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Conserved domains on  [gi|489512300|ref|WP_003417149|]
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MULTISPECIES: sulfurtransferase [Mycobacterium]

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 ...
 26-286 3.25e-104

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


:

Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 304.41  E-value: 3.25e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  26 LSAHMGAPGLAIVESDEDV----LLYDVGHIPGAVKIDWHTDLNDPR---VRDYINGEQFAELMDRKGIARDDTVVIYGD 98
Cdd:COG2897    1 LAAHLDDPDVVILDVRWDLpdgrAAYEAGHIPGAVFLDLDTDLSDPRspgRHPLPSPEAFAALLGALGISNDTTVVVYDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  99 KSNWWAAYALWVFTLFGHADVRLLNGGRDLWLAERRETTLDVPTKTCTGYPVvqRNDAPIRAFRDDVLAILGAQ--PLID 176
Cdd:COG2897   81 GGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTA--RPDPELLADADEVLAALGDPdaVLVD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 177 VRSPEEYTGKRthmpdypEEGALRAGHIPTAVHIPWGKAADESGRFRSREELERLYD--FINPDDQTVVYCRIGERSSHT 254
Cdd:COG2897  159 ARSPERYRGEV-------EPIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAalGIDPDKPVITYCGSGVRAAHT 231

                        250       260       270
                 ....*....|....*....|....*....|..
gi 489512300 255 WFVLtHLLGKADVRNYDGSWTEWGNAVRVPIV 286
Cdd:COG2897  232 WLAL-ELLGYPNVRLYDGSWSEWGSDPDLPVE 262
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 26-286 3.25e-104

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 304.41  E-value: 3.25e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  26 LSAHMGAPGLAIVESDEDV----LLYDVGHIPGAVKIDWHTDLNDPR---VRDYINGEQFAELMDRKGIARDDTVVIYGD 98
Cdd:COG2897    1 LAAHLDDPDVVILDVRWDLpdgrAAYEAGHIPGAVFLDLDTDLSDPRspgRHPLPSPEAFAALLGALGISNDTTVVVYDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  99 KSNWWAAYALWVFTLFGHADVRLLNGGRDLWLAERRETTLDVPTKTCTGYPVvqRNDAPIRAFRDDVLAILGAQ--PLID 176
Cdd:COG2897   81 GGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTA--RPDPELLADADEVLAALGDPdaVLVD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 177 VRSPEEYTGKRthmpdypEEGALRAGHIPTAVHIPWGKAADESGRFRSREELERLYD--FINPDDQTVVYCRIGERSSHT 254
Cdd:COG2897  159 ARSPERYRGEV-------EPIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAalGIDPDKPVITYCGSGVRAAHT 231

                        250       260       270
                 ....*....|....*....|....*....|..
gi 489512300 255 WFVLtHLLGKADVRNYDGSWTEWGNAVRVPIV 286
Cdd:COG2897  232 WLAL-ELLGYPNVRLYDGSWSEWGSDPDLPVE 262
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 160-279 5.04e-43

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: 143.54  E-value: 5.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 160 AFRDDVLAILGAQ--PLIDVRSPEEYTGKRTHMPdypeeGALRAGHIPTAVHIPWGKAADESGRFRSREELERLYD--FI 235
Cdd:cd01449    1 VTAEEVLANLDSGdvQLVDARSPERFRGEVPEPR-----PGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAalGI 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489512300 236 NPDDQTVVYCRIGERSSHTWFVLtHLLGKADVRNYDGSWTEWGN 279
Cdd:cd01449   76 TPDKPVIVYCGSGVTACVLLLAL-ELLGYKNVRLYDGSWSEWGS 118
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 11-285 3.85e-26

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 107.90  E-value: 3.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  11 LSAYAHPERLVTADWLSAHMGAPGLAIVESDEDVLlYDVGHIPGAVKID-WHTDLNDPRVRDYI-NGEQFAELMDRKGIA 88
Cdd:PRK09629   1 MSAFTGLSLVIEPNDLLERLDAPELILVDLTSSAR-YEAGHIRGARFVDpKRTQLGKPPAPGLLpDTADLEQLFGELGHN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  89 RDDTVVIYGDKSNWWAAYALWVFTLFGHADVRLLNGGRDLWLAERRETTLDVPtkTCTGYPV-VQRNDAPIrAFRDDVLA 167
Cdd:PRK09629  80 PDAVYVVYDDEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVP--PVAGGPVtLTLHDEPT-ATREYLQS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 168 ILGAQPLI--DVRSPEEYTGKRTHmpdypeegALRAGHIPTAVHIPWGKAADESGRFRSREEL-ERLYDF-INPDDQTVV 243
Cdd:PRK09629 157 RLGAADLAiwDARAPTEYSGEKVV--------AAKGGHIPGAVNFEWTAGMDKARNLRIRQDMpEILRDLgITPDKEVIT 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 489512300 244 YCRIGERSSHTWFVlTHLLGKADVRNYDGSWTEWGNAVRVPI 285
Cdd:PRK09629 229 HCQTHHRSGFTYLV-AKALGYPRVKAYAGSWGEWGNHPDTPV 269
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 174-282 7.16e-21

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: 85.20  E-value: 7.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300   174 LIDVRSPEEYTGkrthmpdypeegalraGHIPTAVHIPWGKAADESGRFRSREELERLYDF-INPDDQTVVYCRIGERSS 252
Cdd:smart00450   7 LLDVRSPEEYEG----------------GHIPGAVNIPLSELLDRRGELDILEFEELLKRLgLDKDKPVVVYCRSGNRSA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 489512300   253 HTWFVLtHLLGKADVRNYDGSWTEWGNAVR 282
Cdd:smart00450  71 KAAWLL-RELGFKNVYLLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 170-277 8.63e-18

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: 76.75  E-value: 8.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  170 GAQPLIDVRSPEEYtgkrthmpdypeegalRAGHIPTAVHIPWGKAADESGRFRsreELERLYDFINPDDQTVVYCRIGE 249
Cdd:pfam00581   4 GKVVLIDVRPPEEY----------------AKGHIPGAVNVPLSSLSLPPLPLL---ELLEKLLELLKDKPIVVYCNSGN 64

                          90       100
                  ....*....|....*....|....*...
gi 489512300  250 RSSHTWFVLTHlLGKADVRNYDGSWTEW 277
Cdd:pfam00581  65 RAAAAAALLKA-LGYKNVYVLDGGFEAW 91
 
Name Accession Description Interval E-value
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
 26-286 3.25e-104

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 304.41  E-value: 3.25e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  26 LSAHMGAPGLAIVESDEDV----LLYDVGHIPGAVKIDWHTDLNDPR---VRDYINGEQFAELMDRKGIARDDTVVIYGD 98
Cdd:COG2897    1 LAAHLDDPDVVILDVRWDLpdgrAAYEAGHIPGAVFLDLDTDLSDPRspgRHPLPSPEAFAALLGALGISNDTTVVVYDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  99 KSNWWAAYALWVFTLFGHADVRLLNGGRDLWLAERRETTLDVPTKTCTGYPVvqRNDAPIRAFRDDVLAILGAQ--PLID 176
Cdd:COG2897   81 GGGLFAARAWWLLRYAGHEDVRVLDGGLAAWKAAGLPLETGPPTPAPGDFTA--RPDPELLADADEVLAALGDPdaVLVD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 177 VRSPEEYTGKRthmpdypEEGALRAGHIPTAVHIPWGKAADESGRFRSREELERLYD--FINPDDQTVVYCRIGERSSHT 254
Cdd:COG2897  159 ARSPERYRGEV-------EPIDPRAGHIPGAVNLPWTDLLDEDGTFKSAEELRALFAalGIDPDKPVITYCGSGVRAAHT 231

                        250       260       270
                 ....*....|....*....|....*....|..
gi 489512300 255 WFVLtHLLGKADVRNYDGSWTEWGNAVRVPIV 286
Cdd:COG2897  232 WLAL-ELLGYPNVRLYDGSWSEWGSDPDLPVE 262
TST_Repeat_2 cd01449
Thiosulfate sulfurtransferase (TST), C-terminal, catalytic domain. TST contains 2 copies of ...
 160-279 5.04e-43

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: 143.54  E-value: 5.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 160 AFRDDVLAILGAQ--PLIDVRSPEEYTGKRTHMPdypeeGALRAGHIPTAVHIPWGKAADESGRFRSREELERLYD--FI 235
Cdd:cd01449    1 VTAEEVLANLDSGdvQLVDARSPERFRGEVPEPR-----PGLRSGHIPGAVNIPWTSLLDEDGTFKSPEELRALFAalGI 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489512300 236 NPDDQTVVYCRIGERSSHTWFVLtHLLGKADVRNYDGSWTEWGN 279
Cdd:cd01449   76 TPDKPVIVYCGSGVTACVLLLAL-ELLGYKNVRLYDGSWSEWGS 118
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 20-132 1.78e-42

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: 141.99  E-value: 1.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  20 LVTADWLSAHMGAPGLAIVESDEDV------LLYDVGHIPGAVKIDWHTDLND--PRVRDYINGEQFAELMDRKGIARDD 91
Cdd:cd01448    1 LVSPDWLAEHLDDPDVRILDARWYLpdrdgrKEYLEGHIPGAVFFDLDEDLDDksPGPHMLPSPEEFAELLGSLGISNDD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489512300  92 TVVIYGDKSNWWAAYALWVFTLFGHADVRLLNGGRDLWLAE 132
Cdd:cd01448   81 TVVVYDDGGGFFAARAWWTLRYFGHENVRVLDGGLQAWKAE 121
PRK09629 PRK09629
bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional
 11-285 3.85e-26

bifunctional thiosulfate sulfurtransferase/phosphatidylserine decarboxylase; Provisional


Pssm-ID: 104071 [Multi-domain]  Cd Length: 610  Bit Score: 107.90  E-value: 3.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  11 LSAYAHPERLVTADWLSAHMGAPGLAIVESDEDVLlYDVGHIPGAVKID-WHTDLNDPRVRDYI-NGEQFAELMDRKGIA 88
Cdd:PRK09629   1 MSAFTGLSLVIEPNDLLERLDAPELILVDLTSSAR-YEAGHIRGARFVDpKRTQLGKPPAPGLLpDTADLEQLFGELGHN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  89 RDDTVVIYGDKSNWWAAYALWVFTLFGHADVRLLNGGRDLWLAERRETTLDVPtkTCTGYPV-VQRNDAPIrAFRDDVLA 167
Cdd:PRK09629  80 PDAVYVVYDDEGGGWAGRFIWLLDVIGHSGYHYLDGGVLAWEAQALPLSTDVP--PVAGGPVtLTLHDEPT-ATREYLQS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 168 ILGAQPLI--DVRSPEEYTGKRTHmpdypeegALRAGHIPTAVHIPWGKAADESGRFRSREEL-ERLYDF-INPDDQTVV 243
Cdd:PRK09629 157 RLGAADLAiwDARAPTEYSGEKVV--------AAKGGHIPGAVNFEWTAGMDKARNLRIRQDMpEILRDLgITPDKEVIT 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 489512300 244 YCRIGERSSHTWFVlTHLLGKADVRNYDGSWTEWGNAVRVPI 285
Cdd:PRK09629 229 HCQTHHRSGFTYLV-AKALGYPRVKAYAGSWGEWGNHPDTPV 269
sseA PRK11493
3-mercaptopyruvate sulfurtransferase; Provisional
 17-288 1.77e-24

3-mercaptopyruvate sulfurtransferase; Provisional


Pssm-ID: 236917 [Multi-domain]  Cd Length: 281  Bit Score: 99.78  E-value: 1.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  17 PERLVTADWLSAHMGAPGLAIVES--------DEDVLL-YDVGHIPGAV--KIDWHTDLNDPRVRDYINGEQFAELMDRK 85
Cdd:PRK11493   3 TTWFVAADWLAEHIDDPEIQIIDArmappgqeDRDVAAeYRAGHIPGAVffDIEALSDHTSPLPHMMPRPETFAVAMREL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  86 GIARDDTVVIYgDKSNWWAA-YALWVFTLFGHADVRLLNGGRDLW----------LAERRETTLDVPTktctGYPVVQRn 154
Cdd:PRK11493  83 GVNQDKHLVVY-DEGNLFSApRAWWMLRTFGVEKVSILAGGLAGWqrddllleegAVELPEGEFNAAF----NPEAVVR- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 155 dapirafRDDVLAIL---GAQpLIDVRSPEEYTGKrthmPDYPEEGaLRAGHIPTAVHIPWGKAADEsGRFRSREELERL 231
Cdd:PRK11493 157 -------LTDVLLAShekTAQ-IVDARPAARFNAE----VDEPRPG-LRRGHIPGALNVPWTELVRE-GELKTTDELDAI 222

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489512300 232 Y-----DFINPddqTVVYCRIGERSSHTWFVLThLLGKADVRNYDGSWTEWGNAVRVPIVAG 288
Cdd:PRK11493 223 FfgrgvSFDRP---IIASCGSGVTAAVVVLALA-TLDVPNVKLYDGAWSEWGARADLPVEPA 280
PLN02723 PLN02723
3-mercaptopyruvate sulfurtransferase
 12-286 5.91e-24

3-mercaptopyruvate sulfurtransferase


Pssm-ID: 178324 [Multi-domain]  Cd Length: 320  Bit Score: 99.11  E-value: 5.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  12 SAYAHPERLVTADWLSAHMGAPGLAIV--------ESDEDVLLYDVGHIPGAV--KIDWHTDLNDPRVRDYINGEQFAEL 81
Cdd:PLN02723  15 QSISTNEPVVSVDWLHANLREPDVKVLdaswympdEQRNPIQEYQVAHIPGALffDLDGISDRTTDLPHMLPSEEAFAAA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  82 MDRKGIARDDTVVIYGDKSNWWAAYALWVFTLFGHADVRLLNGGRDLWLAERRETTLDVPT----KTCTGYPVVQR---- 153
Cdd:PLN02723  95 VSALGIENKDGVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPKWRASGYDVESSASGdailKASAASEAIEKvyqg 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 154 NDAPIRAFR-----------DDVLAILGAQP--LIDVRSPEEYTGKrthMPDyPEEGaLRAGHIPTAVHIPWGKAADESG 220
Cdd:PLN02723 175 QTVSPITFQtkfqphlvwtlEQVKKNIEDKTyqHIDARSKARFDGA---APE-PRKG-IRSGHIPGSKCVPFPQMLDSSQ 249

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489512300 221 RFRSREELERLYD--FINPDDQTVVYCRIGErsshTWFVLT---HLLGKADVRNYDGSWTEWGNAVRVPIV 286
Cdd:PLN02723 250 TLLPAEELKKRFEqeGISLDSPIVASCGTGV----TACILAlglHRLGKTDVPVYDGSWTEWGALPDTPVA 316
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 174-282 7.16e-21

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: 85.20  E-value: 7.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300   174 LIDVRSPEEYTGkrthmpdypeegalraGHIPTAVHIPWGKAADESGRFRSREELERLYDF-INPDDQTVVYCRIGERSS 252
Cdd:smart00450   7 LLDVRSPEEYEG----------------GHIPGAVNIPLSELLDRRGELDILEFEELLKRLgLDKDKPVVVYCRSGNRSA 70

                           90       100       110
                   ....*....|....*....|....*....|
gi 489512300   253 HTWFVLtHLLGKADVRNYDGSWTEWGNAVR 282
Cdd:smart00450  71 KAAWLL-RELGFKNVYLLDGGYKEWSAAGP 99
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 170-277 8.63e-18

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: 76.75  E-value: 8.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  170 GAQPLIDVRSPEEYtgkrthmpdypeegalRAGHIPTAVHIPWGKAADESGRFRsreELERLYDFINPDDQTVVYCRIGE 249
Cdd:pfam00581   4 GKVVLIDVRPPEEY----------------AKGHIPGAVNVPLSSLSLPPLPLL---ELLEKLLELLKDKPIVVYCNSGN 64

                          90       100
                  ....*....|....*....|....*...
gi 489512300  250 RSSHTWFVLTHlLGKADVRNYDGSWTEW 277
Cdd:pfam00581  65 RAAAAAALLKA-LGYKNVYVLDGGFEAW 91
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 47-135 3.41e-17

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


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 75.19  E-value: 3.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300    47 YDVGHIPGAVKIDWHTDLNDPRvrdYINGEQFAELMDRKGIARDDTVVIYgDKSNWWAAYALWVFTLFGHADVRLLNGGR 126
Cdd:smart00450  16 YEGGHIPGAVNIPLSELLDRRG---ELDILEFEELLKRLGLDKDKPVVVY-CRSGNRSAKAAWLLRELGFKNVYLLDGGY 91


                   ....*....
gi 489512300   127 DLWLAERRE 135
Cdd:smart00450  92 KEWSAAGPP 100
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 162-277 2.90e-15

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: 70.38  E-value: 2.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 162 RDDVLAILGAQP---LIDVRSPEEytgkrthmpdypeegaLRAGHIPTAVHIPWGKAADEsgRFRSREELERLYDFINP- 237
Cdd:cd01519    3 FEEVKNLPNPHPnkvLIDVREPEE----------------LKTGKIPGAINIPLSSLPDA--LALSEEEFEKKYGFPKPs 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489512300 238 -DDQTVVYCRIGERSSHTWFVLTHLlGKADVRNYDGSWTEW 277
Cdd:cd01519   65 kDKELIFYCKAGVRSKAAAELARSL-GYENVGNYPGSWLDW 104
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 163-289 3.94e-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: 64.22  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 163 DDVLAILGAQP--LIDVRSPEEYtgkrthmpdypeegalRAGHIPTAVHIPWGkaadesgrfrsreELERLYDFINPDDQ 240
Cdd:COG0607    9 AELAELLESEDavLLDVREPEEF----------------AAGHIPGAINIPLG-------------ELAERLDELPKDKP 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489512300 241 TVVYCRIGERSSHtwfVLTHL--LGKADVRNYDGSWTEWGNAVRvPIVAGE 289
Cdd:COG0607   60 IVVYCASGGRSAQ---AAALLrrAGYTNVYNLAGGIEAWKAAGL-PVEKGK 106
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 174-277 1.08e-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: 62.70  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 174 LIDVRSPEEYtgkrthmpdypeegalRAGHIPTAVHIPWgkaadesGRFRSREELERLydfiNPDDQTVVYCRIGERSSH 253
Cdd:cd00158   13 LLDVREPEEY----------------AAGHIPGAINIPL-------SELEERAALLEL----DKDKPIVVYCRSGNRSAR 65

                         90       100
                 ....*....|....*....|....
gi 489512300 254 TWFVLTHLLGKaDVRNYDGSWTEW 277
Cdd:cd00158   66 AAKLLRKAGGT-NVYNLEGGMLAW 88
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 47-129 3.43e-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: 58.65  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300   47 YDVGHIPGAVKIDWHTdlndprvrDYINGEQFAELMDR-KGIARDDTVVIYgDKSNWWAAYALWVFTLFGHADVRLLNGG 125
Cdd:pfam00581  17 YAKGHIPGAVNVPLSS--------LSLPPLPLLELLEKlLELLKDKPIVVY-CNSGNRAAAAAALLKALGYKNVYVLDGG 87


                  ....
gi 489512300  126 RDLW 129
Cdd:pfam00581  88 FEAW 91
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 19-130 8.16e-07

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: 47.48  E-value: 8.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  19 RLVTADWLSAHMGAPGLAIVES--DEDVLLYDVGHIPGAVKIDWHT--DLNDPRVRDYINGEQFAELMDRKGIARDDTVV 94
Cdd:cd01445   20 QLLDARAQSPGTREARGEYLETqpEPDAVGLDSGHIPGASFFDFEEclDEAGFEESMEPSEAEFAAMFEAKGIDLDKHLI 99

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489512300  95 IYG--DKSNWWAAYALWVFTLFGHADVRLLNGGRDLWL 130
Cdd:cd01445  100 ATDgdDLGGFTACHIALAARLCGHPDVAILDGGFFEWF 137
PRK08762 PRK08762
molybdopterin-synthase adenylyltransferase MoeB;
174-290 3.00e-06

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 236337 [Multi-domain]  Cd Length: 376  Bit Score: 48.08  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 174 LIDVRSPEEYtgkrthmpdypeegalRAGHIPTAVHIPwgkaadesgrfRSREELERLYDFINPDDQTVVYCRIGERSSH 253
Cdd:PRK08762  20 LIDVREAHER----------------ASGQAEGALRIP-----------RGFLELRIETHLPDRDREIVLICASGTRSAH 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489512300 254 TWFVLtHLLGKADVRNYDGSWTEW---GNAVRVPIVAGEE 290
Cdd:PRK08762  73 AAATL-RELGYTRVASVAGGFSAWkdaGLPLERPRLLTDE 111
PLN02160 PLN02160
thiosulfate sulfurtransferase
 175-293 3.12e-06

thiosulfate sulfurtransferase


Pssm-ID: 177819 [Multi-domain]  Cd Length: 136  Bit Score: 45.85  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 175 IDVRSPEEYtgKRTHMPdypeegALRAGHIPTAVHIPwgkaadeSGRFRSREELERLYDFINPDDQTVVYCRIGERSSHT 254
Cdd:PLN02160  33 LDVRTQDEF--RRGHCE------AAKIVNIPYMLNTP-------QGRVKNQEFLEQVSSLLNPADDILVGCQSGARSLKA 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489512300 255 wfvLTHLL--GKADVRNYDGSWTEWGNAVRVPIVAGEEPGV 293
Cdd:PLN02160  98 ---TTELVaaGYKKVRNKGGGYLAWVDHSFPINQEEEEPSA 135
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 174-278 3.84e-06

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: 44.56  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 174 LIDVRSPEEYtgkrthmpdypeegalRAGHIPTAVHIPWgkaadesgrfrsrEELERLYDFINPDDQTVVYCRIGERSsh 253
Cdd:cd01524   16 LIDVRTPQEF----------------EKGHIKGAINIPL-------------DELRDRLNELPKDKEIIVYCAVGLRG-- 64

                         90       100
                 ....*....|....*....|....*.
gi 489512300 254 tWFVLTHLLGKA-DVRNYDGSWTEWG 278
Cdd:cd01524   65 -YIAARILTQNGfKVKNLDGGYKTYS 89
TST_Repeat_1 cd01448
Thiosulfate sulfurtransferase (TST), N-terminal, inactive domain. TST contains 2 copies of the ...
 163-277 3.98e-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: 42.22  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 163 DDVLAILGAQPL--IDVRSpeeytgkrtHMPDYPEEGALRAGHIPTAVHIPWGKAADESGRFR----SREELERLydF-- 234
Cdd:cd01448    5 DWLAEHLDDPDVriLDARW---------YLPDRDGRKEYLEGHIPGAVFFDLDEDLDDKSPGPhmlpSPEEFAEL--Lgs 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489512300 235 --INPDDQTVVYCRIGERSS-HTWFVLtHLLGKADVRNYDGSWTEW 277
Cdd:cd01448   74 lgISNDDTVVVYDDGGGFFAaRAWWTL-RYFGHENVRVLDGGLQAW 118
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 21-137 5.40e-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: 5.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  21 VTADWLSAHMGAPGLAIV---ESDEdvllYDVGHIPGAVKIDWHtdlndprvrdyingeQFAELMDRkgIARDDTVVIYg 97
Cdd:COG0607    6 ISPAELAELLESEDAVLLdvrEPEE----FAAGHIPGAINIPLG---------------ELAERLDE--LPKDKPIVVY- 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489512300  98 DKSNWWAAYALWVFTLFGHADVRLLNGGRDLWLAERRETT 137
Cdd:COG0607   64 CASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAAGLPVE 103
TST_Repeats cd01445
Thiosulfate sulfurtransferases (TST) contain 2 copies of the Rhodanese Homology Domain. Only ...
 174-277 1.06e-04

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: 41.70  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 174 LIDVR--SPEEYTGKRTHMPDYPEEGA--LRAGHIPTAVHIPWGKAADESGRFRSREELER-LYDF-----INPDDQTVV 243
Cdd:cd01445   21 LLDARaqSPGTREARGEYLETQPEPDAvgLDSGHIPGASFFDFEECLDEAGFEESMEPSEAeFAAMfeakgIDLDKHLIA 100

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489512300 244 YCR---IGERSSHTWFVLtHLLGKADVRNYDGSWTEW 277
Cdd:cd01445  101 TDGddlGGFTACHIALAA-RLCGHPDVAILDGGFFEW 136
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 41-129 4.03e-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: 38.82  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300  41 DEDVLLYDV--------GHIPGAVKIDWhtdlndprvrdyingEQFAELMDRKGIARDDTVVIYgDKSNWWAAYALWVFT 112
Cdd:cd00158    8 DEDAVLLDVrepeeyaaGHIPGAINIPL---------------SELEERAALLELDKDKPIVVY-CRSGNRSARAAKLLR 71

                         90
                 ....*....|....*..
gi 489512300 113 LFGHADVRLLNGGRDLW 129
Cdd:cd00158   72 KAGGTNVYNLEGGMLAW 88
SelU COG2603
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ...
 163-251 7.42e-04

tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442015 [Multi-domain]  Cd Length: 341  Bit Score: 40.52  E-value: 7.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 163 DDVLAILGAQPLIDVRSPEEYTgkrthmpdypeegalrAGHIPTAVHIPW---------G--------KAADE------S 219
Cdd:COG2603    8 DDFLELLDDDPLIDVRSPVEFA----------------EGHIPGAINLPLlddeeraevGtcykqqgpFAAIKlghalvS 71

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489512300 220 GRFrsREELERLYDFINPDDQTVVYC-RIGERS 251
Cdd:COG2603   72 GKL--AAHREEAWAFAPKHPRPLVYCwRGGLRS 102
RHOD_ThiF cd01526
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ...
 170-281 1.05e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.


Pssm-ID: 238784 [Multi-domain]  Cd Length: 122  Bit Score: 38.06  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 170 GAQP-LIDVRSPEEYtgkrthmpdypeegalRAGHIPTAVHIPWGKAADESGRFRSreeLERLYDFINPDDQTVVYCRIG 248
Cdd:cd01526   22 GKKHvLLDVRPKVHF----------------EICRLPEAINIPLSELLSKAAELKS---LQELPLDNDKDSPIYVVCRRG 82

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489512300 249 ERSSHTWFVLTHLLGKADVRNYDGSWTEWGNAV 281
Cdd:cd01526   83 NDSQTAVRKLKELGLERFVRDIIGGLKAWADKV 115
RHOD_YbbB cd01520
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ...
 173-252 1.84e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.


Pssm-ID: 238778 [Multi-domain]  Cd Length: 128  Bit Score: 37.66  E-value: 1.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 173 PLIDVRSPEEYTgkrthmpdypeegalrAGHIPTAVHIPW---------GKAADESGRFRSRE------------ELERL 231
Cdd:cd01520   15 PLIDVRSPKEFF----------------EGHLPGAINLPLlddeeralvGTLYKQQGREAAIElglelvsgklkrILNEA 78

                         90       100
                 ....*....|....*....|...
gi 489512300 232 YDFINPDDQT-VVYC-RIGERSS 252
Cdd:cd01520   79 WEARLERDPKlLIYCaRGGMRSQ 101
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 174-281 2.45e-03

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 38.92  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 174 LIDVRSPEEYtgkrthmpdypeegalRAGHIPTAVHIPwgkaadeSGRFRSREELERLydfiNPDDQTVVYCRIGERSSH 253
Cdd:PRK07878 306 LIDVREPVEW----------------DIVHIPGAQLIP-------KSEILSGEALAKL----PQDRTIVLYCKTGVRSAE 358

                         90       100
                 ....*....|....*....|....*...
gi 489512300 254 TWFVLtHLLGKADVRNYDGSWTEWGNAV 281
Cdd:PRK07878 359 ALAAL-KKAGFSDAVHLQGGVVAWAKQV 385
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 174-258 6.20e-03

Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.


Pssm-ID: 238786 [Multi-domain]  Cd Length: 101  Bit Score: 35.45  E-value: 6.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 174 LIDVRSPEEYTGKRthmpdypeegalraghIPTAVHIPWGKAADESGRFRSreelerlydfINPDDQTVVYCRIGERSSH 253
Cdd:cd01528   20 LIDVREPEELEIAF----------------LPGFLHLPMSEIPERSKELDS----------DNPDKDIVVLCHHGGRSMQ 73


                 ....*
gi 489512300 254 TWFVL 258
Cdd:cd01528   74 VAQWL 78
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 164-277 9.11e-03

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 37.16  E-value: 9.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489512300 164 DVLAILGAQPLIDVRSPEEYTgkrthmpdypeegalrAGHIPTAVHIPWgkAADESGRFRSReelerlydfINPDDQTVV 243
Cdd:PRK05597 267 RVSALPDGVTLIDVREPSEFA----------------AYSIPGAHNVPL--SAIREGANPPS---------VSAGDEVVV 319

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489512300 244 YCRIGERSSHTWFVLTHlLGKADVRNYDGSWTEW 277
Cdd:PRK05597 320 YCAAGVRSAQAVAILER-AGYTGMSSLDGGIEGW 352
 
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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