|
Name |
Accession |
Description |
Interval |
E-value |
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
1-295 |
0e+00 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 521.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 1 MTQFVVCALYKFATLEDFESMRQPLHDVMEANGVRGTLLLAREGVNGTVAGSRQGIDAVLAWLRSDPRLADLSHKESFNE 80
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 81 EMPFYRTKVKLKKEIVTMGVEGIDPRQVVGTYVKPQDWNSLIADPDVVVIDTRNDYEVQIGTFERAVNPLTKTFREFPEF 160
Cdd:COG1054 81 GHPFPRLKVKLKKEIVTMGLPDVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 161 VQQNLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGFDEVYHLEGGILKYLEEVPQESSLWRGECFVFDNRVTVNHDLERGS 240
Cdd:COG1054 161 VEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNLEPGV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522171213 241 FEQCHACRLPIT--QADMESEKYMAGVSCPHCFD-------ALSDEQRSRYAqRELQVRLARQR 295
Cdd:COG1054 241 IGLCHACGTPCDryVNCANDPCYELGVSCPHCADkyeccsdECTEEQRARYE-RQRQLRLAKER 303
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
1-299 |
7.38e-160 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 448.91 E-value: 7.38e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 1 MTQFVVCALYKFATLEDFESMRQPLHDVMEANGVRGTLLLAREGVNGTVAGSRQGIDAVLAWLRSDPRLADLSHKESFNE 80
Cdd:PRK00142 1 MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 81 EMPFYRTKVKLKKEIVTMGVE-GIDPRQVVGTYVKPQDWNSLIADPDVVVIDTRNDYEVQIGTFERAVNPLTKTFREFPE 159
Cdd:PRK00142 81 GHAFPRLSVKVRKEIVALGLDdDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 160 FVQQNLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGFDEVYHLEGGILKYLEEVPQESSLWRGECFVFDNRVTV------- 232
Cdd:PRK00142 161 WVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVpindevp 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522171213 233 -NHDLERG----SFEQCH--ACRLPITQADMESEKYMAGVSCPHCFDALSDEQRSRYAQRELQVRLARQRGEEH 299
Cdd:PRK00142 241 iGHCHQCGtpcdRYVNCAnpACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
110-210 |
9.29e-57 |
|
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: 178.93 E-value: 9.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 110 GTYVKPQDWNSLIADPDVVVIDTRNDYEVQIGTFERAVNPLTKTFREFPEFVQQNLDPAKHTKVAMFCTGGIRCEKSTAY 189
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 522171213 190 LKEQGFDEVYHLEGGILKYLE 210
Cdd:cd01518 81 LKERGFKNVYQLKGGILKYLE 101
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
4-95 |
2.44e-41 |
|
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: 139.17 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 4 FVVCALYKFATLEDFESMRQPLHDVMEANGVRGTLLLAREGVNGTVAGSRQGIDAVLAWLRSDPRLADLSHKESFNEEMP 83
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
|
90
....*....|..
gi 522171213 84 FYRTKVKLKKEI 95
Cdd:pfam17773 81 FRRLKVKLKKEI 92
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
124-214 |
9.77e-17 |
|
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: 74.42 E-value: 9.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 124 DPDVVVIDTRNDYEVQIGTFERAVNPLTKTFREFPEF--------VQQNLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGF 195
Cdd:smart00450 2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeeLLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81
|
90
....*....|....*....
gi 522171213 196 DEVYHLEGGILKYLEEVPQ 214
Cdd:smart00450 82 KNVYLLDGGYKEWSAAGPP 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
1-295 |
0e+00 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 521.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 1 MTQFVVCALYKFATLEDFESMRQPLHDVMEANGVRGTLLLAREGVNGTVAGSRQGIDAVLAWLRSDPRLADLSHKESFNE 80
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 81 EMPFYRTKVKLKKEIVTMGVEGIDPRQVVGTYVKPQDWNSLIADPDVVVIDTRNDYEVQIGTFERAVNPLTKTFREFPEF 160
Cdd:COG1054 81 GHPFPRLKVKLKKEIVTMGLPDVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 161 VQQNLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGFDEVYHLEGGILKYLEEVPQESSLWRGECFVFDNRVTVNHDLERGS 240
Cdd:COG1054 161 VEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNLEPGV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522171213 241 FEQCHACRLPIT--QADMESEKYMAGVSCPHCFD-------ALSDEQRSRYAqRELQVRLARQR 295
Cdd:COG1054 241 IGLCHACGTPCDryVNCANDPCYELGVSCPHCADkyeccsdECTEEQRARYE-RQRQLRLAKER 303
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
1-299 |
7.38e-160 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 448.91 E-value: 7.38e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 1 MTQFVVCALYKFATLEDFESMRQPLHDVMEANGVRGTLLLAREGVNGTVAGSRQGIDAVLAWLRSDPRLADLSHKESFNE 80
Cdd:PRK00142 1 MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 81 EMPFYRTKVKLKKEIVTMGVE-GIDPRQVVGTYVKPQDWNSLIADPDVVVIDTRNDYEVQIGTFERAVNPLTKTFREFPE 159
Cdd:PRK00142 81 GHAFPRLSVKVRKEIVALGLDdDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 160 FVQQNLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGFDEVYHLEGGILKYLEEVPQESSLWRGECFVFDNRVTV------- 232
Cdd:PRK00142 161 WVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVpindevp 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522171213 233 -NHDLERG----SFEQCH--ACRLPITQADMESEKYMAGVSCPHCFDALSDEQRSRYAQRELQVRLARQRGEEH 299
Cdd:PRK00142 241 iGHCHQCGtpcdRYVNCAnpACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
|
|
| PRK01415 |
PRK01415 |
hypothetical protein; Validated |
3-236 |
1.29e-83 |
|
hypothetical protein; Validated
Pssm-ID: 167229 [Multi-domain] Cd Length: 247 Bit Score: 252.94 E-value: 1.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 3 QFVVCALYKFATLEDFESMRQPLHDVMEANGVRGTLLLAREGVNGTVAGSRQGIDAVLAWLRSDPRLADLSHKESFNEEM 82
Cdd:PRK01415 4 KIAILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKLTGPKDVNVKINYSDVH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 83 PFYRTKVKLKKEIVTMGVEGIDPRQVVGTYVKPQDWNSLIADPDVVVIDTRNDYEVQIGTFERAVNPLTKTFREFPEFVQ 162
Cdd:PRK01415 84 PFQKLKVRLKKEIVAMNVDDLNVDLFKGEYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFKQFPAWVQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 522171213 163 QNLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGFDEVYHLEGGILKYLEEVPQESSLWRGECFVFDNRVTVNHDL 236
Cdd:PRK01415 164 QNQELLKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQNKNNLWQGECFVFDDRRAVTDDL 237
|
|
| PRK05320 |
PRK05320 |
rhodanese superfamily protein; Provisional |
2-252 |
1.38e-82 |
|
rhodanese superfamily protein; Provisional
Pssm-ID: 235405 [Multi-domain] Cd Length: 257 Bit Score: 250.71 E-value: 1.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 2 TQFVVCALYKFATLEDFESMRQPLHDVMEANGVRGTLLLAREGVNGTVAGSRQGIDAVLAWLRSDPRLADLSHKESFNEE 81
Cdd:PRK05320 1 MQIVNIAAYKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRADARFADLQVKESLSDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 82 MPFYRTKVKLKKEIVTMGVEGIDPRQVVGTYVKP---QDWNSLIADPD---VVVIDTRNDYEVQIGTFERAVN-PLTKtF 154
Cdd:PRK05320 81 QPFRRMLVKLKREIITMKRPAIRPELGRAPSVDAatlKRWLDQGHDDAgrpVVMLDTRNAFEVDVGTFDGALDyRIDK-F 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 155 REFPEFVQQNLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGFDEVYHLEGGILKYLEEVPQESslWRGECFVFDNRVTVNH 234
Cdd:PRK05320 160 TEFPEALAAHRADLAGKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFEEVGGAH--YDGDCFVFDYRTALDP 237
|
250
....*....|....*...
gi 522171213 235 DLERGSFEQCHACRLPIT 252
Cdd:PRK05320 238 QLAPLVDVTCFACRAVVT 255
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
110-210 |
9.29e-57 |
|
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: 178.93 E-value: 9.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 110 GTYVKPQDWNSLIADPDVVVIDTRNDYEVQIGTFERAVNPLTKTFREFPEFVQQNLDPAKHTKVAMFCTGGIRCEKSTAY 189
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 522171213 190 LKEQGFDEVYHLEGGILKYLE 210
Cdd:cd01518 81 LKERGFKNVYQLKGGILKYLE 101
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
4-95 |
2.44e-41 |
|
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: 139.17 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 4 FVVCALYKFATLEDFESMRQPLHDVMEANGVRGTLLLAREGVNGTVAGSRQGIDAVLAWLRSDPRLADLSHKESFNEEMP 83
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
|
90
....*....|..
gi 522171213 84 FYRTKVKLKKEI 95
Cdd:pfam17773 81 FRRLKVKLKKEI 92
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
124-214 |
9.77e-17 |
|
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: 74.42 E-value: 9.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 124 DPDVVVIDTRNDYEVQIGTFERAVNPLTKTFREFPEF--------VQQNLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGF 195
Cdd:smart00450 2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeeLLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81
|
90
....*....|....*....
gi 522171213 196 DEVYHLEGGILKYLEEVPQ 214
Cdd:smart00450 82 KNVYLLDGGYKEWSAAGPP 100
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
113-211 |
3.20e-15 |
|
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: 70.38 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 113 VKPQDWNSLIADPDVVVIDTRNDYEVQIGTFERAVN-PLtktfREFPEFVQQnLDpaKHTKVAMFCTGGIRCEKSTAYLK 191
Cdd:COG0607 6 ISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINiPL----GELAERLDE-LP--KDKPIVVYCASGGRSAQAAALLR 78
|
90 100
....*....|....*....|
gi 522171213 192 EQGFDEVYHLEGGILKYLEE 211
Cdd:COG0607 79 RAGYTNVYNLAGGIEAWKAA 98
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
120-208 |
2.97e-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: 64.63 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 120 SLIADPDVVVIDTRNDYEVQIGTFERAVN-PLTKTFREFPEfvqqnLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGFDEV 198
Cdd:cd00158 4 ELLDDEDAVLLDVREPEEYAAGHIPGAINiPLSELEERAAL-----LELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNV 78
|
90
....*....|
gi 522171213 199 YHLEGGILKY 208
Cdd:cd00158 79 YNLEGGMLAW 88
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
122-208 |
5.66e-12 |
|
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: 60.96 E-value: 5.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 122 IADPDVVVIDTRNDYEVQIGTFERAVN----PLTKTFREFPEFVQQNLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGFDE 197
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAKGHIPGAVNvplsSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80
|
90
....*....|.
gi 522171213 198 VYHLEGGILKY 208
Cdd:pfam00581 81 VYVLDGGFEAW 91
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
113-211 |
2.31e-09 |
|
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: 53.97 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 113 VKPQDWNSLIADPDVVVIDTRNDYEVQ-IGTFERAVNpLTKTFREF---PE--FVQQNLDPAKhtKVAMFCTGGIRCEKS 186
Cdd:cd01447 1 LSPEDARALLGSPGVLLVDVRDPRELErTGMIPGAFH-APRGMLEFwadPDspYHKPAFAEDK--PFVFYCASGWRSALA 77
|
90 100
....*....|....*....|....*
gi 522171213 187 TAYLKEQGFDEVYHLEGGILKYLEE 211
Cdd:cd01447 78 GKTLQDMGLKPVYNIEGGFKDWKEA 102
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
113-212 |
2.74e-09 |
|
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: 53.94 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 113 VKPQDWNSLIADPD--VVVIDTRNDYEVQIGTFERAVN-PLtktfREFPEFVQQNLDPAKHTKVAMFCTGGIRCEKSTAY 189
Cdd:cd01528 2 ISVAELAEWLADEReePVLIDVREPEELEIAFLPGFLHlPM----SEIPERSKELDSDNPDKDIVVLCHHGGRSMQVAQW 77
|
90 100
....*....|....*....|...
gi 522171213 190 LKEQGFDEVYHLEGGILKYLEEV 212
Cdd:cd01528 78 LLRQGFENVYNLQGGIDAWSLEV 100
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
124-210 |
2.39e-05 |
|
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: 42.64 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 124 DPDVVVIDTRNDYEVQIGTFERAVN-PLTKT----------FREFPEFVQqnldPAKHTKVAMFCTGGIRCEKSTAYLKE 192
Cdd:cd01519 13 HPNKVLIDVREPEELKTGKIPGAINiPLSSLpdalalseeeFEKKYGFPK----PSKDKELIFYCKAGVRSKAAAELARS 88
|
90
....*....|....*...
gi 522171213 193 QGFDEVYHLEGGILKYLE 210
Cdd:cd01519 89 LGYENVGNYPGSWLDWAA 106
|
|
| RHOD_ThiF |
cd01526 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ... |
113-212 |
4.94e-05 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative molybdopterin synthase sulfurylases including the molybdenum cofactor biosynthetic protein (CnxF) of Aspergillus nidulans and the molybdenum cofactor synthesis protein 3 (MOCS3) of Homo sapiens. These rhodanese-like domains are found C-terminal of the ThiF and MoeZ_MoeB domains.
Pssm-ID: 238784 [Multi-domain] Cd Length: 122 Bit Score: 42.30 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 113 VKPQDWNSLI-ADPDVVVIDTRNDYEVQIGTFERAVN-PLTKTFR---EFPEFVQQNLDPAKHTKVAMFCTGGIRCEKST 187
Cdd:cd01526 10 VSVKDYKNILqAGKKHVLLDVRPKVHFEICRLPEAINiPLSELLSkaaELKSLQELPLDNDKDSPIYVVCRRGNDSQTAV 89
|
90 100
....*....|....*....|....*.
gi 522171213 188 AYLKEQGFD-EVYHLEGGILKYLEEV 212
Cdd:cd01526 90 RKLKELGLErFVRDIIGGLKAWADKV 115
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
113-208 |
1.28e-04 |
|
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: 40.33 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 113 VKPQDWNSLIADpDVVVIDTRNDYEVQIGTFERAVN-PLTktfrEFPEFVQQnLDPAKHTKVamFCTGGIRCEKSTAYLK 191
Cdd:cd01524 1 VQWHELDNYRAD-GVTLIDVRTPQEFEKGHIKGAINiPLD----ELRDRLNE-LPKDKEIIV--YCAVGLRGYIAARILT 72
|
90
....*....|....*..
gi 522171213 192 EQGFdEVYHLEGGILKY 208
Cdd:cd01524 73 QNGF-KVKNLDGGYKTY 88
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
121-205 |
1.85e-04 |
|
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: 39.94 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 121 LIADP-DVVVIDTR--NDYEVQIGTFERAVNpltKTFREFPEFVqqnLDPAKHTKVAMFCTGGIRCEKSTAYLKEQGFDE 197
Cdd:cd01444 10 LLAAGeAPVLLDVRdpASYAALPDHIPGAIH---LDEDSLDDWL---GDLDRDRPVVVYCYHGNSSAQLAQALREAGFTD 83
|
....*...
gi 522171213 198 VYHLEGGI 205
Cdd:cd01444 84 VRSLAGGF 91
|
|
| glpE |
PRK00162 |
thiosulfate sulfurtransferase GlpE; |
115-204 |
3.02e-03 |
|
thiosulfate sulfurtransferase GlpE;
Pssm-ID: 178908 [Multi-domain] Cd Length: 108 Bit Score: 36.92 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522171213 115 PQDWNSLIADPDVVVIDTRNDYEVQIGTFERAVNpLTKtfREFPEFVQQN-LDpakhTKVAMFCTGGIRCEKSTAYLKEQ 193
Cdd:PRK00162 9 VEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFH-LTN--DSLGAFMRQAdFD----TPVMVMCYHGNSSQGAAQYLLQQ 81
|
90
....*....|.
gi 522171213 194 GFDEVYHLEGG 204
Cdd:PRK00162 82 GFDVVYSIDGG 92
|
|
| Rhodanese_C |
pfam12368 |
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ... |
220-250 |
3.05e-03 |
|
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: 35.76 E-value: 3.05e-03
10 20 30
....*....|....*....|....*....|.
gi 522171213 220 RGECFVFDNRVTVNHDLERGSFEQCHACRLP 250
Cdd:pfam12368 1 KGKLFVFDERLAVVEPSDDDVIGKCYHCGKP 31
|
|
| |
