|
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
|
|
|