|
Name |
Accession |
Description |
Interval |
E-value |
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
5-297 |
7.59e-180 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 498.13 E-value: 7.59e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 5 PFTVAALYCFAPLPQYESLREPLAQLCCANGIKGTLLLAAEGINGTVAGSAGAIEKLIAHITAIPGLGEPELKYSHASEM 84
Cdd:COG1054 3 PYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEADGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 85 PFHRMKVRLKREIVTMGVEGIDPLKSVGTYIAPKDWNALIADENTVVVDTRNDYEYAIGTFEGAIDPQTRTFREFPEWVK 164
Cdd:COG1054 83 PFPRLKVKLKKEIVTMGLPDVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEWVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 165 QNRDRLEGKKIAMFCTGGIRCEKATAFVKGLGFDDVYHLKGGILKYLEEVPREQSMWNGECFVFDERVAVGHGLAESDVE 244
Cdd:COG1054 163 ENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNLEPGVIG 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 479824272 245 LCRACRRPLTPQDKLSQ--FFEEGVSCAGCYA-------ERTPEDRARYaERQKQVKLAEKR 297
Cdd:COG1054 243 LCHACGTPCDRYVNCANdpCYELGVSCPHCADkyeccsdECTEEQRARY-ERQRQLRLAKER 303
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
5-299 |
2.77e-135 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 385.74 E-value: 2.77e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 5 PFTVAALYCFAPLPQYESLREPLAQLCCANGIKGTLLLAAEGINGTVAGSAGAIEKLIAHITAIPGLGEPELKYSHASEM 84
Cdd:PRK00142 3 PYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDDGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 85 PFHRMKVRLKREIVTMGVE-GIDPLKSVGTYIAPKDWNALIADENTVVVDTRNDYEYAIGTFEGAIDPQTRTFREFPEWV 163
Cdd:PRK00142 83 AFPRLSVKVRKEIVALGLDdDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPPWV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 164 KQNRDRLEGKKIAMFCTGGIRCEKATAFVKGLGFDDVYHLKGGILKYLEEVPREQSMWNGECFVFDERVAV--------G 235
Cdd:PRK00142 163 EENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVpindevpiG 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 236 H----GLAESDVELCR--ACRRPLTPQDKLSQFFEEGVSCAGCYAERTPEDRARYAERQKQVKLAEKRGA 299
Cdd:PRK00142 243 HchqcGTPCDRYVNCAnpACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKE 312
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
112-212 |
6.56e-56 |
|
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: 176.23 E-value: 6.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 112 GTYIAPKDWNALIADENTVVVDTRNDYEYAIGTFEGAIDPQTRTFREFPEWVKQNRDRLEGKKIAMFCTGGIRCEKATAF 191
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 479824272 192 VKGLGFDDVYHLKGGILKYLE 212
Cdd:cd01518 81 LKERGFKNVYQLKGGILKYLE 101
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
6-97 |
1.57e-37 |
|
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: 128.38 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 6 FTVAALYCFAPLPQYESLREPLAQLCCANGIKGTLLLAAEGINGTVAGSAGAIEKLIAHITAIPGLGEPELKYSHASEMP 85
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
|
90
....*....|..
gi 479824272 86 FHRMKVRLKREI 97
Cdd:pfam17773 81 FRRLKVKLKKEI 92
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
126-215 |
7.16e-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: 71.72 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 126 DENTVVVDTRNDYEYAIGTFEGAI---------DPQTRTFREFPEWVKQNrDRLEGKKIAMFCTGGIRCEKATAFVKGLG 196
Cdd:smart00450 2 DEKVVLLDVRSPEEYEGGHIPGAVniplselldRRGELDILEFEELLKRL-GLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90
....*....|....*....
gi 479824272 197 FDDVYHLKGGILKYLEEVP 215
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGP 99
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
5-297 |
7.59e-180 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 498.13 E-value: 7.59e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 5 PFTVAALYCFAPLPQYESLREPLAQLCCANGIKGTLLLAAEGINGTVAGSAGAIEKLIAHITAIPGLGEPELKYSHASEM 84
Cdd:COG1054 3 PYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEADGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 85 PFHRMKVRLKREIVTMGVEGIDPLKSVGTYIAPKDWNALIADENTVVVDTRNDYEYAIGTFEGAIDPQTRTFREFPEWVK 164
Cdd:COG1054 83 PFPRLKVKLKKEIVTMGLPDVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEWVE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 165 QNRDRLEGKKIAMFCTGGIRCEKATAFVKGLGFDDVYHLKGGILKYLEEVPREQSMWNGECFVFDERVAVGHGLAESDVE 244
Cdd:COG1054 163 ENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNLEPGVIG 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 479824272 245 LCRACRRPLTPQDKLSQ--FFEEGVSCAGCYA-------ERTPEDRARYaERQKQVKLAEKR 297
Cdd:COG1054 243 LCHACGTPCDRYVNCANdpCYELGVSCPHCADkyeccsdECTEEQRARY-ERQRQLRLAKER 303
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
5-299 |
2.77e-135 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 385.74 E-value: 2.77e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 5 PFTVAALYCFAPLPQYESLREPLAQLCCANGIKGTLLLAAEGINGTVAGSAGAIEKLIAHITAIPGLGEPELKYSHASEM 84
Cdd:PRK00142 3 PYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDDGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 85 PFHRMKVRLKREIVTMGVE-GIDPLKSVGTYIAPKDWNALIADENTVVVDTRNDYEYAIGTFEGAIDPQTRTFREFPEWV 163
Cdd:PRK00142 83 AFPRLSVKVRKEIVALGLDdDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPPWV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 164 KQNRDRLEGKKIAMFCTGGIRCEKATAFVKGLGFDDVYHLKGGILKYLEEVPREQSMWNGECFVFDERVAV--------G 235
Cdd:PRK00142 163 EENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVpindevpiG 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 236 H----GLAESDVELCR--ACRRPLTPQDKLSQFFEEGVSCAGCYAERTPEDRARYAERQKQVKLAEKRGA 299
Cdd:PRK00142 243 HchqcGTPCDRYVNCAnpACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKE 312
|
|
| PRK01415 |
PRK01415 |
hypothetical protein; Validated |
3-242 |
4.56e-84 |
|
hypothetical protein; Validated
Pssm-ID: 167229 [Multi-domain] Cd Length: 247 Bit Score: 253.33 E-value: 4.56e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 3 NLPFTVAALYCFAPLPQYESLREPLAQLCCANGIKGTLLLAAEGINGTVAGSAGAIEKLIAHITAIPGLGEPELKYSHAS 82
Cdd:PRK01415 2 NEKIAILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKLTGPKDVNVKINYSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 83 EMPFHRMKVRLKREIVTMGVEGIDPLKSVGTYIAPKDWNALIADENTVVVDTRNDYEYAIGTFEGAIDPQTRTFREFPEW 162
Cdd:PRK01415 82 VHPFQKLKVRLKKEIVAMNVDDLNVDLFKGEYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFKQFPAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 163 VKQNRDRLEGKKIAMFCTGGIRCEKATAFVKGLGFDDVYHLKGGILKYLEEVPREQSMWNGECFVFDERVAVGHGLAESD 242
Cdd:PRK01415 162 VQQNQELLKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQNKNNLWQGECFVFDDRRAVTDDLSPVE 241
|
|
| PRK05320 |
PRK05320 |
rhodanese superfamily protein; Provisional |
10-256 |
4.10e-77 |
|
rhodanese superfamily protein; Provisional
Pssm-ID: 235405 [Multi-domain] Cd Length: 257 Bit Score: 235.69 E-value: 4.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 10 ALYCFAPLPQYESLREPLAQLCCANGIKGTLLLAAEGINGTVAGSAGAIEKLIAHITAIPGLGEPELKYSHASEMPFHRM 89
Cdd:PRK05320 7 AAYKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRADARFADLQVKESLSDSQPFRRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 90 KVRLKREIVTMGVEGIDPLKSVGTYIAP---KDWNALIADEN---TVVVDTRNDYEYAIGTFEGAIDPQTRTFREFPEWV 163
Cdd:PRK05320 87 LVKLKREIITMKRPAIRPELGRAPSVDAatlKRWLDQGHDDAgrpVVMLDTRNAFEVDVGTFDGALDYRIDKFTEFPEAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 164 KQNRDRLEGKKIAMFCTGGIRCEKATAFVKGLGFDDVYHLKGGILKYLEEVPREQsmWNGECFVFDERVAVGHGLAESDV 243
Cdd:PRK05320 167 AAHRADLAGKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFEEVGGAH--YDGDCFVFDYRTALDPQLAPLVD 244
|
250
....*....|...
gi 479824272 244 ELCRACRRPLTPQ 256
Cdd:PRK05320 245 VTCFACRAVVTPE 257
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
112-212 |
6.56e-56 |
|
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: 176.23 E-value: 6.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 112 GTYIAPKDWNALIADENTVVVDTRNDYEYAIGTFEGAIDPQTRTFREFPEWVKQNRDRLEGKKIAMFCTGGIRCEKATAF 191
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 479824272 192 VKGLGFDDVYHLKGGILKYLE 212
Cdd:cd01518 81 LKERGFKNVYQLKGGILKYLE 101
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
6-97 |
1.57e-37 |
|
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: 128.38 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 6 FTVAALYCFAPLPQYESLREPLAQLCCANGIKGTLLLAAEGINGTVAGSAGAIEKLIAHITAIPGLGEPELKYSHASEMP 85
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
|
90
....*....|..
gi 479824272 86 FHRMKVRLKREI 97
Cdd:pfam17773 81 FRRLKVKLKKEI 92
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
115-213 |
1.31e-16 |
|
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: 73.85 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 115 IAPKDWNALIADENTVVVDTRNDYEYAIGTFEGAIdpqTRTFREFPEWVkqnrDRL-EGKKIAMFCTGGIRCEKATAFVK 193
Cdd:COG0607 6 ISPAELAELLESEDAVLLDVREPEEFAAGHIPGAI---NIPLGELAERL----DELpKDKPIVVYCASGGRSAQAAALLR 78
|
90 100
....*....|....*....|
gi 479824272 194 GLGFDDVYHLKGGILKYLEE 213
Cdd:COG0607 79 RAGYTNVYNLAGGIEAWKAA 98
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
126-215 |
7.16e-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: 71.72 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 126 DENTVVVDTRNDYEYAIGTFEGAI---------DPQTRTFREFPEWVKQNrDRLEGKKIAMFCTGGIRCEKATAFVKGLG 196
Cdd:smart00450 2 DEKVVLLDVRSPEEYEGGHIPGAVniplselldRRGELDILEFEELLKRL-GLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90
....*....|....*....
gi 479824272 197 FDDVYHLKGGILKYLEEVP 215
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGP 99
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
124-210 |
2.26e-14 |
|
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: 67.51 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 124 IADENTVVVDTRNDYEYAIGTFEGAI----DPQTRTFREFPEWVKQNRDRLEGKKIAMFCTGGIRCEKATAFVKGLGFDD 199
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAKGHIPGAVnvplSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80
|
90
....*....|.
gi 479824272 200 VYHLKGGILKY 210
Cdd:pfam00581 81 VYVLDGGFEAW 91
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
122-210 |
3.89e-13 |
|
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: 63.86 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 122 ALIADENTVVVDTRNDYEYAIGTFEGAIDPQTRTFREFPEWVKQNRDrlegKKIAMFCTGGIRCEKATAFVKGLGFDDVY 201
Cdd:cd00158 4 ELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDKD----KPIVVYCRSGNRSARAAKLLRKAGGTNVY 79
|
....*....
gi 479824272 202 HLKGGILKY 210
Cdd:cd00158 80 NLEGGMLAW 88
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
43-214 |
2.60e-10 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 60.49 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 43 AAEGINGTVAGSAGAIEKLIAhITAIPGLGEP---ELKYSHASEMPFHRMKVRLKREIVTMgVEGID------------P 107
Cdd:PRK07878 204 AEGGVLGVLCASIGSIMGTEA-IKLITGIGEPllgRLMVYDALEMTYRTIKIRKDPSTPKI-TELIDyeafcgvvsdeaQ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 108 LKSVGTYIAPKDWNALI-ADENTVVVDTRNDYEYAIGTFEGA-IDPQTR-----TFREFPewvkQNRdrlegkKIAMFCT 180
Cdd:PRK07878 282 QAAAGSTITPRELKEWLdSGKKIALIDVREPVEWDIVHIPGAqLIPKSEilsgeALAKLP----QDR------TIVLYCK 351
|
170 180 190
....*....|....*....|....*....|....
gi 479824272 181 GGIRCEKATAFVKGLGFDDVYHLKGGILKYLEEV 214
Cdd:PRK07878 352 TGVRSAEALAALKKAGFSDAVHLQGGVVAWAKQV 385
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
115-214 |
7.01e-10 |
|
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: 55.48 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 115 IAPKDWNALIADE--NTVVVDTRNDYEYAIGTFEGAID-PqtrtFREFPEWVKQNRDRLEGKKIAMFCTGGIRCEKATAF 191
Cdd:cd01528 2 ISVAELAEWLADEreEPVLIDVREPEELEIAFLPGFLHlP----MSEIPERSKELDSDNPDKDIVVLCHHGGRSMQVAQW 77
|
90 100
....*....|....*....|...
gi 479824272 192 VKGLGFDDVYHLKGGILKYLEEV 214
Cdd:cd01528 78 LLRQGFENVYNLQGGIDAWSLEV 100
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
115-213 |
1.08e-07 |
|
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as a polysulfide binding and transferase domain in anaerobic gram-negative bacteria, functioning in oxidative phosphorylation with polysulfide-sulfur as a terminal electron acceptor. The active site contains the same conserved cysteine that is the catalytic residue in other Rhodanese Homology Domain proteins.
Pssm-ID: 238724 [Multi-domain] Cd Length: 103 Bit Score: 49.35 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 115 IAPKDWNALIADENTVVVDTRNDYEY-AIGTFEGAIDpQTRTFREF---PEWVKQNRDRLEGKKIAMFCTGGIRCEKATA 190
Cdd:cd01447 1 LSPEDARALLGSPGVLLVDVRDPRELeRTGMIPGAFH-APRGMLEFwadPDSPYHKPAFAEDKPFVFYCASGWRSALAGK 79
|
90 100
....*....|....*....|...
gi 479824272 191 FVKGLGFDDVYHLKGGILKYLEE 213
Cdd:cd01447 80 TLQDMGLKPVYNIEGGFKDWKEA 102
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
115-210 |
1.90e-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: 48.03 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 115 IAPKDWNALIADENTVVvDTRNDYEYAIGTFEGAIDpqtrtfreFPewVKQNRDRL----EGKKIAMFCTGGIRCEKATA 190
Cdd:cd01524 1 VQWHELDNYRADGVTLI-DVRTPQEFEKGHIKGAIN--------IP--LDELRDRLnelpKDKEIIVYCAVGLRGYIAAR 69
|
90 100
....*....|....*....|
gi 479824272 191 FVKGLGFdDVYHLKGGILKY 210
Cdd:cd01524 70 ILTQNGF-KVKNLDGGYKTY 88
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
125-207 |
5.02e-05 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 44.23 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 125 ADENTVVVDTRNDYEYAIGTFEGA--IDpqtRTFREF-PEWVKQNRDRlegkKIAMFCTGGIRCEKATAFVKGLGFDDVY 201
Cdd:PRK08762 14 AAQGAVLIDVREAHERASGQAEGAlrIP---RGFLELrIETHLPDRDR----EIVLICASGTRSAHAAATLRELGYTRVA 86
|
....*.
gi 479824272 202 HLKGGI 207
Cdd:PRK08762 87 SVAGGF 92
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
115-207 |
7.75e-05 |
|
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain superfamily. Unlike other rhodanese sulfurtransferases, GlpE is a single domain protein but indications are that it functions as a dimer. The active site contains a catalytically active cysteine.
Pssm-ID: 238721 [Multi-domain] Cd Length: 96 Bit Score: 40.71 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 115 IAPKDWNALIADENT-VVVDTR--NDYEYAIGTFEGAIdpqTRTFREFPEWVKQNRDrleGKKIAMFCTGGIRCEKATAF 191
Cdd:cd01444 2 ISVDELAELLAAGEApVLLDVRdpASYAALPDHIPGAI---HLDEDSLDDWLGDLDR---DRPVVVYCYHGNSSAQLAQA 75
|
90
....*....|....*.
gi 479824272 192 VKGLGFDDVYHLKGGI 207
Cdd:cd01444 76 LREAGFTDVRSLAGGF 91
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
51-212 |
1.06e-04 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 43.32 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 51 VAGSAGAIEKliahITAIPGLGEP---ELKYSHASEMPFHRMKVR-----LKREIVTMGVEGidPLKSVGTYIAPKDWNA 122
Cdd:PRK05597 197 VVGSAMAMEA----LKLITGVGTPligKLGYYDSLDGTWEYIPVVgnpavLERVRGSTPVHG--ISGGFGEVLDVPRVSA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 123 LIadENTVVVDTRNDYEYAIGTFEGAIDPQTRTFREfpewvKQNRDRLE-GKKIAMFCTGGIRCEKATAFVKGLGFDDVY 201
Cdd:PRK05597 271 LP--DGVTLIDVREPSEFAAYSIPGAHNVPLSAIRE-----GANPPSVSaGDEVVVYCAAGVRSAQAVAILERAGYTGMS 343
|
170
....*....|.
gi 479824272 202 HLKGGILKYLE 212
Cdd:PRK05597 344 SLDGGIEGWLD 354
|
|
| glpE |
PRK00162 |
thiosulfate sulfurtransferase GlpE; |
115-206 |
2.43e-04 |
|
thiosulfate sulfurtransferase GlpE;
Pssm-ID: 178908 [Multi-domain] Cd Length: 108 Bit Score: 39.62 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 115 IAPKDWNALIADENTVVVDTRNDYEYAIGTFEGAIDPQTRTFREFpewvKQNRDrLEGKKIAMfCTGGIRCEKATAFVKG 194
Cdd:PRK00162 7 INVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSLGAF----MRQAD-FDTPVMVM-CYHGNSSQGAAQYLLQ 80
|
90
....*....|..
gi 479824272 195 LGFDDVYHLKGG 206
Cdd:PRK00162 81 QGFDVVYSIDGG 92
|
|
| PRK07411 |
PRK07411 |
molybdopterin-synthase adenylyltransferase MoeB; |
130-214 |
5.02e-04 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 41.26 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 130 VVVDTRNDYEYAIGTFEGAI---DPQTrtfrEFPEWVKQNRDRLEGKKIAMFCTGGIRCEKATAFVKGLGFDDVyHLKGG 206
Cdd:PRK07411 301 VLIDVRNPNEYEIARIPGSVlvpLPDI----ENGPGVEKVKELLNGHRLIAHCKMGGRSAKALGILKEAGIEGT-NVKGG 375
|
....*...
gi 479824272 207 ILKYLEEV 214
Cdd:PRK07411 376 ITAWSREV 383
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
128-212 |
8.53e-04 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.
Pssm-ID: 238777 [Multi-domain] Cd Length: 106 Bit Score: 38.02 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479824272 128 NTVVVDTRNDYEYAIGTFEGAID-PqtrtFREFPEWVKQNRDRLE----------GKKIAMFCTGGIRCEKATAFVKGLG 196
Cdd:cd01519 15 NKVLIDVREPEELKTGKIPGAINiP----LSSLPDALALSEEEFEkkygfpkpskDKELIFYCKAGVRSKAAAELARSLG 90
|
90
....*....|....*.
gi 479824272 197 FDDVYHLKGGILKYLE 212
Cdd:cd01519 91 YENVGNYPGSWLDWAA 106
|
|
| |
