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Conserved domains on  [gi|1449702733|ref|WP_115872338|]
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sulfurtransferase [Enterococcus pseudoavium]

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

 Zoom to residue level

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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 ...
 55-315 6.49e-70

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


:

Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 218.89  E-value: 6.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  55 LHKQLkDDKKTVVIEASYGEG---KEYQKAHIPGALHID-TMEIETEENN--WNILSAETCKEVFLKRGVTKTTPVVVY- 127
Cdd:COG2897     1 LAAHL-DDPDVVILDVRWDLPdgrAAYEAGHIPGAVFLDlDTDLSDPRSPgrHPLPSPEAFAALLGALGISNDTTVVVYd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 128 SSDINAAARVAFVAYWLGVDQVKILDGGLKAWEKADYKVEKGNEEVAAAkDFGAKvpgRPDSLISTSADLLAAKEkNPEL 207
Cdd:COG2897    80 DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPG-DFTAR---PDPELLADADEVLAALG-DPDA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 208 VLASVRSWKEFTGKTSGYDYIenAGEPEGAVyakssktSADVAQLMNNDGTVKEPTKIFKAWEKWGITPDKEVAFYCGTG 287
Cdd:COG2897   155 VLVDARSPERYRGEVEPIDPR--AGHIPGAV-------NLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSG 225

                         250       260
                  ....*....|....*....|....*...
gi 1449702733 288 WRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:COG2897   226 VRAAHTWLALELLGYPNVRLYDGSWSEW 253
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 55-315 6.49e-70

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 218.89  E-value: 6.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  55 LHKQLkDDKKTVVIEASYGEG---KEYQKAHIPGALHID-TMEIETEENN--WNILSAETCKEVFLKRGVTKTTPVVVY- 127
Cdd:COG2897     1 LAAHL-DDPDVVILDVRWDLPdgrAAYEAGHIPGAVFLDlDTDLSDPRSPgrHPLPSPEAFAALLGALGISNDTTVVVYd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 128 SSDINAAARVAFVAYWLGVDQVKILDGGLKAWEKADYKVEKGNEEVAAAkDFGAKvpgRPDSLISTSADLLAAKEkNPEL 207
Cdd:COG2897    80 DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPG-DFTAR---PDPELLADADEVLAALG-DPDA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 208 VLASVRSWKEFTGKTSGYDYIenAGEPEGAVyakssktSADVAQLMNNDGTVKEPTKIFKAWEKWGITPDKEVAFYCGTG 287
Cdd:COG2897   155 VLVDARSPERYRGEVEPIDPR--AGHIPGAV-------NLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSG 225

                         250       260
                  ....*....|....*....|....*...
gi 1449702733 288 WRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:COG2897   226 VRAAHTWLALELLGYPNVRLYDGSWSEW 253
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 196-315 5.67e-31

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: 113.50  E-value: 5.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 196 DLLAAKEkNPELVLASVRSWKEFTGKTSGYDYIENAGEPEGAVyakssktSADVAQLMNNDGTVKEPTKIFKAWEKWGIT 275
Cdd:cd01449     5 EVLANLD-SGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAV-------NIPWTSLLDEDGTFKSPEELRALFAALGIT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1449702733 276 PDKEVAFYCGTGWRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:cd01449    77 PDKPVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 45-315 9.51e-18

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 82.06  E-value: 9.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  45 ASDFFVDAKWLHKQLKDDKKTVvIEASY---GEGK-----EYQKAHIPGALHIDtmeIETEENNWNIL-----SAETCKE 111
Cdd:PRK11493    2 STTWFVAADWLAEHIDDPEIQI-IDARMappGQEDrdvaaEYRAGHIPGAVFFD---IEALSDHTSPLphmmpRPETFAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 112 VFLKRGVTKTTPVVVYSS-DINAAARvafvAYWL----GVDQVKILDGGLKAWEKADYKVEKGNEEVAAAkDFGAKVpgR 186
Cdd:PRK11493   78 AMRELGVNQDKHLVVYDEgNLFSAPR----AWWMlrtfGVEKVSILAGGLAGWQRDDLLLEEGAVELPEG-EFNAAF--N 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 187 PDSLISTSADLLAAKEKNPELVLAsvRSWKEFTGKtsgydyienAGEPEGAVYAKSSKTSADVA--QLMNNdGTVKEPTK 264
Cdd:PRK11493  151 PEAVVRLTDVLLASHEKTAQIVDA--RPAARFNAE---------VDEPRPGLRRGHIPGALNVPwtELVRE-GELKTTDE 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1449702733 265 IFKAWEKWGITPDKEVAFYCGTGWRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:PRK11493  219 LDAIFFGRGVSFDRPIIASCGSGVTAAVVVLALATLDVPNVKLYDGAWSEW 269
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 61-164 1.35e-14

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: 68.64  E-value: 1.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733   61 DDKKTVVIEASYGEgkEYQKAHIPGALHIDTMEIETEENNWNILSAEtckEVFLKRGVTKTTPVVVYSSDINAAARVAFV 140
Cdd:smart00450   1 NDEKVVLLDVRSPE--EYEGGHIPGAVNIPLSELLDRRGELDILEFE---ELLKRLGLDKDKPVVVYCRSGNRSAKAAWL 75

                           90       100
                   ....*....|....*....|....
gi 1449702733  141 AYWLGVDQVKILDGGLKAWEKADY 164
Cdd:smart00450  76 LRELGFKNVYLLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 61-159 3.01e-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: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  61 DDKKTVVIEASYGEgkEYQKAHIPGALHIDTMEIEteennWNILSAETCKEVFLKRGvtKTTPVVVYSSDINAAARVAFV 140
Cdd:pfam00581   2 EDGKVVLIDVRPPE--EYAKGHIPGAVNVPLSSLS-----LPPLPLLELLEKLLELL--KDKPIVVYCNSGNRAAAAAAL 72

                          90
                  ....*....|....*....
gi 1449702733 141 AYWLGVDQVKILDGGLKAW 159
Cdd:pfam00581  73 LKALGYKNVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 55-315 6.49e-70

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 218.89  E-value: 6.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  55 LHKQLkDDKKTVVIEASYGEG---KEYQKAHIPGALHID-TMEIETEENN--WNILSAETCKEVFLKRGVTKTTPVVVY- 127
Cdd:COG2897     1 LAAHL-DDPDVVILDVRWDLPdgrAAYEAGHIPGAVFLDlDTDLSDPRSPgrHPLPSPEAFAALLGALGISNDTTVVVYd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 128 SSDINAAARVAFVAYWLGVDQVKILDGGLKAWEKADYKVEKGNEEVAAAkDFGAKvpgRPDSLISTSADLLAAKEkNPEL 207
Cdd:COG2897    80 DGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPG-DFTAR---PDPELLADADEVLAALG-DPDA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 208 VLASVRSWKEFTGKTSGYDYIenAGEPEGAVyakssktSADVAQLMNNDGTVKEPTKIFKAWEKWGITPDKEVAFYCGTG 287
Cdd:COG2897   155 VLVDARSPERYRGEVEPIDPR--AGHIPGAV-------NLPWTDLLDEDGTFKSAEELRALFAALGIDPDKPVITYCGSG 225

                         250       260
                  ....*....|....*....|....*...
gi 1449702733 288 WRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:COG2897   226 VRAAHTWLALELLGYPNVRLYDGSWSEW 253
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 196-315 5.67e-31

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: 113.50  E-value: 5.67e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 196 DLLAAKEkNPELVLASVRSWKEFTGKTSGYDYIENAGEPEGAVyakssktSADVAQLMNNDGTVKEPTKIFKAWEKWGIT 275
Cdd:cd01449     5 EVLANLD-SGDVQLVDARSPERFRGEVPEPRPGLRSGHIPGAV-------NIPWTSLLDEDGTFKSPEELRALFAALGIT 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1449702733 276 PDKEVAFYCGTGWRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:cd01449    77 PDKPVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 49-163 5.23e-25

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: 97.69  E-value: 5.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  49 FVDAKWLHKQLkDDKKTVVIEASYGEG-----KEYQKAHIPGALHIDTMEIE--TEENNWNILSAETCKEVFLKRGVTKT 121
Cdd:cd01448     1 LVSPDWLAEHL-DDPDVRILDARWYLPdrdgrKEYLEGHIPGAVFFDLDEDLddKSPGPHMLPSPEEFAELLGSLGISND 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1449702733 122 TPVVVYSSDIN-AAARVAFVAYWLGVDQVKILDGGLKAWEKAD 163
Cdd:cd01448    80 DTVVVYDDGGGfFAARAWWTLRYFGHENVRVLDGGLQAWKAEG 122
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 45-315 9.51e-18

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 82.06  E-value: 9.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  45 ASDFFVDAKWLHKQLKDDKKTVvIEASY---GEGK-----EYQKAHIPGALHIDtmeIETEENNWNIL-----SAETCKE 111
Cdd:PRK11493    2 STTWFVAADWLAEHIDDPEIQI-IDARMappGQEDrdvaaEYRAGHIPGAVFFD---IEALSDHTSPLphmmpRPETFAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 112 VFLKRGVTKTTPVVVYSS-DINAAARvafvAYWL----GVDQVKILDGGLKAWEKADYKVEKGNEEVAAAkDFGAKVpgR 186
Cdd:PRK11493   78 AMRELGVNQDKHLVVYDEgNLFSAPR----AWWMlrtfGVEKVSILAGGLAGWQRDDLLLEEGAVELPEG-EFNAAF--N 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 187 PDSLISTSADLLAAKEKNPELVLAsvRSWKEFTGKtsgydyienAGEPEGAVYAKSSKTSADVA--QLMNNdGTVKEPTK 264
Cdd:PRK11493  151 PEAVVRLTDVLLASHEKTAQIVDA--RPAARFNAE---------VDEPRPGLRRGHIPGALNVPwtELVRE-GELKTTDE 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1449702733 265 IFKAWEKWGITPDKEVAFYCGTGWRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:PRK11493  219 LDAIFFGRGVSFDRPIIASCGSGVTAAVVVLALATLDVPNVKLYDGAWSEW 269
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 43-315 1.27e-15

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 76.38  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  43 IKASDFFVDAKWLHKQLKD-DKKtvVIEASY-------GEGKEYQKAHIPGALHIDTMEIETEENNW-NILSAETCKEVF 113
Cdd:PLN02723   17 ISTNEPVVSVDWLHANLREpDVK--VLDASWympdeqrNPIQEYQVAHIPGALFFDLDGISDRTTDLpHMLPSEEAFAAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 114 LKR-GVTKTTPVVVYSSD-INAAARVAFVAYWLGVDQVKILDGGLKAWEKADYKVEKGNEEVAAAKDFGAKVPGRPDSLI 191
Cdd:PLN02723   95 VSAlGIENKDGVVVYDGKgIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGDAILKASAASEAIEKVYQG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 192 STSADLLAAKEKNPELVLASVRSWKEFTGKTsgYDYIE---------NAGEPEGAVYAKSSKTSADV--AQLMNNDGTVK 260
Cdd:PLN02723  175 QTVSPITFQTKFQPHLVWTLEQVKKNIEDKT--YQHIDarskarfdgAAPEPRKGIRSGHIPGSKCVpfPQMLDSSQTLL 252

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1449702733 261 EPTKIFKAWEKWGITPDKEVAFYCGTGWRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:PLN02723  253 PAEELKKRFEQEGISLDSPIVASCGTGVTACILALGLHRLGKTDVPVYDGSWTEW 307
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 61-164 1.35e-14

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: 68.64  E-value: 1.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733   61 DDKKTVVIEASYGEgkEYQKAHIPGALHIDTMEIETEENNWNILSAEtckEVFLKRGVTKTTPVVVYSSDINAAARVAFV 140
Cdd:smart00450   1 NDEKVVLLDVRSPE--EYEGGHIPGAVNIPLSELLDRRGELDILEFE---ELLKRLGLDKDKPVVVYCRSGNRSAKAAWL 75

                           90       100
                   ....*....|....*....|....
gi 1449702733  141 AYWLGVDQVKILDGGLKAWEKADY 164
Cdd:smart00450  76 LRELGFKNVYLLDGGYKEWSAAGP 99
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 50-169 5.44e-13

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: 64.60  E-value: 5.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  50 VDAKWLHKQLKDDKkTVVI---EASygegkEYQKAHIPGALHIDTMEIETEENNWNilsaetckevflkrgvtKTTPVVV 126
Cdd:COG0607     6 ISPAELAELLESED-AVLLdvrEPE-----EFAAGHIPGAINIPLGELAERLDELP-----------------KDKPIVV 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1449702733 127 YSSDINAAARVAFVAYWLGVDQVKILDGGLKAWEKADYKVEKG 169
Cdd:COG0607    63 YCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVEKG 105
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 61-159 3.01e-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: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  61 DDKKTVVIEASYGEgkEYQKAHIPGALHIDTMEIEteennWNILSAETCKEVFLKRGvtKTTPVVVYSSDINAAARVAFV 140
Cdd:pfam00581   2 EDGKVVLIDVRPPE--EYAKGHIPGAVNVPLSSLS-----LPPLPLLELLEKLLELL--KDKPIVVYCNSGNRAAAAAAL 72

                          90
                  ....*....|....*....
gi 1449702733 141 AYWLGVDQVKILDGGLKAW 159
Cdd:pfam00581  73 LKALGYKNVYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 203-315 3.47e-10

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: 56.31  E-value: 3.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  203 KNPELVLASVRSWKEFtgktsgydyieNAGEPEGAVYAKSSKTSADVAQLmnndgtvkEPTKIFKAWEKWGITPDKEVAF 282
Cdd:smart00450   1 NDEKVVLLDVRSPEEY-----------EGGHIPGAVNIPLSELLDRRGEL--------DILEFEELLKRLGLDKDKPVVV 61

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1449702733  283 YCGTGWRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:smart00450  62 YCRSGNRSAKAAWLLRELGFKNVYLLDGGYKEW 94
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 57-160 1.04e-08

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: 51.92  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  57 KQLKDDKKTVVIEASygEGKEYQKAHIPGALHIDTMEIETEENNWNILsaetckevflkrgvtKTTPVVVYSSDINAAAR 136
Cdd:cd00158     3 KELLDDEDAVLLDVR--EPEEYAAGHIPGAINIPLSELEERAALLELD---------------KDKPIVVYCRSGNRSAR 65

                          90       100
                  ....*....|....*....|....
gi 1449702733 137 VAFVAYWLGVDQVKILDGGLKAWE 160
Cdd:cd00158    66 AAKLLRKAGGTNVYNLEGGMLAWK 89
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 78-339 1.94e-08

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 55.89  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  78 YQKAHIPGALHIDTMEIETEENNWNILSAETC--KEVFLKRGVTKTTPVVVYSSDINA-AARVAFVAYWLGVDQVKILDG 154
Cdd:PRK09629   36 YEAGHIRGARFVDPKRTQLGKPPAPGLLPDTAdlEQLFGELGHNPDAVYVVYDDEGGGwAGRFIWLLDVIGHSGYHYLDG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 155 GLKAWEKADYKVekgNEEVAAakdfgakVPGRPDSLI-----STSADLLAAKEKNPELVLASVRSWKEFTGKTSgydYIE 229
Cdd:PRK09629  116 GVLAWEAQALPL---STDVPP-------VAGGPVTLTlhdepTATREYLQSRLGAADLAIWDARAPTEYSGEKV---VAA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733 230 NAGEPEGAV---------YAKSSKTSADVAQLMNNdgtvkeptkifkawekWGITPDKEVAFYCGTGWRAATTFFITKQE 300
Cdd:PRK09629  183 KGGHIPGAVnfewtagmdKARNLRIRQDMPEILRD----------------LGITPDKEVITHCQTHHRSGFTYLVAKAL 246

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1449702733 301 GWKDVKLFDGGWYDWDKaHQKDPSKYPVQVGDPRDKDKV 339
Cdd:PRK09629  247 GYPRVKAYAGSWGEWGN-HPDTPVEVPTVAAAPIEAVEV 284
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 250-315 3.45e-08

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: 50.56  E-value: 3.45e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1449702733 250 AQLMNNDGTVKEPTKIFKAWEKW-GITPDKEVAFYCGTGWRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:pfam00581  25 AVNVPLSSLSLPPLPLLELLEKLlELLKDKPIVVYCNSGNRAAAAAALLKALGYKNVYVLDGGFEAW 91
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 50-161 3.94e-08

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: 51.72  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  50 VDAKWLHKQLKDDKKTVVIEASYGEGKEYQKAHIPGALHIDTMEIETEENNWNIL--SAETCKEVFLKRGVTKTTPVVVY 127
Cdd:cd01445    22 LDARAQSPGTREARGEYLETQPEPDAVGLDSGHIPGASFFDFEECLDEAGFEESMepSEAEFAAMFEAKGIDLDKHLIAT 101

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1449702733 128 SSDINA---AARVAFVAYWLGVDQVKILDGGLKAWEK 161
Cdd:cd01445   102 DGDDLGgftACHIALAARLCGHPDVAILDGGFFEWFH 138
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 50-159 4.43e-08

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: 50.71  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  50 VDAKWLhKQLKDDKKTVVIEA----SY-GEGKEYQKA----HIPGALHIDTMEIETEENNwnILSAETCKEVFLKRGVTK 120
Cdd:cd01449     1 VTAEEV-LANLDSGDVQLVDArspeRFrGEVPEPRPGlrsgHIPGAVNIPWTSLLDEDGT--FKSPEELRALFAALGITP 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1449702733 121 TTPVVVYSSDINAAARVAFVAYWLGVDQVKILDGGLKAW 159
Cdd:cd01449    78 DKPVIVYCGSGVTACVLLLALELLGYKNVRLYDGSWSEW 116
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 276-315 1.88e-05

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: 43.03  E-value: 1.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1449702733 276 PDKEVAFYCGTGWRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:cd01519    65 KDKELIFYCKAGVRSKAAAELARSLGYENVGNYPGSWLDW 104
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
 78-164 2.68e-05

Member of the Rhodanese Homology Domain superfamily. This CD includes the putative rhodanese-like protein, Psp2, of Yersinia pestis biovar Medievalis and other similar uncharacterized proteins.


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 42.72  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  78 YQKAHIPGALHIDTMEIetEENNWNILSaetckevflkrgvtKTTPVVVYSSDI--NAAARVAFVAYWLGVdQVKILDGG 155
Cdd:cd01521    37 YARGHVPGAINLPHREI--CENATAKLD--------------KEKLFVVYCDGPgcNGATKAALKLAELGF-PVKEMIGG 99


                  ....*....
gi 1449702733 156 LKAWEKADY 164
Cdd:cd01521   100 LDWWKREGY 108
GlpE_ST cd01444
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ...
 55-161 4.03e-05

GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.


Pssm-ID: 238721 [Multi-domain]  Cd Length: 96  Bit Score: 41.86  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  55 LHKQLKDDKKTVVIEASYGEGKEYQKAHIPGALHIDtmeieteENNWNILSAETCKEvflkrgvtktTPVVVYSSDINAA 134
Cdd:cd01444     7 LAELLAAGEAPVLLDVRDPASYAALPDHIPGAIHLD-------EDSLDDWLGDLDRD----------RPVVVYCYHGNSS 69

                          90       100
                  ....*....|....*....|....*....
gi 1449702733 135 ARVAfvAYWL--GVDQVKILDGGLKAWEK 161
Cdd:cd01444    70 AQLA--QALReaGFTDVRSLAGGFEAWRR 96
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 274-318 7.88e-05

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: 41.49  E-value: 7.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1449702733 274 ITPDKEVAFYCGTGWRAATTFFITKQEGWKDVKLFDGGWYDWDKA 318
Cdd:COG0607    54 LPKDKPIVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAA 98
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 276-315 1.53e-04

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 39.98  E-value: 1.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1449702733 276 PDKEVAFYCGTGWRAATTFFITKQEGWKDVKLFDGGWYDW 315
Cdd:cd00158    49 KDKPIVVYCRSGNRSARAAKLLRKAGGTNVYNLEGGMLAW 88
Polysulfide_ST cd01447
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ...
 276-318 5.20e-04

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: 38.95  E-value: 5.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1449702733 276 PDKEVAFYCGTGWRAATTFFITKQEGWKDVKLFDGGWYDWDKA 318
Cdd:cd01447    60 EDKPFVFYCASGWRSALAGKTLQDMGLKPVYNIEGGFKDWKEA 102
4RHOD_Repeats cd01529
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ...
 52-159 1.34e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.


Pssm-ID: 238787 [Multi-domain]  Cd Length: 96  Bit Score: 37.66  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  52 AKWLHKQlkdDKKTVVIEASygEGKEYQKAHIPGALHIDTmeieteeNNWNILSAETCKEVFLKRGvtktTPVVVYSSDi 131
Cdd:cd01529     3 ADWLGEH---EPGTALLDVR--AEDEYAAGHLPGKRSIPG-------AALVLRSQELQALEAPGRA----TRYVLTCDG- 65

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1449702733 132 naAARVAFVAYWL---GVDQVKILDGGLKAW 159
Cdd:cd01529    66 --SLLARFAAQELlalGGKPVALLDGGTSAW 94
4RHOD_Repeat_4 cd01535
Member of the Rhodanese Homology Domain superfamily, repeat 4. This CD includes putative ...
 52-169 1.59e-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: 38.26  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449702733  52 AKWLHKQlkdDKKTVVieaSYGEGKEYQKAHIPGAlhidtmeieteennWNILSAETCKEvfLKRGVTKTTPVVVYSSDI 131
Cdd:cd01535     3 AAWLGEG---GQTAVV---DVTASANYVKRHIPGA--------------WWVLRAQLAQA--LEKLPAAERYVLTCGSSL 60

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1449702733 132 NAAARVAFVAYwLGVDQVKILDGGLKAWEKADYKVEKG 169
Cdd:cd01535    61 LARFAAADLAA-LTVKPVFVLEGGTAAWIAAGLPVESG 97
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 261-334 4.47e-03

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 38.23  E-value: 4.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1449702733 261 EPTKIFKAWEKWGITPDKEVAFY-CGTGWRAATTFFITKQEGWKDVKLFDGGWYDWDKAhqkdpsKYPVQVGDPR 334
Cdd:COG2897    56 SPEAFAALLGALGISNDTTVVVYdDGGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAA------GLPLETGPPT 124
 
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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