|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11784 |
PRK11784 |
tRNA 2-selenouridine synthase; Provisional |
3-362 |
1.11e-163 |
|
tRNA 2-selenouridine synthase; Provisional
Pssm-ID: 236982 [Multi-domain] Cd Length: 345 Bit Score: 461.22 E-value: 1.11e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 3 STLSAQNIRRLLANETPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGHQLVKGEIKAHRVAA 82
Cdd:PRK11784 1 MRPDAQDFRALFLNDTPLIDVRSPIEFAEGHIPGAINLPLLNDEERAEVGTCYKQQGQFAAIALGHALVAGNIAAHREEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 83 WREACERFPSGFICCARGGMRSHIVQKWLAEIGIDYPLIEGGYKALRQATIEMTNELVQR-PIILIGGCTGNGKTTLVRS 161
Cdd:PRK11784 81 WADFPRANPRGLLYCWRGGLRSGSVQQWLKEAGIDVPRLEGGYKAYRRFVIDTLEEAPAQfPLVVLGGNTGSGKTELLQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 162 LPE----GIDLEGFAHHRGSSFGRTVEAQFAQATFENYLAVDMLKKSSyHSRWVLEDEGRAIGANGLPESLRIQMATAHL 237
Cdd:PRK11784 161 LANagaqVLDLEGLANHRGSSFGRLGGPQPSQKDFENLLAEALLKLDP-ARPIVVEDESRRIGRVHLPEALYEAMQQAPI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 238 VVVDDPFERRMARLKEEYFDRMTHDFIEAYGEekgwqeysdYLHHGLYAIRRRLGAQRAAELTQLLDNalaaqkisantE 317
Cdd:PRK11784 240 VVVEAPLEERVERLLEDYVLRMHAAGFQAYPE---------YLAEALQRIRKRLGGERYQELLALLDA-----------G 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 194682608 318 VHFSWLSPLLKEYYDPMYRYQLSKKQDKIIYTGSYEEVEQWFANH 362
Cdd:PRK11784 300 GHLAWIEELLLEYYDPMYRYQLEKKADRIDFRGDLAEVAEWLRAL 344
|
|
| SelU |
COG2603 |
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ... |
1-362 |
4.81e-163 |
|
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442015 [Multi-domain] Cd Length: 341 Bit Score: 459.24 E-value: 4.81e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 1 MESTLSAQNIRRLLANeTPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGHQLVKGEIKAHRV 80
Cdd:COG2603 1 MSKRITLDDFLELLDD-DPLIDVRSPVEFAEGHIPGAINLPLLDDEERAEVGTCYKQQGPFAAIKLGHALVSGKLAAHRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 81 AAWrEACERFPSGFICCARGGMRSHIVQKWLAEIGIDYPLIEGGYKALRQATIEMTNELV-QRPIILIGGCTGNGKTTLV 159
Cdd:COG2603 80 EAW-AFAPKHPRPLVYCWRGGLRSGSVAQWLREAGIDVPRLEGGYKAYRRFVLDELERLPaPLPLIVLGGPTGSGKTRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 160 RSLPE----GIDLEGFAHHRGSSFGRTV-EAQFAQATFENYLAVDMLKKSSyHSRWVLEDEGRAIGANGLPESLRIQMAT 234
Cdd:COG2603 159 HALAAqgaqVLDLEGLANHRGSSFGRIGlGPQPSQKDFENLLAIALLKLDP-ARPVVVEDESRRIGRVHLPDALYEAMRQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 235 AHLVVVDDPFERRMARLKEEYFDRMTHDfieaygeekgwqeySDYLHHGLYAIRRRLGAQRAAELTQLLDNalaaqkisa 314
Cdd:COG2603 238 APLVLLEAPLEERVERLLEDYVDLMLAD--------------PEYLKEALDRIRKRLGGERYQELLALLEA--------- 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 194682608 315 ntEVHFSWLSPLLKEYYDPMYRYQLSKKQDKIIYTGSYEEVEQWFANH 362
Cdd:COG2603 295 --GDHEEWIEELLEEYYDPMYRYSLEKKADRIVFRGDAEEVLAFLAAL 340
|
|
| tRNA_sel_U_synt |
TIGR03167 |
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ... |
16-347 |
1.91e-120 |
|
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274463 [Multi-domain] Cd Length: 311 Bit Score: 350.36 E-value: 1.91e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 16 NETPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGHQLVKGEIKAHrVAAWREACERFPSGFI 95
Cdd:TIGR03167 1 AFDPLIDVRSPAEFAEGHLPGAINLPLLNDEERAEVGTLYKQVGPFAAIKLGLALVSPNLAAH-VEQWRAFADGPPQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 96 CCARGGMRSHIVQKWLAEIGIDYPLIEGGYKALRQATIEMTNELVQR-PIILIGGCTGNGKTTLVRSLPEG----IDLEG 170
Cdd:TIGR03167 80 YCWRGGMRSGSLAWLLAQIGFRVPRLEGGYKAYRRFVIDQLEELPQPfPLIVLGGMTGSGKTELLHALANAgaqvLDLEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 171 FAHHRGSSFGRTV-EAQFAQATFENYLAVDMLKKSSyHSRWVLEDEGRAIGANGLPESLRIQMATAHLVVVDDPFERRMA 249
Cdd:TIGR03167 160 LANHRGSSFGALGlGPQPSQKRFENALAEALRRLDP-GRPIFVEDESRRIGRVALPDALFEAMRAAPLVELEASLEERVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 250 RLKEEYfdrmthdfieaygeeKGWQEYSDYLHHGLYAIRRRLGAQRAAELTQLLDnalAAQkisantevHFSWLSPLLKE 329
Cdd:TIGR03167 239 RLVEEY---------------AGFEEDPEFLAAALERIRKRLGGERYQQLLALLE---AGD--------HREWIRALLED 292
|
330
....*....|....*...
gi 194682608 330 YYDPMYRYQLSKKQDKII 347
Cdd:TIGR03167 293 YYDPMYAYQLAKKAERVS 310
|
|
| RHOD_YbbB |
cd01520 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ... |
5-132 |
9.73e-60 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.
Pssm-ID: 238778 [Multi-domain] Cd Length: 128 Bit Score: 188.66 E-value: 9.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 5 LSAQNIRRLLANETPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGHQLVKGEIKAHRVAAWR 84
Cdd:cd01520 1 ITAEDLLALRKADGPLIDVRSPKEFFEGHLPGAINLPLLDDEERALVGTLYKQQGREAAIELGLELVSGKLKRILNEAWE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 194682608 85 EACERFPSGFICCARGGMRSHIVQkWLAE-IGIDYPLIEGGYKALRQAT 132
Cdd:cd01520 81 ARLERDPKLLIYCARGGMRSQSLA-WLLEsLGIDVPLLEGGYKAYRKFV 128
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
15-131 |
2.39e-10 |
|
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: 57.08 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 15 ANETPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGhqlvkgeiKAHRVaawreacerfpsgF 94
Cdd:smart00450 2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLD--------KDKPV-------------V 60
|
90 100 110
....*....|....*....|....*....|....*...
gi 194682608 95 ICCaRGGMRSHIVQKWLAEIGI-DYPLIEGGYKALRQA 131
Cdd:smart00450 61 VYC-RSGNRSAKAAWLLRELGFkNVYLLDGGYKEWSAA 97
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
145-266 |
6.83e-04 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 39.33 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 145 ILIGGCTGNGKTT----LVRSLPEGIDLEGFAHHRGSSFGRTVEAQFAQATFENYL--AVDMLKKSSY---HSRWVLEDe 215
Cdd:pfam13238 1 ILITGTPGVGKTTlakeLSKRLGFGDNVRDLALENGLVLGDDPETRESKRLDEDKLdrLLDLLEENAAleeGGNLIIDG- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 194682608 216 graIGANGLPESLRIqmatAHLVVVDDPFERRMARLKE-EYFDRMTHDFIEA 266
Cdd:pfam13238 80 ---HLAELEPERAKD----LVGIVLRASPEELLERLEKrGYEEAKIKENEEA 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11784 |
PRK11784 |
tRNA 2-selenouridine synthase; Provisional |
3-362 |
1.11e-163 |
|
tRNA 2-selenouridine synthase; Provisional
Pssm-ID: 236982 [Multi-domain] Cd Length: 345 Bit Score: 461.22 E-value: 1.11e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 3 STLSAQNIRRLLANETPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGHQLVKGEIKAHRVAA 82
Cdd:PRK11784 1 MRPDAQDFRALFLNDTPLIDVRSPIEFAEGHIPGAINLPLLNDEERAEVGTCYKQQGQFAAIALGHALVAGNIAAHREEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 83 WREACERFPSGFICCARGGMRSHIVQKWLAEIGIDYPLIEGGYKALRQATIEMTNELVQR-PIILIGGCTGNGKTTLVRS 161
Cdd:PRK11784 81 WADFPRANPRGLLYCWRGGLRSGSVQQWLKEAGIDVPRLEGGYKAYRRFVIDTLEEAPAQfPLVVLGGNTGSGKTELLQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 162 LPE----GIDLEGFAHHRGSSFGRTVEAQFAQATFENYLAVDMLKKSSyHSRWVLEDEGRAIGANGLPESLRIQMATAHL 237
Cdd:PRK11784 161 LANagaqVLDLEGLANHRGSSFGRLGGPQPSQKDFENLLAEALLKLDP-ARPIVVEDESRRIGRVHLPEALYEAMQQAPI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 238 VVVDDPFERRMARLKEEYFDRMTHDFIEAYGEekgwqeysdYLHHGLYAIRRRLGAQRAAELTQLLDNalaaqkisantE 317
Cdd:PRK11784 240 VVVEAPLEERVERLLEDYVLRMHAAGFQAYPE---------YLAEALQRIRKRLGGERYQELLALLDA-----------G 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 194682608 318 VHFSWLSPLLKEYYDPMYRYQLSKKQDKIIYTGSYEEVEQWFANH 362
Cdd:PRK11784 300 GHLAWIEELLLEYYDPMYRYQLEKKADRIDFRGDLAEVAEWLRAL 344
|
|
| SelU |
COG2603 |
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal ... |
1-362 |
4.81e-163 |
|
tRNA 2-selenouridine synthase SelU, contains rhodanese domain [Translation, ribosomal structure and biogenesis]; tRNA 2-selenouridine synthase SelU, contains rhodanese domain is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442015 [Multi-domain] Cd Length: 341 Bit Score: 459.24 E-value: 4.81e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 1 MESTLSAQNIRRLLANeTPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGHQLVKGEIKAHRV 80
Cdd:COG2603 1 MSKRITLDDFLELLDD-DPLIDVRSPVEFAEGHIPGAINLPLLDDEERAEVGTCYKQQGPFAAIKLGHALVSGKLAAHRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 81 AAWrEACERFPSGFICCARGGMRSHIVQKWLAEIGIDYPLIEGGYKALRQATIEMTNELV-QRPIILIGGCTGNGKTTLV 159
Cdd:COG2603 80 EAW-AFAPKHPRPLVYCWRGGLRSGSVAQWLREAGIDVPRLEGGYKAYRRFVLDELERLPaPLPLIVLGGPTGSGKTRLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 160 RSLPE----GIDLEGFAHHRGSSFGRTV-EAQFAQATFENYLAVDMLKKSSyHSRWVLEDEGRAIGANGLPESLRIQMAT 234
Cdd:COG2603 159 HALAAqgaqVLDLEGLANHRGSSFGRIGlGPQPSQKDFENLLAIALLKLDP-ARPVVVEDESRRIGRVHLPDALYEAMRQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 235 AHLVVVDDPFERRMARLKEEYFDRMTHDfieaygeekgwqeySDYLHHGLYAIRRRLGAQRAAELTQLLDNalaaqkisa 314
Cdd:COG2603 238 APLVLLEAPLEERVERLLEDYVDLMLAD--------------PEYLKEALDRIRKRLGGERYQELLALLEA--------- 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 194682608 315 ntEVHFSWLSPLLKEYYDPMYRYQLSKKQDKIIYTGSYEEVEQWFANH 362
Cdd:COG2603 295 --GDHEEWIEELLEEYYDPMYRYSLEKKADRIVFRGDAEEVLAFLAAL 340
|
|
| tRNA_sel_U_synt |
TIGR03167 |
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a ... |
16-347 |
1.91e-120 |
|
tRNA 2-selenouridine synthase; The Escherichia coli YbbB protein was shown to encode a selenophosphate-dependent tRNA 2-selenouridine synthase, essential for modification of some tRNAs to replace a sulfur atom with selenium. This enzyme works with SelD, the selenium donor protein, which also acts in selenocysteine incorporation. Although the members of this protein family show a fairly deep split, sequences from both sides of the split are supported by co-occurence with, and often proximity to, the selD gene. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 274463 [Multi-domain] Cd Length: 311 Bit Score: 350.36 E-value: 1.91e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 16 NETPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGHQLVKGEIKAHrVAAWREACERFPSGFI 95
Cdd:TIGR03167 1 AFDPLIDVRSPAEFAEGHLPGAINLPLLNDEERAEVGTLYKQVGPFAAIKLGLALVSPNLAAH-VEQWRAFADGPPQPLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 96 CCARGGMRSHIVQKWLAEIGIDYPLIEGGYKALRQATIEMTNELVQR-PIILIGGCTGNGKTTLVRSLPEG----IDLEG 170
Cdd:TIGR03167 80 YCWRGGMRSGSLAWLLAQIGFRVPRLEGGYKAYRRFVIDQLEELPQPfPLIVLGGMTGSGKTELLHALANAgaqvLDLEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 171 FAHHRGSSFGRTV-EAQFAQATFENYLAVDMLKKSSyHSRWVLEDEGRAIGANGLPESLRIQMATAHLVVVDDPFERRMA 249
Cdd:TIGR03167 160 LANHRGSSFGALGlGPQPSQKRFENALAEALRRLDP-GRPIFVEDESRRIGRVALPDALFEAMRAAPLVELEASLEERVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 250 RLKEEYfdrmthdfieaygeeKGWQEYSDYLHHGLYAIRRRLGAQRAAELTQLLDnalAAQkisantevHFSWLSPLLKE 329
Cdd:TIGR03167 239 RLVEEY---------------AGFEEDPEFLAAALERIRKRLGGERYQQLLALLE---AGD--------HREWIRALLED 292
|
330
....*....|....*...
gi 194682608 330 YYDPMYRYQLSKKQDKII 347
Cdd:TIGR03167 293 YYDPMYAYQLAKKAERVS 310
|
|
| RHOD_YbbB |
cd01520 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP ... |
5-132 |
9.73e-60 |
|
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ATP /GTP binding proteins including E. coli YbbB.
Pssm-ID: 238778 [Multi-domain] Cd Length: 128 Bit Score: 188.66 E-value: 9.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 5 LSAQNIRRLLANETPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGHQLVKGEIKAHRVAAWR 84
Cdd:cd01520 1 ITAEDLLALRKADGPLIDVRSPKEFFEGHLPGAINLPLLDDEERALVGTLYKQQGREAAIELGLELVSGKLKRILNEAWE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 194682608 85 EACERFPSGFICCARGGMRSHIVQkWLAE-IGIDYPLIEGGYKALRQAT 132
Cdd:cd01520 81 ARLERDPKLLIYCARGGMRSQSLA-WLLEsLGIDVPLLEGGYKAYRKFV 128
|
|
| arch_SelU_Nterm |
TIGR04568 |
selenouridine synthase, SelU N-terminal-like subunit; This protein is involved in biosynthesis ... |
1-131 |
1.47e-16 |
|
selenouridine synthase, SelU N-terminal-like subunit; This protein is involved in biosynthesis of a selenonucleotide, probably 2-selenouridine, in tRNA of some archaea, such as Methanococcus maripaludis. This protein resembles the N-terminal region of bacterial SelU, and its partner protein resembles the C-terminal region. [Protein synthesis, tRNA and rRNA base modification]
Pssm-ID: 275361 Cd Length: 215 Bit Score: 77.58 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 1 MESTLSAQNIRRLLANETPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGHQLVKGEIKahRV 80
Cdd:TIGR04568 87 VDNVITVSEFLELIKEDVIIVDARSPREFKEKTIPGAINIPLFLDDEHETIGKTYKQEGREKAIEIATDIIEKSIK--RI 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 194682608 81 AAWREACERFPSGFICCARGGMRSHIVQKWLAEIGIDYPLIEGGYKALRQA 131
Cdd:TIGR04568 165 LNEAKKLDRNKLIVVFCARGGMRSQTMATILKLLGFKVKRLIGGFKAYNHA 215
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
15-131 |
2.39e-10 |
|
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: 57.08 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 15 ANETPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKQHGSQKAVELGhqlvkgeiKAHRVaawreacerfpsgF 94
Cdd:smart00450 2 DEKVVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELDILEFEELLKRLGLD--------KDKPV-------------V 60
|
90 100 110
....*....|....*....|....*....|....*...
gi 194682608 95 ICCaRGGMRSHIVQKWLAEIGI-DYPLIEGGYKALRQA 131
Cdd:smart00450 61 VYC-RSGNRSAKAAWLLRELGFkNVYLLDGGYKEWSAA 97
|
|
| PspE |
COG0607 |
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ... |
4-131 |
4.55e-10 |
|
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: 56.13 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 4 TLSAQNIRRLLANETP-IIDVRAPIEFNQGAMPNAINLPLMNNEERAAvgtcykqhgsqkAVELGHQLVkgeikahrvaa 82
Cdd:COG0607 5 EISPAELAELLESEDAvLLDVREPEEFAAGHIPGAINIPLGELAERLD------------ELPKDKPIV----------- 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 194682608 83 wreacerfpsgFICcaRGGMRSHIVQKWLAEIGID--YPLiEGGYKALRQA 131
Cdd:COG0607 62 -----------VYC--ASGGRSAQAAALLRRAGYTnvYNL-AGGIEAWKAA 98
|
|
| RHOD |
cd00158 |
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ... |
10-129 |
2.91e-07 |
|
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: 47.68 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 10 IRRLLANETPIIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGTCYKqhgsqkavelGHQLVkgeikahrvaawreacer 89
Cdd:cd00158 3 KELLDDEDAVLLDVREPEEYAAGHIPGAINIPLSELEERAALLELDK----------DKPIV------------------ 54
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 194682608 90 fpsgFICcaRGGMRSHIVQKWLAEIG-IDYPLIEGGYKALR 129
Cdd:cd00158 55 ----VYC--RSGNRSARAAKLLRKAGgTNVYNLEGGMLAWK 89
|
|
| RHOD_HSP67B2 |
cd01519 |
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ... |
8-42 |
2.55e-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: 42.64 E-value: 2.55e-05
10 20 30
....*....|....*....|....*....|....*..
gi 194682608 8 QNIRRLLAN--ETPIIDVRAPIEFNQGAMPNAINLPL 42
Cdd:cd01519 4 EEVKNLPNPhpNKVLIDVREPEELKTGKIPGAINIPL 40
|
|
| RHOD_Pyr_redox |
cd01524 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the Lactococcus ... |
10-42 |
3.85e-05 |
|
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: 41.87 E-value: 3.85e-05
10 20 30
....*....|....*....|....*....|...
gi 194682608 10 IRRLLANETPIIDVRAPIEFNQGAMPNAINLPL 42
Cdd:cd01524 6 LDNYRADGVTLIDVRTPQEFEKGHIKGAINIPL 38
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
145-266 |
6.83e-04 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 39.33 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 145 ILIGGCTGNGKTT----LVRSLPEGIDLEGFAHHRGSSFGRTVEAQFAQATFENYL--AVDMLKKSSY---HSRWVLEDe 215
Cdd:pfam13238 1 ILITGTPGVGKTTlakeLSKRLGFGDNVRDLALENGLVLGDDPETRESKRLDEDKLdrLLDLLEENAAleeGGNLIIDG- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 194682608 216 graIGANGLPESLRIqmatAHLVVVDDPFERRMARLKE-EYFDRMTHDFIEA 266
Cdd:pfam13238 80 ---HLAELEPERAKD----LVGIVLRASPEELLERLEKrGYEEAKIKENEEA 124
|
|
| RHOD_ThiF |
cd01526 |
Member of the Rhodanese Homology Domain superfamily. This CD includes several putative ... |
2-121 |
2.65e-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: 37.29 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 2 ESTLSAQNIRRLLANETP--IIDVRAPIEFNQGAMPNAINLPLMNNEERAAVGT------------------CYKQHGSQ 61
Cdd:cd01526 7 EERVSVKDYKNILQAGKKhvLLDVRPKVHFEICRLPEAINIPLSELLSKAAELKslqelpldndkdspiyvvCRRGNDSQ 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 194682608 62 KAVelghQLVKgeikahrvaawreacERFPSGFICCARGGMRshivqKWLAEIGIDYPLI 121
Cdd:cd01526 87 TAV----RKLK---------------ELGLERFVRDIIGGLK-----AWADKVDPTFPLY 122
|
|
| RHOD_Kc |
cd01525 |
Member of the Rhodanese Homology Domain superfamily. Included in this CD are the ... |
5-41 |
4.52e-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: 36.28 E-value: 4.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 194682608 5 LSAQNIRRLLANETP---IIDVRAPIEFNQGAMPNAINLP 41
Cdd:cd01525 1 ISVYDVIRLLDNSPAklaAVDIRSSPDFRRGHIEGSINIP 40
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
15-43 |
6.70e-03 |
|
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: 35.54 E-value: 6.70e-03
10 20
....*....|....*....|....*....
gi 194682608 15 ANETPIIDVRAPIEFNQGAMPNAINLPLM 43
Cdd:pfam00581 3 DGKVVLIDVRPPEEYAKGHIPGAVNVPLS 31
|
|
| |
