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Conserved domains on  [gi|1624525603|ref|NP_001356834|]
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3-mercaptopyruvate sulfurtransferase isoform 3 [Homo sapiens]

Protein Classification

sulfurtransferase( domain architecture ID 11458420)

sulfurtransferase such as thiosulfate sulfurtransferase or 3-mercaptopyruvate sulfurtransferase, which catalyzes the transfer of sulfur to cyanide from donor compounds such as thiosulfate or 3-mercaptopyruvate

CATH:  3.40.250.10
EC:  2.8.1.-
Gene Ontology:  GO:0016783|GO:0000098
PubMed:  12151332|17454295

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 36-219 6.42e-62

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


:

Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 194.62  E-value: 6.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  36 VAEALRAPragqPLQLLDASWYLPklgrDARREFEERHIPGAAFFDIDQC-SDRTSPYDHMLPGAEHFAEYAGRLGVGAA 114
Cdd:COG2897     1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603 115 THVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLE 194
Cdd:COG2897    73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150

                         170       180
                  ....*....|....*....|....*
gi 1624525603 195 SRRFQVVDSRATGRFRGtEPEPRDA 219
Cdd:COG2897   151 DPDAVLVDARSPERYRG-EVEPIDP 174
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 36-219 6.42e-62

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 194.62  E-value: 6.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  36 VAEALRAPragqPLQLLDASWYLPklgrDARREFEERHIPGAAFFDIDQC-SDRTSPYDHMLPGAEHFAEYAGRLGVGAA 114
Cdd:COG2897     1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603 115 THVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLE 194
Cdd:COG2897    73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150

                         170       180
                  ....*....|....*....|....*
gi 1624525603 195 SRRFQVVDSRATGRFRGtEPEPRDA 219
Cdd:COG2897   151 DPDAVLVDARSPERYRG-EVEPIDP 174
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 6-217 4.75e-58

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 186.55  E-value: 4.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603   6 SRESETRARSPSvAAMASPQlcrALVSAQWVAEALRAPRagqpLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQC 85
Cdd:PLN02723    3 SSGSETKANYST-QSISTNE---PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  86 SDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDAsdQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSG 165
Cdd:PLN02723   75 SDRTTDLPHMLPSEEAFAAAVSALGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESS 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525603 166 KSQPA---------------------PAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATGRFRGTEPEPR 217
Cdd:PLN02723  153 ASGDAilkasaaseaiekvyqgqtvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPR 225
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 30-159 2.03e-52

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 165.49  E-value: 2.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  30 LVSAQWVAEALRAPRagqpLQLLDASWYLPklGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRL 109
Cdd:cd01448     1 LVSPDWLAEHLDDPD----VRILDARWYLP--DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1624525603 110 GVGAATHVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQN 159
Cdd:cd01448    75 GISNDDTVVVYD--DGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 64-161 2.45e-19

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 79.81  E-value: 2.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603   64 DARR--EFEERHIPGAAFFDIDQCSDRTSPYDHMlpgaeHFAEYAGRLGVGAATHVVIYDASDqglYSAPRVWWMFRAFG 141
Cdd:smart00450   9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 1624525603  142 HHAVSLLDGGLRHWLRQNLP 161
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 64-155 1.04e-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: 59.42  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  64 DARR--EFEERHIPGAAFFDIDqcsdrtSPYDHMLPGAEHFAEYAGRLGvgaATHVVIYDASDQglySAPRVWWMFRAFG 141
Cdd:pfam00581  10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77

                          90
                  ....*....|....
gi 1624525603 142 HHAVSLLDGGLRHW 155
Cdd:pfam00581  78 YKNVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 36-219 6.42e-62

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 194.62  E-value: 6.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  36 VAEALRAPragqPLQLLDASWYLPklgrDARREFEERHIPGAAFFDIDQC-SDRTSPYDHMLPGAEHFAEYAGRLGVGAA 114
Cdd:COG2897     1 LAAHLDDP----DVVILDVRWDLP----DGRAAYEAGHIPGAVFLDLDTDlSDPRSPGRHPLPSPEAFAALLGALGISND 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603 115 THVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLE 194
Cdd:COG2897    73 TTVVVYD--DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTARPDPELLADADEVLAALG 150

                         170       180
                  ....*....|....*....|....*
gi 1624525603 195 SRRFQVVDSRATGRFRGtEPEPRDA 219
Cdd:COG2897   151 DPDAVLVDARSPERYRG-EVEPIDP 174
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 6-217 4.75e-58

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 186.55  E-value: 4.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603   6 SRESETRARSPSvAAMASPQlcrALVSAQWVAEALRAPRagqpLQLLDASWYLPKLGRDARREFEERHIPGAAFFDIDQC 85
Cdd:PLN02723    3 SSGSETKANYST-QSISTNE---PVVSVDWLHANLREPD----VKVLDASWYMPDEQRNPIQEYQVAHIPGALFFDLDGI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  86 SDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDAsdQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSG 165
Cdd:PLN02723   75 SDRTTDLPHMLPSEEAFAAAVSALGIENKDGVVVYDG--KGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESS 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1624525603 166 KSQPA---------------------PAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATGRFRGTEPEPR 217
Cdd:PLN02723  153 ASGDAilkasaaseaiekvyqgqtvsPITFQTKFQPHLVWTLEQVKKNIEDKTYQHIDARSKARFDGAAPEPR 225
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 31-217 1.18e-52

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 171.43  E-value: 1.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  31 VSAQWVAEALRAPRagqpLQLLDASWYLPKL-GRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRL 109
Cdd:PRK11493    7 VAADWLAEHIDDPE----IQIIDARMAPPGQeDRDVAAEYRAGHIPGAVFFDIEALSDHTSPLPHMMPRPETFAVAMREL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603 110 GVGAATHVVIYDASDqgLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDI 189
Cdd:PRK11493   83 GVNQDKHLVVYDEGN--LFSAPRAWWMLRTFGVEKVSILAGGLAGWQRDDLLLEEGAVELPEGEFNAAFNPEAVVRLTDV 160

                         170       180
                  ....*....|....*....|....*...
gi 1624525603 190 KENLESRRFQVVDSRATGRFRGTEPEPR 217
Cdd:PRK11493  161 LLASHEKTAQIVDARPAARFNAEVDEPR 188
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 30-159 2.03e-52

Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the Rhodanese Homology Domain; this is the 1st repeat, which does not contain the catalytically active Cys residue. The role of the 1st repeat is uncertain, but it is believed to be involved in protein interaction.


Pssm-ID: 238725 [Multi-domain]  Cd Length: 122  Bit Score: 165.49  E-value: 2.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  30 LVSAQWVAEALRAPRagqpLQLLDASWYLPklGRDARREFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRL 109
Cdd:cd01448     1 LVSPDWLAEHLDDPD----VRILDARWYLP--DRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPHMLPSPEEFAELLGSL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1624525603 110 GVGAATHVVIYDasDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQN 159
Cdd:cd01448    75 GISNDDTVVVYD--DGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 31-157 5.51e-37

Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only the second repeat contains the catalytically active Cys residue. The role of the 1st repeat is uncertain, but believed to be involved in protein interaction. This CD aligns the 1st and 2nd repeats.


Pssm-ID: 238722 [Multi-domain]  Cd Length: 138  Bit Score: 126.83  E-value: 5.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  31 VSAQWVAEALRAPRAGQPLQLLDASWYLPKLgRDARREF------------EERHIPGAAFFDIDQCSDRTSPYDHMLPG 98
Cdd:cd01445     1 KSTEQLAENLEAGKVGKGFQLLDARAQSPGT-REARGEYletqpepdavglDSGHIPGASFFDFEECLDEAGFEESMEPS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1624525603  99 AEHFAEYAGRLGVGAATHVVIYDASDQGLYSAPRVWWMFRAFGHHAVSLLDGGLRHWLR 157
Cdd:cd01445    80 EAEFAAMFEAKGIDLDKHLIATDGDDLGGFTACHIALAARLCGHPDVAILDGGFFEWFH 138
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 64-161 2.45e-19

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 79.81  E-value: 2.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603   64 DARR--EFEERHIPGAAFFDIDQCSDRTSPYDHMlpgaeHFAEYAGRLGVGAATHVVIYDASDqglYSAPRVWWMFRAFG 141
Cdd:smart00450   9 DVRSpeEYEGGHIPGAVNIPLSELLDRRGELDIL-----EFEELLKRLGLDKDKPVVVYCRSG---NRSAKAAWLLRELG 80

                           90       100
                   ....*....|....*....|
gi 1624525603  142 HHAVSLLDGGLRHWLRQNLP 161
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 64-155 1.04e-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: 59.42  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  64 DARR--EFEERHIPGAAFFDIDqcsdrtSPYDHMLPGAEHFAEYAGRLGvgaATHVVIYDASDQglySAPRVWWMFRAFG 141
Cdd:pfam00581  10 DVRPpeEYAKGHIPGAVNVPLS------SLSLPPLPLLELLEKLLELLK---DKPIVVYCNSGN---RAAAAAALLKALG 77

                          90
                  ....*....|....
gi 1624525603 142 HHAVSLLDGGLRHW 155
Cdd:pfam00581  78 YKNVYVLDGGFEAW 91
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 49-211 2.46e-09

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 57.05  E-value: 2.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  49 LQLLDA-SWYLPKLGRDARreFEERHIPGAAFFDIDQCSDRTSPYDHMLPGAEHFAEYAGRLGVGAATHVVIYDasDQGL 127
Cdd:PRK09629   17 LERLDApELILVDLTSSAR--YEAGHIRGARFVDPKRTQLGKPPAPGLLPDTADLEQLFGELGHNPDAVYVVYD--DEGG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603 128 YSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGKSQPAPAEFRAQLDPAFIKTYEDIKENLESRRFQVVDSRATG 207
Cdd:PRK09629   93 GWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVPPVAGGPVTLTLHDEPTATREYLQSRLGAADLAIWDARAPT 172


                  ....
gi 1624525603 208 RFRG 211
Cdd:PRK09629  173 EYSG 176
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 184-217 4.86e-07

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: 47.24  E-value: 4.86e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1624525603 184 KTYEDIKENLESRRFQVVDSRATGRFRGTEPEPR 217
Cdd:cd01449     1 VTAEEVLANLDSGDVQLVDARSPERFRGEVPEPR 34
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 31-166 1.00e-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: 46.11  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  31 VSAQWVAEALRAPRAgqplQLLDAswylpklgRDARrEFEERHIPGAAFFDIDQCSDRTSPYDhmlpgaehfaeyagrlg 110
Cdd:COG0607     6 ISPAELAELLESEDA----VLLDV--------REPE-EFAAGHIPGAINIPLGELAERLDELP----------------- 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1624525603 111 vgAATHVVIYDASDqglYSAPRVWWMFRAFGHHAVSLLDGGLRHWLRQNLPLSSGK 166
Cdd:COG0607    56 --KDKPIVVYCASG---GRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 64-155 4.88e-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: 38.05  E-value: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624525603  64 DAR--REFEERHIPGAAFFDIDQcsdrtspydhmlpgaehFAEYAGRLGVGAATHVVIYDASDQglySAPRVWWMFRAFG 141
Cdd:cd00158    15 DVRepEEYAAGHIPGAINIPLSE-----------------LEERAALLELDKDKPIVVYCRSGN---RSARAAKLLRKAG 74

                          90
                  ....*....|....
gi 1624525603 142 HHAVSLLDGGLRHW 155
Cdd:cd00158    75 GTNVYNLEGGMLAW 88
 
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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