|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
4-317 |
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 488014878 4 TKPYRVLLYYMYTTIENPEEFAEQHLEFCKSLELKGRILVATEGINGTCSGTVEQTEKYVEAMNNDPRFAGIVFKIDEAD 83
Cdd:PRK00142 1 MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 84 EHAFKKMHVRPRSELVTLRLEDDINPKEITGKYLEPKDFYEAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPD 163
Cdd:PRK00142 81 GHAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 164 WIRENKETLEGKKILTYCTGGIRCEKFSGWLVREGYEDVSQLHGGIVTYGKDPEVQGELWDGQCYVFDERIAVPVNqkEH 243
Cdd:PRK00142 161 WVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVPIN--DE 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488014878 244 VIVGKDHFTGEPCERYVNCANPECNKKILCSEESEAKHLRACSHECRVHPRNRYIVQHELTEEQVAATLEKIEA 317
Cdd:PRK00142 239 VPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKE 312
|
|
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
4-307 |
9.18e-173 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 480.79 E-value: 9.18e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 4 TKPYRVLLYYMYTTIENPEEFAEQHLEFCKSLELKGRILVATEGINGTCSGTVEQTEKYVEAMNNDPRFAGIVFKIDEAD 83
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 84 EHAFKKMHVRPRSELVTLRLEDdINPKEITGKYLEPKDFYEAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPD 163
Cdd:COG1054 81 GHPFPRLKVKLKKEIVTMGLPD-VDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 164 WIRENKETLEGKKILTYCTGGIRCEKFSGWLVREGYEDVSQLHGGIVTYGKDPEVQGELWDGQCYVFDERIAVPVNQkEH 243
Cdd:COG1054 160 WVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNL-EP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488014878 244 VIVGKDHFTGEPCERYVNCANPECNKKILCSEESEAKHLrACSHECRVHPRNRYIVQHELTEEQ 307
Cdd:COG1054 239 GVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADKYE-CCSDECTEEQRARYERQRQLRLAK 301
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
114-214 |
1.28e-49 |
|
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: 160.44 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 114 GKYLEPKDFYEAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPDWIRENKETLEGKKILTYCTGGIRCEKFSGW 193
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 488014878 194 LVREGYEDVSQLHGGIVTYGK 214
Cdd:cd01518 81 LKERGFKNVYQLKGGILKYLE 101
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
7-97 |
2.47e-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: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 7 YRVLLYYMYTTIENPEEFAEQHLEFCKSLELKGRILVATEGINGTCSGTVEQTEKYVEAMNNDPRFAGIVFKIDEADEHA 86
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
|
90
....*....|.
gi 488014878 87 FKKMHVRPRSE 97
Cdd:pfam17773 81 FRRLKVKLKKE 91
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
127-216 |
2.31e-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: 73.26 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 127 KQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPDW--------IRENKETLEGKKILTYCTGGIRCEKFSGWLVREG 198
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeeLLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90
....*....|....*...
gi 488014878 199 YEDVSQLHGGIVTYGKDP 216
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAG 98
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00142 |
PRK00142 |
rhodanese-related sulfurtransferase; |
4-317 |
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 488014878 4 TKPYRVLLYYMYTTIENPEEFAEQHLEFCKSLELKGRILVATEGINGTCSGTVEQTEKYVEAMNNDPRFAGIVFKIDEAD 83
Cdd:PRK00142 1 MKPYRVLLYYKYTPIEDPEAFRDEHLALCKSLGLKGRILVAEEGINGTVSGTIEQTEAYMAWLKADPRFADIRFKISEDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 84 EHAFKKMHVRPRSELVTLRLEDDINPKEITGKYLEPKDFYEAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPD 163
Cdd:PRK00142 81 GHAFPRLSVKVRKEIVALGLDDDIDPLENVGTYLKPKEVNELLDDPDVVFIDMRNDYEYEIGHFENAIEPDIETFREFPP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 164 WIRENKETLEGKKILTYCTGGIRCEKFSGWLVREGYEDVSQLHGGIVTYGKDPEVQGELWDGQCYVFDERIAVPVNqkEH 243
Cdd:PRK00142 161 WVEENLDPLKDKKVVMYCTGGIRCEKASAWMKHEGFKEVYQLEGGIITYGEDPETQGLLWDGKLYVFDERMAVPIN--DE 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488014878 244 VIVGKDHFTGEPCERYVNCANPECNKKILCSEESEAKHLRACSHECRVHPRNRYIVQHELTEEQVAATLEKIEA 317
Cdd:PRK00142 239 VPIGHCHQCGTPCDRYVNCANPACNLLILQCEECEEKYLGCCSEECCEHPRNRYVEQRGRRRERENELLIFNKE 312
|
|
| TrhO |
COG1054 |
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and ... |
4-307 |
9.18e-173 |
|
tRNA U34 5'-hydroxylase TrhO, rhodanese family [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440674 [Multi-domain] Cd Length: 304 Bit Score: 480.79 E-value: 9.18e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 4 TKPYRVLLYYMYTTIENPEEFAEQHLEFCKSLELKGRILVATEGINGTCSGTVEQTEKYVEAMNNDPRFAGIVFKIDEAD 83
Cdd:COG1054 1 MKPYVVLAFYKFVPLEDPEALRDPLLALCEELGLKGRILLAPEGINGTVSGPREAIDAYLAFLRADPRFADLEFKESEAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 84 EHAFKKMHVRPRSELVTLRLEDdINPKEITGKYLEPKDFYEAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPD 163
Cdd:COG1054 81 GHPFPRLKVKLKKEIVTMGLPD-VDPNEGVGTYLSPEEWNALIEDPDVVVIDTRNDYEVEIGTFKGAIDPDTDTFREFPE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 164 WIRENKETLEGKKILTYCTGGIRCEKFSGWLVREGYEDVSQLHGGIVTYGKDPEVQGELWDGQCYVFDERIAVPVNQkEH 243
Cdd:COG1054 160 WVEENLDDLKDKKVAMYCTGGIRCEKASAYLKEQGFEEVYQLEGGILKYLEEVPEEGSLWEGECFVFDERVAVDHNL-EP 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488014878 244 VIVGKDHFTGEPCERYVNCANPECNKKILCSEESEAKHLrACSHECRVHPRNRYIVQHELTEEQ 307
Cdd:COG1054 239 GVIGLCHACGTPCDRYVNCANDPCYELGVSCPHCADKYE-CCSDECTEEQRARYERQRQLRLAK 301
|
|
| PRK01415 |
PRK01415 |
hypothetical protein; Validated |
9-236 |
2.95e-62 |
|
hypothetical protein; Validated
Pssm-ID: 167229 [Multi-domain] Cd Length: 247 Bit Score: 197.86 E-value: 2.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 9 VLLYYMYTTIENPEEFAEQHLEFCKSLELKGRILVATEGINGTCSGTVEQTEKYVEAMNNDPRFAGIVFKIDEADEHAFK 88
Cdd:PRK01415 7 ILSAYSFVNIEEPANLIPKLLLIGKRKYVRGTILLANEGFNGSFSGSYENVNLVLEELIKLTGPKDVNVKINYSDVHPFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 89 KMHVRPRSELVTLRLeDDINPKEITGKYLEPKDFYEAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPDWIREN 168
Cdd:PRK01415 87 KLKVRLKKEIVAMNV-DDLNVDLFKGEYIEPKDWDEFITKQDVIVIDTRNDYEVEVGTFKSAINPNTKTFKQFPAWVQQN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488014878 169 KETLEGKKILTYCTGGIRCEKFSGWLVREGYEDVSQLHGGIVTYGKDPEVQGELWDGQCYVFDERIAV 236
Cdd:PRK01415 166 QELLKGKKIAMVCTGGIRCEKSTSLLKSIGYDEVYHLKGGILQYLEDTQNKNNLWQGECFVFDDRRAV 233
|
|
| PRK05320 |
PRK05320 |
rhodanese superfamily protein; Provisional |
13-236 |
6.05e-61 |
|
rhodanese superfamily protein; Provisional
Pssm-ID: 235405 [Multi-domain] Cd Length: 257 Bit Score: 194.86 E-value: 6.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 13 YMYTTIENPEEFAEQHLEFCKSLELKGRILVATEGINGTCSGTVEQTEKYVEAMNNDPRFAGIVFKIDEADEHAFKKMHV 92
Cdd:PRK05320 9 YKFVSLDDPETLRPLVLARCEALGLKGTILLAPEGINLFLAGTREAIDAFYAWLRADARFADLQVKESLSDSQPFRRMLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 93 RPRSELVTLRlEDDINPKEITGKYLEPKDFYEAMKQ--EDT----VIIDARNDYEFDLGHFKGAIKPDIESFRELPDWIR 166
Cdd:PRK05320 89 KLKREIITMK-RPAIRPELGRAPSVDAATLKRWLDQghDDAgrpvVMLDTRNAFEVDVGTFDGALDYRIDKFTEFPEALA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 167 ENKETLEGKKILTYCTGGIRCEKFSGWLVREGYEDVSQLHGGIVTYGKdpEVQGELWDGQCYVFDERIAV 236
Cdd:PRK05320 168 AHRADLAGKTVVSFCTGGIRCEKAAIHMQEVGIDNVYQLEGGILKYFE--EVGGAHYDGDCFVFDYRTAL 235
|
|
| RHOD_YceA |
cd01518 |
Member of the Rhodanese Homology Domain superfamily. This CD includes Escherichia coli YceA, ... |
114-214 |
1.28e-49 |
|
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: 160.44 E-value: 1.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 114 GKYLEPKDFYEAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPDWIRENKETLEGKKILTYCTGGIRCEKFSGW 193
Cdd:cd01518 1 GTYLSPAEWNELLEDPEVVLLDVRNDYEYDIGHFKGAVNPDVDTFREFPFWLDENLDLLKGKKVLMYCTGGIRCEKASAY 80
|
90 100
....*....|....*....|.
gi 488014878 194 LVREGYEDVSQLHGGIVTYGK 214
Cdd:cd01518 81 LKERGFKNVYQLKGGILKYLE 101
|
|
| UPF0176_N |
pfam17773 |
UPF0176 acylphosphatase like domain; This domain is found at the N-terminus of UPF0176 family ... |
7-97 |
2.47e-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: 2.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 7 YRVLLYYMYTTIENPEEFAEQHLEFCKSLELKGRILVATEGINGTCSGTVEQTEKYVEAMNNDPRFAGIVFKIDEADEHA 86
Cdd:pfam17773 1 YVVIAFYKFVPLDDPAALREELLELCEELGLRGTILLAPEGINGTIAGPREAIDAFIEFLRADPGFADLDFKESYSDEHP 80
|
90
....*....|.
gi 488014878 87 FKKMHVRPRSE 97
Cdd:pfam17773 81 FRRLKVKLKKE 91
|
|
| Rhodanese_C |
pfam12368 |
Rhodanase C-terminal; Rhodanase_C is found as the domain-extension to Rhodanase enzyme in some ... |
224-290 |
1.27e-25 |
|
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: 97.00 E-value: 1.27e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488014878 224 DGQCYVFDERIAVPvNQKEHVIVGKDHFTGEPCERYVNCANPECNKKILCSEESEAKHLRACSHECR 290
Cdd:pfam12368 1 KGKLFVFDERLAVV-EPSDDDVIGKCYHCGKPCDRYVNCANPDCNRLFLQCEECAEKYEGCCSEECA 66
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
115-209 |
2.05e-17 |
|
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: 76.54 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 115 KYLEPKDFYEAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPDWIRENKEtlegkkILTYCTGGIRCEKFSGWL 194
Cdd:COG0607 4 KEISPAELAELLESEDAVLLDVREPEEFAAGHIPGAINIPLGELAERLDELPKDKP------IVVYCASGGRSAQAAALL 77
|
90
....*....|....*
gi 488014878 195 VREGYEDVSQLHGGI 209
Cdd:COG0607 78 RRAGYTNVYNLAGGI 92
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
127-216 |
2.31e-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: 73.26 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 127 KQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPDW--------IRENKETLEGKKILTYCTGGIRCEKFSGWLVREG 198
Cdd:smart00450 1 NDEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGEldilefeeLLKRLGLDKDKPVVVYCRSGNRSAKAAWLLRELG 80
|
90
....*....|....*...
gi 488014878 199 YEDVSQLHGGIVTYGKDP 216
Cdd:smart00450 81 FKNVYLLDGGYKEWSAAG 98
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
121-209 |
2.62e-14 |
|
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: 67.32 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 121 DFYEAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPDWIRENKetleGKKILTYCTGGIRCEKFSGWLVREGYE 200
Cdd:cd00158 1 ELKELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDK----DKPIVVYCRSGNRSARAAKLLRKAGGT 76
|
....*....
gi 488014878 201 DVSQLHGGI 209
Cdd:cd00158 77 NVYNLEGGM 85
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
126-210 |
4.35e-13 |
|
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: 64.04 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 126 MKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPDWIRENKETLE----GKKILTYCTGGIRCEKFSGWLVREGYED 201
Cdd:pfam00581 1 LEDGKVVLIDVRPPEEYAKGHIPGAVNVPLSSLSLPPLPLLELLEKLLellkDKPIVVYCNSGNRAAAAAALLKALGYKN 80
|
....*....
gi 488014878 202 VSQLHGGIV 210
Cdd:pfam00581 81 VYVLDGGFE 89
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
124-214 |
1.95e-08 |
|
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: 51.11 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 124 EAMKQEDTVIIDARNDYEFDLGHFKGAIKPDIESFRELPDWIRENKEtlegkkILTYCTGGIRCEKFSGWLVREGYeDVS 203
Cdd:cd01524 7 DNYRADGVTLIDVRTPQEFEKGHIKGAINIPLDELRDRLNELPKDKE------IIVYCAVGLRGYIAARILTQNGF-KVK 79
|
90
....*....|.
gi 488014878 204 QLHGGIVTYGK 214
Cdd:cd01524 80 NLDGGYKTYST 90
|
|
| RHOD_2 |
cd01528 |
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes ... |
129-212 |
8.59e-08 |
|
Member of the Rhodanese Homology Domain superfamily, subgroup 2. Subgroup 2 includes uncharacterized putative rhodanese-related domains.
Pssm-ID: 238786 [Multi-domain] Cd Length: 101 Bit Score: 49.32 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 129 EDTVIIDARNDYEFDLGHFKGAIKPDIesfRELPDWIRENKETLEGKKILTYCTGGIRCEKFSGWLVREGYEDVSQLHGG 208
Cdd:cd01528 16 EEPVLIDVREPEELEIAFLPGFLHLPM---SEIPERSKELDSDNPDKDIVVLCHHGGRSMQVAQWLLRQGFENVYNLQGG 92
|
....
gi 488014878 209 IVTY 212
Cdd:cd01528 93 IDAW 96
|
|
| GlpE_ST |
cd01444 |
GlpE sulfurtransferase (ST) and homologs are members of the Rhodanese Homology Domain ... |
129-209 |
7.30e-07 |
|
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: 46.87 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 129 EDTVIIDAR--NDYEFDLGHFKGAIKPDIESfreLPDWIRenkETLEGKKILTYCTGGIRCEKFSGWLVREGYEDVSQLH 206
Cdd:cd01444 15 EAPVLLDVRdpASYAALPDHIPGAIHLDEDS---LDDWLG---DLDRDRPVVVYCYHGNSSAQLAQALREAGFTDVRSLA 88
|
...
gi 488014878 207 GGI 209
Cdd:cd01444 89 GGF 91
|
|
| PRK05597 |
PRK05597 |
molybdopterin biosynthesis protein MoeB; Validated |
129-209 |
1.47e-04 |
|
molybdopterin biosynthesis protein MoeB; Validated
Pssm-ID: 235526 [Multi-domain] Cd Length: 355 Bit Score: 42.94 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 129 EDTVIIDARNDYEFDLGHFKGAIKPDIESFRE--LPDwirenkETLEGKKILTYCTGGIRCEKFSGWLVREGYEDVSQLH 206
Cdd:PRK05597 273 DGVTLIDVREPSEFAAYSIPGAHNVPLSAIREgaNPP------SVSAGDEVVVYCAAGVRSAQAVAILERAGYTGMSSLD 346
|
...
gi 488014878 207 GGI 209
Cdd:PRK05597 347 GGI 349
|
|
| PRK07878 |
PRK07878 |
molybdopterin biosynthesis-like protein MoeZ; Validated |
129-217 |
2.48e-04 |
|
molybdopterin biosynthesis-like protein MoeZ; Validated
Pssm-ID: 181156 [Multi-domain] Cd Length: 392 Bit Score: 42.39 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 129 EDTVIIDARNDYEFDLGHFKGAI---KPDIES---FRELPdwirenketlEGKKILTYCTGGIRCEKFSGWLVREGYEDV 202
Cdd:PRK07878 302 KKIALIDVREPVEWDIVHIPGAQlipKSEILSgeaLAKLP----------QDRTIVLYCKTGVRSAEALAALKKAGFSDA 371
|
90
....*....|....*..
gi 488014878 203 SQLHGGIVTYGK--DPE 217
Cdd:PRK07878 372 VHLQGGVVAWAKqvDPS 388
|
|
| Polysulfide_ST |
cd01447 |
Polysulfide-sulfurtransferase - Rhodanese Homology Domain. This domain is believed to serve as ... |
117-208 |
3.41e-03 |
|
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: 36.64 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 117 LEPKDFYEAMKQEDTVIIDARNDYEFDL-GHFKGA--IKPDIESFRELPDWIRENKETLEGKKILTYCTGGIRcEKFSGW 193
Cdd:cd01447 1 LSPEDARALLGSPGVLLVDVRDPRELERtGMIPGAfhAPRGMLEFWADPDSPYHKPAFAEDKPFVFYCASGWR-SALAGK 79
|
90
....*....|....*.
gi 488014878 194 LVRE-GYEDVSQLHGG 208
Cdd:cd01447 80 TLQDmGLKPVYNIEGG 95
|
|
| PRK08762 |
PRK08762 |
molybdopterin-synthase adenylyltransferase MoeB; |
132-209 |
7.56e-03 |
|
molybdopterin-synthase adenylyltransferase MoeB;
Pssm-ID: 236337 [Multi-domain] Cd Length: 376 Bit Score: 37.68 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488014878 132 VIIDARNDYEFDLGHFKGAI-------KPDIESfrELPDWIREnketlegkkILTYCTGGIRCEKFSGWLVREGYEDVSQ 204
Cdd:PRK08762 19 VLIDVREAHERASGQAEGALriprgflELRIET--HLPDRDRE---------IVLICASGTRSAHAAATLRELGYTRVAS 87
|
....*
gi 488014878 205 LHGGI 209
Cdd:PRK08762 88 VAGGF 92
|
|
| |
