|
Name |
Accession |
Description |
Interval |
E-value |
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
13-299 |
9.52e-105 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 307.84 E-value: 9.52e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 13 KEKKTISFYRYFHIQNPKKLQLILLNKLKELKILGRIYIAQEGINAQIYIYKKYIYILKNFLYELnPIFKNVKFNFSTDD 92
Cdd:COG1054 2 KPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRAD-PRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 93 HsISFYKLQVKVRPHIVNDGIKNFKFNvEKLGKCISVKQFNTMSNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRNQL 172
Cdd:COG1054 81 G-HPFPRLKVKLKKEIVTMGLPDVDPN-EGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 173 TNMTRALKNYQHKKIVLYCTGGIRCEKASAWLIQNNFEHVFFLKGGIINYINYMRKKKyaVKFLGKMFVFDARLFENTNI 252
Cdd:COG1054 159 EWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEG--SLWEGECFVFDERVAVDHNL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 504119882 253 N--IVSYCHQCKiNQSYLHKNCARKKCNVLFLQCKICNEKFkEFCSSYC 299
Cdd:COG1054 237 EpgVIGLCHACG-TPCDRYVNCANDPCYELGVSCPHCADKY-ECCSDEC 283
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
13-299 |
1.36e-97 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 289.83 E-value: 1.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 13 KEKKTISFYRYFHIQNPKKLQLILLNKLKELKILGRIYIAQEGINAQIYIYKKYIYILKNFLYElNPIFKNVKFNFSTDD 92
Cdd:PRK00142 2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKA-DPRFADIRFKISEDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 93 HSiSFYKLQVKVRPHIVNDGIKNFKFNVEKLGKCISVKQFNTMSNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRNQL 172
Cdd:PRK00142 81 GH-AFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 173 TNMTRALKNYQHKKIVLYCTGGIRCEKASAWLIQNNFEHVFFLKGGIINYINYMRKKKYavKFLGKMFVFDARLFENTNI 252
Cdd:PRK00142 160 PWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGL--LWDGKLYVFDERMAVPIND 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 504119882 253 N-IVSYCHQCKINQSYlHKNCARKKCNVLFLQCKICNEKFKEFCSSYC 299
Cdd:PRK00142 238 EvPIGHCHQCGTPCDR-YVNCANPACNLLILQCEECEEKYLGCCSEEC 284
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
124-222 |
7.32e-36 |
|
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: 124.61 E-value: 7.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 124 GKCISVKQFNTMSNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRNQLTNMTRALKNYQHKKIVLYCTGGIRCEKASAW 203
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90
....*....|....*....
gi 504119882 204 LIQNNFEHVFFLKGGIINY 222
Cdd:cd01518 81 LKERGFKNVYQLKGGILKY 99
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
137-222 |
5.48e-20 |
|
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: 82.89 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 137 NSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFR--------NQLTNMTRALKNYQHKKIVLYCTGGIRCEKASAWLIQNN 208
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLdrrgeldiLEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90
....*....|....
gi 504119882 209 FEHVFFLKGGIINY 222
Cdd:smart00450 81 FKNVYLLDGGYKEW 94
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
16-108 |
9.25e-20 |
|
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: 82.16 E-value: 9.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 16 KTISFYRYFHIQNPKKLQLILLNKLKELKILGRIYIAQEGINAQIYIYKKYIYILKNFLyELNPIFKNVKFNFSTDDhSI 95
Cdd:pfam17773 2 VVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFL-RADPGFADLDFKESYSD-EH 79
|
90
....*....|...
gi 504119882 96 SFYKLQVKVRPHI 108
Cdd:pfam17773 80 PFRRLKVKLKKEI 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
13-299 |
9.52e-105 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 307.84 E-value: 9.52e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 13 KEKKTISFYRYFHIQNPKKLQLILLNKLKELKILGRIYIAQEGINAQIYIYKKYIYILKNFLYELnPIFKNVKFNFSTDD 92
Cdd:COG1054 2 KPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRAD-PRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 93 HsISFYKLQVKVRPHIVNDGIKNFKFNvEKLGKCISVKQFNTMSNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRNQL 172
Cdd:COG1054 81 G-HPFPRLKVKLKKEIVTMGLPDVDPN-EGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 173 TNMTRALKNYQHKKIVLYCTGGIRCEKASAWLIQNNFEHVFFLKGGIINYINYMRKKKyaVKFLGKMFVFDARLFENTNI 252
Cdd:COG1054 159 EWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEG--SLWEGECFVFDERVAVDHNL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 504119882 253 N--IVSYCHQCKiNQSYLHKNCARKKCNVLFLQCKICNEKFkEFCSSYC 299
Cdd:COG1054 237 EpgVIGLCHACG-TPCDRYVNCANDPCYELGVSCPHCADKY-ECCSDEC 283
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
13-299 |
1.36e-97 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 289.83 E-value: 1.36e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 13 KEKKTISFYRYFHIQNPKKLQLILLNKLKELKILGRIYIAQEGINAQIYIYKKYIYILKNFLYElNPIFKNVKFNFSTDD 92
Cdd:PRK00142 2 KPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKA-DPRFADIRFKISEDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 93 HSiSFYKLQVKVRPHIVNDGIKNFKFNVEKLGKCISVKQFNTMSNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRNQL 172
Cdd:PRK00142 81 GH-AFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 173 TNMTRALKNYQHKKIVLYCTGGIRCEKASAWLIQNNFEHVFFLKGGIINYINYMRKKKYavKFLGKMFVFDARLFENTNI 252
Cdd:PRK00142 160 PWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGL--LWDGKLYVFDERMAVPIND 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 504119882 253 N-IVSYCHQCKINQSYlHKNCARKKCNVLFLQCKICNEKFKEFCSSYC 299
Cdd:PRK00142 238 EvPIGHCHQCGTPCDR-YVNCANPACNLLILQCEECEEKYLGCCSEEC 284
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
124-222 |
7.32e-36 |
|
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: 124.61 E-value: 7.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 124 GKCISVKQFNTMSNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRNQLTNMTRALKNYQHKKIVLYCTGGIRCEKASAW 203
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90
....*....|....*....
gi 504119882 204 LIQNNFEHVFFLKGGIINY 222
Cdd:cd01518 81 LKERGFKNVYQLKGGILKY 99
|
|
| PRK01415 |
PRK01415 |
hypothetical protein; Validated |
14-245 |
3.37e-29 |
|
hypothetical protein; Validated
Pssm-ID: 167229 [Multi-domain] Cd Length: 247 Bit Score: 111.57 E-value: 3.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 14 EKKTI-SFYRYFHIQNPKKL--QLILLNKLKELKilGRIYIAQEGINAQIYIYKKYIYILKNFLYEL-NPIFKNVKFNFS 89
Cdd:PRK01415 3 EKIAIlSAYSFVNIEEPANLipKLLLIGKRKYVR--GTILLANEGFNGSFSGSYENVNLVLEELIKLtGPKDVNVKINYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 90 tDDHSisFYKLQVKVRPHIVNDGIKNFKFNVEKlGKCISVKQFNTMSNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFR 169
Cdd:PRK01415 81 -DVHP--FQKLKVRLKKEIVAMNVDDLNVDLFK-GEYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504119882 170 NQLTNMTRALKNYQHKKIVLYCTGGIRCEKASAWLIQNNFEHVFFLKGGIINYINYMRKKKYAvkFLGKMFVFDAR 245
Cdd:PRK01415 157 QFPAWVQQNQELLKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQNKNNL--WQGECFVFDDR 230
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
125-219 |
2.08e-21 |
|
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: 86.95 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 125 KCISVKQFNTMSNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRNQLTNMTRalknyqHKKIVLYCTGGIRCEKASAWL 204
Cdd:COG0607 4 KEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPK------DKPIVVYCASGGRSAQAAALL 77
|
90
....*....|....*
gi 504119882 205 IQNNFEHVFFLKGGI 219
Cdd:COG0607 78 RRAGYTNVYNLAGGI 92
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
131-219 |
7.53e-21 |
|
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: 84.66 E-value: 7.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 131 QFNTMSNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRNQLtnmtRALKNYQHKKIVLYCTGGIRCEKASAWLIQNNFE 210
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERA----ALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGT 76
|
....*....
gi 504119882 211 HVFFLKGGI 219
Cdd:cd00158 77 NVYNLEGGM 85
|
|
| PRK05320 |
PRK05320 |
rhodanese superfamily protein; Provisional |
18-245 |
4.61e-20 |
|
rhodanese superfamily protein; Provisional
Pssm-ID: 235405 [Multi-domain] Cd Length: 257 Bit Score: 87.39 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 18 ISFYRYFHIQNPKKLQLILLNKLKELKILGRIYIAQEGINaqiYIYKKYIYILKNFLYEL--NPIFKNVKFNFSTDDHSi 95
Cdd:PRK05320 6 IAAYKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGIN---LFLAGTREAIDAFYAWLraDARFADLQVKESLSDSQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 96 SFYKLQVKVRPHIVN---DGIKnfkfnvEKLGKCISVKQfNTMS---------NSKNCLIVDVRNNYEYEIGHFENSIHV 163
Cdd:PRK05320 82 PFRRMLVKLKREIITmkrPAIR------PELGRAPSVDA-ATLKrwldqghddAGRPVVMLDTRNAFEVDVGTFDGALDY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 164 PAQTFrnqlTNMTRALKNYQH----KKIVLYCTGGIRCEKASAWLIQNNFEHVFFLKGGIINYINYMRKKKYAvkflGKM 239
Cdd:PRK05320 155 RIDKF----TEFPEALAAHRAdlagKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFEEVGGAHYD----GDC 226
|
....*.
gi 504119882 240 FVFDAR 245
Cdd:PRK05320 227 FVFDYR 232
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
137-222 |
5.48e-20 |
|
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: 82.89 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 137 NSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFR--------NQLTNMTRALKNYQHKKIVLYCTGGIRCEKASAWLIQNN 208
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLdrrgeldiLEFEELLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90
....*....|....
gi 504119882 209 FEHVFFLKGGIINY 222
Cdd:smart00450 81 FKNVYLLDGGYKEW 94
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
16-108 |
9.25e-20 |
|
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: 82.16 E-value: 9.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 16 KTISFYRYFHIQNPKKLQLILLNKLKELKILGRIYIAQEGINAQIYIYKKYIYILKNFLyELNPIFKNVKFNFSTDDhSI 95
Cdd:pfam17773 2 VVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFL-RADPGFADLDFKESYSD-EH 79
|
90
....*....|...
gi 504119882 96 SFYKLQVKVRPHI 108
Cdd:pfam17773 80 PFRRLKVKLKKEI 92
|
|
| Rhodanese_C |
pfam12368 |
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ... |
237-299 |
2.47e-15 |
|
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: 69.27 E-value: 2.47e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504119882 237 GKMFVFDARL--FENTNINIVSYCHQCKiNQSYLHKNCARKKCNVLFLQCKICNEKFKEFCSSYC 299
Cdd:pfam12368 2 GKLFVFDERLavVEPSDDDVIGKCYHCG-KPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEEC 65
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
137-219 |
3.00e-15 |
|
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: 69.82 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 137 NSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFR----NQLTNMTRALKNYQHKKIVLYCTGGIRCEKASAWLIQNNFEHV 212
Cdd:pfam00581 2 EDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSlpplPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKNV 81
|
....*..
gi 504119882 213 FFLKGGI 219
Cdd:pfam00581 82 YVLDGGF 88
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
127-219 |
1.01e-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: 54.71 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 127 ISVKQFNTMSNSKN---CLIvDVRNNYEYEIGHFENSIHVPA---QTFRNQLTNMTRalknyqHKKIVLYCTGGIRCEKA 200
Cdd:cd01528 2 ISVAELAEWLADEReepVLI-DVREPEELEIAFLPGFLHLPMseiPERSKELDSDNP------DKDIVVLCHHGGRSMQV 74
|
90
....*....|....*....
gi 504119882 201 SAWLIQNNFEHVFFLKGGI 219
Cdd:cd01528 75 AQWLLRQGFENVYNLQGGI 93
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
142-222 |
7.76e-09 |
|
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: 51.88 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 142 LIVDVRNNYEYEIGHFENSIHVPAQTFRNQLTNMTRalknyqHKKIVLYCTGGIRCEKASAWLIQNNFEhVFFLKGGIIN 221
Cdd:cd01524 15 TLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPK------DKEIIVYCAVGLRGYIAARILTQNGFK-VKNLDGGYKT 87
|
.
gi 504119882 222 Y 222
Cdd:cd01524 88 Y 88
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
124-226 |
2.70e-08 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 54.33 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 124 GKCISVKQFNTMSNS-KNCLIVDVRNNYEYEIGHFENSIHVPAQTFrnqltNMTRALKNY-QHKKIVLYCTGGIRCEKAS 201
Cdd:PRK07878 286 GSTITPRELKEWLDSgKKIALIDVREPVEWDIVHIPGAQLIPKSEI-----LSGEALAKLpQDRTIVLYCKTGVRSAEAL 360
|
90 100
....*....|....*....|....*
gi 504119882 202 AWLIQNNFEHVFFLKGGIINYINYM 226
Cdd:PRK07878 361 AALKKAGFSDAVHLQGGVVAWAKQV 385
|
|
| Cdc25_Acr2p |
cd01443 |
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ... |
142-219 |
6.34e-08 |
|
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included in this CD are eukaryotic arsenate resistance proteins such as Saccharomyces cerevisiae Acr2p and similar proteins. Cdc25 phosphatases activate the cell division kinases throughout the cell cycle progression. Cdc25 phosphatases dephosphorylate phosphotyrosine and phosphothreonine residues, in order to activate their Cdk/cyclin substrates. The Cdc25 and Acr2p RHOD domains have the signature motif (H/YCxxxxxR).
Pssm-ID: 238720 [Multi-domain] Cd Length: 113 Bit Score: 50.10 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 142 LIVDVRNNyEYEIGHFENSIHVPAQTFRNQLTNMTRALKNYQHKKIVLYCTGG-IRCEKASAWL-------IQNNFEhVF 213
Cdd:cd01443 25 VVVDLRRD-DYEGGHIKGSINLPAQSCYQTLPQVYALFSLAGVKLAIFYCGSSqGRGPRAARWFadylrkvGESLPK-SY 102
|
....*.
gi 504119882 214 FLKGGI 219
Cdd:cd01443 103 ILTGGI 108
|
|
| 4RHOD_Repeats |
cd01529 |
Member of the Rhodanese Homology Domain superfamily. This CD includes putative ... |
143-224 |
6.35e-07 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. Only the second and most of the fourth repeats contain the putative catalytic Cys residue. This CD aligns the 1st , 2nd, 3rd, and 4th repeats.
Pssm-ID: 238787 [Multi-domain] Cd Length: 96 Bit Score: 46.90 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 143 IVDVRNNYEYEIGHFENSIHVPAQTF--RNQLTNMTRALKnyQHKKIVLYCTGGIRCEKASAWLIQNNFEHVFFLKGGII 220
Cdd:cd01529 15 LLDVRAEDEYAAGHLPGKRSIPGAALvlRSQELQALEAPG--RATRYVLTCDGSLLARFAAQELLALGGKPVALLDGGTS 92
|
....
gi 504119882 221 NYIN 224
Cdd:cd01529 93 AWVA 96
|
|
| Acr2p |
cd01531 |
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ... |
135-218 |
7.60e-07 |
|
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain superfamily. Included in this CD is the Saccharomyces cerevisiae arsenate reductase protein, Acr2p, and other yeast and plant homologs.
Pssm-ID: 238789 [Multi-domain] Cd Length: 113 Bit Score: 47.02 E-value: 7.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 135 MSNSKNCLIVDVRNnYEYEIGHFENSIHVPAQTFRNQLTNMTRALKNYQHKKIVLYCTGG-IRCEKASAWLI-------- 205
Cdd:cd01531 14 RNGRPPFQVVDVRD-EDYAGGHIKGSWHYPSTRFKAQLNQLVQLLSGSKKDTVVFHCALSqVRGPSAARKFLryldeedl 92
|
90
....*....|....
gi 504119882 206 -QNNFEhVFFLKGG 218
Cdd:cd01531 93 eTSKFE-VYVLHGG 105
|
|
| RHOD_ThiF |
cd01526 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ... |
127-224 |
9.72e-07 |
|
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: 46.92 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 127 ISVKQF-NTMSNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRNQLTNMTRALK----NYQHKKIVLYCTGGIRCEKAS 201
Cdd:cd01526 10 VSVKDYkNILQAGKKHVLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKSLQElpldNDKDSPIYVVCRRGNDSQTAV 89
|
90 100
....*....|....*....|....
gi 504119882 202 AWLIQNNFEH-VFFLKGGIINYIN 224
Cdd:cd01526 90 RKLKELGLERfVRDIIGGLKAWAD 113
|
|
| glpE |
PRK00162 |
thiosulfate sulfurtransferase GlpE; |
125-218 |
1.48e-06 |
|
thiosulfate sulfurtransferase GlpE;
Pssm-ID: 178908 [Multi-domain] Cd Length: 108 Bit Score: 46.17 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 125 KCISVKQFNTMSNSKNCLIVDVRNNYEYEIGHFENSIHvpaqtfrnqLTNMTRALKNYQH---KKIVLYCTGGIRCEKAS 201
Cdd:PRK00162 5 ECINVEQAHQKLQEGGAVLVDIRDPQSFAMGHAPGAFH---------LTNDSLGAFMRQAdfdTPVMVMCYHGNSSQGAA 75
|
90
....*....|....*..
gi 504119882 202 AWLIQNNFEHVFFLKGG 218
Cdd:PRK00162 76 QYLLQQGFDVVYSIDGG 92
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
136-212 |
2.98e-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: 45.34 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 136 SNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRNQLTNMTRALKN-YQHKK------IVLYCTGGIRCEKASAWLIQNN 208
Cdd:cd01519 11 NPHPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALALSEEEFEKkYGFPKpskdkeLIFYCKAGVRSKAAAELARSLG 90
|
....
gi 504119882 209 FEHV 212
Cdd:cd01519 91 YENV 94
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
126-219 |
3.99e-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: 41.86 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 126 CISVKQFNTMSNS-KNCLIVDVRNN--YEYEIGHFENSIHVpaqTFRNQLTNMTRALKnyqHKKIVLYCTGGIRCEKASA 202
Cdd:cd01444 1 RISVDELAELLAAgEAPVLLDVRDPasYAALPDHIPGAIHL---DEDSLDDWLGDLDR---DRPVVVYCYHGNSSAQLAQ 74
|
90
....*....|....*..
gi 504119882 203 WLIQNNFEHVFFLKGGI 219
Cdd:cd01444 75 ALREAGFTDVRSLAGGF 91
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
142-219 |
4.01e-05 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 44.62 E-value: 4.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504119882 142 LIVDVRNNYEYEIGHFENSIHVPaqtfRNQLTNMTRALKNYQHKKIVLYCTGGIRCEKASAWLIQNNFEHVFFLKGGI 219
Cdd:PRK08762 19 VLIDVREAHERASGQAEGALRIP----RGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRELGYTRVASVAGGF 92
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
143-219 |
1.55e-04 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 42.94 E-value: 1.55e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504119882 143 IVDVRNNYEYEIGHFENSIHVPAQTFRNQLtNMTRALKNyqhKKIVLYCTGGIRCEKASAWLIQNNFEHVFFLKGGI 219
Cdd:PRK05597 277 LIDVREPSEFAAYSIPGAHNVPLSAIREGA-NPPSVSAG---DEVVVYCAAGVRSAQAVAILERAGYTGMSSLDGGI 349
|
|
| 4RHOD_Repeat_3 |
cd01534 |
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative ... |
145-218 |
3.63e-04 |
|
Member of the Rhodanese Homology Domain superfamily, repeat 3. This CD includes putative rhodanese-related sulfurtransferases which contain 4 copies of the Rhodanese Homology Domain. This CD aligns the 3rd repeat which does not contain the putative catalytic Cys residue.
Pssm-ID: 238792 [Multi-domain] Cd Length: 95 Bit Score: 38.99 E-value: 3.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504119882 145 DVRNNYEYEIGHFENSIHVPAqtfrNQLTNMTRALKNYQHKKIVLYCTGGIRCEKASAWLIQNNFEhVFFLKGG 218
Cdd:cd01534 21 DVRTPEEYEAGHLPGFRHTPG----GQLVQETDHFAPVRGARIVLADDDGVRADMTASWLAQMGWE-VYVLEGG 89
|
|
| RHOD_Kc |
cd01525 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the ... |
142-219 |
1.03e-03 |
|
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the rhodanese-like domains found C-terminal of the serine/threonine protein kinases catalytic (S_TKc) domain and the Tre-2, BUB2p, Cdc16p (TBC) domain. The putative active site Cys residue is not present in this CD.
Pssm-ID: 238783 [Multi-domain] Cd Length: 105 Bit Score: 37.82 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 142 LIVDVRNNYEYEIGHFENSIHVP---AQTFRNQLT--NMTRALKNYQHKKIVlyCTGGIRCEKA--SAWLIQNNFEHVFF 214
Cdd:cd01525 18 AAVDIRSSPDFRRGHIEGSINIPfssVFLKEGELEqlPTVPRLENYKGKIIV--IVSHSHKHAAlfAAFLVKCGVPRVCI 95
|
....*
gi 504119882 215 LKGGI 219
Cdd:cd01525 96 LDGGI 100
|
|
| PRK07411 |
PRK07411 |
molybdopterin-synthase adenylyltransferase MoeB; |
127-219 |
3.88e-03 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 38.56 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504119882 127 ISVKQFNTM--SNSKNCLIVDVRNNYEYEIGHFENSIHVPAQTFRN--QLTNMTRALKNYqhkKIVLYCTGGIRCEKASA 202
Cdd:PRK07411 284 MTVTELKALldSGADDFVLIDVRNPNEYEIARIPGSVLVPLPDIENgpGVEKVKELLNGH---RLIAHCKMGGRSAKALG 360
|
90
....*....|....*..
gi 504119882 203 WLIQNNFEHVfFLKGGI 219
Cdd:PRK07411 361 ILKEAGIEGT-NVKGGI 376
|
|
| |
