|
Name |
Accession |
Description |
Interval |
E-value |
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
16-308 |
5.19e-164 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 458.07 E-value: 5.19e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 16 TTTWVVAALYQFKEVADPADLQQRLLDLVNSINLCGTLIVAGEGINGTVAGDRAAIDQVHQFL-LDEGFTAMEYKESHSS 94
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLrADPRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 95 EKPFRKMKIKLKKEIVTLGVE-VKPRDLVGHYLDPKEWNELIARDDVILIDTRNDYEYKAGTFKGAIDPKTETFREFPEY 173
Cdd:COG1054 81 GHPFPRLKVKLKKEIVTMGLPdVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 174 VKQNLEQHKDKKIAMFCTGGIRCEKSTSLLLQEGFTEVYHLKGGVLKYLEETPADESLWEGECFVFDGRTAVTHGMQEGQ 253
Cdd:COG1054 161 VEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNLEPGV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491113778 254 NTKCHACGWPLLPEE--VELPSYEHGVSCVYCIDK-------TSEKQKEGFrMRQSQIAAAKRK 308
Cdd:COG1054 241 IGLCHACGTPCDRYVncANDPCYELGVSCPHCADKyeccsdeCTEEQRARY-ERQRQLRLAKER 303
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
20-306 |
1.76e-123 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 356.08 E-value: 1.76e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 20 VVAALYQFKEVADPADLQQRLLDLVNSINLCGTLIVAGEGINGTVAGDRAAIDQVHQFLL-DEGFTAMEYKESHSSEKPF 98
Cdd:PRK00142 5 RVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKaDPRFADIRFKISEDDGHAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 99 RKMKIKLKKEIVTLGVEVK--PRDLVGHYLDPKEWNELIARDDVILIDTRNDYEYKAGTFKGAIDPKTETFREFPEYVKQ 176
Cdd:PRK00142 85 PRLSVKVRKEIVALGLDDDidPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPPWVEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 177 NLEQHKDKKIAMFCTGGIRCEKSTSLLLQEGFTEVYHLKGGVLKYLEETPADESLWEGECFVFDGRTAVTHGMQEGQNtK 256
Cdd:PRK00142 165 NLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVPINDEVPIG-H 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113778 257 CHACGWP---------------LLPEEVELPSYEHGVSCVYCIDKTSEKQKEGFRMRQSQIAAAK 306
Cdd:PRK00142 244 CHQCGTPcdryvncanpacnllILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLI 308
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
123-223 |
6.64e-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: 6.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 123 GHYLDPKEWNELIARDDVILIDTRNDYEYKAGTFKGAIDPKTETFREFPEYVKQNLEQHKDKKIAMFCTGGIRCEKSTSL 202
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 491113778 203 LLQEGFTEVYHLKGGVLKYLE 223
Cdd:cd01518 81 LKERGFKNVYQLKGGILKYLE 101
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
19-109 |
2.28e-37 |
|
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family proteins. It adopts a fold similar to the pfam00708 family.
Pssm-ID: 465497 [Multi-domain] Cd Length: 92 Bit Score: 128.38 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 19 WVVAALYQFKEVADPADLQQRLLDLVNSINLCGTLIVAGEGINGTVAGDRAAIDQVHQFL-LDEGFTAMEYKESHSSEKP 97
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLrADPGFADLDFKESYSDEHP 80
|
90
....*....|..
gi 491113778 98 FRKMKIKLKKEI 109
Cdd:pfam17773 81 FRRLKVKLKKEI 92
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
137-227 |
1.14e-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: 76.73 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 137 RDDVILIDTRNDYEYKAGTFKGAIDPKTETFREFPEYVK--------QNLEQHKDKKIAMFCTGGIRCEKSTSLLLQEGF 208
Cdd:smart00450 2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81
|
90
....*....|....*....
gi 491113778 209 TEVYHLKGGVLKYLEETPA 227
Cdd:smart00450 82 KNVYLLDGGYKEWSAAGPP 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
16-308 |
5.19e-164 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 458.07 E-value: 5.19e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 16 TTTWVVAALYQFKEVADPADLQQRLLDLVNSINLCGTLIVAGEGINGTVAGDRAAIDQVHQFL-LDEGFTAMEYKESHSS 94
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLrADPRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 95 EKPFRKMKIKLKKEIVTLGVE-VKPRDLVGHYLDPKEWNELIARDDVILIDTRNDYEYKAGTFKGAIDPKTETFREFPEY 173
Cdd:COG1054 81 GHPFPRLKVKLKKEIVTMGLPdVDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 174 VKQNLEQHKDKKIAMFCTGGIRCEKSTSLLLQEGFTEVYHLKGGVLKYLEETPADESLWEGECFVFDGRTAVTHGMQEGQ 253
Cdd:COG1054 161 VEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNLEPGV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491113778 254 NTKCHACGWPLLPEE--VELPSYEHGVSCVYCIDK-------TSEKQKEGFrMRQSQIAAAKRK 308
Cdd:COG1054 241 IGLCHACGTPCDRYVncANDPCYELGVSCPHCADKyeccsdeCTEEQRARY-ERQRQLRLAKER 303
|
|
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
20-306 |
1.76e-123 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 356.08 E-value: 1.76e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 20 VVAALYQFKEVADPADLQQRLLDLVNSINLCGTLIVAGEGINGTVAGDRAAIDQVHQFLL-DEGFTAMEYKESHSSEKPF 98
Cdd:PRK00142 5 RVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKaDPRFADIRFKISEDDGHAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 99 RKMKIKLKKEIVTLGVEVK--PRDLVGHYLDPKEWNELIARDDVILIDTRNDYEYKAGTFKGAIDPKTETFREFPEYVKQ 176
Cdd:PRK00142 85 PRLSVKVRKEIVALGLDDDidPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPPWVEE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 177 NLEQHKDKKIAMFCTGGIRCEKSTSLLLQEGFTEVYHLKGGVLKYLEETPADESLWEGECFVFDGRTAVTHGMQEGQNtK 256
Cdd:PRK00142 165 NLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVPINDEVPIG-H 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491113778 257 CHACGWP---------------LLPEEVELPSYEHGVSCVYCIDKTSEKQKEGFRMRQSQIAAAK 306
Cdd:PRK00142 244 CHQCGTPcdryvncanpacnllILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLI 308
|
|
| PRK01415 |
PRK01415 |
hypothetical protein; Validated |
25-246 |
5.43e-81 |
|
hypothetical protein; Validated
Pssm-ID: 167229 [Multi-domain] Cd Length: 247 Bit Score: 245.62 E-value: 5.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 25 YQFKEVADPADLQQRLLDLVNSINLCGTLIVAGEGINGTVAGDRAAIDQVHQFLLD-EGFTAMEYKESHSSEKPFRKMKI 103
Cdd:PRK01415 11 YSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKlTGPKDVNVKINYSDVHPFQKLKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 104 KLKKEIVTLGVEVKPRDLV-GHYLDPKEWNELIARDDVILIDTRNDYEYKAGTFKGAIDPKTETFREFPEYVKQNLEQHK 182
Cdd:PRK01415 91 RLKKEIVAMNVDDLNVDLFkGEYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFKQFPAWVQQNQELLK 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491113778 183 DKKIAMFCTGGIRCEKSTSLLLQEGFTEVYHLKGGVLKYLEETPADESLWEGECFVFDGRTAVT 246
Cdd:PRK01415 171 GKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQNKNNLWQGECFVFDDRRAVT 234
|
|
| PRK05320 |
PRK05320 |
rhodanese superfamily protein; Provisional |
23-267 |
2.61e-66 |
|
rhodanese superfamily protein; Provisional
Pssm-ID: 235405 [Multi-domain] Cd Length: 257 Bit Score: 208.34 E-value: 2.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 23 ALYQFKEVADPADLQQRLLDLVNSINLCGTLIVAGEGINGTVAGDRAAIDQVHQFL-LDEGFTAMEYKESHSSEKPFRKM 101
Cdd:PRK05320 7 AAYKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLrADARFADLQVKESLSDSQPFRRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 102 KIKLKKEIVTLGVE-VKPRDLVGHYLDP---KEWNELiARDD----VILIDTRNDYEYKAGTFKGAIDPKTETFREFPEY 173
Cdd:PRK05320 87 LVKLKREIITMKRPaIRPELGRAPSVDAatlKRWLDQ-GHDDagrpVVMLDTRNAFEVDVGTFDGALDYRIDKFTEFPEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 174 VKQNLEQHKDKKIAMFCTGGIRCEKSTSLLLQEGFTEVYHLKGGVLKYLEETPADEslWEGECFVFDGRTAVTHGMQEGQ 253
Cdd:PRK05320 166 LAAHRADLAGKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFEEVGGAH--YDGDCFVFDYRTALDPQLAPLV 243
|
250
....*....|....
gi 491113778 254 NTKCHACGWPLLPE 267
Cdd:PRK05320 244 DVTCFACRAVVTPE 257
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
123-223 |
6.64e-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: 6.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 123 GHYLDPKEWNELIARDDVILIDTRNDYEYKAGTFKGAIDPKTETFREFPEYVKQNLEQHKDKKIAMFCTGGIRCEKSTSL 202
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 491113778 203 LLQEGFTEVYHLKGGVLKYLE 223
Cdd:cd01518 81 LKERGFKNVYQLKGGILKYLE 101
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
19-109 |
2.28e-37 |
|
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family proteins. It adopts a fold similar to the pfam00708 family.
Pssm-ID: 465497 [Multi-domain] Cd Length: 92 Bit Score: 128.38 E-value: 2.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 19 WVVAALYQFKEVADPADLQQRLLDLVNSINLCGTLIVAGEGINGTVAGDRAAIDQVHQFL-LDEGFTAMEYKESHSSEKP 97
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLrADPGFADLDFKESYSDEHP 80
|
90
....*....|..
gi 491113778 98 FRKMKIKLKKEI 109
Cdd:pfam17773 81 FRRLKVKLKKEI 92
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
137-227 |
1.14e-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: 76.73 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 137 RDDVILIDTRNDYEYKAGTFKGAIDPKTETFREFPEYVK--------QNLEQHKDKKIAMFCTGGIRCEKSTSLLLQEGF 208
Cdd:smart00450 2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDilefeellKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELGF 81
|
90
....*....|....*....
gi 491113778 209 TEVYHLKGGVLKYLEETPA 227
Cdd:smart00450 82 KNVYLLDGGYKEWSAAGPP 100
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
126-224 |
2.10e-16 |
|
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440372 [Multi-domain] Cd Length: 106 Bit Score: 73.46 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 126 LDPKEWNELIARDDVILIDTRNDYEYKAGTFKGA--IDpktetFREFPEYVKqnlEQHKDKKIAMFCTGGIRCEKSTSLL 203
Cdd:COG0607 6 ISPAELAELLESEDAVLLDVREPEEFAAGHIPGAinIP-----LGELAERLD---ELPKDKPIVVYCASGGRSAQAAALL 77
|
90 100
....*....|....*....|.
gi 491113778 204 LQEGFTEVYHLKGGVLKYLEE 224
Cdd:COG0607 78 RRAGYTNVYNLAGGIEAWKAA 98
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
133-221 |
3.35e-15 |
|
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: 69.64 E-value: 3.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 133 ELIARDDVILIDTRNDYEYKAGTFKGAID-PKTETFREFPEyvkqnLEQHKDKKIAMFCTGGIRCEKSTSLLLQEGFTEV 211
Cdd:cd00158 4 ELLDDEDAVLLDVREPEEYAAGHIPGAINiPLSELEERAAL-----LELDKDKPIVVYCRSGNRSARAAKLLRKAGGTNV 78
|
90
....*....|
gi 491113778 212 YHLKGGVLKY 221
Cdd:cd00158 79 YNLEGGMLAW 88
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
135-221 |
1.13e-14 |
|
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.
Pssm-ID: 425764 [Multi-domain] Cd Length: 92 Bit Score: 68.28 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 135 IARDDVILIDTRNDYEYKAGTFKGAI----DPKTETFREFPEYVKQNLEQHKDKKIAMFCTGGIRCEKSTSLLLQEGFTE 210
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAKGHIPGAVnvplSSLSLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80
|
90
....*....|.
gi 491113778 211 VYHLKGGVLKY 221
Cdd:pfam00581 81 VYVLDGGFEAW 91
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
129-221 |
8.08e-11 |
|
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: 57.66 E-value: 8.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 129 KEWNELIAR--DDVILIDTRNDYEYKAGTFKGAIDPKTETFREfpeyvKQNlEQHKDKKIAMFCTGGIRCEKSTSLLLQE 206
Cdd:cd01524 1 VQWHELDNYraDGVTLIDVRTPQEFEKGHIKGAINIPLDELRD-----RLN-ELPKDKEIIVYCAVGLRGYIAARILTQN 74
|
90
....*....|....*
gi 491113778 207 GFtEVYHLKGGVLKY 221
Cdd:cd01524 75 GF-KVKNLDGGYKTY 88
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
126-218 |
3.46e-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: 53.55 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 126 LDPKEWNELIA--RDDVILIDTRNDYEYKAGTFKGAID-PktetFREFPEYVKQNLEQHKDKKIAMFCTGGIRCEKSTSL 202
Cdd:cd01528 2 ISVAELAEWLAdeREEPVLIDVREPEELEIAFLPGFLHlP----MSEIPERSKELDSDNPDKDIVVLCHHGGRSMQVAQW 77
|
90
....*....|....*.
gi 491113778 203 LLQEGFTEVYHLKGGV 218
Cdd:cd01528 78 LLRQGFENVYNLQGGI 93
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
126-224 |
3.64e-08 |
|
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: 50.50 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 126 LDPKEWNELIARDDVILIDTRNDYEYKA-GTFKGAIDP---KTEtFREFPE--YVKQNLEQhkDKKIAMFCTGGIRCEKS 199
Cdd:cd01447 1 LSPEDARALLGSPGVLLVDVRDPRELERtGMIPGAFHAprgMLE-FWADPDspYHKPAFAE--DKPFVFYCASGWRSALA 77
|
90 100
....*....|....*....|....*
gi 491113778 200 TSLLLQEGFTEVYHLKGGVLKYLEE 224
Cdd:cd01447 78 GKTLQDMGLKPVYNIEGGFKDWKEA 102
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|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
138-223 |
1.10e-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: 43.41 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 138 DDVILIDTRNDYEYKAGTFKGAID-PktetFREFPEYVK---QNLEQH-------KDKKIAMFCTGGIRCEKSTSLLLQE 206
Cdd:cd01519 14 PNKVLIDVREPEELKTGKIPGAINiP----LSSLPDALAlseEEFEKKygfpkpsKDKELIFYCKAGVRSKAAAELARSL 89
|
90
....*....|....*..
gi 491113778 207 GFTEVYHLKGGVLKYLE 223
Cdd:cd01519 90 GYENVGNYPGSWLDWAA 106
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| Cdc25_Acr2p |
cd01443 |
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ... |
125-217 |
1.66e-05 |
|
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: 43.16 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 125 YLDPKEWNELI------ARDDVILIDTRNDyEYKAGTFKGAIDPKTETFREFPEYVKQNLEQHKDKKIAMFCTG----GI 194
Cdd:cd01443 3 YISPEELVALLensdsnAGKDFVVVDLRRD-DYEGGHIKGSINLPAQSCYQTLPQVYALFSLAGVKLAIFYCGSsqgrGP 81
|
90 100
....*....|....*....|....*.
gi 491113778 195 RCEKSTSLLLQE---GFTEVYHLKGG 217
Cdd:cd01443 82 RAARWFADYLRKvgeSLPKSYILTGG 107
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|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
122-219 |
2.23e-05 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 45.47 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 122 VGHYLDPKEWNELI-ARDDVILIDTRNDYEYKAGTFKGA-IDPKT-----ETFREFPEyvkqnleqhkDKKIAMFCTGGI 194
Cdd:PRK07878 285 AGSTITPRELKEWLdSGKKIALIDVREPVEWDIVHIPGAqLIPKSeilsgEALAKLPQ----------DRTIVLYCKTGV 354
|
90 100
....*....|....*....|....*
gi 491113778 195 RCEKSTSLLLQEGFTEVYHLKGGVL 219
Cdd:PRK07878 355 RSAEALAALKKAGFSDAVHLQGGVV 379
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| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
124-217 |
5.98e-05 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 44.23 E-value: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 124 HYLDPKEWNELiARDDVILIDTRNDYEYKAGTFKGAID-PKTetfrefpeYVKQNLEQH---KDKKIAMFCTGGIRCEKS 199
Cdd:PRK08762 3 REISPAEARAR-AAQGAVLIDVREAHERASGQAEGALRiPRG--------FLELRIETHlpdRDREIVLICASGTRSAHA 73
|
90
....*....|....*...
gi 491113778 200 TSLLLQEGFTEVYHLKGG 217
Cdd:PRK08762 74 AATLRELGYTRVASVAGG 91
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|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
133-217 |
2.89e-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: 39.17 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 133 ELIARD-DVILIDTR--NDYEYKAGTFKGAIdpkTETFREFPEYVKQNleqHKDKKIAMFCTGGIRCEKSTSLLLQEGFT 209
Cdd:cd01444 9 ELLAAGeAPVLLDVRdpASYAALPDHIPGAI---HLDEDSLDDWLGDL---DRDRPVVVYCYHGNSSAQLAQALREAGFT 82
|
....*...
gi 491113778 210 EVYHLKGG 217
Cdd:cd01444 83 DVRSLAGG 90
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
123-223 |
6.72e-04 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 41.01 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491113778 123 GHYLDPKEWNELIarDDVILIDTRNDYEYKAGTFKGAIDPKTETFREfpEYVKQNLEqhKDKKIAMFCTGGIRCEKSTSL 202
Cdd:PRK05597 260 GEVLDVPRVSALP--DGVTLIDVREPSEFAAYSIPGAHNVPLSAIRE--GANPPSVS--AGDEVVVYCAAGVRSAQAVAI 333
|
90 100
....*....|....*....|.
gi 491113778 203 LLQEGFTEVYHLKGGVLKYLE 223
Cdd:PRK05597 334 LERAGYTGMSSLDGGIEGWLD 354
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|
| Rhodanese_C |
pfam12368 |
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ... |
233-261 |
6.02e-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: 34.60 E-value: 6.02e-03
10 20
....*....|....*....|....*....
gi 491113778 233 EGECFVFDGRTAVTHGMQEGQNTKCHACG 261
Cdd:pfam12368 1 KGKLFVFDERLAVVEPSDDDVIGKCYHCG 29
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