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Conserved domains on  [gi|488431861|ref|WP_002501246|]
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rhodanese-related sulfurtransferase [Staphylococcus epidermidis]

Protein Classification

tRNA uridine(34) hydroxylase( domain architecture ID 11478196)

tRNA uridine(34) hydroxylase catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs

CATH:  3.40.250.10
EC:  1.14.-.-
Gene Ontology:  GO:0016705|GO:0006400
PubMed:  12151332
SCOP:  4000452

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
1-312 0e+00

rhodanese-related sulfurtransferase;


:

Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 512.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861   1 MDYRVLLYYKYVTIDDPETFAAEHLKFCKEHHLKGRILVSTEGINGTLSGTKEDTDKYIEHMHADSRFADLTFKIDEAES 80
Cdd:PRK00142   2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDDG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861  81 HAFKKMHVRPRREIVALDLEEDINPREITGKYYSPKEFKAALEDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLPEW 160
Cdd:PRK00142  82 HAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPPW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 161 VRNNKEQLDGKNIVTYCTGGIRCEKFSGWLVKEGFENVGQLHGGIATYGKDPETKGQYWDGKMYVFDERISVDVNqiDKT 240
Cdd:PRK00142 162 VEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVPIN--DEV 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488431861 241 VIGKEHFDGTPCERYINCANPECNKQILVSEENEEKYLGACSYDCAKHERNRYVARHHISNEEWQRRLNNFK 312
Cdd:PRK00142 240 PIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNK 311
 
Name Accession Description Interval E-value
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
1-312 0e+00

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 512.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861   1 MDYRVLLYYKYVTIDDPETFAAEHLKFCKEHHLKGRILVSTEGINGTLSGTKEDTDKYIEHMHADSRFADLTFKIDEAES 80
Cdd:PRK00142   2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDDG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861  81 HAFKKMHVRPRREIVALDLEEDINPREITGKYYSPKEFKAALEDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLPEW 160
Cdd:PRK00142  82 HAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPPW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 161 VRNNKEQLDGKNIVTYCTGGIRCEKFSGWLVKEGFENVGQLHGGIATYGKDPETKGQYWDGKMYVFDERISVDVNqiDKT 240
Cdd:PRK00142 162 VEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVPIN--DEV 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488431861 241 VIGKEHFDGTPCERYINCANPECNKQILVSEENEEKYLGACSYDCAKHERNRYVARHHISNEEWQRRLNNFK 312
Cdd:PRK00142 240 PIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNK 311
TrhO COG1054
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
1-303 1.30e-172

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


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 480.41  E-value: 1.30e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861   1 MDYRVLLYYKYVTIDDPETFAAEHLKFCKEHHLKGRILVSTEGINGTLSGTKEDTDKYIEHMHADSRFADLTFKIDEAES 80
Cdd:COG1054    2 KPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEADG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861  81 HAFKKMHVRPRREIVALDLEeDINPREITGKYYSPKEFKAALEDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLPEW 160
Cdd:COG1054   82 HPFPRLKVKLKKEIVTMGLP-DVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 161 VRNNKEQLDGKNIVTYCTGGIRCEKFSGWLVKEGFENVGQLHGGIATYGKDPETKGQYWDGKMYVFDERISVDVNQiDKT 240
Cdd:COG1054  161 VEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNL-EPG 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488431861 241 VIGKEHFDGTPCERYINCANPECNKQILVSEENEEKYLgACSYDCAKHERNRYVARHHISNEE 303
Cdd:COG1054  240 VIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADKYE-CCSDECTEEQRARYERQRQLRLAK 301
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
110-210 1.76e-48

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: 157.36  E-value: 1.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 110 GKYYSPKEFKAALEDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLPEWVRNNKEQLDGKNIVTYCTGGIRCEKFSGW 189
Cdd:cd01518    1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
                         90       100
                 ....*....|....*....|.
gi 488431861 190 LVKEGFENVGQLHGGIATYGK 210
Cdd:cd01518   81 LKERGFKNVYQLKGGILKYLE 101
UPF0176_N pfam17773
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ...
3-94 9.34e-40

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: 134.54  E-value: 9.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861    3 YRVLLYYKYVTIDDPETFAAEHLKFCKEHHLKGRILVSTEGINGTLSGTKEDTDKYIEHMHADSRFADLTFKIDEAESHA 82
Cdd:pfam17773   1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
                          90
                  ....*....|..
gi 488431861   83 FKKMHVRPRREI 94
Cdd:pfam17773  81 FRRLKVKLKKEI 92
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
123-212 6.57e-16

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: 72.11  E-value: 6.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861   123 EDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLP--------EWVRNNKEQLDGKNIVTYCTGGIRCEKFSGWLVKEG 194
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRgeldilefEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
                           90
                   ....*....|....*...
gi 488431861   195 FENVGQLHGGIATYGKDP 212
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAG 98
 
Name Accession Description Interval E-value
PRK00142 PRK00142
rhodanese-related sulfurtransferase;
1-312 0e+00

rhodanese-related sulfurtransferase;


Pssm-ID: 234663 [Multi-domain]  Cd Length: 314  Bit Score: 512.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861   1 MDYRVLLYYKYVTIDDPETFAAEHLKFCKEHHLKGRILVSTEGINGTLSGTKEDTDKYIEHMHADSRFADLTFKIDEAES 80
Cdd:PRK00142   2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDDG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861  81 HAFKKMHVRPRREIVALDLEEDINPREITGKYYSPKEFKAALEDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLPEW 160
Cdd:PRK00142  82 HAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPPW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 161 VRNNKEQLDGKNIVTYCTGGIRCEKFSGWLVKEGFENVGQLHGGIATYGKDPETKGQYWDGKMYVFDERISVDVNqiDKT 240
Cdd:PRK00142 162 VEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVPIN--DEV 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488431861 241 VIGKEHFDGTPCERYINCANPECNKQILVSEENEEKYLGACSYDCAKHERNRYVARHHISNEEWQRRLNNFK 312
Cdd:PRK00142 240 PIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNK 311
TrhO COG1054
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ...
1-303 1.30e-172

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


Pssm-ID: 440674 [Multi-domain]  Cd Length: 304  Bit Score: 480.41  E-value: 1.30e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861   1 MDYRVLLYYKYVTIDDPETFAAEHLKFCKEHHLKGRILVSTEGINGTLSGTKEDTDKYIEHMHADSRFADLTFKIDEAES 80
Cdd:COG1054    2 KPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEADG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861  81 HAFKKMHVRPRREIVALDLEeDINPREITGKYYSPKEFKAALEDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLPEW 160
Cdd:COG1054   82 HPFPRLKVKLKKEIVTMGLP-DVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 161 VRNNKEQLDGKNIVTYCTGGIRCEKFSGWLVKEGFENVGQLHGGIATYGKDPETKGQYWDGKMYVFDERISVDVNQiDKT 240
Cdd:COG1054  161 VEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNL-EPG 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488431861 241 VIGKEHFDGTPCERYINCANPECNKQILVSEENEEKYLgACSYDCAKHERNRYVARHHISNEE 303
Cdd:COG1054  240 VIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADKYE-CCSDECTEEQRARYERQRQLRLAK 301
PRK05320 PRK05320
rhodanese superfamily protein; Provisional
9-233 5.98e-67

rhodanese superfamily protein; Provisional


Pssm-ID: 235405 [Multi-domain]  Cd Length: 257  Bit Score: 210.27  E-value: 5.98e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861   9 YKYVTIDDPETFAAEHLKFCKEHHLKGRILVSTEGINGTLSGTKEDTDKYIEHMHADSRFADLTFKIDEAESHAFKKMHV 88
Cdd:PRK05320   9 YKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRADARFADLQVKESLSDSQPFRRMLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861  89 RPRREIVALDlEEDINPREITGKYYSPKEFKAALE----DEN--TVILDARNDYEYDLGHFRGAIRPDITRFRDLPEWVR 162
Cdd:PRK05320  89 KLKREIITMK-RPAIRPELGRAPSVDAATLKRWLDqghdDAGrpVVMLDTRNAFEVDVGTFDGALDYRIDKFTEFPEALA 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488431861 163 NNKEQLDGKNIVTYCTGGIRCEKFSGWLVKEGFENVGQLHGGIATYGKdpETKGQYWDGKMYVFDERISVD 233
Cdd:PRK05320 168 AHRADLAGKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFE--EVGGAHYDGDCFVFDYRTALD 236
PRK01415 PRK01415
hypothetical protein; Validated
5-232 2.36e-57

hypothetical protein; Validated


Pssm-ID: 167229 [Multi-domain]  Cd Length: 247  Bit Score: 185.53  E-value: 2.36e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861   5 VLLYYKYVTIDDPETFAAEHLKFCKEHHLKGRILVSTEGINGTLSGTKEDTDKYIEHMHADSRFADLTFKIDEAESHAFK 84
Cdd:PRK01415   7 ILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKLTGPKDVNVKINYSDVHPFQ 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861  85 KMHVRPRREIVALDLEeDINPREITGKYYSPKEFKAALEDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLPEWVRNN 164
Cdd:PRK01415  87 KLKVRLKKEIVAMNVD-DLNVDLFKGEYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFKQFPAWVQQN 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488431861 165 KEQLDGKNIVTYCTGGIRCEKFSGWLVKEGFENVGQLHGGIATYGKDPETKGQYWDGKMYVFDERISV 232
Cdd:PRK01415 166 QELLKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQNKNNLWQGECFVFDDRRAV 233
RHOD_YceA cd01518
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ...
110-210 1.76e-48

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: 157.36  E-value: 1.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 110 GKYYSPKEFKAALEDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLPEWVRNNKEQLDGKNIVTYCTGGIRCEKFSGW 189
Cdd:cd01518    1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
                         90       100
                 ....*....|....*....|.
gi 488431861 190 LVKEGFENVGQLHGGIATYGK 210
Cdd:cd01518   81 LKERGFKNVYQLKGGILKYLE 101
UPF0176_N pfam17773
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ...
3-94 9.34e-40

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: 134.54  E-value: 9.34e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861    3 YRVLLYYKYVTIDDPETFAAEHLKFCKEHHLKGRILVSTEGINGTLSGTKEDTDKYIEHMHADSRFADLTFKIDEAESHA 82
Cdd:pfam17773   1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
                          90
                  ....*....|..
gi 488431861   83 FKKMHVRPRREI 94
Cdd:pfam17773  81 FRRLKVKLKKEI 92
Rhodanese_C pfam12368
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ...
220-286 1.02e-26

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: 100.08  E-value: 1.02e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488431861  220 DGKMYVFDERISVdVNQIDKTVIGKEHFDGTPCERYINCANPECNKQILVSEENEEKYLGACSYDCA 286
Cdd:pfam12368   1 KGKLFVFDERLAV-VEPSDDDVIGKCYHCGKPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEECA 66
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
114-208 1.02e-18

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: 80.01  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 114 SPKEFKAALEDENTVILDARNDYEYDLGHFRGAIR-PditrFRDLPEWVrnnkEQLD-GKNIVTYCTGGIRCEKFSGWLV 191
Cdd:COG0607    7 SPAELAELLESEDAVLLDVREPEEFAAGHIPGAINiP----LGELAERL----DELPkDKPIVVYCASGGRSAQAAALLR 78
                         90
                 ....*....|....*..
gi 488431861 192 KEGFENVGQLHGGIATY 208
Cdd:COG0607   79 RAGYTNVYNLAGGIEAW 95
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
123-212 6.57e-16

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: 72.11  E-value: 6.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861   123 EDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLP--------EWVRNNKEQLDGKNIVTYCTGGIRCEKFSGWLVKEG 194
Cdd:smart00450   1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRgeldilefEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
                           90
                   ....*....|....*...
gi 488431861   195 FENVGQLHGGIATYGKDP 212
Cdd:smart00450  81 FKNVYLLDGGYKEWSAAG 98
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
117-206 3.10e-14

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: 67.32  E-value: 3.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 117 EFKAALEDENTVILDARNDYEYDLGHFRGAIRPDITRFRDLPEWVRNNKeqldGKNIVTYCTGGIRCEKFSGWLVKEGFE 196
Cdd:cd00158    1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDK----DKPIVVYCRSGNRSARAAKLLRKAGGT 76
                         90
                 ....*....|
gi 488431861 197 NVGQLHGGIA 206
Cdd:cd00158   77 NVYNLEGGML 86
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
122-205 7.30e-13

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: 63.66  E-value: 7.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861  122 LEDENTVILDARNDYEYDLGHFRGA--IRPDITRFRDLP--EWVRNNKEQLDGKNIVTYCTGGIRCEKFSGWLVKEGFEN 197
Cdd:pfam00581   1 LEDGKVVLIDVRPPEEYAKGHIPGAvnVPLSSLSLPPLPllELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80

                  ....*...
gi 488431861  198 VGQLHGGI 205
Cdd:pfam00581  81 VYVLDGGF 88
RHOD_2 cd01528
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ...
114-208 5.91e-11

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: 58.56  E-value: 5.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 114 SPKEFKAAL--EDENTVILDARNDYEYDLGHFRGAIRPDITRFrdlPEWVRNNKEQLDGKNIVTYCTGGIRCEKFSGWLV 191
Cdd:cd01528    3 SVAELAEWLadEREEPVLIDVREPEELEIAFLPGFLHLPMSEI---PERSKELDSDNPDKDIVVLCHHGGRSMQVAQWLL 79
                         90
                 ....*....|....*..
gi 488431861 192 KEGFENVGQLHGGIATY 208
Cdd:cd01528   80 RQGFENVYNLQGGIDAW 96
RHOD_Pyr_redox cd01524
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ...
115-210 4.47e-07

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: 47.26  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 115 PKEFKAALEDENTvILDARNDYEYDLGHFRGAIRPDITRFRDlpewvRNNkeQLD-GKNIVTYCTGGIRCEKFSGWLVKE 193
Cdd:cd01524    3 WHELDNYRADGVT-LIDVRTPQEFEKGHIKGAINIPLDELRD-----RLN--ELPkDKEIIVYCAVGLRGYIAARILTQN 74
                         90
                 ....*....|....*..
gi 488431861 194 GFeNVGQLHGGIATYGK 210
Cdd:cd01524   75 GF-KVKNLDGGYKTYST 90
Acr2p cd01531
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ...
111-204 3.15e-04

Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.


Pssm-ID: 238789 [Multi-domain]  Cd Length: 113  Bit Score: 39.70  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 111 KYYSPKEFKAALED--ENTVILDARnDYEYDLGHFRGAIRPDITRFRDLPEWVRNNKEQLDGKNIVTYCTG----GIRC- 183
Cdd:cd01531    2 SYISPAQLKGWIRNgrPPFQVVDVR-DEDYAGGHIKGSWHYPSTRFKAQLNQLVQLLSGSKKDTVVFHCALsqvrGPSAa 80
                         90       100
                 ....*....|....*....|....*
gi 488431861 184 EKFSGWL----VKEGFENVGQLHGG 204
Cdd:cd01531   81 RKFLRYLdeedLETSKFEVYVLHGG 105
SseA COG2897
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ...
88-198 4.88e-04

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


Pssm-ID: 442142 [Multi-domain]  Cd Length: 262  Bit Score: 40.93  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861  88 VRPRREIVAlDLEEdinpreitgkyyspkeFKAALEDENTVILDARNDYEY-------DL--GHFRGAI-RP------DI 151
Cdd:COG2897  132 ARPDPELLA-DADE----------------VLAALGDPDAVLVDARSPERYrgevepiDPraGHIPGAVnLPwtdlldED 194
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488431861 152 TRFRDLPEwVRNNKEQL---DGKNIVTYCTGGIR-CEkfsGWLVKE--GFENV 198
Cdd:COG2897  195 GTFKSAEE-LRALFAALgidPDKPVITYCGSGVRaAH---TWLALEllGYPNV 243
RHOD_PspE2 cd01521
Member of the Rhodanese Homology Domain superfamily. This CD includes the putative ...
123-211 1.38e-03

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


Pssm-ID: 238779 [Multi-domain]  Cd Length: 110  Bit Score: 37.72  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 123 EDENTVILDARNDYEYDLGHFRGAIrpditrfrDLP--EWVRNNKEQLD-GKNIVTYCTgGIRC---EKFSGWLVKEGFE 196
Cdd:cd01521   22 GKPDFVLVDVRSAEAYARGHVPGAI--------NLPhrEICENATAKLDkEKLFVVYCD-GPGCngaTKAALKLAELGFP 92
                         90
                 ....*....|....*
gi 488431861 197 nVGQLHGGIATYGKD 211
Cdd:cd01521   93 -VKEMIGGLDWWKRE 106
PRK07411 PRK07411
molybdopterin-synthase adenylyltransferase MoeB;
116-211 1.82e-03

molybdopterin-synthase adenylyltransferase MoeB;


Pssm-ID: 180967 [Multi-domain]  Cd Length: 390  Bit Score: 39.72  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 116 KEFKAALE--DENTVILDARNDYEYDLGHFRGAI---RPDITRfrdlPEWVRNNKEQLDGKNIVTYCTGGIRCEKFSGWL 190
Cdd:PRK07411 287 TELKALLDsgADDFVLIDVRNPNEYEIARIPGSVlvpLPDIEN----GPGVEKVKELLNGHRLIAHCKMGGRSAKALGIL 362
                         90       100
                 ....*....|....*....|.
gi 488431861 191 VKEGFENVgQLHGGIATYGKD 211
Cdd:PRK07411 363 KEAGIEGT-NVKGGITAWSRE 382
PRK07878 PRK07878
molybdopterin biosynthesis-like protein MoeZ; Validated
109-213 4.43e-03

molybdopterin biosynthesis-like protein MoeZ; Validated


Pssm-ID: 181156 [Multi-domain]  Cd Length: 392  Bit Score: 38.54  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488431861 109 TGKYYSPKEFKAALED-ENTVILDARNDYEYDLGHFRGAI---RPDI---TRFRDLPEwvrnnkeqldGKNIVTYCTGGI 181
Cdd:PRK07878 285 AGSTITPRELKEWLDSgKKIALIDVREPVEWDIVHIPGAQlipKSEIlsgEALAKLPQ----------DRTIVLYCKTGV 354
                         90       100       110
                 ....*....|....*....|....*....|....
gi 488431861 182 RCEKFSGWLVKEGFENVGQLHGGIATYGK--DPE 213
Cdd:PRK07878 355 RSAEALAALKKAGFSDAVHLQGGVVAWAKqvDPS 388
 
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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