|
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: 528.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 1 MTSIVVAALYKFVTLDDYVALREPLLQTLLDNGVKGTLLLAEEGINGTVSGSREGIDALFAWLRSDPRLADIEHKESYCD 80
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 81 EQPFYRTKVKLKKEIVTLGVPGVDPNKQVGQYVEAKDWNALISDPEVLLIDTRNDYEVAIGTFEGAVDPKTRSFREFPEY 160
Cdd:COG1054 81 GHPFPRLKVKLKKEIVTMGLPDVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 161 IKAHYDPARHKKVAMFCTGGIRCEKASSYMLGAGFEEVFHLKGGILKYLEEVPQEQSLWRGDCFVFDNRVTVRHDLSEGE 240
Cdd:COG1054 161 VEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNLEPGV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596055 241 YDQCHACRNPVS--LEDRQSEHYVPGISCPHCWD-------SLSEKTRAGArERQKQIELARQR 295
Cdd:COG1054 241 IGLCHACGTPCDryVNCANDPCYELGVSCPHCADkyeccsdECTEEQRARY-ERQRQLRLAKER 303
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
1-299 |
4.76e-168 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 468.94 E-value: 4.76e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 1 MTSIVVAALYKFVTLDDYVALREPLLQTLLDNGVKGTLLLAEEGINGTVSGSREGIDALFAWLRSDPRLADIEHKESYCD 80
Cdd:PRK00142 1 MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 81 EQPFYRTKVKLKKEIVTLGVP-GVDPNKQVGQYVEAKDWNALISDPEVLLIDTRNDYEVAIGTFEGAVDPKTRSFREFPE 159
Cdd:PRK00142 81 GHAFPRLSVKVRKEIVALGLDdDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 160 YIKAHYDPARHKKVAMFCTGGIRCEKASSYMLGAGFEEVFHLKGGILKYLEEVPQEQSLWRGDCFVFDNRVTVR------ 233
Cdd:PRK00142 161 WVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVPindevp 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596055 234 --HDLSEGE----YDQCH--ACRNPVSLEDRQSEHYVPGISCPHCWDSLSEKTRAGARERQKQIELARQRNQPH 299
Cdd:PRK00142 241 igHCHQCGTpcdrYVNCAnpACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
110-210 |
5.82e-55 |
|
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: 173.92 E-value: 5.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 110 GQYVEAKDWNALISDPEVLLIDTRNDYEVAIGTFEGAVDPKTRSFREFPEYIKAHYDPARHKKVAMFCTGGIRCEKASSY 189
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 15596055 190 MLGAGFEEVFHLKGGILKYLE 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 |
3.34e-44 |
|
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: 146.10 E-value: 3.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 4 IVVAALYKFVTLDDYVALREPLLQTLLDNGVKGTLLLAEEGINGTVSGSREGIDALFAWLRSDPRLADIEHKESYCDEQP 83
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
|
90
....*....|..
gi 15596055 84 FYRTKVKLKKEI 95
Cdd:pfam17773 81 FRRLKVKLKKEI 92
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
123-214 |
7.54e-14 |
|
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: 66.33 E-value: 7.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 123 SDPEVLLIDTRNDYEVAIGTFEGAVDPKTRSFREFPEYIKAHYDPARH--------KKVAMFCTGGIRCEKASSYMLGAG 194
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLkrlgldkdKPVVVYCRSGNRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 15596055 195 FEEVFHLKGGILKYLEEVPQ 214
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGPP 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: 528.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 1 MTSIVVAALYKFVTLDDYVALREPLLQTLLDNGVKGTLLLAEEGINGTVSGSREGIDALFAWLRSDPRLADIEHKESYCD 80
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 81 EQPFYRTKVKLKKEIVTLGVPGVDPNKQVGQYVEAKDWNALISDPEVLLIDTRNDYEVAIGTFEGAVDPKTRSFREFPEY 160
Cdd:COG1054 81 GHPFPRLKVKLKKEIVTMGLPDVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 161 IKAHYDPARHKKVAMFCTGGIRCEKASSYMLGAGFEEVFHLKGGILKYLEEVPQEQSLWRGDCFVFDNRVTVRHDLSEGE 240
Cdd:COG1054 161 VEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNLEPGV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596055 241 YDQCHACRNPVS--LEDRQSEHYVPGISCPHCWD-------SLSEKTRAGArERQKQIELARQR 295
Cdd:COG1054 241 IGLCHACGTPCDryVNCANDPCYELGVSCPHCADkyeccsdECTEEQRARY-ERQRQLRLAKER 303
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
1-299 |
4.76e-168 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 468.94 E-value: 4.76e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 1 MTSIVVAALYKFVTLDDYVALREPLLQTLLDNGVKGTLLLAEEGINGTVSGSREGIDALFAWLRSDPRLADIEHKESYCD 80
Cdd:PRK00142 1 MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 81 EQPFYRTKVKLKKEIVTLGVP-GVDPNKQVGQYVEAKDWNALISDPEVLLIDTRNDYEVAIGTFEGAVDPKTRSFREFPE 159
Cdd:PRK00142 81 GHAFPRLSVKVRKEIVALGLDdDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 160 YIKAHYDPARHKKVAMFCTGGIRCEKASSYMLGAGFEEVFHLKGGILKYLEEVPQEQSLWRGDCFVFDNRVTVR------ 233
Cdd:PRK00142 161 WVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVPindevp 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596055 234 --HDLSEGE----YDQCH--ACRNPVSLEDRQSEHYVPGISCPHCWDSLSEKTRAGARERQKQIELARQRNQPH 299
Cdd:PRK00142 241 igHCHQCGTpcdrYVNCAnpACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
|
|
| PRK05320 |
PRK05320 |
rhodanese superfamily protein; Provisional |
2-254 |
3.29e-89 |
|
rhodanese superfamily protein; Provisional
Pssm-ID: 235405 [Multi-domain] Cd Length: 257 Bit Score: 266.89 E-value: 3.29e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 2 TSIVVAALYKFVTLDDYVALREPLLQTLLDNGVKGTLLLAEEGINGTVSGSREGIDALFAWLRSDPRLADIEHKESYCDE 81
Cdd:PRK05320 1 MQIVNIAAYKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRADARFADLQVKESLSDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 82 QPFYRTKVKLKKEIVTLGVPGVDPNKQVGQYVEA---KDWNALISDPE---VLLIDTRNDYEVAIGTFEGAVDPKTRSFR 155
Cdd:PRK05320 81 QPFRRMLVKLKREIITMKRPAIRPELGRAPSVDAatlKRWLDQGHDDAgrpVVMLDTRNAFEVDVGTFDGALDYRIDKFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 156 EFPEYIKAHYDPARHKKVAMFCTGGIRCEKASSYMLGAGFEEVFHLKGGILKYLEEVPQEQslWRGDCFVFDNRVTVRHD 235
Cdd:PRK05320 161 EFPEALAAHRADLAGKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFEEVGGAH--YDGDCFVFDYRTALDPQ 238
|
250
....*....|....*....
gi 15596055 236 LSEGEYDQCHACRNPVSLE 254
Cdd:PRK05320 239 LAPLVDVTCFACRAVVTPE 257
|
|
| PRK01415 |
PRK01415 |
hypothetical protein; Validated |
4-240 |
1.41e-77 |
|
hypothetical protein; Validated
Pssm-ID: 167229 [Multi-domain] Cd Length: 247 Bit Score: 236.76 E-value: 1.41e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 4 IVVAALYKFVTLDDYVALREPLLQTLLDNGVKGTLLLAEEGINGTVSGSREGIDALFAWLRSDPRLADIEHKESYCDEQP 83
Cdd:PRK01415 5 IAILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKLTGPKDVNVKINYSDVHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 84 FYRTKVKLKKEIVTLGVPGVDPNKQVGQYVEAKDWNALISDPEVLLIDTRNDYEVAIGTFEGAVDPKTRSFREFPEYIKA 163
Cdd:PRK01415 85 FQKLKVRLKKEIVAMNVDDLNVDLFKGEYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFKQFPAWVQQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596055 164 HYDPARHKKVAMFCTGGIRCEKASSYMLGAGFEEVFHLKGGILKYLEEVPQEQSLWRGDCFVFDNRVTVRHDLSEGE 240
Cdd:PRK01415 165 NQELLKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQNKNNLWQGECFVFDDRRAVTDDLSPVE 241
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
110-210 |
5.82e-55 |
|
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: 173.92 E-value: 5.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 110 GQYVEAKDWNALISDPEVLLIDTRNDYEVAIGTFEGAVDPKTRSFREFPEYIKAHYDPARHKKVAMFCTGGIRCEKASSY 189
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 15596055 190 MLGAGFEEVFHLKGGILKYLE 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 |
3.34e-44 |
|
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: 146.10 E-value: 3.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 4 IVVAALYKFVTLDDYVALREPLLQTLLDNGVKGTLLLAEEGINGTVSGSREGIDALFAWLRSDPRLADIEHKESYCDEQP 83
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
|
90
....*....|..
gi 15596055 84 FYRTKVKLKKEI 95
Cdd:pfam17773 81 FRRLKVKLKKEI 92
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
123-214 |
7.54e-14 |
|
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: 66.33 E-value: 7.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 123 SDPEVLLIDTRNDYEVAIGTFEGAVDPKTRSFREFPEYIKAHYDPARH--------KKVAMFCTGGIRCEKASSYMLGAG 194
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLkrlgldkdKPVVVYCRSGNRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 15596055 195 FEEVFHLKGGILKYLEEVPQ 214
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGPP 100
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
111-211 |
2.12e-13 |
|
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: 65.37 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 111 QYVEAKDWNALISDPEVLLIDTRNDYEVAIGTFEGAVdpkTRSFREFPEYIKAHydpARHKKVAMFCTGGIRCEKASSYM 190
Cdd:COG0607 4 KEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAI---NIPLGELAERLDEL---PKDKPIVVYCASGGRSAQAAALL 77
|
90 100
....*....|....*....|.
gi 15596055 191 LGAGFEEVFHLKGGILKYLEE 211
Cdd:COG0607 78 RRAGYTNVYNLAGGIEAWKAA 98
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
120-208 |
7.98e-12 |
|
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: 60.39 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 120 ALISDPEVLLIDTRNDYEVAIGTFEGAVDpktRSFREFPEYIKAHyDPARHKKVAMFCTGGIRCEKASSYMLGAGFEEVF 199
Cdd:cd00158 4 ELLDDEDAVLLDVREPEEYAAGHIPGAIN---IPLSELEERAALL-ELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNVY 79
|
....*....
gi 15596055 200 HLKGGILKY 208
Cdd:cd00158 80 NLEGGMLAW 88
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
122-208 |
2.40e-09 |
|
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.
Pssm-ID: 425764 [Multi-domain] Cd Length: 92 Bit Score: 53.64 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 122 ISDPEVLLIDTRNDYEVAIGTFEGAV----DPKTRSFREFPEYIKAHYDPARHKKVAMFCTGGIRCEKASSYMLGAGFEE 197
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAKGHIPGAVnvplSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80
|
90
....*....|.
gi 15596055 198 VFHLKGGILKY 208
Cdd:pfam00581 81 VYVLDGGFEAW 91
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
113-211 |
9.87e-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: 52.04 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 113 VEAKDWNALISDPEVLLIDTRNDYEV-AIGTFEGAVDpKTRSFREF---PE--YIKAHYDPArhKKVAMFCTGGIRCEKA 186
Cdd:cd01447 1 LSPEDARALLGSPGVLLVDVRDPRELeRTGMIPGAFH-APRGMLEFwadPDspYHKPAFAED--KPFVFYCASGWRSALA 77
|
90 100
....*....|....*....|....*
gi 15596055 187 SSYMLGAGFEEVFHLKGGILKYLEE 211
Cdd:cd01447 78 GKTLQDMGLKPVYNIEGGFKDWKEA 102
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
124-212 |
5.69e-08 |
|
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: 50.09 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 124 DPEVLLIDTRNDYEVAIGTFEGAVD-PktrsFREFPEYIKAHYDPARHKKVAMFCTGGIRCEKASSYMLGAGFEEVFHLK 202
Cdd:cd01528 15 REEPVLIDVREPEELEIAFLPGFLHlP----MSEIPERSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQGFENVYNLQ 90
|
90
....*....|
gi 15596055 203 GGILKYLEEV 212
Cdd:cd01528 91 GGIDAWSLEV 100
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
119-210 |
7.99e-07 |
|
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: 46.88 E-value: 7.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 119 NALISDPEVLLIDTRNDYEVAIGTFEGAVDPKTRSFREF----PEYIKAHY---DPARHKKVAMFCTGGIRCEKASSYML 191
Cdd:cd01519 8 NLPNPHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDAlalsEEEFEKKYgfpKPSKDKELIFYCKAGVRSKAAAELAR 87
|
90
....*....|....*....
gi 15596055 192 GAGFEEVFHLKGGILKYLE 210
Cdd:cd01519 88 SLGYENVGNYPGSWLDWAA 106
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
114-212 |
8.62e-05 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 43.93 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 114 EAKDWnaLISDPEVLLIDTRNDYEVAIGTFEGAV-DPKTR-----SFREFPEyikahydparHKKVAMFCTGGIRCEKAS 187
Cdd:PRK07878 293 ELKEW--LDSGKKIALIDVREPVEWDIVHIPGAQlIPKSEilsgeALAKLPQ----------DRTIVLYCKTGVRSAEAL 360
|
90 100
....*....|....*....|....*
gi 15596055 188 SYMLGAGFEEVFHLKGGILKYLEEV 212
Cdd:PRK07878 361 AALKKAGFSDAVHLQGGVVAWAKQV 385
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
125-205 |
1.06e-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: 40.71 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 125 PEVLLIDTR--NDYEVAIGTFEGAVdpkTRSFREFPEYIKahyDPARHKKVAMFCTGGIRCEKASSYMLGAGFEEVFHLK 202
Cdd:cd01444 15 EAPVLLDVRdpASYAALPDHIPGAI---HLDEDSLDDWLG---DLDRDRPVVVYCYHGNSSAQLAQALREAGFTDVRSLA 88
|
...
gi 15596055 203 GGI 205
Cdd:cd01444 89 GGF 91
|
|
| Rhodanese_C |
pfam12368 |
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ... |
220-270 |
7.60e-04 |
|
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: 37.30 E-value: 7.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 220 RGDCFVFDNRVTVRHDLSEGEYDQCHACRNPvsledrqSEHYV---------PGISCPHC 270
Cdd:pfam12368 1 KGKLFVFDERLAVVEPSDDDVIGKCYHCGKP-------CDRYVncanpdcnrLFLQCEEC 53
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
94-210 |
9.54e-04 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 40.24 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 94 EIVTLGVPGVDPNKQVGQYVEAKDWNALISDpeVLLIDTRNDYEVAIGTFEGAVDPKTRSFREfpEYIKAHYDPArhKKV 173
Cdd:PRK05597 244 ERVRGSTPVHGISGGFGEVLDVPRVSALPDG--VTLIDVREPSEFAAYSIPGAHNVPLSAIRE--GANPPSVSAG--DEV 317
|
90 100 110
....*....|....*....|....*....|....*..
gi 15596055 174 AMFCTGGIRCEKASSYMLGAGFEEVFHLKGGILKYLE 210
Cdd:PRK05597 318 VVYCAAGVRSAQAVAILERAGYTGMSSLDGGIEGWLD 354
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
117-208 |
2.89e-03 |
|
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: 36.48 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596055 117 DWNALISDpEVLLIDTRNDYEVAIGTFEGAVDpktrsfreFP-EYIKAHYDPARH-KKVAMFCTGGIRCEKASSYMLGAG 194
Cdd:cd01524 5 ELDNYRAD-GVTLIDVRTPQEFEKGHIKGAIN--------IPlDELRDRLNELPKdKEIIVYCAVGLRGYIAARILTQNG 75
|
90
....*....|....
gi 15596055 195 FeEVFHLKGGILKY 208
Cdd:cd01524 76 F-KVKNLDGGYKTY 88
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
127-205 |
3.05e-03 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 38.84 E-value: 3.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596055 127 VLLIDTRNDYEVAIGTFEGAVdpktRSFREFPEYIKAHYDPARHKKVAMFCTGGIRCEKASSYMLGAGFEEVFHLKGGI 205
Cdd:PRK08762 18 AVLIDVREAHERASGQAEGAL----RIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYTRVASVAGGF 92
|
|
| |
