NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|145327743|ref|NP_001077847|]
View 

mercaptopyruvate sulfurtransferase 1 [Arabidopsis thaliana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02723 super family cl31924
3-mercaptopyruvate sulfurtransferase
 83-280 3.03e-157

3-mercaptopyruvate sulfurtransferase


The actual alignment was detected with superfamily member PLN02723:

Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 440.78  E-value: 3.03e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743  83 MFRVFGHEKVWVLDGGLPRWRASGYDVESSASGDAILKASAASEAIEKIYQGQTVSPITFQTKFQPHLVWTLDQVKNNME 162
Cdd:PLN02723 123 MFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAILKASAASEAIEKVYQGQTVSPITFQTKFQPHLVWTLEQVKKNIE 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 163 DPTYQHIDARSKARFDGTAPEPRKGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPIMASCGTGVTA 242
Cdd:PLN02723 203 DKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLPAEELKKRFEQEGISLDSPIVASCGTGVTA 282

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 145327743 243 CILAMGLHRLGKTDVPIYDGSWTEWATQPDLPIESVES 280
Cdd:PLN02723 283 CILALGLHRLGKTDVPVYDGSWTEWGALPDTPVATSTS 320
 
Name Accession Description Interval E-value
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 83-280 3.03e-157

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 440.78  E-value: 3.03e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743  83 MFRVFGHEKVWVLDGGLPRWRASGYDVESSASGDAILKASAASEAIEKIYQGQTVSPITFQTKFQPHLVWTLDQVKNNME 162
Cdd:PLN02723 123 MFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAILKASAASEAIEKVYQGQTVSPITFQTKFQPHLVWTLEQVKKNIE 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 163 DPTYQHIDARSKARFDGTAPEPRKGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPIMASCGTGVTA 242
Cdd:PLN02723 203 DKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLPAEELKKRFEQEGISLDSPIVASCGTGVTA 282

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 145327743 243 CILAMGLHRLGKTDVPIYDGSWTEWATQPDLPIESVES 280
Cdd:PLN02723 283 CILALGLHRLGKTDVPVYDGSWTEWGALPDTPVATSTS 320
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 83-276 5.53e-70

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 216.97  E-value: 5.53e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743  83 MFRVFGHEKVWVLDGGLPRWRASGYDVESSASgdailkasaaseaiekiyqgqTVSPITFQTKFQPHLVWTLDQVKNNME 162
Cdd:COG2897   92 LLRYAGHEDVRVLDGGLAAWKAAGLPLETGPP---------------------TPAPGDFTARPDPELLADADEVLAALG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 163 DPTYQHIDARSKARFDGTApEPRkGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPIMASCGTGVTA 242
Cdd:COG2897  151 DPDAVLVDARSPERYRGEV-EPI-DPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228

                        170       180       190
                 ....*....|....*....|....*....|....
gi 145327743 243 CILAMGLHRLGKTDVPIYDGSWTEWATQPDLPIE 276
Cdd:COG2897  229 AHTWLALELLGYPNVRLYDGSWSEWGSDPDLPVE 262
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 153-268 4.31e-56

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: 176.28  E-value: 4.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 153 TLDQVKNNMEDPTYQHIDARSKARFDGTAPEPRKGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPI 232
Cdd:cd01449    2 TAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKPV 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145327743 233 MASCGTGVTACILAMGLHRLGKTDVPIYDGSWTEWA 268
Cdd:cd01449   82 IVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWG 117
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 162-272 5.59e-20

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: 82.51  E-value: 5.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743   162 EDPTYQHIDARSKARFDGtapeprkgirsGHIPGSKCIPFPQMFDScNTLLPAEELKKRFDQEDISLDKPIMASCGTGVT 241
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELLDR-RGELDILEFEELLKRLGLDKDKPVVVYCRSGNR 68

                           90       100       110
                   ....*....|....*....|....*....|.
gi 145327743   242 ACILAMGLHRLGKTDVPIYDGSWTEWATQPD 272
Cdd:smart00450  69 SAKAAWLLRELGFKNVYLLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 161-268 1.99e-14

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: 67.51  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743  161 MEDPTYQHIDARSKARFDGtapeprkgirsGHIPGSKCIPFPQMFDSCNTLLPAEElkkrfDQEDISLDKPIMASCGTGV 240
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAK-----------GHIPGAVNVPLSSLSLPPLPLLELLE-----KLLELLKDKPIVVYCNSGN 64

                          90       100
                  ....*....|....*....|....*...
gi 145327743  241 TACILAMGLHRLGKTDVPIYDGSWTEWA 268
Cdd:pfam00581  65 RAAAAAALLKALGYKNVYVLDGGFEAWK 92
 
Name Accession Description Interval E-value
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 83-280 3.03e-157

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 440.78  E-value: 3.03e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743  83 MFRVFGHEKVWVLDGGLPRWRASGYDVESSASGDAILKASAASEAIEKIYQGQTVSPITFQTKFQPHLVWTLDQVKNNME 162
Cdd:PLN02723 123 MFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAILKASAASEAIEKVYQGQTVSPITFQTKFQPHLVWTLEQVKKNIE 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 163 DPTYQHIDARSKARFDGTAPEPRKGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPIMASCGTGVTA 242
Cdd:PLN02723 203 DKTYQHIDARSKARFDGAAPEPRKGIRSGHIPGSKCVPFPQMLDSSQTLLPAEELKKRFEQEGISLDSPIVASCGTGVTA 282

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 145327743 243 CILAMGLHRLGKTDVPIYDGSWTEWATQPDLPIESVES 280
Cdd:PLN02723 283 CILALGLHRLGKTDVPVYDGSWTEWGALPDTPVATSTS 320
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 83-276 5.53e-70

3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 216.97  E-value: 5.53e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743  83 MFRVFGHEKVWVLDGGLPRWRASGYDVESSASgdailkasaaseaiekiyqgqTVSPITFQTKFQPHLVWTLDQVKNNME 162
Cdd:COG2897   92 LLRYAGHEDVRVLDGGLAAWKAAGLPLETGPP---------------------TPAPGDFTARPDPELLADADEVLAALG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 163 DPTYQHIDARSKARFDGTApEPRkGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPIMASCGTGVTA 242
Cdd:COG2897  151 DPDAVLVDARSPERYRGEV-EPI-DPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSGVRA 228

                        170       180       190
                 ....*....|....*....|....*....|....
gi 145327743 243 CILAMGLHRLGKTDVPIYDGSWTEWATQPDLPIE 276
Cdd:COG2897  229 AHTWLALELLGYPNVRLYDGSWSEWGSDPDLPVE 262
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 153-268 4.31e-56

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: 176.28  E-value: 4.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 153 TLDQVKNNMEDPTYQHIDARSKARFDGTAPEPRKGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPI 232
Cdd:cd01449    2 TAEEVLANLDSGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAALGITPDKPV 81

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145327743 233 MASCGTGVTACILAMGLHRLGKTDVPIYDGSWTEWA 268
Cdd:cd01449   82 IVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEWG 117
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 83-276 1.30e-45

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 154.87  E-value: 1.30e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743  83 MFRVFGHEKVWVLDGGLPRWRASGYDVESsasGDAilkasaaseaiekiyqgqTVSPITFQTKFQPHLVWTLDQVKNNME 162
Cdd:PRK11493 107 MLRTFGVEKVSILAGGLAGWQRDDLLLEE---GAV------------------ELPEGEFNAAFNPEAVVRLTDVLLASH 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 163 DPTYQHIDARSKARFDGTAPEPRKGIRSGHIPGSKCIPFPQMFdSCNTLLPAEELKKRFDQEDISLDKPIMASCGTGVTA 242
Cdd:PRK11493 166 EKTAQIVDARPAARFNAEVDEPRPGLRRGHIPGALNVPWTELV-REGELKTTDELDAIFFGRGVSFDRPIIASCGSGVTA 244

                        170       180       190
                 ....*....|....*....|....*....|....
gi 145327743 243 CILAMGLHRLGKTDVPIYDGSWTEWATQPDLPIE 276
Cdd:PRK11493 245 AVVVLALATLDVPNVKLYDGAWSEWGARADLPVE 278
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 162-272 5.59e-20

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: 82.51  E-value: 5.59e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743   162 EDPTYQHIDARSKARFDGtapeprkgirsGHIPGSKCIPFPQMFDScNTLLPAEELKKRFDQEDISLDKPIMASCGTGVT 241
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEG-----------GHIPGAVNIPLSELLDR-RGELDILEFEELLKRLGLDKDKPVVVYCRSGNR 68

                           90       100       110
                   ....*....|....*....|....*....|.
gi 145327743   242 ACILAMGLHRLGKTDVPIYDGSWTEWATQPD 272
Cdd:smart00450  69 SAKAAWLLRELGFKNVYLLDGGYKEWSAAGP 99
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 152-267 1.41e-16

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: 74.44  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 152 WTLDQVKNNMEDPTYQHIDAR--------SKARFDGTAPEPRK-GIRSGHIPGSKCIPFPQMFDSCN---TLLPAE-ELK 218
Cdd:cd01445    5 QLAENLEAGKVGKGFQLLDARaqspgtreARGEYLETQPEPDAvGLDSGHIPGASFFDFEECLDEAGfeeSMEPSEaEFA 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145327743 219 KRFDQEDISLDKPIMASCG---TGVTACILAMGLHRLGKTDVPIYDGSWTEW 267
Cdd:cd01445   85 AMFEAKGIDLDKHLIATDGddlGGFTACHIALAARLCGHPDVAILDGGFFEW 136
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 161-268 1.99e-14

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: 67.51  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743  161 MEDPTYQHIDARSKARFDGtapeprkgirsGHIPGSKCIPFPQMFDSCNTLLPAEElkkrfDQEDISLDKPIMASCGTGV 240
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAK-----------GHIPGAVNVPLSSLSLPPLPLLELLE-----KLLELLKDKPIVVYCNSGN 64

                          90       100
                  ....*....|....*....|....*...
gi 145327743  241 TACILAMGLHRLGKTDVPIYDGSWTEWA 268
Cdd:pfam00581  65 RAAAAAALLKALGYKNVYVLDGGFEAWK 92
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 156-268 9.21e-12

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: 60.01  E-value: 9.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 156 QVKNNMEDPTYQHIDARSKARFDgtapeprkgirSGHIPGSKCIPFPqmfdscntllpaeELKKRFDQEDISLDKPIMAS 235
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYA-----------AGHIPGAINIPLS-------------ELEERAALLELDKDKPIVVY 56

                         90       100       110
                 ....*....|....*....|....*....|...
gi 145327743 236 CGTGVTACILAMGLHRLGKTDVPIYDGSWTEWA 268
Cdd:cd00158   57 CRSGNRSARAAKLLRKAGGTNVYNLEGGMLAWK 89
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 152-269 1.49e-10

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: 57.28  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 152 WTLDQVKN-NMEDPTYQHIDARskarfdgtapEPRKgIRSGHIPGSKCIPFPQMFDSCNtlLPAEELKKRFDQEDISLDK 230
Cdd:cd01519    1 YSFEEVKNlPNPHPNKVLIDVR----------EPEE-LKTGKIPGAINIPLSSLPDALA--LSEEEFEKKYGFPKPSKDK 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 145327743 231 PIMASCGTGV---TACILAMglhRLGKTDVPIYDGSWTEWAT 269
Cdd:cd01519   68 ELIFYCKAGVrskAAAELAR---SLGYENVGNYPGSWLDWAA 106
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 152-277 2.90e-10

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: 56.13  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 152 WTLDQVKNNMEDPTYQHIDARSKARFDgtapeprkgirSGHIPGSKCIPFpqmfdscntllpaEELKKRFDQedISLDKP 231
Cdd:COG0607    6 ISPAELAELLESEDAVLLDVREPEEFA-----------AGHIPGAINIPL-------------GELAERLDE--LPKDKP 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 145327743 232 IMASCGTGVTACILAMGLHRLGKTDVPIYDGSWTEWATQpDLPIES 277
Cdd:COG0607   60 IVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAA-GLPVEK 104
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 83-276 4.13e-08

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 53.97  E-value: 4.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743  83 MFRVFGHEKVWVLDGGLPRWRAsgydvessasgdailKASAASEAIEKIYQGqtvsPITFQTKFQPhlVWTLDQVKNNME 162
Cdd:PRK09629 101 LLDVIGHSGYHYLDGGVLAWEA---------------QALPLSTDVPPVAGG----PVTLTLHDEP--TATREYLQSRLG 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 163 DPTYQHIDARSKARFDGTAPEPRKGirsGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPIMASCGTGVTA 242
Cdd:PRK09629 160 AADLAIWDARAPTEYSGEKVVAAKG---GHIPGAVNFEWTAGMDKARNLRIRQDMPEILRDLGITPDKEVITHCQTHHRS 236

                        170       180       190
                 ....*....|....*....|....*....|....
gi 145327743 243 CILAMGLHRLGKTDVPIYDGSWTEWATQPDLPIE 276
Cdd:PRK09629 237 GFTYLVAKALGYPRVKAYAGSWGEWGNHPDTPVE 270
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 83-106 1.57e-07

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: 49.15  E-value: 1.57e-07
                         10        20
                 ....*....|....*....|....
gi 145327743  83 MFRVFGHEKVWVLDGGLPRWRASG 106
Cdd:cd01448   99 TLRYFGHENVRVLDGGLQAWKAEG 122
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 153-267 1.30e-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: 43.76  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145327743 153 TLDQVKNNMEDPTYQHIDARskarFDGTAPEPRKGIRSGHIPGSKCIPFPQMFDSC----NTLLPAEELKKRFDQEDISL 228
Cdd:cd01448    3 SPDWLAEHLDDPDVRILDAR----WYLPDRDGRKEYLEGHIPGAVFFDLDEDLDDKspgpHMLPSPEEFAELLGSLGISN 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 145327743 229 DKPIMA-SCGTGVTACILAMGLHRLGKTDVPIYDGSWTEW 267
Cdd:cd01448   79 DDTVVVyDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAW 118
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 166-241 3.99e-03

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: 35.70  E-value: 3.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145327743 166 YQHIDARSKARFdgtapeprkgiRSGHIPGSKCIPFpqmfdscntllpaEELKKRFDQedISLDKPIMASCGTGVT 241
Cdd:cd01524   14 VTLIDVRTPQEF-----------EKGHIKGAINIPL-------------DELRDRLNE--LPKDKEIIVYCAVGLR 63
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 83-108 8.32e-03

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: 35.13  E-value: 8.32e-03
                           10        20
                   ....*....|....*....|....*.
gi 145327743    83 MFRVFGHEKVWVLDGGLPRWRASGYD 108
Cdd:smart00450  75 LLRELGFKNVYLLDGGYKEWSAAGPP 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH