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Conserved domains on  [gi|568926774|ref|XP_006538023|]
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thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 2 isoform X1 [Mus musculus]

Protein Classification

rhodanese-related sulfurtransferase( domain architecture ID 1903298)

rhodanese-related sulfurtransferase such as tRNA uridine(34) hydroxylase, which catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TrhO super family cl43319
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
169-461 7.14e-93

tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG1054:

Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 284.34  E-value: 7.14e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 169 VLLYYCYCDLEDPHWVCAWQTALCHHLHLTGKIRIATEGINGTVGGSKVATRLYVEVMLSCPLFKDYlsedDFKSSKGGS 248
Cdd:COG1054    6 VLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADL----EFKESEADG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 249 HCFPELRVGVFEEIVPMG---ISPSqvsyKKPGIHLSPGEFHKEIEkllsqsseeQGNTIILDCRNFYESKIGRFQGCLA 325
Cdd:COG1054   82 HPFPRLKVKLKKEIVTMGlpdVDPN----EGVGTYLSPEEWNALIE---------DPDVVVIDTRNDYEVEIGTFKGAID 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 326 PDIRKFSYFPSYVDKNLDIFRQKRVLMYCTGGIRCERGSAYLRAKGVcKEVFQLKGGIHKYLEEFPD--GFYKGKLFVFD 403
Cdd:COG1054  149 PDTDTFREFPEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGF-EEVYQLEGGILKYLEEVPEegSLWEGECFVFD 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 404 ERFALAYNSS--VVSECSYCGAPWDQYKLCSTPQCRQLVLTCSACQGQgFTACCVTCQDK 461
Cdd:COG1054  228 ERVAVDHNLEpgVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADK-YECCSDECTEE 286
 
Name Accession Description Interval E-value
TrhO COG1054
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
169-461 7.14e-93

tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 284.34  E-value: 7.14e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 169 VLLYYCYCDLEDPHWVCAWQTALCHHLHLTGKIRIATEGINGTVGGSKVATRLYVEVMLSCPLFKDYlsedDFKSSKGGS 248
Cdd:COG1054    6 VLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADL----EFKESEADG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 249 HCFPELRVGVFEEIVPMG---ISPSqvsyKKPGIHLSPGEFHKEIEkllsqsseeQGNTIILDCRNFYESKIGRFQGCLA 325
Cdd:COG1054   82 HPFPRLKVKLKKEIVTMGlpdVDPN----EGVGTYLSPEEWNALIE---------DPDVVVIDTRNDYEVEIGTFKGAID 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 326 PDIRKFSYFPSYVDKNLDIFRQKRVLMYCTGGIRCERGSAYLRAKGVcKEVFQLKGGIHKYLEEFPD--GFYKGKLFVFD 403
Cdd:COG1054  149 PDTDTFREFPEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGF-EEVYQLEGGILKYLEEVPEegSLWEGECFVFD 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 404 ERFALAYNSS--VVSECSYCGAPWDQYKLCSTPQCRQLVLTCSACQGQgFTACCVTCQDK 461
Cdd:COG1054  228 ERVAVDHNLEpgVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADK-YECCSDECTEE 286
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
169-459 5.10e-92

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 282.51  E-value: 5.10e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 169 VLLYYCYCDLEDPHWVCAWQTALCHHLHLTGKIRIATEGINGTVGGSKVATRLYVEVMLSCPLFKDYlsedDFKSSKGGS 248
Cdd:PRK00142   6 VLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADI----RFKISEDDG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 249 HCFPELRVGVFEEIVPMGISPSQVSYKKPGIHLSPGEFHKEIEkllsqsseeQGNTIILDCRNFYESKIGRFQGCLAPDI 328
Cdd:PRK00142  82 HAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLD---------DPDVVFIDMRNDYEYEIGHFENAIEPDI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 329 RKFSYFPSYVDKNLDIFRQKRVLMYCTGGIRCERGSAYLRAKGVcKEVFQLKGGIHKYLEEFPDG--FYKGKLFVFDERF 406
Cdd:PRK00142 153 ETFREFPPWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGF-KEVYQLEGGIITYGEDPETQglLWDGKLYVFDERM 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568926774 407 ALAYN-SSVVSECSYCGAPWDQYKLCSTPQCRQLVLTCSACQGQGFTACCVTCQ 459
Cdd:PRK00142 232 AVPINdEVPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECC 285
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
278-388 8.55e-47

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 157.74  E-value: 8.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 278 GIHLSPGEFHKEIEkllsqsseeQGNTIILDCRNFYESKIGRFQGCLAPDIRKFSYFPSYVDKNLDIFRQKRVLMYCTGG 357
Cdd:cd01518    1 GTYLSPAEWNELLE---------DPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGG 71
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568926774 358 IRCERGSAYLRAKGvCKEVFQLKGGIHKYLE 388
Cdd:cd01518   72 IRCEKASAYLKERG-FKNVYQLKGGILKYLE 101
Rhodanese_C pfam12368
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ...
396-459 3.18e-22

Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some members of the Rhodanase family. Rhodanase is pfam00581.


Pssm-ID: 463552 [Multi-domain]  Cd Length: 66  Bit Score: 90.07  E-value: 3.18e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568926774  396 KGKLFVFDERFALAYNSS--VVSECSYCGAPWDQYKLCSTPQCRQLVLTCSACQGQGFTACCVTCQ 459
Cdd:pfam12368   1 KGKLFVFDERLAVVEPSDddVIGKCYHCGKPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEECA 66
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
300-392 3.49e-12

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: 62.48  E-value: 3.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774   300 EQGNTIILDCRNFYESKIGRFQGCLAPDIRKFSYFPSYVD--------KNLDIFRQKRVLMYCTGGIRCERGSAYLRAKG 371
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
                           90       100
                   ....*....|....*....|.
gi 568926774   372 VcKEVFQLKGGIHKYLEEFPD 392
Cdd:smart00450  81 F-KNVYLLDGGYKEWSAAGPP 100
 
Name Accession Description Interval E-value
TrhO COG1054
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
169-461 7.14e-93

tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 284.34  E-value: 7.14e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 169 VLLYYCYCDLEDPHWVCAWQTALCHHLHLTGKIRIATEGINGTVGGSKVATRLYVEVMLSCPLFKDYlsedDFKSSKGGS 248
Cdd:COG1054    6 VLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADL----EFKESEADG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 249 HCFPELRVGVFEEIVPMG---ISPSqvsyKKPGIHLSPGEFHKEIEkllsqsseeQGNTIILDCRNFYESKIGRFQGCLA 325
Cdd:COG1054   82 HPFPRLKVKLKKEIVTMGlpdVDPN----EGVGTYLSPEEWNALIE---------DPDVVVIDTRNDYEVEIGTFKGAID 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 326 PDIRKFSYFPSYVDKNLDIFRQKRVLMYCTGGIRCERGSAYLRAKGVcKEVFQLKGGIHKYLEEFPD--GFYKGKLFVFD 403
Cdd:COG1054  149 PDTDTFREFPEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGF-EEVYQLEGGILKYLEEVPEegSLWEGECFVFD 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 404 ERFALAYNSS--VVSECSYCGAPWDQYKLCSTPQCRQLVLTCSACQGQgFTACCVTCQDK 461
Cdd:COG1054  228 ERVAVDHNLEpgVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADK-YECCSDECTEE 286
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
169-459 5.10e-92

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 282.51  E-value: 5.10e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 169 VLLYYCYCDLEDPHWVCAWQTALCHHLHLTGKIRIATEGINGTVGGSKVATRLYVEVMLSCPLFKDYlsedDFKSSKGGS 248
Cdd:PRK00142   6 VLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADI----RFKISEDDG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 249 HCFPELRVGVFEEIVPMGISPSQVSYKKPGIHLSPGEFHKEIEkllsqsseeQGNTIILDCRNFYESKIGRFQGCLAPDI 328
Cdd:PRK00142  82 HAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLD---------DPDVVFIDMRNDYEYEIGHFENAIEPDI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 329 RKFSYFPSYVDKNLDIFRQKRVLMYCTGGIRCERGSAYLRAKGVcKEVFQLKGGIHKYLEEFPDG--FYKGKLFVFDERF 406
Cdd:PRK00142 153 ETFREFPPWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGF-KEVYQLEGGIITYGEDPETQglLWDGKLYVFDERM 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568926774 407 ALAYN-SSVVSECSYCGAPWDQYKLCSTPQCRQLVLTCSACQGQGFTACCVTCQ 459
Cdd:PRK00142 232 AVPINdEVPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECC 285
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
278-388 8.55e-47

Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, Bacillus subtilis YbfQ, and similar uncharacterized proteins.


Pssm-ID: 238776 [Multi-domain]  Cd Length: 101  Bit Score: 157.74  E-value: 8.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 278 GIHLSPGEFHKEIEkllsqsseeQGNTIILDCRNFYESKIGRFQGCLAPDIRKFSYFPSYVDKNLDIFRQKRVLMYCTGG 357
Cdd:cd01518    1 GTYLSPAEWNELLE---------DPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGG 71
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568926774 358 IRCERGSAYLRAKGvCKEVFQLKGGIHKYLE 388
Cdd:cd01518   72 IRCEKASAYLKERG-FKNVYQLKGGILKYLE 101
PRK05320 PRK05320
rhodanese superfamily protein; Provisional
173-408 4.17e-35

rhodanese superfamily protein; Provisional


Pssm-ID: 235405 [Multi-domain]  Cd Length: 257  Bit Score: 131.69  E-value: 4.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 173 YCYCDLEDPHWVCAWQTALCHHLHLTGKIRIATEGINGTVGGSKVATRLYVEVMLSCPLFKDYlsedDFKSSKGGSHCFP 252
Cdd:PRK05320   9 YKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRADARFADL----QVKESLSDSQPFR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 253 ELRVGVFEEIVPM---GISPSQvsYKKPGIhlSPgefhKEIEKLLSQSSEEQGNTII-LDCRNFYESKIGRFQGCLAPDI 328
Cdd:PRK05320  85 RMLVKLKREIITMkrpAIRPEL--GRAPSV--DA----ATLKRWLDQGHDDAGRPVVmLDTRNAFEVDVGTFDGALDYRI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 329 RKFSYFPSYVDKNLDIFRQKRVLMYCTGGIRCERGSAYLRAKGVcKEVFQLKGGIHKYLEEFPDGFYKGKLFVFDERFAL 408
Cdd:PRK05320 157 DKFTEFPEALAAHRADLAGKTVVSFCTGGIRCEKAAIHMQEVGI-DNVYQLEGGILKYFEEVGGAHYDGDCFVFDYRTAL 235
PRK01415 PRK01415
hypothetical protein; Validated
164-409 9.49e-34

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 127.75  E-value: 9.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 164 DEEGEVLLYYCYCDLEDPHWVCAWQTALCHHLHLTGKIRIATEGINGTVGGSKVATRLYVEVMLSCPLFKDYlsedDFKS 243
Cdd:PRK01415   2 NEKIAILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKLTGPKDV----NVKI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 244 SKGGSHCFPELRVGVFEEIVPMGISPSQVSYKKpGIHLSPGEFHKEIEKllsqsseeqGNTIILDCRNFYESKIGRFQGC 323
Cdd:PRK01415  78 NYSDVHPFQKLKVRLKKEIVAMNVDDLNVDLFK-GEYIEPKDWDEFITK---------QDVIVIDTRNDYEVEVGTFKSA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 324 LAPDIRKFSYFPSYVDKNLDIFRQKRVLMYCTGGIRCERGSAYLRAKGVcKEVFQLKGGIHKYLEEF--PDGFYKGKLFV 401
Cdd:PRK01415 148 INPNTKTFKQFPAWVQQNQELLKGKKIAMVCTGGIRCEKSTSLLKSIGY-DEVYHLKGGILQYLEDTqnKNNLWQGECFV 226

                 ....*...
gi 568926774 402 FDERFALA 409
Cdd:PRK01415 227 FDDRRAVT 234
Rhodanese_C pfam12368
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ...
396-459 3.18e-22

Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some members of the Rhodanase family. Rhodanase is pfam00581.


Pssm-ID: 463552 [Multi-domain]  Cd Length: 66  Bit Score: 90.07  E-value: 3.18e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568926774  396 KGKLFVFDERFALAYNSS--VVSECSYCGAPWDQYKLCSTPQCRQLVLTCSACQGQGFTACCVTCQ 459
Cdd:pfam12368   1 KGKLFVFDERLAVVEPSDddVIGKCYHCGKPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEECA 66
UPF0176_N pfam17773
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ...
169-262 2.19e-16

UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family proteins. It adopts a fold similar to the pfam00708 family.


Pssm-ID: 465497 [Multi-domain]  Cd Length: 92  Bit Score: 74.07  E-value: 2.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774  169 VLLYYCYCDLEDPHWVCAWQTALCHHLHLTGKIRIATEGINGTVGGSKVATRLYVEVMLSCPLFKDYlsedDFKSSKGGS 248
Cdd:pfam17773   3 VIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADL----DFKESYSDE 78
                          90
                  ....*....|....
gi 568926774  249 HCFPELRVGVFEEI 262
Cdd:pfam17773  79 HPFRRLKVKLKKEI 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
300-392 3.49e-12

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: 62.48  E-value: 3.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774   300 EQGNTIILDCRNFYESKIGRFQGCLAPDIRKFSYFPSYVD--------KNLDIFRQKRVLMYCTGGIRCERGSAYLRAKG 371
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
                           90       100
                   ....*....|....*....|.
gi 568926774   372 VcKEVFQLKGGIHKYLEEFPD 392
Cdd:smart00450  81 F-KNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
300-386 6.47e-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: 50.18  E-value: 6.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774  300 EQGNTIILDCRNFYESKIGRFQG----CLAPDIRKFSYFPSYVDKNLDIFRQKRVLMYCTGGIRCERGSAYLRAKGVcKE 375
Cdd:pfam00581   2 EDGKVVLIDVRPPEEYAKGHIPGavnvPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGY-KN 80
                          90
                  ....*....|.
gi 568926774  376 VFQLKGGIHKY 386
Cdd:pfam00581  81 VYVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
280-389 2.34e-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: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926774 280 HLSPGEFHKEIEkllsqsseeQGNTIILDCRNFYESKIGRFQGCL-APdirkFSYFPSYVDKnLDifRQKRVLMYCTGGI 358
Cdd:COG0607    5 EISPAELAELLE---------SEDAVLLDVREPEEFAAGHIPGAInIP----LGELAERLDE-LP--KDKPIVVYCASGG 68
                         90       100       110
                 ....*....|....*....|....*....|.
gi 568926774 359 RCERGSAYLRAKGVcKEVFQLKGGIHKYLEE 389
Cdd:COG0607   69 RSAQAAALLRRAGY-TNVYNLAGGIEAWKAA 98
 
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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