|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
21-337 |
0e+00 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 520.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 21 TEPRTTISFYKYFTIVDPQATRDALWVALTQLKVFGRIYLAREGINAQISVPQSNVEALREFLYGfDPALAGLRFNIAvE 100
Cdd:PRK00142 1 MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKA-DPRFADIRFKIS-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 101 DDGKSFWVLRLKVRDRIVADGIDDPSFDASNVGEYLKAAEVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFRDQ 180
Cdd:PRK00142 79 DDGHAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 181 LPKAVEMMQDHKDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARRAREQGLpvRFIGKNFVFDERMGERIS 260
Cdd:PRK00142 159 PPWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGL--LWDGKLYVFDERMAVPIN 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488988211 261 N-DVIAHCHQCGAPCDTHTNCLNDGCHLLFIQCPSCAEKFAGCCSEACMEEHKLPEEEQRKLRAGRENGNKIFNKSRG 337
Cdd:PRK00142 237 DeVPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
|
|
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
21-327 |
4.41e-163 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 457.68 E-value: 4.41e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 21 TEPRTTISFYKYFTIVDPQATRDALWVALTQLKVFGRIYLAREGINAQISVPQSNVEALREFLYGfDPALAGLRFNIAvE 100
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRA-DPRFADLEFKES-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 101 DDGKSFWVLRLKVRDRIVADGIDDpsFDAS-NVGEYLKAAEVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFRD 179
Cdd:COG1054 79 ADGHPFPRLKVKLKKEIVTMGLPD--VDPNeGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 180 QLPKAVEMMQDHKDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARRAREQGlpVRFIGKNFVFDERMGERI 259
Cdd:COG1054 157 FPEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEG--SLWEGECFVFDERVAVDH 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 260 SN--DVIAHCHQCGAPCDTHTNCLNDGCHLLFIQCPSCAEKFAgCCSEACMEEHKLPEEEQRKLRAGREN 327
Cdd:COG1054 235 NLepGVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADKYE-CCSDECTEEQRARYERQRQLRLAKER 303
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
133-233 |
1.11e-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: 177.00 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 133 GEYLKAAEVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFRDQLPKAVEMMQDHKDKKIVMYCTGGIRCEKASAW 212
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 488988211 213 MKHNGFNKVWHIEGGIIEYAR 233
Cdd:cd01518 81 LKERGFKNVYQLKGGILKYLE 101
|
|
| Rhodanese_C |
pfam12368 |
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ... |
245-307 |
8.68e-31 |
|
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: 111.25 E-value: 8.68e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488988211 245 IGKNFVFDERM--GERISNDVIAHCHQCGAPCDTHTNCLNDGCHLLFIQCPSCAEKFAGCCSEAC 307
Cdd:pfam12368 1 KGKLFVFDERLavVEPSDDDVIGKCYHCGKPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEEC 65
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
146-237 |
8.92e-21 |
|
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: 85.97 E-value: 8.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 146 DDPDAVFIDMRNHYEYEVGHFENALEIPADTFRDQLPKAVEMMQD--------HKDKKIVMYCTGGIRCEKASAWMKHNG 217
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEellkrlglDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 488988211 218 FNKVWHIEGGIIEYARRARE 237
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGPP 100
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
21-337 |
0e+00 |
|
rhodanese-related sulfurtransferase;
Pssm-ID: 234663 [Multi-domain] Cd Length: 314 Bit Score: 520.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 21 TEPRTTISFYKYFTIVDPQATRDALWVALTQLKVFGRIYLAREGINAQISVPQSNVEALREFLYGfDPALAGLRFNIAvE 100
Cdd:PRK00142 1 MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKA-DPRFADIRFKIS-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 101 DDGKSFWVLRLKVRDRIVADGIDDPSFDASNVGEYLKAAEVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFRDQ 180
Cdd:PRK00142 79 DDGHAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 181 LPKAVEMMQDHKDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARRAREQGLpvRFIGKNFVFDERMGERIS 260
Cdd:PRK00142 159 PPWVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGL--LWDGKLYVFDERMAVPIN 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488988211 261 N-DVIAHCHQCGAPCDTHTNCLNDGCHLLFIQCPSCAEKFAGCCSEACMEEHKLPEEEQRKLRAGRENGNKIFNKSRG 337
Cdd:PRK00142 237 DeVPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKERH 314
|
|
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
21-327 |
4.41e-163 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 457.68 E-value: 4.41e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 21 TEPRTTISFYKYFTIVDPQATRDALWVALTQLKVFGRIYLAREGINAQISVPQSNVEALREFLYGfDPALAGLRFNIAvE 100
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRA-DPRFADLEFKES-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 101 DDGKSFWVLRLKVRDRIVADGIDDpsFDAS-NVGEYLKAAEVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFRD 179
Cdd:COG1054 79 ADGHPFPRLKVKLKKEIVTMGLPD--VDPNeGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFRE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 180 QLPKAVEMMQDHKDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARRAREQGlpVRFIGKNFVFDERMGERI 259
Cdd:COG1054 157 FPEWVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEG--SLWEGECFVFDERVAVDH 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 260 SN--DVIAHCHQCGAPCDTHTNCLNDGCHLLFIQCPSCAEKFAgCCSEACMEEHKLPEEEQRKLRAGREN 327
Cdd:COG1054 235 NLepGVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADKYE-CCSDECTEEQRARYERQRQLRLAKER 303
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
133-233 |
1.11e-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: 177.00 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 133 GEYLKAAEVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFRDQLPKAVEMMQDHKDKKIVMYCTGGIRCEKASAW 212
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 488988211 213 MKHNGFNKVWHIEGGIIEYAR 233
Cdd:cd01518 81 LKERGFKNVYQLKGGILKYLE 101
|
|
| PRK05320 |
PRK05320 |
rhodanese superfamily protein; Provisional |
27-254 |
1.12e-36 |
|
rhodanese superfamily protein; Provisional
Pssm-ID: 235405 [Multi-domain] Cd Length: 257 Bit Score: 132.84 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 27 ISFYKYFTIVDPQATRDALWVALTQLKVFGRIYLAREGINAQISVPQSNVEALREFLYGfDPALAGLRFNIAVEDDgKSF 106
Cdd:PRK05320 6 IAAYKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRA-DARFADLQVKESLSDS-QPF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 107 WVLRLKVRDRIVADGIDD--------PSFDASNVGEYLKAAEvnamlDDP--DAVFIDMRNHYEYEVGHFENALEIPADT 176
Cdd:PRK05320 84 RRMLVKLKREIITMKRPAirpelgraPSVDAATLKRWLDQGH-----DDAgrPVVMLDTRNAFEVDVGTFDGALDYRIDK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488988211 177 FrDQLPKAVEMMQDH-KDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARRAREQGlpvrFIGKNFVFDER 254
Cdd:PRK05320 159 F-TEFPEALAAHRADlAGKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFEEVGGAH----YDGDCFVFDYR 232
|
|
| PRK01415 |
PRK01415 |
hypothetical protein; Validated |
21-254 |
1.44e-33 |
|
hypothetical protein; Validated
Pssm-ID: 167229 [Multi-domain] Cd Length: 247 Bit Score: 124.67 E-value: 1.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 21 TEPRTTISFYKYFTIVDPQATRDALWVALTQLKVFGRIYLAREGINAQISVPQSNVE-ALREFLYGFDPALAGLRFNIAv 99
Cdd:PRK01415 2 NEKIAILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNlVLEELIKLTGPKDVNVKINYS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 100 edDGKSFWVLRLKVRDRIVADGIDDPSFDASNvGEYLKAAEVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFRd 179
Cdd:PRK01415 81 --DVHPFQKLKVRLKKEIVAMNVDDLNVDLFK-GEYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFK- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488988211 180 QLPKAVEMMQDH-KDKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARRAREQGlpVRFIGKNFVFDER 254
Cdd:PRK01415 157 QFPAWVQQNQELlKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQNKN--NLWQGECFVFDDR 230
|
|
| Rhodanese_C |
pfam12368 |
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ... |
245-307 |
8.68e-31 |
|
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: 111.25 E-value: 8.68e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488988211 245 IGKNFVFDERM--GERISNDVIAHCHQCGAPCDTHTNCLNDGCHLLFIQCPSCAEKFAGCCSEAC 307
Cdd:pfam12368 1 KGKLFVFDERLavVEPSDDDVIGKCYHCGKPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEEC 65
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
24-117 |
2.06e-29 |
|
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: 108.73 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 24 RTTISFYKYFTIVDPQATRDALWVALTQLKVFGRIYLAREGINAQISVPQSNVEALREFLYGfDPALAGLRFNIAVEDDg 103
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRA-DPGFADLDFKESYSDE- 78
|
90
....*....|....
gi 488988211 104 KSFWVLRLKVRDRI 117
Cdd:pfam17773 79 HPFRRLKVKLKKEI 92
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
134-242 |
7.76e-25 |
|
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: 96.96 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 134 EYLKAAEVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFRDQLPKAvemmqdHKDKKIVMYCTGGIRCEKASAWM 213
Cdd:COG0607 4 KEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDEL------PKDKPIVVYCASGGRSAQAAALL 77
|
90 100
....*....|....*....|....*....
gi 488988211 214 KHNGFNKVWHIEGGIIEYarraREQGLPV 242
Cdd:COG0607 78 RRAGYTNVYNLAGGIEAW----KAAGLPV 102
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
140-232 |
1.01e-22 |
|
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: 90.82 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 140 EVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADtfrdQLPKAVEMMQDHKDKKIVMYCTGGIRCEKASAWMKHNGFN 219
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLS----ELEERAALLELDKDKPIVVYCRSGNRSARAAKLLRKAGGT 76
|
90
....*....|...
gi 488988211 220 KVWHIEGGIIEYA 232
Cdd:cd00158 77 NVYNLEGGMLAWK 89
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
146-237 |
8.92e-21 |
|
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: 85.97 E-value: 8.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 146 DDPDAVFIDMRNHYEYEVGHFENALEIPADTFRDQLPKAVEMMQD--------HKDKKIVMYCTGGIRCEKASAWMKHNG 217
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEellkrlglDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90 100
....*....|....*....|
gi 488988211 218 FNKVWHIEGGIIEYARRARE 237
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAGPP 100
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
145-232 |
1.73e-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: 70.98 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 145 LDDPDAVFIDMRNHYEYEVGHFENALEIPADTFR----DQLPKAVEMMQDHKDKKIVMYCTGGIRCEKASAWMKHNGFNK 220
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSlpplPLLELLEKLLELLKDKPIVVYCNSGNRAAAAAALLKALGYKN 80
|
90
....*....|..
gi 488988211 221 VWHIEGGIIEYA 232
Cdd:pfam00581 81 VYVLDGGFEAWK 92
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
136-233 |
5.51e-13 |
|
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: 64.34 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 136 LKAAEVNAMLDDPDA--VFIDMRNHYEYEVGHFENALEIPADTFRDQLPkavEMMQDHKDKKIVMYCTGGIRCEKASAWM 213
Cdd:cd01528 2 ISVAELAEWLADEREepVLIDVREPEELEIAFLPGFLHLPMSEIPERSK---ELDSDNPDKDIVVLCHHGGRSMQVAQWL 78
|
90 100
....*....|....*....|
gi 488988211 214 KHNGFNKVWHIEGGIIEYAR 233
Cdd:cd01528 79 LRQGFENVYNLQGGIDAWSL 98
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
132-242 |
1.49e-10 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 62.03 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 132 VGEYLKAAEVNAMLDDPDAVF-IDMRNHYEYEVGHFENALEIPADTFR-----DQLPKavemmqdhkDKKIVMYCTGGIR 205
Cdd:PRK07878 285 AGSTITPRELKEWLDSGKKIAlIDVREPVEWDIVHIPGAQLIPKSEILsgealAKLPQ---------DRTIVLYCKTGVR 355
|
90 100 110
....*....|....*....|....*....|....*..
gi 488988211 206 CEKASAWMKHNGFNKVWHIEGGIIEYARRArEQGLPV 242
Cdd:PRK07878 356 SAEALAALKKAGFSDAVHLQGGVVAWAKQV-DPSLPM 391
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
140-231 |
8.73e-10 |
|
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: 54.96 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 140 EVNAMLDDpDAVFIDMRNHYEYEVGHFENALEIPADTFRD---QLPkavemmqdhKDKKIVMYCTGGIRCEKASAWMKHN 216
Cdd:cd01524 5 ELDNYRAD-GVTLIDVRTPQEFEKGHIKGAINIPLDELRDrlnELP---------KDKEIIVYCAVGLRGYIAARILTQN 74
|
90
....*....|....*
gi 488988211 217 GFnKVWHIEGGIIEY 231
Cdd:cd01524 75 GF-KVKNLDGGYKTY 88
|
|
| Cdc25_Acr2p |
cd01443 |
Cdc25 enzymes are members of the Rhodanese Homology Domain (RHOD) superfamily. Also included ... |
135-233 |
2.89e-09 |
|
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: 54.33 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 135 YLKAAEVNAMLDDP------DAVFIDMRNHyEYEVGHFENALEIPADTFRDQLPKAVEMMQDHKDKKIVMYCTGG-IRCE 207
Cdd:cd01443 3 YISPEELVALLENSdsnagkDFVVVDLRRD-DYEGGHIKGSINLPAQSCYQTLPQVYALFSLAGVKLAIFYCGSSqGRGP 81
|
90 100 110
....*....|....*....|....*....|..
gi 488988211 208 KASAWM----KHNGFN--KVWHIEGGIIEYAR 233
Cdd:cd01443 82 RAARWFadylRKVGESlpKSYILTGGIKAWYH 113
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
147-232 |
3.62e-09 |
|
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: 53.81 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 147 DPDAVFIDMRNHYEYEVGHFENALEIPADTFRDQLPKAVEMMQDH-------KDKKIVMYCTGGIRCEKASAWMKHNGFN 219
Cdd:cd01519 13 HPNKVLIDVREPEELKTGKIPGAINIPLSSLPDALALSEEEFEKKygfpkpsKDKELIFYCKAGVRSKAAAELARSLGYE 92
|
90
....*....|...
gi 488988211 220 KVWHIEGGIIEYA 232
Cdd:cd01519 93 NVGNYPGSWLDWA 105
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
136-233 |
1.36e-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: 52.04 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 136 LKAAEVNAMLDDPDAVFIDMRNHYEYE-VGHFENALEIPADTFRDQLPKAVEMMQDH--KDKKIVMYCTGGIRCEKASAW 212
Cdd:cd01447 1 LSPEDARALLGSPGVLLVDVRDPRELErTGMIPGAFHAPRGMLEFWADPDSPYHKPAfaEDKPFVFYCASGWRSALAGKT 80
|
90 100
....*....|....*....|.
gi 488988211 213 MKHNGFNKVWHIEGGIIEYAR 233
Cdd:cd01447 81 LQDMGLKPVYNIEGGFKDWKE 101
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
136-242 |
1.77e-08 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 55.40 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 136 LKAAEVNAMLDDpDAVFIDMRNHYEYEVGHFENALEIPadtfRDQLPKAVEMMQDHKDKKIVMYCTGGIRCEKASAWMKH 215
Cdd:PRK08762 5 ISPAEARARAAQ-GAVLIDVREAHERASGQAEGALRIP----RGFLELRIETHLPDRDREIVLICASGTRSAHAAATLRE 79
|
90 100
....*....|....*....|....*..
gi 488988211 216 NGFNKVWHIEGGIieyaRRAREQGLPV 242
Cdd:PRK08762 80 LGYTRVASVAGGF----SAWKDAGLPL 102
|
|
| glpE |
PRK00162 |
thiosulfate sulfurtransferase GlpE; |
143-227 |
4.07e-06 |
|
thiosulfate sulfurtransferase GlpE;
Pssm-ID: 178908 [Multi-domain] Cd Length: 108 Bit Score: 45.01 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 143 AMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFrdqlpkaVEMMQDHK-DKKIVMYCTGGIRCEKASAWMKHNGFNKV 221
Cdd:PRK00162 14 QKLQEGGAVLVDIRDPQSFAMGHAPGAFHLTNDSL-------GAFMRQADfDTPVMVMCYHGNSSQGAAQYLLQQGFDVV 86
|
....*.
gi 488988211 222 WHIEGG 227
Cdd:PRK00162 87 YSIDGG 92
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
139-228 |
5.66e-06 |
|
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: 44.17 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 139 AEVNAMLDDP-DAVFIDMR--NHYEYEVGHfenaleIPADTFRDQLPKAVEMMQDHKDKKIVMYCTGGIR-CEKASAWMK 214
Cdd:cd01444 5 DELAELLAAGeAPVLLDVRdpASYAALPDH------IPGAIHLDEDSLDDWLGDLDRDRPVVVYCYHGNSsAQLAQALRE 78
|
90
....*....|....
gi 488988211 215 HnGFNKVWHIEGGI 228
Cdd:cd01444 79 A-GFTDVRSLAGGF 91
|
|
| RHOD_1 |
cd01522 |
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative ... |
136-226 |
2.19e-05 |
|
Member of the Rhodanese Homology Domain superfamily, subgroup 1. This CD includes the putative rhodanese-related sulfurtransferases of several uncharacterized proteins.
Pssm-ID: 238780 [Multi-domain] Cd Length: 117 Bit Score: 43.08 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 136 LKAAEVNAML-DDPDAVFIDMRNHYE-YEVGHFENALEI---------PADTFRDQLPKAVEmmqdhKDKKIVMYCTGGI 204
Cdd:cd01522 1 LTPAEAWALLqADPQAVLVDVRTEAEwKFVGGVPDAVHVawqvypdmeINPNFLAELEEKVG-----KDRPVLLLCRSGN 75
|
90 100
....*....|....*....|...
gi 488988211 205 RCEKASAWMKHNGFNKVWHI-EG 226
Cdd:cd01522 76 RSIAAAEAAAQAGFTNVYNVlEG 98
|
|
| Acr2p |
cd01531 |
Eukaryotic arsenate resistance proteins are members of the Rhodanese Homology Domain ... |
135-226 |
3.61e-05 |
|
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: 42.40 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 135 YLKAAEVNAMLDD--PDAVFIDMRNhYEYEVGHFENALEIPADTFRDQLPKAVEMMQDHKDKKIVMYCTGG-IRCEKASA 211
Cdd:cd01531 3 YISPAQLKGWIRNgrPPFQVVDVRD-EDYAGGHIKGSWHYPSTRFKAQLNQLVQLLSGSKKDTVVFHCALSqVRGPSAAR 81
|
90 100 110
....*....|....*....|....*....|...
gi 488988211 212 ------------------WMKHNGFNKvWHIEG 226
Cdd:cd01531 82 kflryldeedletskfevYVLHGGFNA-WESSY 113
|
|
| PRK07411 |
PRK07411 |
molybdopterin-synthase adenylyltransferase MoeB; |
138-233 |
5.02e-05 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 180967 [Multi-domain] Cd Length: 390 Bit Score: 44.73 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 138 AAEVNAMLD--DPDAVFIDMRNHYEYEVGHFENALEIPADTFR--DQLPKAVEMMQDHkdkKIVMYCTGGIRCEKASAWM 213
Cdd:PRK07411 286 VTELKALLDsgADDFVLIDVRNPNEYEIARIPGSVLVPLPDIEngPGVEKVKELLNGH---RLIAHCKMGGRSAKALGIL 362
|
90 100
....*....|....*....|
gi 488988211 214 KHNGFNKVwHIEGGIIEYAR 233
Cdd:PRK07411 363 KEAGIEGT-NVKGGITAWSR 381
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
125-228 |
6.67e-05 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 44.48 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 125 PSFDASNVGEYLKAAEVNAMLddPDAVFIDMRNHYEYEVGHFENALEIPADTFR-DQLPKAVEMmqdhkDKKIVMYCTGG 203
Cdd:PRK05597 252 VHGISGGFGEVLDVPRVSALP--DGVTLIDVREPSEFAAYSIPGAHNVPLSAIReGANPPSVSA-----GDEVVVYCAAG 324
|
90 100
....*....|....*....|....*
gi 488988211 204 IRCEKASAWMKHNGFNKVWHIEGGI 228
Cdd:PRK05597 325 VRSAQAVAILERAGYTGMSSLDGGI 349
|
|
| SseA |
COG2897 |
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion ... |
138-242 |
1.59e-03 |
|
3-mercaptopyruvate sulfurtransferase SseA, contains two rhodanese domains [Inorganic ion transport and metabolism];
Pssm-ID: 442142 [Multi-domain] Cd Length: 262 Bit Score: 39.77 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 138 AAEVNAMLDDPDAVFIDMRNHYEY--EV-------GHFENALEIPADTFRDQ----LPKAV--EMMQD---HKDKKIVMY 199
Cdd:COG2897 142 ADEVLAALGDPDAVLVDARSPERYrgEVepidpraGHIPGAVNLPWTDLLDEdgtfKSAEElrALFAAlgiDPDKPVITY 221
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488988211 200 CTGGIRcekAS-AW--MKHNGFNKVWHIEGGIIEYARRAreqGLPV 242
Cdd:COG2897 222 CGSGVR---AAhTWlaLELLGYPNVRLYDGSWSEWGSDP---DLPV 261
|
|
| RHOD_ThiF |
cd01526 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ... |
151-233 |
1.92e-03 |
|
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: 37.67 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488988211 151 VFIDMRNHYEYEVGHFENALEIPADTFRD---QLPKAVEMMQDH-KDKKIVMYCTGGIRCEKASAWMKH-NGFNKVWHIE 225
Cdd:cd01526 26 VLLDVRPKVHFEICRLPEAINIPLSELLSkaaELKSLQELPLDNdKDSPIYVVCRRGNDSQTAVRKLKElGLERFVRDII 105
|
....*...
gi 488988211 226 GGIIEYAR 233
Cdd:cd01526 106 GGLKAWAD 113
|
|
| |
