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Conserved domains on  [gi|111038120|ref|NP_640339|]
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thiosulfate sulfurtransferase/rhodanese-like domain-containing protein 2 [Homo sapiens]

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 ...
170-462 2.07e-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: 286.65  E-value: 2.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 170 VLLYYCYHDLEDPQWICAWQTALCQHLHLTGKIRIAAEGINGTVGGSKLATRLYVEVMLSFPLFKDdLckdDFKTSKGGA 249
Cdd:COG1054    6 VLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFAD-L---EFKESEADG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 250 HCFPELRVGVFEEIVPMG---ISPKKisykKPGIHLSPGEFHKEVEkflsqanqeQSDTILLDCRNFYESKIGRFQGCLA 326
Cdd:COG1054   82 HPFPRLKVKLKKEIVTMGlpdVDPNE----GVGTYLSPEEWNALIE---------DPDVVVIDTRNDYEVEIGTFKGAID 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 327 PDIRKFSYFPSYVDKNLELFREKRVLMYCTGGIRCERGSAYLKAKGVcKEVFQLKGGIHKYLEEFPD--GFYKGKLFVFD 404
Cdd:COG1054  149 PDTDTFREFPEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGF-EEVYQLEGGILKYLEEVPEegSLWEGECFVFD 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 405 ERYALSYNS--DVVSECSYCGARWDQYKLCSTPQCRQLVLTCPACQGQgFTACCVTCQDK 462
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 ...
170-462 2.07e-93

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


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 286.65  E-value: 2.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 170 VLLYYCYHDLEDPQWICAWQTALCQHLHLTGKIRIAAEGINGTVGGSKLATRLYVEVMLSFPLFKDdLckdDFKTSKGGA 249
Cdd:COG1054    6 VLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFAD-L---EFKESEADG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 250 HCFPELRVGVFEEIVPMG---ISPKKisykKPGIHLSPGEFHKEVEkflsqanqeQSDTILLDCRNFYESKIGRFQGCLA 326
Cdd:COG1054   82 HPFPRLKVKLKKEIVTMGlpdVDPNE----GVGTYLSPEEWNALIE---------DPDVVVIDTRNDYEVEIGTFKGAID 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 327 PDIRKFSYFPSYVDKNLELFREKRVLMYCTGGIRCERGSAYLKAKGVcKEVFQLKGGIHKYLEEFPD--GFYKGKLFVFD 404
Cdd:COG1054  149 PDTDTFREFPEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGF-EEVYQLEGGILKYLEEVPEegSLWEGECFVFD 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 405 ERYALSYNS--DVVSECSYCGARWDQYKLCSTPQCRQLVLTCPACQGQgFTACCVTCQDK 462
Cdd:COG1054  228 ERVAVDHNLepGVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADK-YECCSDECTEE 286
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
170-484 8.56e-92

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 282.89  E-value: 8.56e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 170 VLLYYCYHDLEDPQWICAWQTALCQHLHLTGKIRIAAEGINGTVGGSKLATRLYVEVMLSFPLFKDDlckdDFKTSKGGA 249
Cdd:PRK00142   6 VLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADI----RFKISEDDG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 250 HCFPELRVGVFEEIVPMGISPKKISYKKPGIHLSPGEFHKEVEkflsqanqeQSDTILLDCRNFYESKIGRFQGCLAPDI 329
Cdd:PRK00142  82 HAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLD---------DPDVVFIDMRNDYEYEIGHFENAIEPDI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 330 RKFSYFPSYVDKNLELFREKRVLMYCTGGIRCERGSAYLKAKGVcKEVFQLKGGIHKYLEEFPDG--FYKGKLFVFDERY 407
Cdd:PRK00142 153 ETFREFPPWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGF-KEVYQLEGGIITYGEDPETQglLWDGKLYVFDERM 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 111038120 408 ALSYN-SDVVSECSYCGARWDQYKLCSTPQCRQLVLTCPACQGQGFTACCVTCQ-DKGSRKVSGPMQDSFKEECECTAR 484
Cdd:PRK00142 232 AVPINdEVPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCeHPRNRYVEQRGRRRERENELLIFN 310
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
279-389 5.56e-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: 158.51  E-value: 5.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 279 GIHLSPGEFHKEVEkflsqanqeQSDTILLDCRNFYESKIGRFQGCLAPDIRKFSYFPSYVDKNLELFREKRVLMYCTGG 358
Cdd:cd01518    1 GTYLSPAEWNELLE---------DPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGG 71
                         90       100       110
                 ....*....|....*....|....*....|.
gi 111038120 359 IRCERGSAYLKAKGvCKEVFQLKGGIHKYLE 389
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 ...
397-460 5.80e-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: 89.30  E-value: 5.80e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111038120  397 KGKLFVFDERYALSYNS--DVVSECSYCGARWDQYKLCSTPQCRQLVLTCPACQGQGFTACCVTCQ 460
Cdd:pfam12368   1 KGKLFVFDERLAVVEPSddDVIGKCYHCGKPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEECA 66
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
301-393 1.11e-11

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: 61.32  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120   301 EQSDTILLDCRNFYESKIGRFQGCLAPDIRKFSYFPSYVD--------KNLELFREKRVLMYCTGGIRCERGSAYLKAKG 372
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
                           90       100
                   ....*....|....*....|.
gi 111038120   373 VcKEVFQLKGGIHKYLEEFPD 393
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 ...
170-462 2.07e-93

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


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 286.65  E-value: 2.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 170 VLLYYCYHDLEDPQWICAWQTALCQHLHLTGKIRIAAEGINGTVGGSKLATRLYVEVMLSFPLFKDdLckdDFKTSKGGA 249
Cdd:COG1054    6 VLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFAD-L---EFKESEADG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 250 HCFPELRVGVFEEIVPMG---ISPKKisykKPGIHLSPGEFHKEVEkflsqanqeQSDTILLDCRNFYESKIGRFQGCLA 326
Cdd:COG1054   82 HPFPRLKVKLKKEIVTMGlpdVDPNE----GVGTYLSPEEWNALIE---------DPDVVVIDTRNDYEVEIGTFKGAID 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 327 PDIRKFSYFPSYVDKNLELFREKRVLMYCTGGIRCERGSAYLKAKGVcKEVFQLKGGIHKYLEEFPD--GFYKGKLFVFD 404
Cdd:COG1054  149 PDTDTFREFPEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGF-EEVYQLEGGILKYLEEVPEegSLWEGECFVFD 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 405 ERYALSYNS--DVVSECSYCGARWDQYKLCSTPQCRQLVLTCPACQGQgFTACCVTCQDK 462
Cdd:COG1054  228 ERVAVDHNLepGVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADK-YECCSDECTEE 286
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
170-484 8.56e-92

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 282.89  E-value: 8.56e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 170 VLLYYCYHDLEDPQWICAWQTALCQHLHLTGKIRIAAEGINGTVGGSKLATRLYVEVMLSFPLFKDDlckdDFKTSKGGA 249
Cdd:PRK00142   6 VLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADI----RFKISEDDG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 250 HCFPELRVGVFEEIVPMGISPKKISYKKPGIHLSPGEFHKEVEkflsqanqeQSDTILLDCRNFYESKIGRFQGCLAPDI 329
Cdd:PRK00142  82 HAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLD---------DPDVVFIDMRNDYEYEIGHFENAIEPDI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 330 RKFSYFPSYVDKNLELFREKRVLMYCTGGIRCERGSAYLKAKGVcKEVFQLKGGIHKYLEEFPDG--FYKGKLFVFDERY 407
Cdd:PRK00142 153 ETFREFPPWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGF-KEVYQLEGGIITYGEDPETQglLWDGKLYVFDERM 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 111038120 408 ALSYN-SDVVSECSYCGARWDQYKLCSTPQCRQLVLTCPACQGQGFTACCVTCQ-DKGSRKVSGPMQDSFKEECECTAR 484
Cdd:PRK00142 232 AVPINdEVPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCeHPRNRYVEQRGRRRERENELLIFN 310
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
279-389 5.56e-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: 158.51  E-value: 5.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 279 GIHLSPGEFHKEVEkflsqanqeQSDTILLDCRNFYESKIGRFQGCLAPDIRKFSYFPSYVDKNLELFREKRVLMYCTGG 358
Cdd:cd01518    1 GTYLSPAEWNELLE---------DPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGG 71
                         90       100       110
                 ....*....|....*....|....*....|.
gi 111038120 359 IRCERGSAYLKAKGvCKEVFQLKGGIHKYLE 389
Cdd:cd01518   72 IRCEKASAYLKERG-FKNVYQLKGGILKYLE 101
PRK01415 PRK01415
hypothetical protein; Validated
165-410 3.71e-36

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 134.69  E-value: 3.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 165 SEEGEVLLYYCYHDLEDPQWICAWQTALCQHLHLTGKIRIAAEGINGTVGGSKLATRLYVEVMLSFPLFKDDlckdDFKT 244
Cdd:PRK01415   2 NEKIAILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKLTGPKDV----NVKI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 245 SKGGAHCFPELRVGVFEEIVPMGISPKKISYKKpGIHLSPgefhKEVEKFLSQanqeqSDTILLDCRNFYESKIGRFQGC 324
Cdd:PRK01415  78 NYSDVHPFQKLKVRLKKEIVAMNVDDLNVDLFK-GEYIEP----KDWDEFITK-----QDVIVIDTRNDYEVEVGTFKSA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 325 LAPDIRKFSYFPSYVDKNLELFREKRVLMYCTGGIRCERGSAYLKAKGVcKEVFQLKGGIHKYLEEF--PDGFYKGKLFV 402
Cdd:PRK01415 148 INPNTKTFKQFPAWVQQNQELLKGKKIAMVCTGGIRCEKSTSLLKSIGY-DEVYHLKGGILQYLEDTqnKNNLWQGECFV 226

                 ....*...
gi 111038120 403 FDERYALS 410
Cdd:PRK01415 227 FDDRRAVT 234
PRK05320 PRK05320
rhodanese superfamily protein; Provisional
175-409 1.28e-35

rhodanese superfamily protein; Provisional


Pssm-ID: 235405 [Multi-domain]  Cd Length: 257  Bit Score: 133.61  E-value: 1.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 175 CYH--DLEDPQWICAWQTALCQHLHLTGKIRIAAEGINGTVGGSKLATRLYVEVMLSFPLFKDDlckdDFKTSKGGAHCF 252
Cdd:PRK05320   8 AYKfvSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRADARFADL----QVKESLSDSQPF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 253 PELRVGVFEEIvpmgispkkISYKKPGIH----LSPGEFHKEVEKFLSQANQEQS-DTILLDCRNFYESKIGRFQGCLAP 327
Cdd:PRK05320  84 RRMLVKLKREI---------ITMKRPAIRpelgRAPSVDAATLKRWLDQGHDDAGrPVVMLDTRNAFEVDVGTFDGALDY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 328 DIRKFSYFPSYVDKNLELFREKRVLMYCTGGIRCERGSAYLKAKGVcKEVFQLKGGIHKYLEEFPDGFYKGKLFVFDERY 407
Cdd:PRK05320 155 RIDKFTEFPEALAAHRADLAGKTVVSFCTGGIRCEKAAIHMQEVGI-DNVYQLEGGILKYFEEVGGAHYDGDCFVFDYRT 233

                 ..
gi 111038120 408 AL 409
Cdd:PRK05320 234 AL 235
Rhodanese_C pfam12368
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ...
397-460 5.80e-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: 89.30  E-value: 5.80e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111038120  397 KGKLFVFDERYALSYNS--DVVSECSYCGARWDQYKLCSTPQCRQLVLTCPACQGQGFTACCVTCQ 460
Cdd:pfam12368   1 KGKLFVFDERLAVVEPSddDVIGKCYHCGKPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEECA 66
UPF0176_N pfam17773
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ...
170-263 9.66e-18

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: 78.30  E-value: 9.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120  170 VLLYYCYHDLEDPQWICAWQTALCQHLHLTGKIRIAAEGINGTVGGSKLATRLYVEVMLSFPLFKDdlckDDFKTSKGGA 249
Cdd:pfam17773   3 VIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFAD----LDFKESYSDE 78
                          90
                  ....*....|....
gi 111038120  250 HCFPELRVGVFEEI 263
Cdd:pfam17773  79 HPFRRLKVKLKKEI 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
301-393 1.11e-11

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: 61.32  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120   301 EQSDTILLDCRNFYESKIGRFQGCLAPDIRKFSYFPSYVD--------KNLELFREKRVLMYCTGGIRCERGSAYLKAKG 372
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
                           90       100
                   ....*....|....*....|.
gi 111038120   373 VcKEVFQLKGGIHKYLEEFPD 393
Cdd:smart00450  81 F-KNVYLLDGGYKEWSAAGPP 100
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
300-387 1.06e-07

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: 49.79  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120  300 QEQSDTILLDCRNFYESKIGRFQG----CLAPDIRKFSYFPSYVDKNLELFREKRVLMYCTGGIRCERGSAYLKAKGVcK 375
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGavnvPLSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGY-K 79
                          90
                  ....*....|..
gi 111038120  376 EVFQLKGGIHKY 387
Cdd:pfam00581  80 NVYVLDGGFEAW 91
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
281-390 1.40e-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: 46.88  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111038120 281 HLSPGEFHKEVEkflsqanqeQSDTILLDCRNFYESKIGRFQGCL-APdirkFSYFPSYVDknlELFREKRVLMYCTGGI 359
Cdd:COG0607    5 EISPAELAELLE---------SEDAVLLDVREPEEFAAGHIPGAInIP----LGELAERLD---ELPKDKPIVVYCASGG 68
                         90       100       110
                 ....*....|....*....|....*....|.
gi 111038120 360 RCERGSAYLKAKGVcKEVFQLKGGIHKYLEE 390
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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