|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
165-424 |
1.96e-81 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 251.63 E-value: 1.96e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 165 AGDWKVIEAAW---GAPKLYLLSHIPGAGYIDTNEV----ESEPLWNKVSDDRLKTMLAKHGIRHDTTVILYGRDV-YAA 236
Cdd:COG2897 7 DPDVVILDVRWdlpDGRAAYEAGHIPGAVFLDLDTDlsdpRSPGRHPLPSPEAFAALLGALGISNDTTVVVYDDGGgLFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 237 ARVAQIMLYAGVKDVRILDGGWKAWSDAGLPVERGTPanvTPAP-EFGAPIpgQPQLMVDMDQARGMLHRQDASLVSIRS 315
Cdd:COG2897 87 ARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPP---TPAPgDFTARP--DPELLADADEVLAALGDPDAVLVDARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 316 WPEFIGETSgySYIKPKGEIAGARWghagsdaTHMEDFHNPDGTMRSADDIAAMWKTWHILPEQQVAFYCGTGWRASETF 395
Cdd:COG2897 162 PERYRGEVE--PIDPRAGHIPGAVN-------LPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTW 232
|
250 260
....*....|....*....|....*....
gi 695703173 396 MYARAMGWKNVAVYDGGWYEWSSHPQNPV 424
Cdd:COG2897 233 LALELLGYPNVRLYDGSWSEWGSDPDLPV 261
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
294-418 |
6.90e-38 |
|
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: 133.53 E-value: 6.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 294 VDMDQARGMLHRQDASLVSIRSWPEFIGETSGYSYIKPKGEIAGARWGHAGsdathmeDFHNPDGTMRSADDIAAMWKTW 373
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWT-------SLLDEDGTFKSPEELRALFAAL 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 695703173 374 HILPEQQVAFYCGTGWRASETFMYARAMGWKNVAVYDGGWYEWSS 418
Cdd:cd01449 74 GITPDKPVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
137-426 |
7.61e-19 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 86.78 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 137 QRLPHFEQLVYPQWI-QRLQQGktvtaapagDWKVIEAAWGAP-------KLYLLSHIPGAGYIDTNeveseplwnKVSD 208
Cdd:PLN02723 15 QSISTNEPVVSVDWLhANLREP---------DVKVLDASWYMPdeqrnpiQEYQVAHIPGALFFDLD---------GISD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 209 DR--LKTMLAKH----------GIRHDTTVILY-GRDVYAAARVAQIMLYAGVKDVRILDGGWKAWSDAGLPVERGTPAN 275
Cdd:PLN02723 77 RTtdLPHMLPSEeafaaavsalGIENKDGVVVYdGKGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 276 ----------VTPAPEFGAPIPG-------QPQLMVDMDQARGMLHRQDASLVSIRSWPEFIGETSgysyiKPKgeiAGA 338
Cdd:PLN02723 157 ailkasaaseAIEKVYQGQTVSPitfqtkfQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAP-----EPR---KGI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 339 RWGHA-GSDATHMEDFHNPDGTMRSADDIAAMWKTWHILPEQQVAFYCGTGWRASETFMYARAMGWKNVAVYDGGWYEWS 417
Cdd:PLN02723 229 RSGHIpGSKCVPFPQMLDSSQTLLPAEELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEWG 308
|
....*....
gi 695703173 418 SHPQNPVTT 426
Cdd:PLN02723 309 ALPDTPVAT 317
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
165-267 |
2.12e-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: 77.11 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 165 AGDWKVIEAAWgaPKLYLLSHIPGAGYIDTNEVESEPLWNKVSDdrLKTMLAKHGIRHDTTVILYGRDVYAAARVAQIML 244
Cdd:smart00450 2 DEKVVLLDVRS--PEEYEGGHIPGAVNIPLSELLDRRGELDILE--FEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLR 77
|
90 100
....*....|....*....|...
gi 695703173 245 YAGVKDVRILDGGWKAWSDAGLP 267
Cdd:smart00450 78 ELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
303-417 |
2.12e-12 |
|
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: 62.89 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 303 LHRQDASLVSIRSWPEFIgetsgysyikpKGEIAGARwghagsdatHMedfhNPDGTMRSADDIAAMWKTW-HILPEQQV 381
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYA-----------KGHIPGAV---------NV----PLSSLSLPPLPLLELLEKLlELLKDKPI 56
|
90 100 110
....*....|....*....|....*....|....*.
gi 695703173 382 AFYCGTGWRASETFMYARAMGWKNVAVYDGGWYEWS 417
Cdd:pfam00581 57 VVYCNSGNRAAAAAALLKALGYKNVYVLDGGFEAWK 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
165-424 |
1.96e-81 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 251.63 E-value: 1.96e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 165 AGDWKVIEAAW---GAPKLYLLSHIPGAGYIDTNEV----ESEPLWNKVSDDRLKTMLAKHGIRHDTTVILYGRDV-YAA 236
Cdd:COG2897 7 DPDVVILDVRWdlpDGRAAYEAGHIPGAVFLDLDTDlsdpRSPGRHPLPSPEAFAALLGALGISNDTTVVVYDDGGgLFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 237 ARVAQIMLYAGVKDVRILDGGWKAWSDAGLPVERGTPanvTPAP-EFGAPIpgQPQLMVDMDQARGMLHRQDASLVSIRS 315
Cdd:COG2897 87 ARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPP---TPAPgDFTARP--DPELLADADEVLAALGDPDAVLVDARS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 316 WPEFIGETSgySYIKPKGEIAGARWghagsdaTHMEDFHNPDGTMRSADDIAAMWKTWHILPEQQVAFYCGTGWRASETF 395
Cdd:COG2897 162 PERYRGEVE--PIDPRAGHIPGAVN-------LPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRAAHTW 232
|
250 260
....*....|....*....|....*....
gi 695703173 396 MYARAMGWKNVAVYDGGWYEWSSHPQNPV 424
Cdd:COG2897 233 LALELLGYPNVRLYDGSWSEWGSDPDLPV 261
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
294-418 |
6.90e-38 |
|
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: 133.53 E-value: 6.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 294 VDMDQARGMLHRQDASLVSIRSWPEFIGETSGYSYIKPKGEIAGARWGHAGsdathmeDFHNPDGTMRSADDIAAMWKTW 373
Cdd:cd01449 1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWT-------SLLDEDGTFKSPEELRALFAAL 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 695703173 374 HILPEQQVAFYCGTGWRASETFMYARAMGWKNVAVYDGGWYEWSS 418
Cdd:cd01449 74 GITPDKPVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWGS 118
|
|
| TST_Repeat_1 |
cd01448 |
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ... |
145-265 |
4.06e-27 |
|
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: 104.62 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 145 LVYPQWIQRLQQGKtvtaapagDWKVIEAAW-----GAPKLYLLSHIPGAGYIDTNEVES---EPLWNKVSDDRLKTMLA 216
Cdd:cd01448 1 LVSPDWLAEHLDDP--------DVRILDARWylpdrDGRKEYLEGHIPGAVFFDLDEDLDdksPGPHMLPSPEEFAELLG 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 695703173 217 KHGIRHDTTVILYGRD-VYAAARVAQIMLYAGVKDVRILDGGWKAWSDAG 265
Cdd:cd01448 73 SLGISNDDTVVVYDDGgGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
|
|
| PLN02723 |
PLN02723 |
3-mercaptopyruvate sulfurtransferase |
137-426 |
7.61e-19 |
|
3-mercaptopyruvate sulfurtransferase
Pssm-ID: 178324 [Multi-domain] Cd Length: 320 Bit Score: 86.78 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 137 QRLPHFEQLVYPQWI-QRLQQGktvtaapagDWKVIEAAWGAP-------KLYLLSHIPGAGYIDTNeveseplwnKVSD 208
Cdd:PLN02723 15 QSISTNEPVVSVDWLhANLREP---------DVKVLDASWYMPdeqrnpiQEYQVAHIPGALFFDLD---------GISD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 209 DR--LKTMLAKH----------GIRHDTTVILY-GRDVYAAARVAQIMLYAGVKDVRILDGGWKAWSDAGLPVERGTPAN 275
Cdd:PLN02723 77 RTtdLPHMLPSEeafaaavsalGIENKDGVVVYdGKGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 276 ----------VTPAPEFGAPIPG-------QPQLMVDMDQARGMLHRQDASLVSIRSWPEFIGETSgysyiKPKgeiAGA 338
Cdd:PLN02723 157 ailkasaaseAIEKVYQGQTVSPitfqtkfQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAP-----EPR---KGI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 339 RWGHA-GSDATHMEDFHNPDGTMRSADDIAAMWKTWHILPEQQVAFYCGTGWRASETFMYARAMGWKNVAVYDGGWYEWS 417
Cdd:PLN02723 229 RSGHIpGSKCVPFPQMLDSSQTLLPAEELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEWG 308
|
....*....
gi 695703173 418 SHPQNPVTT 426
Cdd:PLN02723 309 ALPDTPVAT 317
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
165-267 |
2.12e-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: 77.11 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 165 AGDWKVIEAAWgaPKLYLLSHIPGAGYIDTNEVESEPLWNKVSDdrLKTMLAKHGIRHDTTVILYGRDVYAAARVAQIML 244
Cdd:smart00450 2 DEKVVLLDVRS--PEEYEGGHIPGAVNIPLSELLDRRGELDILE--FEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLR 77
|
90 100
....*....|....*....|...
gi 695703173 245 YAGVKDVRILDGGWKAWSDAGLP 267
Cdd:smart00450 78 ELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| sseA |
PRK11493 |
3-mercaptopyruvate sulfurtransferase; Provisional |
181-427 |
4.88e-15 |
|
3-mercaptopyruvate sulfurtransferase; Provisional
Pssm-ID: 236917 [Multi-domain] Cd Length: 281 Bit Score: 75.13 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 181 YLLSHIPGAGYIDTnevesEPLWNKVSD--------DRLKTMLAKHGIRHDTTVILYGR-DVYAAARVAQIMLYAGVKDV 251
Cdd:PRK11493 42 YRAGHIPGAVFFDI-----EALSDHTSPlphmmprpETFAVAMRELGVNQDKHLVVYDEgNLFSAPRAWWMLRTFGVEKV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 252 RILDGGWKAWSDAGLPVERGtpaNVTPAP-EFGAPIpgQPQLMVDMDQARGMLHRQDASLVSIRSWPEFIGETSgysyiK 330
Cdd:PRK11493 117 SILAGGLAGWQRDDLLLEEG---AVELPEgEFNAAF--NPEAVVRLTDVLLASHEKTAQIVDARPAARFNAEVD-----E 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 331 PKgeiAGARWGH-AGSDATHMEDFHNpDGTMRSADDIAAmwktwhILPEQQVAFY------CGTGWRASETFMYARAMGW 403
Cdd:PRK11493 187 PR---PGLRRGHiPGALNVPWTELVR-EGELKTTDELDA------IFFGRGVSFDrpiiasCGSGVTAAVVVLALATLDV 256
|
250 260
....*....|....*....|....
gi 695703173 404 KNVAVYDGGWYEWSSHPQNPVTTG 427
Cdd:PRK11493 257 PNVKLYDGAWSEWGARADLPVEPA 280
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
304-420 |
5.65e-15 |
|
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: 70.18 E-value: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 304 HRQDASLVSIRSWPEFIGetsgysyikpkGEIAGARWGHAGSDATHMEDFHNPDgtmrsaddIAAMWKTWHILPEQQVAF 383
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELLDRRGELDILE--------FEELLKRLGLDKDKPVVV 61
|
90 100 110
....*....|....*....|....*....|....*..
gi 695703173 384 YCGTGWRASETFMYARAMGWKNVAVYDGGWYEWSSHP 420
Cdd:smart00450 62 YCRSGNRSAKAAWLLRELGFKNVYLLDGGYKEWSAAG 98
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
303-417 |
2.12e-12 |
|
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: 62.89 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 303 LHRQDASLVSIRSWPEFIgetsgysyikpKGEIAGARwghagsdatHMedfhNPDGTMRSADDIAAMWKTW-HILPEQQV 381
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYA-----------KGHIPGAV---------NV----PLSSLSLPPLPLLELLEKLlELLKDKPI 56
|
90 100 110
....*....|....*....|....*....|....*.
gi 695703173 382 AFYCGTGWRASETFMYARAMGWKNVAVYDGGWYEWS 417
Cdd:pfam00581 57 VVYCNSGNRAAAAAALLKALGYKNVYVLDGGFEAWK 92
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
181-262 |
3.17e-12 |
|
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: 62.12 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 181 YLLSHIPGAGYIDTNEVESEPLWNKVSDDRLKTMLakhgirHDTTVILYGRDVYAAARVAQIMLYAGVKDVRILDGGWKA 260
Cdd:pfam00581 17 YAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLELL------KDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLDGGFEA 90
|
..
gi 695703173 261 WS 262
Cdd:pfam00581 91 WK 92
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
185-272 |
8.05e-12 |
|
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: 61.52 E-value: 8.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 185 HIPGAGYIDTNEVEseplwnkvsdDRLKTmlakhgIRHDTTVILYGRDVYAAARVAQIMLYAGVKDVRILDGGWKAWSDA 264
Cdd:COG0607 35 HIPGAINIPLGELA----------ERLDE------LPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAA 98
|
....*...
gi 695703173 265 GLPVERGT 272
Cdd:COG0607 99 GLPVEKGK 106
|
|
| PRK09629 |
PRK09629 |
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional |
181-424 |
2.13e-10 |
|
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
Pssm-ID: 104071 [Multi-domain] Cd Length: 610 Bit Score: 62.83 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 181 YLLSHIPGAGYIDTNEVE--SEPLWNKVSDDR-LKTMLAKHGIRHDTTVILYGRDVYA-AARVAQIMLYAGVKDVRILDG 256
Cdd:PRK09629 36 YEAGHIRGARFVDPKRTQlgKPPAPGLLPDTAdLEQLFGELGHNPDAVYVVYDDEGGGwAGRFIWLLDVIGHSGYHYLDG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 257 GWKAWSDAGLPVERGTPanvtpaPEFGAPIP----GQPQLMVDMDQARgmLHRQDASLVSIRSWPEFIGEtsgysyikpk 332
Cdd:PRK09629 116 GVLAWEAQALPLSTDVP------PVAGGPVTltlhDEPTATREYLQSR--LGAADLAIWDARAPTEYSGE---------- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 333 gEIAGARWGHAgSDATHMEDFHNPDGT--MRSADDIAAMWKTWHILPEQQVAFYCGTGWRASETFMYARAMGWKNVAVYD 410
Cdd:PRK09629 178 -KVVAAKGGHI-PGAVNFEWTAGMDKArnLRIRQDMPEILRDLGITPDKEVITHCQTHHRSGFTYLVAKALGYPRVKAYA 255
|
250
....*....|....
gi 695703173 411 GGWYEWSSHPQNPV 424
Cdd:PRK09629 256 GSWGEWGNHPDTPV 269
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
294-428 |
1.38e-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: 49.58 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 294 VDMDQARGMLHRQDASLVSIRSWPEFigetsgysyikPKGEIAGARwghagsdathmedfHNPDGTMRS-ADDIAamwkt 372
Cdd:COG0607 6 ISPAELAELLESEDAVLLDVREPEEF-----------AAGHIPGAI--------------NIPLGELAErLDELP----- 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 695703173 373 whilPEQQVAFYCGTGWRASETFMYARAMGWKNVAVYDGGWYEWSSHpQNPVTTGE 428
Cdd:COG0607 56 ----KDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAA-GLPVEKGK 106
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
298-416 |
3.51e-07 |
|
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: 47.68 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 298 QARGMLHRQDASLVSIRSWPEFIgetsgysyikpKGEIAGARwghagsdathmedfHNPdgtmrsADDIAAMWKTWHILP 377
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEYA-----------AGHIPGAI--------------NIP------LSELEERAALLELDK 49
|
90 100 110
....*....|....*....|....*....|....*....
gi 695703173 378 EQQVAFYCGTGWRASETFMYARAMGWKNVAVYDGGWYEW 416
Cdd:cd00158 50 DKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
294-416 |
1.26e-06 |
|
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.
Pssm-ID: 238724 [Multi-domain] Cd Length: 103 Bit Score: 46.65 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 294 VDMDQARGMLHRQDASLVSIRSWPEfigetsgysyIKPKGEIAGArwghagsdathmedFHNPDGTMRSADDIAAMWKTW 373
Cdd:cd01447 1 LSPEDARALLGSPGVLLVDVRDPRE----------LERTGMIPGA--------------FHAPRGMLEFWADPDSPYHKP 56
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 695703173 374 HILPEQQVAFYCGTGWRASETFMYARAMGWKNVAVYDGGWYEW 416
Cdd:cd01447 57 AFAEDKPFVFYCASGWRSALAGKTLQDMGLKPVYNIEGGFKDW 99
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
178-261 |
1.80e-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: 45.75 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 178 PKLYLLSHIPGAGYIdtnevesePLwnkvsdDRLKTMLAKHGIRHDTTVILYGRDVYAAARVAQIMLYAGVKDVRILDGG 257
Cdd:cd00158 19 PEEYAAGHIPGAINI--------PL------SELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGG 84
|
....
gi 695703173 258 WKAW 261
Cdd:cd00158 85 MLAW 88
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
181-293 |
2.33e-06 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 49.24 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 181 YLLSHIPGAGYIDTNEVESEPlwnkvsddrlktmlAKHGIRHDTTVILY----GRDVYAAARVAQimlyAGVKDVRILDG 256
Cdd:PRK08762 29 RASGQAEGALRIPRGFLELRI--------------ETHLPDRDREIVLIcasgTRSAHAAATLRE----LGYTRVASVAG 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 695703173 257 GWKAWSDAGLPVERgtPANVTPA-----------PEFGapIPGQPQLM 293
Cdd:PRK08762 91 GFSAWKDAGLPLER--PRLLTDEqderysrhlrlPEVG--EEGQRRLL 134
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
377-418 |
6.53e-06 |
|
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: 44.57 E-value: 6.53e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 695703173 377 PEQQVAFYCGTGWRASETFMYARAMGWKNVAVYDGGWYEWSS 418
Cdd:cd01519 65 KDKELIFYCKAGVRSKAAAELARSLGYENVGNYPGSWLDWAA 106
|
|
| TST_Repeats |
cd01445 |
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ... |
185-261 |
1.14e-05 |
|
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: 44.78 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695703173 185 HIPGAGYIDTNEVESEPLWNKV---SDDRLKTMLAKHGIRHDTTVILYGRDV---YAAARVAQIMLYAGVKDVRILDGGW 258
Cdd:cd01445 54 HIPGASFFDFEECLDEAGFEESmepSEAEFAAMFEAKGIDLDKHLIATDGDDlggFTACHIALAARLCGHPDVAILDGGF 133
|
...
gi 695703173 259 KAW 261
Cdd:cd01445 134 FEW 136
|
|
| TST_Repeat_2 |
cd01449 |
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ... |
185-262 |
1.72e-05 |
|
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: 43.78 E-value: 1.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695703173 185 HIPGAGYID-TNEVESEPLWnkVSDDRLKTMLAKHGIRHDTTVILYGRDVYAAARVAQIMLYAGVKDVRILDGGWKAWS 262
Cdd:cd01449 41 HIPGAVNIPwTSLLDEDGTF--KSPEELRALFAALGITPDKPVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWG 117
|
|
| 4RHOD_Repeat_4 |
cd01535 |
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ... |
234-271 |
4.30e-03 |
|
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 4th repeat which, in general, contains the putative catalytic Cys residue.
Pssm-ID: 238793 [Multi-domain] Cd Length: 145 Bit Score: 37.49 E-value: 4.30e-03
10 20 30
....*....|....*....|....*....|....*...
gi 695703173 234 YAAARVAQImlyaGVKDVRILDGGWKAWSDAGLPVERG 271
Cdd:cd01535 64 FAAADLAAL----TVKPVFVLEGGTAAWIAAGLPVESG 97
|
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