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Conserved domains on  [gi|334182661|ref|NP_001185025|]
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Rhodanese/Cell cycle control phosphatase superfamily protein [Arabidopsis thaliana]

Protein Classification

rhodanese-like domain-containing protein( domain architecture ID 13)

rhodanese-like domain-containing protein may have sulfurtransferase activity if an active site cysteine is present

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 81-443 2.90e-88

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.


The actual alignment was detected with superfamily member PRK00142:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 314  Bit Score: 271.34  E-value: 2.90e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661  81 EDFIVVNFYRFVSIGDPEAEIEKHLSFLKDLNIRGRIYLNEQGINAQYSGPSKDALAYVEWLKGDDRFSDLLVQMSPAmN 160
Cdd:PRK00142   2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISED-D 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 161 RHAFPKLKLQNKPSLVqyeggisHLPLLDP--PMR--AKPLEPSEWKRKLkdltDDDEAspsnsgksyILLDVRNGYEWD 236
Cdd:PRK00142  81 GHAFPRLSVKVRKEIV-------ALGLDDDidPLEnvGTYLKPKEVNELL----DDPDV---------VFIDMRNDYEYE 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 237 VGHFRGAHRPEVDCFRNtsfgLSDEKEAPSDPLinvdKEKtDILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLK 316
Cdd:PRK00142 141 IGHFENAIEPDIETFRE----FPPWVEENLDPL----KDK-KVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGE 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 317 EEGTAE--WVGNLFVFDSRLSLPpaayndnvvdkaVGDNVVdeagrtpqtpvdtsFARCYLCNSQVQelRHRNCANLDCN 394
Cdd:PRK00142 212 DPETQGllWDGKLYVFDERMAVP------------INDEVP--------------IGHCHQCGTPCD--RYVNCANPACN 263

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 334182661 395 RLFLCCAECVVDLKGCCCSDCISAPRLRPVL-HGVKRYEKWHVYRDSEEQ 443
Cdd:PRK00142 264 LLILQCEECEEKYLGCCSEECCEHPRNRYVEqRGRRRERENELLIFNKER 313
 
Name Accession Description Interval E-value
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
81-443 2.90e-88

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 271.34  E-value: 2.90e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661  81 EDFIVVNFYRFVSIGDPEAEIEKHLSFLKDLNIRGRIYLNEQGINAQYSGPSKDALAYVEWLKGDDRFSDLLVQMSPAmN 160
Cdd:PRK00142   2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISED-D 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 161 RHAFPKLKLQNKPSLVqyeggisHLPLLDP--PMR--AKPLEPSEWKRKLkdltDDDEAspsnsgksyILLDVRNGYEWD 236
Cdd:PRK00142  81 GHAFPRLSVKVRKEIV-------ALGLDDDidPLEnvGTYLKPKEVNELL----DDPDV---------VFIDMRNDYEYE 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 237 VGHFRGAHRPEVDCFRNtsfgLSDEKEAPSDPLinvdKEKtDILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLK 316
Cdd:PRK00142 141 IGHFENAIEPDIETFRE----FPPWVEENLDPL----KDK-KVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGE 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 317 EEGTAE--WVGNLFVFDSRLSLPpaayndnvvdkaVGDNVVdeagrtpqtpvdtsFARCYLCNSQVQelRHRNCANLDCN 394
Cdd:PRK00142 212 DPETQGllWDGKLYVFDERMAVP------------INDEVP--------------IGHCHQCGTPCD--RYVNCANPACN 263

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 334182661 395 RLFLCCAECVVDLKGCCCSDCISAPRLRPVL-HGVKRYEKWHVYRDSEEQ 443
Cdd:PRK00142 264 LLILQCEECEEKYLGCCSEECCEHPRNRYVEqRGRRRERENELLIFNKER 313
TrhO COG1054
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
 81-442 3.58e-81

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


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 252.75  E-value: 3.58e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661  81 EDFIVVNFYRFVSIGDPEAEIEKHLSFLKDLNIRGRIYLNEQGINAQYSGPSKDALAYVEWLKGDDRFSDLLVQMSPAmN 160
Cdd:COG1054    2 KPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEA-D 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 161 RHAFPKLKLQNKPSLVQyeggiSHLPLLDP-PMRAKPLEPSEWkrklKDLTDDDEAspsnsgksyILLDVRNGYEWDVGH 239
Cdd:COG1054   81 GHPFPRLKVKLKKEIVT-----MGLPDVDPnEGVGTYLSPEEW----NALIEDPDV---------VVIDTRNDYEVEIGT 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 240 FRGAHRPEVDCFRNtsfgLSDEKEAPSDPLinvdKEKTdILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLKEEG 319
Cdd:COG1054  143 FKGAIDPDTDTFRE----FPEWVEENLDDL----KDKK-VAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVP 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 320 TAE--WVGNLFVFDSRLSLPPaayndnvvdkavgdnvvdeagrtpqTPVDTSFARCYLCNSQVqeLRHRNCANLDCNRLF 397
Cdd:COG1054  214 EEGslWEGECFVFDERVAVDH-------------------------NLEPGVIGLCHACGTPC--DRYVNCANDPCYELG 266

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 334182661 398 LCCAECvVDLKGCCCSDCISAPRlrpvlhgvKRYEKWHVYRDSEE 442
Cdd:COG1054  267 VSCPHC-ADKYECCSDECTEEQR--------ARYERQRQLRLAKE 302
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 197-316 2.29e-45

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: 152.73  E-value: 2.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 197 LEPSEWKRKLKDltdddeaspsnsgKSYILLDVRNGYEWDVGHFRGAHRPEVDCFRNTSFGLSDEKEapsdplinvDKEK 276
Cdd:cd01518    4 LSPAEWNELLED-------------PEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLD---------LLKG 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 334182661 277 TDILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLK 316
Cdd:cd01518   62 KKVLMYCTGGIRCEKASAYLKERGFKNVYQLKGGILKYLE 101
UPF0176_N pfam17773
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ...
 83-168 5.02e-23

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: 92.56  E-value: 5.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661   83 FIVVNFYRFVSIGDPEAEIEKHLSFLKDLNIRGRIYLNEQGINAQYSGPSKDALAYVEWLKGDDRFSDLLVQMSPAmNRH 162
Cdd:pfam17773   1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYS-DEH 79


                  ....*.
gi 334182661  163 AFPKLK 168
Cdd:pfam17773  80 PFRRLK 85
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 220-319 9.11e-13

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: 64.02  E-value: 9.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661   220 SGKSYILLDVRNGYEWDVGHFRGA-HRPEVDCFRNTSFGLSDEKEAPsDPLINVDKEKTdILMYCTGGIRCDVYSTVLRQ 298
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAvNIPLSELLDRRGELDILEFEEL-LKRLGLDKDKP-VVVYCRSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|.
gi 334182661   299 RGFKNLYTLKGGVSHYLKEEG 319
Cdd:smart00450  79 LGFKNVYLLDGGYKEWSAAGP 99
 
Name Accession Description Interval E-value
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
81-443 2.90e-88

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 271.34  E-value: 2.90e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661  81 EDFIVVNFYRFVSIGDPEAEIEKHLSFLKDLNIRGRIYLNEQGINAQYSGPSKDALAYVEWLKGDDRFSDLLVQMSPAmN 160
Cdd:PRK00142   2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISED-D 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 161 RHAFPKLKLQNKPSLVqyeggisHLPLLDP--PMR--AKPLEPSEWKRKLkdltDDDEAspsnsgksyILLDVRNGYEWD 236
Cdd:PRK00142  81 GHAFPRLSVKVRKEIV-------ALGLDDDidPLEnvGTYLKPKEVNELL----DDPDV---------VFIDMRNDYEYE 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 237 VGHFRGAHRPEVDCFRNtsfgLSDEKEAPSDPLinvdKEKtDILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLK 316
Cdd:PRK00142 141 IGHFENAIEPDIETFRE----FPPWVEENLDPL----KDK-KVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGE 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 317 EEGTAE--WVGNLFVFDSRLSLPpaayndnvvdkaVGDNVVdeagrtpqtpvdtsFARCYLCNSQVQelRHRNCANLDCN 394
Cdd:PRK00142 212 DPETQGllWDGKLYVFDERMAVP------------INDEVP--------------IGHCHQCGTPCD--RYVNCANPACN 263

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 334182661 395 RLFLCCAECVVDLKGCCCSDCISAPRLRPVL-HGVKRYEKWHVYRDSEEQ 443
Cdd:PRK00142 264 LLILQCEECEEKYLGCCSEECCEHPRNRYVEqRGRRRERENELLIFNKER 313
TrhO COG1054
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
 81-442 3.58e-81

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


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 252.75  E-value: 3.58e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661  81 EDFIVVNFYRFVSIGDPEAEIEKHLSFLKDLNIRGRIYLNEQGINAQYSGPSKDALAYVEWLKGDDRFSDLLVQMSPAmN 160
Cdd:COG1054    2 KPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEA-D 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 161 RHAFPKLKLQNKPSLVQyeggiSHLPLLDP-PMRAKPLEPSEWkrklKDLTDDDEAspsnsgksyILLDVRNGYEWDVGH 239
Cdd:COG1054   81 GHPFPRLKVKLKKEIVT-----MGLPDVDPnEGVGTYLSPEEW----NALIEDPDV---------VVIDTRNDYEVEIGT 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 240 FRGAHRPEVDCFRNtsfgLSDEKEAPSDPLinvdKEKTdILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLKEEG 319
Cdd:COG1054  143 FKGAIDPDTDTFRE----FPEWVEENLDDL----KDKK-VAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVP 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 320 TAE--WVGNLFVFDSRLSLPPaayndnvvdkavgdnvvdeagrtpqTPVDTSFARCYLCNSQVqeLRHRNCANLDCNRLF 397
Cdd:COG1054  214 EEGslWEGECFVFDERVAVDH-------------------------NLEPGVIGLCHACGTPC--DRYVNCANDPCYELG 266

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 334182661 398 LCCAECvVDLKGCCCSDCISAPRlrpvlhgvKRYEKWHVYRDSEE 442
Cdd:COG1054  267 VSCPHC-ADKYECCSDECTEEQR--------ARYERQRQLRLAKE 302
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
 197-316 2.29e-45

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: 152.73  E-value: 2.29e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 197 LEPSEWKRKLKDltdddeaspsnsgKSYILLDVRNGYEWDVGHFRGAHRPEVDCFRNTSFGLSDEKEapsdplinvDKEK 276
Cdd:cd01518    4 LSPAEWNELLED-------------PEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLD---------LLKG 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 334182661 277 TDILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLK 316
Cdd:cd01518   62 KKVLMYCTGGIRCEKASAYLKERGFKNVYQLKGGILKYLE 101
PRK05320 PRK05320
rhodanese superfamily protein; Provisional
 85-339 3.74e-33

rhodanese superfamily protein; Provisional


Pssm-ID: 235405 [Multi-domain]  Cd Length: 257  Bit Score: 125.52  E-value: 3.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661  85 VVNF--YRFVSIGDPEAEIEKHLSFLKDLNIRGRIYLNEQGINAQYSGPSKDALAYVEWLKGDDRFSDLLVQMSPAMNRh 162
Cdd:PRK05320   3 IVNIaaYKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRADARFADLQVKESLSDSQ- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 163 AFPKLKLQNKPSLVQYeggisHLPLLDPPM-RAKPLEPSEWKRKLKDLTDDDeaspsnsGKSYILLDVRNGYEWDVGHFR 241
Cdd:PRK05320  82 PFRRMLVKLKREIITM-----KRPAIRPELgRAPSVDAATLKRWLDQGHDDA-------GRPVVMLDTRNAFEVDVGTFD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 242 GAHRPEVDCFRNTSFGLSDEKEAPSDplinvdkeKTdILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLKEEGTA 321
Cdd:PRK05320 150 GALDYRIDKFTEFPEALAAHRADLAG--------KT-VVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFEEVGGA 220

                        250
                 ....*....|....*...
gi 334182661 322 EWVGNLFVFDSRLSLPPA 339
Cdd:PRK05320 221 HYDGDCFVFDYRTALDPQ 238
PRK01415 PRK01415
hypothetical protein; Validated
 81-333 3.97e-25

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 103.49  E-value: 3.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661  81 EDFIVVNFYRFVSIGDPEAEIEKHLSFLKDLNIRGRIYLNEQGINAQYSGPSKDALAYVEWLKGDDRFSDLLVQMSPAmN 160
Cdd:PRK01415   3 EKIAILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKLTGPKDVNVKINYS-D 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 161 RHAFPKLKLQNKPSLVQYEGGISHLPLLdppmRAKPLEPSEWKRKLkdltdddeaspsnSGKSYILLDVRNGYEWDVGHF 240
Cdd:PRK01415  82 VHPFQKLKVRLKKEIVAMNVDDLNVDLF----KGEYIEPKDWDEFI-------------TKQDVIVIDTRNDYEVEVGTF 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 241 RGAHRPEVDCFRNTSFGLSDEKEapsdpLINVDKektdILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLKEEGT 320
Cdd:PRK01415 145 KSAINPNTKTFKQFPAWVQQNQE-----LLKGKK----IAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQN 215

                        250
                 ....*....|....*
gi 334182661 321 AE--WVGNLFVFDSR 333
Cdd:PRK01415 216 KNnlWQGECFVFDDR 230
UPF0176_N pfam17773
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ...
 83-168 5.02e-23

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: 92.56  E-value: 5.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661   83 FIVVNFYRFVSIGDPEAEIEKHLSFLKDLNIRGRIYLNEQGINAQYSGPSKDALAYVEWLKGDDRFSDLLVQMSPAmNRH 162
Cdd:pfam17773   1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYS-DEH 79


                  ....*.
gi 334182661  163 AFPKLK 168
Cdd:pfam17773  80 PFRRLK 85
Rhodanese_C pfam12368
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ...
 325-415 2.89e-18

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: 78.51  E-value: 2.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661  325 GNLFVFDSRLSLPPAayndnvvdkaVGDNVVdeagrtpqtpvdtsfARCYLCNSQVQelRHRNCANLDCNRLFLCCAECV 404
Cdd:pfam12368   2 GKLFVFDERLAVVEP----------SDDDVI---------------GKCYHCGKPCD--RYVNCANPDCNRLFLQCEECA 54

                          90
                  ....*....|.
gi 334182661  405 VDLKGCCCSDC 415
Cdd:pfam12368  55 EKYEGCCSEEC 65
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 220-319 9.11e-13

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: 64.02  E-value: 9.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661   220 SGKSYILLDVRNGYEWDVGHFRGA-HRPEVDCFRNTSFGLSDEKEAPsDPLINVDKEKTdILMYCTGGIRCDVYSTVLRQ 298
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAvNIPLSELLDRRGELDILEFEEL-LKRLGLDKDKP-VVVYCRSGNRSAKAAWLLRE 78

                           90       100
                   ....*....|....*....|.
gi 334182661   299 RGFKNLYTLKGGVSHYLKEEG 319
Cdd:smart00450  79 LGFKNVYLLDGGYKEWSAAGP 99
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 221-312 3.37e-11

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: 59.24  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 221 GKSYILLDVRNGYEWDVGHFRGAHrpevdcfrntSFGLSDEKEAPSDPLINVDKEktdILMYCTGGIRCDVYSTVLRQRG 300
Cdd:cd00158    8 DEDAVLLDVREPEEYAAGHIPGAI----------NIPLSELEERAALLELDKDKP---IVVYCRSGNRSARAAKLLRKAG 74

                         90
                 ....*....|..
gi 334182661 301 FKNLYTLKGGVS 312
Cdd:cd00158   75 GTNVYNLEGGML 86
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 192-317 5.57e-10

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: 56.51  E-value: 5.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 192 MRAKPLEPSEWKRKLKDltdddeaspsnsgKSYILLDVRNGYEWDVGHFRGAhrpevdcfRNTSFGLSDEKeapsdpLIN 271
Cdd:COG0607    1 ASVKEISPAELAELLES-------------EDAVLLDVREPEEFAAGHIPGA--------INIPLGELAER------LDE 53

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 334182661 272 VDKEKTdILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLKE 317
Cdd:COG0607   54 LPKDKP-IVVYCASGGRSAQAAALLRRAGYTNVYNLAGGIEAWKAA 98
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 221-312 3.17e-09

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: 53.64  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661  221 GKSYILLDVRNGYEWDVGHFRGAhrpevdcfRNTSFGLSDEKEAPSDPLINVDKEK---TDILMYCTGGIRCDVYSTVLR 297
Cdd:pfam00581   3 DGKVVLIDVRPPEEYAKGHIPGA--------VNVPLSSLSLPPLPLLELLEKLLELlkdKPIVVYCNSGNRAAAAAALLK 74

                          90
                  ....*....|....*
gi 334182661  298 QRGFKNLYTLKGGVS 312
Cdd:pfam00581  75 ALGYKNVYVLDGGFE 89
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
 221-314 4.40e-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: 44.95  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 221 GKSYILLDVRNGYEWDVGHFRGAHRPEVDCFRntsfglsdekeapsDPLINVDKEKTdILMYCTGGIRCDVYSTVLRQRG 300
Cdd:cd01524   11 ADGVTLIDVRTPQEFEKGHIKGAINIPLDELR--------------DRLNELPKDKE-IIVYCAVGLRGYIAARILTQNG 75

                         90
                 ....*....|....
gi 334182661 301 FKnLYTLKGGVSHY 314
Cdd:cd01524   76 FK-VKNLDGGYKTY 88
PRK05597 PRK05597
molybdopterin biosynthesis protein MoeB; Validated
 187-315 1.93e-04

molybdopterin biosynthesis protein MoeB; Validated


Pssm-ID: 235526 [Multi-domain]  Cd Length: 355  Bit Score: 43.32  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 187 LLDPPMRAKPLEPSEWKRKLKDLTdddeASPSNSgksyILLDVRNGYEWDVGHFRGAHRPEVDCFRNtsfGLSDEKEAPS 266
Cdd:PRK05597 246 VRGSTPVHGISGGFGEVLDVPRVS----ALPDGV----TLIDVREPSEFAAYSIPGAHNVPLSAIRE---GANPPSVSAG 314

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 334182661 267 DplinvdkektDILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYL 315
Cdd:PRK05597 315 D----------EVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGWL 353
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
 204-317 1.18e-03

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 40.85  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 204 RKLKDLTDddeaspsnSGKSYILLDVRNGYEWDVGHFRGAHRPEVDCFrNTSFGLSdekEAPSDplinvdkekTDILMYC 283
Cdd:PRK07878 292 RELKEWLD--------SGKKIALIDVREPVEWDIVHIPGAQLIPKSEI-LSGEALA---KLPQD---------RTIVLYC 350

                         90       100       110
                 ....*....|....*....|....*....|....
gi 334182661 284 TGGIRCDVYSTVLRQRGFKNLYTLKGGVSHYLKE 317
Cdd:PRK07878 351 KTGVRSAEALAALKKAGFSDAVHLQGGVVAWAKQ 384
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
 197-314 4.75e-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: 36.60  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182661 197 LEPSEWKRKLKDltDDDEAspsnsgksyILLDVRNGYEWDVGHFRGA-HRPevdcfrntsfgLSdEKEAPSDPLINVDKE 275
Cdd:cd01528    2 ISVAELAEWLAD--EREEP---------VLIDVREPEELEIAFLPGFlHLP-----------MS-EIPERSKELDSDNPD 58

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 334182661 276 KtDILMYCTGGIRCDVYSTVLRQRGFKNLYTLKGGVSHY 314
Cdd:cd01528   59 K-DIVVLCHHGGRSMQVAQWLLRQGFENVYNLQGGIDAW 96
 
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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