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Conserved domains on  [gi|1958787605|ref|XP_038934288|]
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3-mercaptopyruvate sulfurtransferase isoform X2 [Rattus norvegicus]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 10106650)

rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present; similar to Caenorhabditis elegans thiosulfate sulfurtransferase mpst-4

PubMed:  8702871

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 10-139 2.42e-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: 165.87  E-value: 2.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  10 LVSAQWVAEALKSPRasqpLKLLDASWYLPklGRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGSL 89
Cdd:cd01448     1 LVSPDWLAEHLDDPD----VRILDARWYLP--DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958787605  90 GVSAATHVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQN 139
Cdd:cd01448    75 GISNDDTVVVYD--DGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
 
Name Accession Description Interval E-value
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 10-139 2.42e-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: 165.87  E-value: 2.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  10 LVSAQWVAEALKSPRasqpLKLLDASWYLPklGRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGSL 89
Cdd:cd01448     1 LVSPDWLAEHLDDPD----VRILDARWYLP--DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958787605  90 GVSAATHVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQN 139
Cdd:cd01448    75 GISNDDTVVVYD--DGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 16-179 2.08e-52

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 168.43  E-value: 2.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  16 VAEALKSPrasqPLKLLDASWYLPklgrDARREFEERHIPGAAFFDIDRC-SDHTSPYDHMLPSATHFADYAGSLGVSAA 94
Cdd:COG2897     1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  95 THVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISSGKSPSEPAEFCAQLDPSFIKTHEDILENLD 174
Cdd:COG2897    73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150


                  ....*
gi 1958787605 175 ARRFQ 179
Cdd:COG2897   151 DPDAV 155
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 11-180 4.36e-46

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 152.94  E-value: 4.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  11 VSAQWVAEALKSPRasqpLKLLDASWYLPKL-GRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGSL 89
Cdd:PRK11493    7 VAADWLAEHIDDPE----IQIIDARMAPPGQeDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMREL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  90 GVSAATHVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISSGKSPSEPAEFCAQLDPSFIKTHEDI 169
Cdd:PRK11493   83 GVNQDKHLVVYD--EGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDV 160

                         170       180
                  ....*....|....*....|..
gi 1958787605 170 L--------ENLDAR---RFQA 180
Cdd:PRK11493  161 LlashektaQIVDARpaaRFNA 182
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 44-141 6.14e-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: 74.80  E-value: 6.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605   44 DARR--EFEERHIPGAAFFDIDRCSDHTSPYDHMlpsatHFADYAGSLGVSAATHVVIYDGSDqglYSAPRVWWMFRAFG 121
Cdd:smart00450   9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 1958787605  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 3.54e-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: 59.81  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  44 DARR--EFEERHIPGAAFFDIDrcsdhtSPYDHMLPSATHFADYAGSLGvsaATHVVIYDGSDQglySAPRVWWMFRAFG 121
Cdd:pfam00581  10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77

                          90
                  ....*....|....
gi 1958787605 122 HHSVSLLDGGFRYW 135
Cdd:pfam00581  78 YKNVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 10-139 2.42e-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: 165.87  E-value: 2.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  10 LVSAQWVAEALKSPRasqpLKLLDASWYLPklGRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGSL 89
Cdd:cd01448     1 LVSPDWLAEHLDDPD----VRILDARWYLP--DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958787605  90 GVSAATHVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQN 139
Cdd:cd01448    75 GISNDDTVVVYD--DGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 16-179 2.08e-52

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 168.43  E-value: 2.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  16 VAEALKSPrasqPLKLLDASWYLPklgrDARREFEERHIPGAAFFDIDRC-SDHTSPYDHMLPSATHFADYAGSLGVSAA 94
Cdd:COG2897     1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  95 THVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISSGKSPSEPAEFCAQLDPSFIKTHEDILENLD 174
Cdd:COG2897    73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150


                  ....*
gi 1958787605 175 ARRFQ 179
Cdd:COG2897   151 DPDAV 155
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 11-180 4.36e-46

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 152.94  E-value: 4.36e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  11 VSAQWVAEALKSPRasqpLKLLDASWYLPKL-GRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGSL 89
Cdd:PRK11493    7 VAADWLAEHIDDPE----IQIIDARMAPPGQeDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMREL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  90 GVSAATHVVIYDgsDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISSGKSPSEPAEFCAQLDPSFIKTHEDI 169
Cdd:PRK11493   83 GVNQDKHLVVYD--EGNLFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDV 160

                         170       180
                  ....*....|....*....|..
gi 1958787605 170 L--------ENLDAR---RFQA 180
Cdd:PRK11493  161 LlashektaQIVDARpaaRFNA 182
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 9-179 1.60e-45

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 152.26  E-value: 1.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605   9 ALVSAQWVAEALKSPRasqpLKLLDASWYLPKLGRDARREFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGS 88
Cdd:PLN02723   22 PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGISDRTTDLPHMLPSEEAFAAAVSA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  89 LGVSAATHVVIYDGsdQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISS---------GKSPSE--------- 150
Cdd:PLN02723   98 LGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESsasgdailkASAASEaiekvyqgq 175

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1958787605 151 ---PAEFCAQLDPSFIKTHEDILENLDARRFQ 179
Cdd:PLN02723  176 tvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQ 207
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 11-136 8.23e-41

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: 134.92  E-value: 8.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  11 VSAQWVAEALKSPRASQPLKLLDASWYLPKLgRDARREF------------EERHIPGAAFFDIDRCSDHTSPYDHMLPS 78
Cdd:cd01445     1 KSTEQLAENLEAGKVGKGFQLLDARAQSPGT-REARGEYletqpepdavglDSGHIPGASFFDFEECLDEAGFEESMEPS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958787605  79 ATHFADYAGSLGVSAATHVVIYDGSDQGLYSAPRVWWMFRAFGHHSVSLLDGGFRYWL 136
Cdd:cd01445    80 EAEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWF 137
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 44-141 6.14e-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: 74.80  E-value: 6.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605   44 DARR--EFEERHIPGAAFFDIDRCSDHTSPYDHMlpsatHFADYAGSLGVSAATHVVIYDGSDqglYSAPRVWWMFRAFG 121
Cdd:smart00450   9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 1958787605  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 3.54e-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: 59.81  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  44 DARR--EFEERHIPGAAFFDIDrcsdhtSPYDHMLPSATHFADYAGSLGvsaATHVVIYDGSDQglySAPRVWWMFRAFG 121
Cdd:pfam00581  10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77

                          90
                  ....*....|....
gi 1958787605 122 HHSVSLLDGGFRYW 135
Cdd:pfam00581  78 YKNVYVLDGGFEAW 91
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 29-148 4.76e-10

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 57.82  E-value: 4.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  29 LKLLDA-SWYLPKLGRDARreFEERHIPGAAFFDIDRCSDHTSPYDHMLPSATHFADYAGSLGVSAATHVVIYDgsDQGL 107
Cdd:PRK09629   17 LERLDApELILVDLTSSAR--YEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVYD--DEGG 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1958787605 108 YSAPRVWWMFRAFGHHSVSLLDGGFRYWLSQNLPISSGKSP 148
Cdd:PRK09629   93 GWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPP 133
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 11-146 1.75e-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: 44.57  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  11 VSAQWVAEALKSPRAsqplKLLDAswylpklgRDARrEFEERHIPGAAFFDIDRCSDHTSPYDhmlpsathfadyagslg 90
Cdd:COG0607     6 ISPAELAELLESEDA----VLLDV--------REPE-EFAAGHIPGAINIPLGELAERLDELP----------------- 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958787605  91 vsAATHVVIYDGSdqGLYSAPRVWWMfRAFGHHSVSLLDGGFRYWLSQNLPISSGK 146
Cdd:COG0607    56 --KDKPIVVYCAS--GGRSAQAAALL-RRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 44-135 7.91e-05

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: 39.98  E-value: 7.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  44 DAR--REFEERHIPGAAFFDIDRcsdhtspydhmlpsathFADYAGSLGVSAATHVVIYDGSDQglySAPRVWWMFRAFG 121
Cdd:cd00158    15 DVRepEEYAAGHIPGAINIPLSE-----------------LEERAALLELDKDKPIVVYCRSGN---RSARAAKLLRKAG 74

                          90
                  ....*....|....
gi 1958787605 122 HHSVSLLDGGFRYW 135
Cdd:cd00158    75 GTNVYNLEGGMLAW 88
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 11-135 4.84e-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: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  11 VSAQWVAEALKSPRAsqplKLLDAswylpklgRDARREFEER----------HIPGAAFFDIDRCSDHtspyDHMLPSAT 80
Cdd:cd01449     1 VTAEEVLANLDSGDV----QLVDA--------RSPERFRGEVpeprpglrsgHIPGAVNIPWTSLLDE----DGTFKSPE 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958787605  81 HFADYAGSLGVSAATHVVIYDGSdqGLySAPRVWWMFRAFGHHSVSLLDGGFRYW 135
Cdd:cd01449    65 ELRALFAALGITPDKPVIVYCGS--GV-TACVLLLALELLGYKNVRLYDGSWSEW 116
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 10-142 5.88e-04

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 39.39  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958787605  10 LVSAQWVAEALKSPRAsqplKLLDAswylpklgRDARR---EFEER-----HIPGAAFFDIDRCSDHtspyDHMLPSATH 81
Cdd:COG2897   139 LADADEVLAALGDPDA----VLVDA--------RSPERyrgEVEPIdpragHIPGAVNLPWTDLLDE----DGTFKSAEE 202

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958787605  82 FADYAGSLGVSAATHVVIYDGSdqGLYSAPrVWWMFRAFGHHSVSLLDGGFRYWLSQ-NLPI 142
Cdd:COG2897   203 LRALFAALGIDPDKPVITYCGS--GVRAAH-TWLALELLGYPNVRLYDGSWSEWGSDpDLPV 261
 
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.
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