|
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: 523.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 1 MSKVVVCAMYKFVSLPDFERIQKPLLIVMEKSGIKGTLLLAKEGINGTVAGSQSAIDALLAWLATQPGLDNIVHKLSFDD 80
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 81 DMPFYRTKVKLKKEIVTMGVEGIDPNEVVGTYVKPKDWNALISDPEVLLVDTRNDYEVKIGTFENALDPQTATFREFPEY 160
Cdd:COG1054 81 GHPFPRLKVKLKKEIVTMGLPDVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 161 VKQNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQGFEDVYHLEGGILKYLEEVKQEESMWQGECFVFDNRVAVNHDLEKGQ 240
Cdd:COG1054 161 VEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNLEPGV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527111562 241 YDQCNACRMPITEAE--KASSQFEQGVSCPHCIDK-------VTDKQRERFlERERQVQLSKQR 295
Cdd:COG1054 241 IGLCHACGTPCDRYVncANDPCYELGVSCPHCADKyeccsdeCTEEQRARY-ERQRQLRLAKER 303
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
1-299 |
2.50e-163 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 457.77 E-value: 2.50e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 1 MSKVVVCAMYKFVSLPDFERIQKPLLIVMEKSGIKGTLLLAKEGINGTVAGSQSAIDALLAWLATQPGLDNIVHKLSFDD 80
Cdd:PRK00142 1 MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 81 DMPFYRTKVKLKKEIVTMGVE-GIDPNEVVGTYVKPKDWNALISDPEVLLVDTRNDYEVKIGTFENALDPQTATFREFPE 159
Cdd:PRK00142 81 GHAFPRLSVKVRKEIVALGLDdDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 160 YVKQNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQGFEDVYHLEGGILKYLEEVKQEESMWQGECFVFDNRVAV------- 232
Cdd:PRK00142 161 WVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVpindevp 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527111562 233 -NHDLEKG----QYDQCN--ACRMPITEAEKASSQFEQGVSCPHCIDKVTDKQRERFLERERQVQLSKQRGEAH 299
Cdd:PRK00142 241 iGHCHQCGtpcdRYVNCAnpACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
110-210 |
2.05e-58 |
|
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: 183.16 E-value: 2.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 110 GTYVKPKDWNALISDPEVLLVDTRNDYEVKIGTFENALDPQTATFREFPEYVKQNLDPTKHKKVAMFCTGGIRCEKSTAY 189
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 527111562 190 LKEQGFEDVYHLEGGILKYLE 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 |
2.61e-35 |
|
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: 123.37 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 4 VVVCAMYKFVSLPDFERIQKPLLIVMEKSGIKGTLLLAKEGINGTVAGSQSAIDALLAWLATQPGLDNIVHKLSFDDDMP 83
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
|
90
....*....|..
gi 527111562 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 |
4.20e-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: 72.88 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 123 SDPEVLLVDTRNDYEVKIGTFENALDPQTATFREFPEYVK--------QNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQG 194
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 527111562 195 FEDVYHLEGGILKYLEEVKQ 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: 523.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 1 MSKVVVCAMYKFVSLPDFERIQKPLLIVMEKSGIKGTLLLAKEGINGTVAGSQSAIDALLAWLATQPGLDNIVHKLSFDD 80
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 81 DMPFYRTKVKLKKEIVTMGVEGIDPNEVVGTYVKPKDWNALISDPEVLLVDTRNDYEVKIGTFENALDPQTATFREFPEY 160
Cdd:COG1054 81 GHPFPRLKVKLKKEIVTMGLPDVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 161 VKQNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQGFEDVYHLEGGILKYLEEVKQEESMWQGECFVFDNRVAVNHDLEKGQ 240
Cdd:COG1054 161 VEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNLEPGV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527111562 241 YDQCNACRMPITEAE--KASSQFEQGVSCPHCIDK-------VTDKQRERFlERERQVQLSKQR 295
Cdd:COG1054 241 IGLCHACGTPCDRYVncANDPCYELGVSCPHCADKyeccsdeCTEEQRARY-ERQRQLRLAKER 303
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
1-299 |
2.50e-163 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 457.77 E-value: 2.50e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 1 MSKVVVCAMYKFVSLPDFERIQKPLLIVMEKSGIKGTLLLAKEGINGTVAGSQSAIDALLAWLATQPGLDNIVHKLSFDD 80
Cdd:PRK00142 1 MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 81 DMPFYRTKVKLKKEIVTMGVE-GIDPNEVVGTYVKPKDWNALISDPEVLLVDTRNDYEVKIGTFENALDPQTATFREFPE 159
Cdd:PRK00142 81 GHAFPRLSVKVRKEIVALGLDdDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 160 YVKQNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQGFEDVYHLEGGILKYLEEVKQEESMWQGECFVFDNRVAV------- 232
Cdd:PRK00142 161 WVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVpindevp 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527111562 233 -NHDLEKG----QYDQCN--ACRMPITEAEKASSQFEQGVSCPHCIDKVTDKQRERFLERERQVQLSKQRGEAH 299
Cdd:PRK00142 241 iGHCHQCGtpcdRYVNCAnpACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
|
|
| PRK01415 |
PRK01415 |
hypothetical protein; Validated |
3-236 |
1.36e-85 |
|
hypothetical protein; Validated
Pssm-ID: 167229 [Multi-domain] Cd Length: 247 Bit Score: 257.95 E-value: 1.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 3 KVVVCAMYKFVSLPDFERIQKPLLIVMEKSGIKGTLLLAKEGINGTVAGSQSAIDALLAWLATQPGLDNIVHKLSFDDDM 82
Cdd:PRK01415 4 KIAILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKLTGPKDVNVKINYSDVH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 83 PFYRTKVKLKKEIVTMGVEGIDPNEVVGTYVKPKDWNALISDPEVLLVDTRNDYEVKIGTFENALDPQTATFREFPEYVK 162
Cdd:PRK01415 84 PFQKLKVRLKKEIVAMNVDDLNVDLFKGEYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFKQFPAWVQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527111562 163 QNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQGFEDVYHLEGGILKYLEEVKQEESMWQGECFVFDNRVAVNHDL 236
Cdd:PRK01415 164 QNQELLKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQNKNNLWQGECFVFDDRRAVTDDL 237
|
|
| PRK05320 |
PRK05320 |
rhodanese superfamily protein; Provisional |
4-252 |
5.51e-79 |
|
rhodanese superfamily protein; Provisional
Pssm-ID: 235405 [Multi-domain] Cd Length: 257 Bit Score: 241.47 E-value: 5.51e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 4 VVVCAMYKFVSLPDFERIQKPLLIVMEKSGIKGTLLLAKEGINGTVAGSQSAIDALLAWLATQPGLDNIVHKLSFDDDMP 83
Cdd:PRK05320 3 IVNIAAYKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRADARFADLQVKESLSDSQP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 84 FYRTKVKLKKEIVTMGVEGIDPNEVVGTYVKP---KDWNALISDPE---VLLVDTRNDYEVKIGTFENALDPQTATFREF 157
Cdd:PRK05320 83 FRRMLVKLKREIITMKRPAIRPELGRAPSVDAatlKRWLDQGHDDAgrpVVMLDTRNAFEVDVGTFDGALDYRIDKFTEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 158 PEYVKQNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQGFEDVYHLEGGILKYLEEVKQEEsmWQGECFVFDNRVAVNHDLE 237
Cdd:PRK05320 163 PEALAAHRADLAGKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFEEVGGAH--YDGDCFVFDYRTALDPQLA 240
|
250
....*....|....*
gi 527111562 238 KGQYDQCNACRMPIT 252
Cdd:PRK05320 241 PLVDVTCFACRAVVT 255
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
110-210 |
2.05e-58 |
|
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: 183.16 E-value: 2.05e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 110 GTYVKPKDWNALISDPEVLLVDTRNDYEVKIGTFENALDPQTATFREFPEYVKQNLDPTKHKKVAMFCTGGIRCEKSTAY 189
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 527111562 190 LKEQGFEDVYHLEGGILKYLE 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 |
2.61e-35 |
|
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: 123.37 E-value: 2.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 4 VVVCAMYKFVSLPDFERIQKPLLIVMEKSGIKGTLLLAKEGINGTVAGSQSAIDALLAWLATQPGLDNIVHKLSFDDDMP 83
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
|
90
....*....|..
gi 527111562 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 |
4.20e-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: 72.88 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 123 SDPEVLLVDTRNDYEVKIGTFENALDPQTATFREFPEYVK--------QNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQG 194
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 527111562 195 FEDVYHLEGGILKYLEEVKQ 214
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGPP 100
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
113-217 |
1.41e-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: 65.76 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 113 VKPKDWNALISDPEVLLVDTRNDYEVKIGTFENALdpqTATFREFPEYVKQnLDptKHKKVAMFCTGGIRCEKSTAYLKE 192
Cdd:COG0607 6 ISPAELAELLESEDAVLLDVREPEEFAAGHIPGAI---NIPLGELAERLDE-LP--KDKPIVVYCASGGRSAQAAALLRR 79
|
90 100
....*....|....*....|....*
gi 527111562 193 QGFEDVYHLEGGILKYLEEVKQEES 217
Cdd:COG0607 80 AGYTNVYNLAGGIEAWKAAGLPVEK 104
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
120-208 |
4.38e-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: 61.16 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 120 ALISDPEVLLVDTRNDYEVKIGTFENALD-PqtatFREFPEYVKQNLDPtKHKKVAMFCTGGIRCEKSTAYLKEQGFEDV 198
Cdd:cd00158 4 ELLDDEDAVLLDVREPEEYAAGHIPGAINiP----LSELEERAALLELD-KDKPIVVYCRSGNRSARAAKLLRKAGGTNV 78
|
90
....*....|
gi 527111562 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 |
5.31e-11 |
|
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: 58.26 E-value: 5.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 122 ISDPEVLLVDTRNDYEVKIGTFENA--LDPQTATFREFP--EYVKQNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQGFED 197
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAKGHIPGAvnVPLSSLSLPPLPllELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80
|
90
....*....|.
gi 527111562 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 |
5.46e-10 |
|
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: 55.90 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 113 VKPKDWNALISDPEVLLVDTRNDYEVKI------------GTFENALDPQTatfrefpEYVKQNLDPTKhkKVAMFCTGG 180
Cdd:cd01447 1 LSPEDARALLGSPGVLLVDVRDPRELERtgmipgafhaprGMLEFWADPDS-------PYHKPAFAEDK--PFVFYCASG 71
|
90 100 110
....*....|....*....|....*....|.
gi 527111562 181 IRCEKSTAYLKEQGFEDVYHLEGGILKYLEE 211
Cdd:cd01447 72 WRSALAGKTLQDMGLKPVYNIEGGFKDWKEA 102
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
124-212 |
8.73e-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: 52.40 E-value: 8.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 124 DPEVLLVDTRNDYEVKIGTFENALD-PqtatFREFPEYVKQNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQGFEDVYHLE 202
Cdd:cd01528 15 REEPVLIDVREPEELEIAFLPGFLHlP----MSEIPERSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQGFENVYNLQ 90
|
90
....*....|
gi 527111562 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 |
2.38e-06 |
|
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: 45.72 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 119 NALISDPEVLLVDTRNDYEVKIG-----------TFENALDPQTATFREFPEYVKqnldPTKHKKVAMFCTGGIRCEKST 187
Cdd:cd01519 8 NLPNPHPNKVLIDVREPEELKTGkipgainiplsSLPDALALSEEEFEKKYGFPK----PSKDKELIFYCKAGVRSKAAA 83
|
90 100
....*....|....*....|...
gi 527111562 188 AYLKEQGFEDVYHLEGGILKYLE 210
Cdd:cd01519 84 ELARSLGYENVGNYPGSWLDWAA 106
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
108-219 |
5.79e-05 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 44.31 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 108 VVGTYVKPKDWNALI-SDPEVLLVDTRNDYEVKIGTFENA-LDPQTA-----TFREFPEyvkqnldptkHKKVAMFCTGG 180
Cdd:PRK07878 284 AAGSTITPRELKEWLdSGKKIALIDVREPVEWDIVHIPGAqLIPKSEilsgeALAKLPQ----------DRTIVLYCKTG 353
|
90 100 110
....*....|....*....|....*....|....*....
gi 527111562 181 IRCEKSTAYLKEQGFEDVYHLEGGILKYLEEVKQEESMW 219
Cdd:PRK07878 354 VRSAEALAALKKAGFSDAVHLQGGVVAWAKQVDPSLPMY 392
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
125-205 |
1.30e-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: 40.32 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 125 PEVLLVDTR--NDYEVKIGTFENAldpQTATFREFPEYVKQNldpTKHKKVAMFCTGGIRCEKSTAYLKEQGFEDVYHLE 202
Cdd:cd01444 15 EAPVLLDVRdpASYAALPDHIPGA---IHLDEDSLDDWLGDL---DRDRPVVVYCYHGNSSAQLAQALREAGFTDVRSLA 88
|
...
gi 527111562 203 GGI 205
Cdd:cd01444 89 GGF 91
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
127-205 |
1.08e-03 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 40.38 E-value: 1.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 527111562 127 VLLVDTRNDYEVKIGTFENALdpqtATFREFPEYVKQNLDPTKHKKVAMFCTGGIRCEKSTAYLKEQGFEDVYHLEGGI 205
Cdd:PRK08762 18 AVLIDVREAHERASGQAEGAL----RIPRGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYTRVASVAGGF 92
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
49-210 |
1.28e-03 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 40.24 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 49 VAGSQSAIDAL-LAWLATQPGLDNIVHKLSFD---DDMPFYRTKVKLKKEIVTMGVEGIDPNEvvGTYVKPKDWNALISD 124
Cdd:PRK05597 197 VVGSAMAMEALkLITGVGTPLIGKLGYYDSLDgtwEYIPVVGNPAVLERVRGSTPVHGISGGF--GEVLDVPRVSALPDG 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 125 peVLLVDTRNDYEVKIGTFENALDPQTATFREfpEYVKQNLDPTKhkKVAMFCTGGIRCEKSTAYLKEQGFEDVYHLEGG 204
Cdd:PRK05597 275 --VTLIDVREPSEFAAYSIPGAHNVPLSAIRE--GANPPSVSAGD--EVVVYCAAGVRSAQAVAILERAGYTGMSSLDGG 348
|
....*.
gi 527111562 205 ILKYLE 210
Cdd:PRK05597 349 IEGWLD 354
|
|
| Rhodanese_C |
pfam12368 |
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ... |
220-273 |
1.99e-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: 36.14 E-value: 1.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 527111562 220 QGECFVFDNRVAVNHDLEKGQYDQCNACRMPITEAEKASSQF--EQGVSCPHCIDK 273
Cdd:pfam12368 1 KGKLFVFDERLAVVEPSDDDVIGKCYHCGKPCDRYVNCANPDcnRLFLQCEECAEK 56
|
|
| glpE |
PRK00162 |
thiosulfate sulfurtransferase GlpE; |
115-216 |
2.99e-03 |
|
thiosulfate sulfurtransferase GlpE;
Pssm-ID: 178908 [Multi-domain] Cd Length: 108 Bit Score: 36.92 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527111562 115 PKDWNALISDPEVLLVDTRNDYEVKIGTFENA--LDPQTatfreFPEYVKQN-LDptkhKKVAMFCTGGIRCEKSTAYLK 191
Cdd:PRK00162 9 VEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAfhLTNDS-----LGAFMRQAdFD----TPVMVMCYHGNSSQGAAQYLL 79
|
90 100
....*....|....*....|....*....
gi 527111562 192 EQGFEDVYHLEGGI----LKYLEEVKQEE 216
Cdd:PRK00162 80 QQGFDVVYSIDGGFeawrRTFPAEVASGA 108
|
|
| |
