DPDAVLVDARSPERYRGEV-EPIDPR-AGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228
|
250 260
....*....|....*....|....*
gi 20304123 255 CHVVLGAFLCGKPDVPVYDGSWVEW 279
Cdd:COG2897 229 AHTWLALELLGYPNVRLYDGSWSEW 253
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
9-287 |
3.47e-96 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 286.31 E-value: 3.47e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 9 ALVSAQWVAEALKSPRasqpLKLLDASWYLPKLGRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGS 88
Cdd:PLN02723 22 PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 89 LGVSAATHVVIYDGsdQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISS---------GKSPSE--------- 150
Cdd:PLN02723 98 LGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESsasgdailkASAASEaiekvyqgq 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 151 ---PAEFCAQLDPSFIKTHEDILENLDARRFQVVDARAAGRFQGTQPEPRDGIEPGHIPGSVNIPFTEFLTSEGLEKSPE 227
Cdd:PLN02723 176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLPAE 255
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 228 EIQRLFQEKKVDLSKPLVATCGSGVTACHVVLGAFLCGKPDVPVYDGSWVEWymRAQPEH 287
Cdd:PLN02723 256 ELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW--GALPDT 313
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
11-283 |
7.56e-91 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 271.20 E-value: 7.56e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 11 VSAQWVAEALKSPRasqpLKLLDASWYLPKL-GRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGSL 89
Cdd:PRK11493 7 VAADWLAEHIDDPE----IQIIDARMAPPGQeDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMREL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 90 GVSAATHVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISSGKSPSEPAEFCAQLDPSFIKTHEDI 169
Cdd:PRK11493 83 GVNQDKHLVVYD--EGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 170 LENLDARRFQVVDARAAGRFQGTQPEPRDGIEPGHIPGSVNIPFTEfLTSEGLEKSPEEIQRLFQEKKVDLSKPLVATCG 249
Cdd:PRK11493 161 LLASHEKTAQIVDARPAARFNAEVDEPRPGLRRGHIPGALNVPWTE-LVREGELKTTDELDAIFFGRGVSFDRPIIASCG 239
|
250 260 270
....*....|....*....|....*....|....
gi 20304123 250 SGVTACHVVLGAFLCGKPDVPVYDGSWVEWYMRA 283
Cdd:PRK11493 240 SGVTAAVVVLALATLDVPNVKLYDGAWSEWGARA 273
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
164-279 |
3.05e-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: 3.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 164 KTHEDILENLDARRFQVVDARAAGRFQGTQPEPRDGIEPGHIPGSVNIPFTEFLTSEGLEKSPEEIQRLFQEKKVDLSKP 243
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKP 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 20304123 244 LVATCGSGVTACHVVLGAFLCGKPDVPVYDGSWVEW 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 |
5.64e-53 |
|
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: 168.95 E-value: 5.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 10 LVSAQWVAEALKSPRasqpLKLLDASWYLPklGRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGSL 89
Cdd:cd01448 1 LVSPDWLAEHLDDPD----VRILDARWYLP--DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 20304123 90 GVSAATHVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQN 139
Cdd:cd01448 75 GISNDDTVVVYD--DGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
11-136 |
1.62e-39 |
|
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: 135.30 E-value: 1.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 11 VSAQWVAEALKSPRASQPLKLLDASWYLPKLgRDARREF------------EERHIPGAAFFDIDRCSDHTSPYDHMLPS 78
Cdd:cd01445 1 KSTEQLAENLEAGKVGKGFQLLDARAQSPGT-REARGEYletqpepdavglDSGHIPGASFFDFEECLDEAGFEESMEPS 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 20304123 79 ATHFADYAGSLGVSAATHVVIYDGSDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWL 136
Cdd:cd01445 80 EAEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWF 137
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
164-280 |
3.70e-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: 118.74 E-value: 3.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 164 KTHEDILENLDA----RRFQVVDAR--------AAGRFQGTQPEPRD-GIEPGHIPGSVNIPFTEFLTSEGLEKSPE--- 227
Cdd:cd01445 1 KSTEQLAENLEAgkvgKGFQLLDARaqspgtreARGEYLETQPEPDAvGLDSGHIPGASFFDFEECLDEAGFEESMEpse 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 20304123 228 -EIQRLFQEKKVDLSKPLVATCG---SGVTACHVVLGAFLCGKPDVPVYDGSWVEWY 280
Cdd:cd01445 81 aEFAAMFEAKGIDLDKHLIATDGddlGGFTACHIALAARLCGHPDVAILDGGFFEWF 137
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
29-279 |
4.56e-21 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 93.26 E-value: 4.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 29 LKLLDA-SWYLPKLGRDARreFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGSLGVSAATHVVIYDgsDQGL 107
Cdd:PRK09629 17 LERLDApELILVDLTSSAR--YEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVYD--DEGG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 108 YSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISSGKSPSEPAEFCAQLDPSFIKTHEDILENLDARRFQVVDARAAG 187
Cdd:PRK09629 93 GWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQSRLGAADLAIWDARAPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 188 RFQGTQPEPRDGiepGHIPGSVNIPFTEFLTSEGLEKSPEEIQRLFQEKKVDLSKPLVATCGSGVTACHVVLGAFLCGKP 267
Cdd:PRK09629 173 EYSGEKVVAAKG---GHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYP 249
|
250
....*....|..
gi 20304123 268 DVPVYDGSWVEW 279
Cdd:PRK09629 250 RVKAYAGSWGEW 261
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
174-285 |
3.53e-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: 77.88 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 174 DARRFQVVDARAAGRFQGtqpeprdgiepGHIPGSVNIPFTEFLTSEGlEKSPEEIQRLFQEKKVDLSKPLVATCGSGVT 253
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELLDRRG-ELDILEFEELLKRLGLDKDKPVVVYCRSGNR 68
|
90 100 110
....*....|....*....|....*....|..
gi 20304123 254 ACHVVLGAFLCGKPDVPVYDGSWVEWYMRAQP 285
Cdd:smart00450 69 SAKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
44-141 |
2.89e-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: 75.57 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 44 DARR--EFEERHIPGAAFFDIDRCSDHTSPYDHMlpsatHFADYAGSLGVSAATHVVIYDGSDqglYSAPRVWWMFRAFG 121
Cdd:smart00450 9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 20304123 122 HHSVSLLDGGFRYWLSQNLP 141
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
44-135 |
1.01e-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: 60.19 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 44 DARR--EFEERHIPGAAFFDIDrcsdhtSPYDHMLPSATHFADYAGSLGvsaATHVVIYDGSDQglySAPRVWWMFRAFG 121
Cdd:pfam00581 10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77
|
90
....*....|....
gi 20304123 122 HHSVSLLDGGFRYW 135
Cdd:pfam00581 78 YKNVYVLDGGFEAW 91
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
173-279 |
1.18e-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: 59.81 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 173 LDARRFQVVDARAAGRFQGtqpeprdgiepGHIPGSVNIPFTEF-LTSEGLEKSPEEIQRLFQEKKVdlskplVATCGSG 251
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAK-----------GHIPGAVNVPLSSLsLPPLPLLELLEKLLELLKDKPI------VVYCNSG 63
|
90 100
....*....|....*....|....*...
gi 20304123 252 VTACHVVLGAFLCGKPDVPVYDGSWVEW 279
Cdd:pfam00581 64 NRAAAAAALLKALGYKNVYVLDGGFEAW 91
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
203-279 |
2.02e-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: 59.59 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 203 GHIPGSVNIPFTEFltSEGLEKSPEEIQRLFQEKKVDLSKPLVATCGSGV---TACHVVLGAflcGKPDVPVYDGSWVEW 279
Cdd:cd01519 30 GKIPGAINIPLSSL--PDALALSEEEFEKKYGFPKPSKDKELIFYCKAGVrskAAAELARSL---GYENVGNYPGSWLDW 104
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
168-279 |
5.72e-10 |
|
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: 55.00 E-value: 5.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 168 DILENLDARRFQVVDARAAGRFQGtqpeprdgiepGHIPGSVNIPFTEFLTSEGLEKSPEEiqrlfqekkvdlsKPLVAT 247
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEYAA-----------GHIPGAINIPLSELEERAALLELDKD-------------KPIVVY 56
|
90 100 110
....*....|....*....|....*....|..
gi 20304123 248 CGSGVTACHVVLGAFLCGKPDVPVYDGSWVEW 279
Cdd:cd00158 57 CRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
165-285 |
1.99e-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: 48.43 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 165 THEDILENLDARRFQVVDARAAGRFQGtqpeprdgiepGHIPGSVNIPFTEFltsegleksPEEIQRLfqekkvDLSKPL 244
Cdd:COG0607 7 SPAELAELLESEDAVLLDVREPEEFAA-----------GHIPGAINIPLGEL---------AERLDEL------PKDKPI 60
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 20304123 245 VATCGSGVTACHVVlgAFLC--GKPDVPVYDGSWVEWYMRAQP 285
Cdd:COG0607 61 VVYCASGGRSAQAA--ALLRraGYTNVYNLAGGIEAWKAAGLP 101
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
11-146 |
3.45e-06 |
|
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: 44.96 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 11 VSAQWVAEALKSPRAsqplKLLDAswylpklgRDARrEFEERHIPGAAFFDIDRCSDHTSPYDhmlpsathfadyagslg 90
Cdd:COG0607 6 ISPAELAELLESEDA----VLLDV--------REPE-EFAAGHIPGAINIPLGELAERLDELP----------------- 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 20304123 91 vsAATHVVIYDGSdqGLYSAPRVWWMfRAFGHHSVSLLDGGFRYWLSQNLPISSGK 146
Cdd:COG0607 56 --KDKPIVVYCAS--GGRSAQAAALL-RRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
170-279 |
1.68e-05 |
|
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: 43.38 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 170 LENLDARRFQVVDARAAgrfqgtqPEPRDGIEP---GHIPGSVNIPFTEFL-TSEGLEK---SPEEIQRLFQEKKVDLSK 242
Cdd:cd01448 8 AEHLDDPDVRILDARWY-------LPDRDGRKEyleGHIPGAVFFDLDEDLdDKSPGPHmlpSPEEFAELLGSLGISNDD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 20304123 243 PLVA-TCGSGVTACHV--VLGAFlcGKPDVPVYDGSWVEW 279
Cdd:cd01448 81 TVVVyDDGGGFFAARAwwTLRYF--GHENVRVLDGGLQAW 118
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
44-135 |
1.69e-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: 39.59 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 44 DAR--REFEERHIPGAAFFDIDRcsdhtspydhmlpsathFADYAGSLGVSAATHVVIYDGSDQglySAPRVWWMFRAFG 121
Cdd:cd00158 15 DVRepEEYAAGHIPGAINIPLSE-----------------LEERAALLELDKDKPIVVYCRSGN---RSARAAKLLRKAG 74
|
90
....*....|....
gi 20304123 122 HHSVSLLDGGFRYW 135
Cdd:cd00158 75 GTNVYNLEGGMLAW 88
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
163-253 |
3.08e-04 |
|
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus lactis NADH oxidase, Bacillus cereus NADH dehydrogenase, and Bacteroides thetaiotaomicron pyridine nucleotide-disulphide oxidoreductase, and similar rhodanese-like domains found C-terminal of the pyridine nucleotide-disulphide oxidoreductase (Pyr-redox) domain and the Pyr-redox dimerization domain.
Pssm-ID: 238782 [Multi-domain] Cd Length: 90 Bit Score: 39.17 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 163 IKTHEdiLENLDARRFQVVDARAAGRFqgtqpeprdgiEPGHIPGSVNIPFtefltseglekspEEIQRLFQEkkVDLSK 242
Cdd:cd01524 1 VQWHE--LDNYRADGVTLIDVRTPQEF-----------EKGHIKGAINIPL-------------DELRDRLNE--LPKDK 52
|
90
....*....|.
gi 20304123 243 PLVATCGSGVT 253
Cdd:cd01524 53 EIIVYCAVGLR 63
|
|
| RHOD_Kc |
cd01525 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the ... |
163-274 |
5.02e-04 |
|
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the rhodanese-like domains found C-terminal of the serine/threonine protein kinases catalytic (S_TKc) domain and the Tre-2, BUB2p, Cdc16p (TBC) domain. The putative active site Cys residue is not present in this CD.
Pssm-ID: 238783 [Multi-domain] Cd Length: 105 Bit Score: 38.97 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 163 IKTHEDILENLDARRFqVVDARAAGRFqgtqpeprdgiEPGHIPGSVNIPFTEFLTSEGlekspeEIQRLFQEKKVDLSK 242
Cdd:cd01525 3 VYDVIRLLDNSPAKLA-AVDIRSSPDF-----------RRGHIEGSINIPFSSVFLKEG------ELEQLPTVPRLENYK 64
|
90 100 110
....*....|....*....|....*....|....
gi 20304123 243 PLVATCGSGVTACHVVLGAFL--CGKPDVPVYDG 274
Cdd:cd01525 65 GKIIVIVSHSHKHAALFAAFLvkCGVPRVCILDG 98
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
11-135 |
8.68e-04 |
|
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the second repeat. Only the second repeat contains the catalytically active Cys residue.
Pssm-ID: 238726 [Multi-domain] Cd Length: 118 Bit Score: 38.38 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 11 VSAQWVAEALKSPRAsqplKLLDAswylpklgRDARREFEER----------HIPGAAFFDIDRCSDHtspyDHMLPSAT 80
Cdd:cd01449 1 VTAEEVLANLDSGDV----QLVDA--------RSPERFRGEVpeprpglrsgHIPGAVNIPWTSLLDE----DGTFKSPE 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 20304123 81 HFADYAGSLGVSAATHVVIYDGSdqGLySAPRVWWMFRAFGHHSVSLLDGGFRYW 135
Cdd:cd01449 65 ELRALFAALGITPDKPVIVYCGS--GV-TACVLLLALELLGYKNVRLYDGSWSEW 116
|
|
| Cdc25_Acr2p |
cd01443 |
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ... |
151-250 |
1.34e-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: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20304123 151 PAEFCAQLDPSFikthedileNLDARRFQVVDARaagrfqgtqpepRDGIEPGHIPGSVNIPFTEFltsegLEKSPEEIQ 230
Cdd:cd01443 6 PEELVALLENSD---------SNAGKDFVVVDLR------------RDDYEGGHIKGSINLPAQSC-----YQTLPQVYA 59
|
90 100
....*....|....*....|
gi 20304123 231 RLFQEKKVDlskpLVATCGS 250
Cdd:cd01443 60 LFSLAGVKL----AIFYCGS 75
|
|
| |
