|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
1-377 |
0e+00 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 691.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 1 MSDGIVIIGSGFAARQLVKNIRKQDPNIPLTLIAADSMDEYNKPDLSHVVSRGQNADDLTLQTAGEFAEQYNLRLFPHTW 80
Cdd:PRK04965 1 MSNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVFSQGQRADDLTRQSAGEFAEQFNLRLFPHTW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 81 VSDIDADNQVVKSQDREWRYDKLVLATGATPFIPPVPGRELMLTLNSQREYGAAQSQLRDAKRVLIVGGGLIGCELAMDF 160
Cdd:PRK04965 81 VTDIDAEAQVVKSQGNQWQYDKLVLATGASAFVPPIPGRELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAMDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 161 CRAGKAVTVVDNSASVLSALMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQRTLTVDAVVAAAGLRPE 240
Cdd:PRK04965 161 CRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRATLDSGRSIEVDAVIAAAGLRPN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 241 TALARHAGLQTHRGVVVNSQLQTSHPAIYALGDCAEINGMVLPFLQPILLSAMCLGKNLLTQQGELKLPPMLVKVKTPDL 320
Cdd:PRK04965 241 TALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEINGQVLPFLQPIQLSAMALAKNLLGQNTPLKLPAMLVKVKTPEL 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1730651606 321 PLHLAGDTRREDLTWHIVAAKDGLVAKGVDAENQLRAFVVSEDRMKDAFALLKQLVS 377
Cdd:PRK04965 321 PLQLAGETQRQDLRWQINAESQGMVAKGVDEAGQLRAFVVSEDRMKEAFPLLKELPV 377
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
2-376 |
1.18e-113 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 336.73 E-value: 1.18e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 2 SDGIVIIGSGFAARQLVKNIRKQDPNIPLTLIAADSMDEYNKPDLSHVVSRGQNADDLTLQTAgEFAEQYNLRLFPHTWV 81
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPA-DFYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 82 SDIDADNQVVKSQD-REWRYDKLVLATGATPFIPPVPGREL--MLTLNSQREYGAAQSQLRDAKRVLIVGGGLIGCELAM 158
Cdd:COG1251 80 TAIDRAARTVTLADgETLPYDKLVLATGSRPRVPPIPGADLpgVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 159 DFCRAGKAVTVVDNSASVLSALMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQRTLTVDAVVAAAGLR 238
Cdd:COG1251 160 ALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 239 PETALARHAGLQTHRGVVVNSQLQTSHPAIYALGDCAEINGMV-----LPFLQPILLSAMCLGKNLLTQQGELKLPPMLV 313
Cdd:COG1251 240 PNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVygrrvLELVAPAYEQARVAAANLAGGPAAYEGSVPST 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1730651606 314 KVKTPDLPLHLAGDTRREDLTWHIVAAKDGLVAKGVDAENQLRAFVVSEDrmKDAFALLKQLV 376
Cdd:COG1251 320 KLKVFGVDVASAGDAEGDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGD--TSDAGALRQLI 380
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
23-277 |
2.38e-64 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 207.74 E-value: 2.38e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 23 KQDPNIPLTLIAADSMDEYNKPDLSHVVSRG-QNADDLTLQTAgEFAEQYNLRLFPHTWVSDIDADNQVVKSQD-REWRY 100
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGiKDPEDLLVRTP-ESFERKGIDVRTGTEVTAIDPEAKTVTLRDgETLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 101 DKLVLATGATPFIPPVPGREL--MLTLNSQREYGAAQSQLR--DAKRVLIVGGGLIGCELAMDFCRAGKAVTVVDNSASV 176
Cdd:COG0446 80 DKLVLATGARPRPPPIPGLDLpgVFTLRTLDDADALREALKefKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 177 LSAlMPPEASSRLQHRLTDMGVDLMLKSQLQSLaQNADGIRVTLDRQRTLTVDAVVAAAGLRPETALARHAGLQTHR--G 254
Cdd:COG0446 160 LGV-LDPEMAALLEEELREHGVELRLGETVVAI-DGDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGErgW 237
|
250 260
....*....|....*....|...
gi 1730651606 255 VVVNSQLQTSHPAIYALGDCAEI 277
Cdd:COG0446 238 IKVDETLQTSDPDVYAAGDCAEV 260
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
5-363 |
2.13e-51 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 183.11 E-value: 2.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 5 IVIIGSGFAARQLVKNIRKQDP-NIPLTLIAADSMDEYNKPDLSHVVSRGQNADDLTLQTAGeFAEQYNLRLFPHTWVSD 83
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNRhMFEITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKD-WYEKHGITLYTGETVIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 84 IDADNQ-VVKSQDREWRYDKLVLATGATPFIPPVPGREL--MLTLNSQREYGAAQSQLRDAKRVLIVGGGLIGCELAMDF 160
Cdd:TIGR02374 80 IDTDQKqVITDAGRTLSYDKLILATGSYPFILPIPGADKkgVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 161 CRAGKAVTVVDNSASVLSALMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQRTLTVDAVVAAAGLRPE 240
Cdd:TIGR02374 160 QNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 241 TALARHAGLQTHRGVVVNSQLQTSHPAIYALGDCAEINGMVLPFLQPILLSAMCLGKNLL-TQQGELKLPPMLVKVKTPD 319
Cdd:TIGR02374 240 DELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICgVECEEYEGSDLSAKLKLLG 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1730651606 320 LPLHLAGDTRREDLTWHIVA--AKDGLVAKGVDAENQLRAFVVSED 363
Cdd:TIGR02374 320 VDVWSAGDAQETERTTSIKIydEQKGIYKKLVLSDDKLLGAVLFGD 365
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
5-274 |
1.61e-50 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 171.35 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 5 IVIIGSGFAARQLVKNIRKQDPNIplTLIAADSMDEYNKPDLSHVVSRGQNADDlTLQTAGEFAEQY---------NLRL 75
Cdd:pfam07992 3 VVVIGGGPAGLAAALTLAQLGGKV--TLIEDEGTCPYGGCVLSKALLGAAEAPE-IASLWADLYKRKeevvkklnnGIEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 76 FPHTWVSDIDADNQVVKSQD------REWRYDKLVLATGATPFIPPVPGRELMLTLNsQREYGAAQsQLRDA---KRVLI 146
Cdd:pfam07992 80 LLGTEVVSIDPGAKKVVLEElvdgdgETITYDRLVIATGARPRLPPIPGVELNVGFL-VRTLDSAE-ALRLKllpKRVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 147 VGGGLIGCELAMDFCRAGKAVTVVDNSASVLSAlMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQRTL 226
Cdd:pfam07992 158 VGGGYIGVELAAALAKLGKEVTLIEALDRLLRA-FDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEI 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1730651606 227 TVDAVVAAAGLRPETALARHAGLQT--HRGVVVNSQLQTSHPAIYALGDC 274
Cdd:pfam07992 237 DADLVVVAIGRRPNTELLEAAGLELdeRGGIVVDEYLRTSVPGIYAAGDC 286
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
84-275 |
1.06e-37 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 140.99 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 84 IDADNQVVKSQDREWRYDKLVLATGATPFIPPVPGRELMLTLNSqreygaaqsqlRDA-------KRVLIVGGGLIGCEL 156
Cdd:COG1249 115 FVDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTS-----------DEAleleelpKSLVVIGGGYIGLEF 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 157 AMDFCRAGKAVTVVDNSASVLSAlMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTL---DRQRTLTVDAVVA 233
Cdd:COG1249 184 AQIFARLGSEVTLVERGDRLLPG-EDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLedgGGEEAVEADKVLV 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1730651606 234 AAGLRPETA---LArHAGLQT--HRGVVVNSQLQTSHPAIYALGDCA 275
Cdd:COG1249 263 ATGRRPNTDglgLE-AAGVELdeRGGIKVDEYLRTSVPGIYAIGDVT 308
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
5-300 |
6.12e-35 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 132.18 E-value: 6.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 5 IVIIGSGFAARQLVKNIRKQ-DPNIPLTLIAADSMDEYnKPDLSHVVSRGQNADDLTLQTAgEFAEQYNLRLFpHTWVSD 83
Cdd:COG1252 4 IVIVGGGFAGLEAARRLRKKlGGDAEVTLIDPNPYHLF-QPLLPEVAAGTLSPDDIAIPLR-ELLRRAGVRFI-QGEVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 84 IDADNQVVKSQDREW-RYDKLVLATGATPFIPPVPG-RELMLTLNSQREYGAAQSQLRDA---------KRVLIVGGGLI 152
Cdd:COG1252 81 IDPEARTVTLADGRTlSYDYLVIATGSVTNFFGIPGlAEHALPLKTLEDALALRERLLAAferaerrrlLTIVVVGGGPT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 153 GCELAM---DFCRAGKA----------VTVVDNSASVLSAlMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNadgiRVT 219
Cdd:COG1252 161 GVELAGelaELLRKLLRypgidpdkvrITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTEVDAD----GVT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 220 LDRQRTLTVDAVVAAAGLRPeTALARHAGLQTHRG--VVVNSQLQT-SHPAIYALGDCAEINGMVLPFL----QPILLSA 292
Cdd:COG1252 236 LEDGEEIPADTVIWAAGVKA-PPLLADLGLPTDRRgrVLVDPTLQVpGHPNVFAIGDCAAVPDPDGKPVpktaQAAVQQA 314
|
....*...
gi 1730651606 293 MCLGKNLL 300
Cdd:COG1252 315 KVLAKNIA 322
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
5-275 |
1.35e-31 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 123.11 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 5 IVIIGSGFAARQLVKNIRKQDPNIPLTLIAADSMDEYNKPDLSHVVSRgQNADDLTLQTAGEFAEQYNLRLFPHTWVSDI 84
Cdd:PRK09754 6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLL-EDSPQLQQVLPANWWQENNVHLHSGVTIKTL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 85 DADNQ-VVKSQDREWRYDKLVLATGATPFIPPVPGR--ELMLTLNSQREYGAAQSQLRDAKRVLIVGGGLIGCELAMDFC 161
Cdd:PRK09754 85 GRDTReLVLTNGESWHWDQLFIATGAAARPLPLLDAlgERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASAT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 162 RAGKAVTVVDNSASVLSALMPPEASSRLQHRLTDMGVDLMLKSQLQSlAQNADGIRVTLDRQRTLTVDAVVAAAGLRPET 241
Cdd:PRK09754 165 QRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEH-VVDGEKVELTLQSGETLQADVVIYGIGISAND 243
|
250 260 270
....*....|....*....|....*....|....
gi 1730651606 242 ALARHAGLQTHRGVVVNSQLQTSHPAIYALGDCA 275
Cdd:PRK09754 244 QLAREANLDTANGIVIDEACRTCDPAIFAGGDVA 277
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
5-287 |
3.80e-31 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 125.23 E-value: 3.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 5 IVIIGSGFAARQLVKN-IRKQDP-NIPLTLIAADSMDEYNKPDLSHVVSRgQNADDLTLQTAGeFAEQYNLRLFPHTWVS 82
Cdd:PRK14989 6 LAIIGNGMVGHRFIEDlLDKADAaNFDITVFCEEPRIAYDRVHLSSYFSH-HTAEELSLVREG-FYEKHGIKVLVGERAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 83 DIDADNQVVKS-QDREWRYDKLVLATGATPFIPPVPGRELM--LTLNSQREYGAAQSQLRDAKRVLIVGGGLIGCELAMD 159
Cdd:PRK14989 84 TINRQEKVIHSsAGRTVFYDKLIMATGSYPWIPPIKGSETQdcFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLEAAGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 160 FCRAGKAVTVVDNSASVLSALMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLD--RQRTLTVDAVVAAAGL 237
Cdd:PRK14989 164 LKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKTMRfaDGSELEVDFIVFSTGI 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1730651606 238 RPETALARHAGLQTHR--GVVVNSQLQTSHPAIYALGDCAEINGMVLPFLQP 287
Cdd:PRK14989 244 RPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAP 295
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
91-274 |
6.20e-31 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 122.62 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 91 VKSQDREWRYDKLVLATGATPFIPPVPG--------RELMLTLNSQREygaaqsqlrdakRVLIVGGGLIGCELAMDFCR 162
Cdd:PRK06370 125 VRVGGETLRAKRIFINTGARAAIPPIPGldevgyltNETIFSLDELPE------------HLVIIGGGYIGLEFAQMFRR 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 163 AGKAVTVVDNSASVLSAlMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLD---RQRTLTVDAVVAAAGLRP 239
Cdd:PRK06370 193 FGSEVTVIERGPRLLPR-EDEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLDcngGAPEITGSHILVAVGRVP 271
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1730651606 240 ET---ALARhAGLQT--HRGVVVNSQLQTSHPAIYALGDC 274
Cdd:PRK06370 272 NTddlGLEA-AGVETdaRGYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
5-282 |
3.85e-30 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 120.15 E-value: 3.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 5 IVIIGSGFAARQLVKNIRKQDPNIPLTLiaadsmdeYNKPDlshVVSRG------------QNADDLTLQTAGEFAEQyN 72
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNKELEITV--------YEKTD---IVSFGacglpyfvggffDDPNTMIARTPEEFIKS-G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 73 LRLFPHTWVSDIDADNQVVKSQDR------EWRYDKLVLATGATPFIPPVPGREL--MLTLNSQREYGAAQSQLRDA--K 142
Cdd:PRK09564 71 IDVKTEHEVVKVDAKNKTITVKNLktgsifNDTYDKLMIATGARPIIPPIKNINLenVYTLKSMEDGLALKELLKDEeiK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 143 RVLIVGGGLIGCELAMDFCRAGKAVTVVDNSASVLSALMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDR 222
Cdd:PRK09564 151 NIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730651606 223 qRTLTVDAVVAAAGLRPETALARHAGLQTHR--GVVVNSQLQTSHPAIYALGDCAEINGMVL 282
Cdd:PRK09564 231 -GEYEADVVIVATGVKPNTEFLEDTGLKTLKngAIIVDEYGETSIENIYAAGDCATIYNIVS 291
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
84-273 |
2.34e-23 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 100.99 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 84 IDADNQV-VKSQDREWRY--DKLVLATGATPFIPP--VPGRELMLTlnsqreYGAAQSQLRDAKRVLIVGGGLIGCELAm 158
Cdd:PRK06416 116 LVDPNTVrVMTEDGEQTYtaKNIILATGSRPRELPgiEIDGRVIWT------SDEALNLDEVPKSLVVIGGGYIGVEFA- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 159 DFCRA-GKAVTVVDnsasVLSALMP---PEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLD---RQRTLTVDAV 231
Cdd:PRK06416 189 SAYASlGAEVTIVE----ALPRILPgedKEISKLAERALKKRGIKIKTGAKAKKVEQTDDGVTVTLEdggKEETLEADYV 264
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1730651606 232 VAAAGLRPETA---LARhAGLQTHRG-VVVNSQLQTSHPAIYALGD 273
Cdd:PRK06416 265 LVAVGRRPNTEnlgLEE-LGVKTDRGfIEVDEQLRTNVPNIYAIGD 309
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
86-274 |
3.77e-23 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 100.19 E-value: 3.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 86 ADNQVVKSQD-REWRYDKLVL-ATGATPFIPPVPG-RELMLTLNSQreygaAQSQLRDAKRVLIVGGGLIGCELAMDFCR 162
Cdd:TIGR02053 113 KDPKTVKVDLgREVRGAKRFLiATGARPAIPPIPGlKEAGYLTSEE-----ALALDRIPESLAVIGGGAIGVELAQAFAR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 163 AGKAVTVVDNSASVLSAlMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLD---RQRTLTVDAVVAAAGLRP 239
Cdd:TIGR02053 188 LGSEVTILQRSDRLLPR-EEPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITVEkpgGQGEVEADELLVATGRRP 266
|
170 180 190
....*....|....*....|....*....|....*....
gi 1730651606 240 ETALA--RHAGLQTHR--GVVVNSQLQTSHPAIYALGDC 274
Cdd:TIGR02053 267 NTDGLglEKAGVKLDErgGILVDETLRTSNPGIYAAGDV 305
|
|
| Nterm_to_SelD |
TIGR03169 |
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family ... |
81-275 |
5.09e-23 |
|
pyridine nucleotide-disulfide oxidoreductase family protein; Members of this protein family include N-terminal sequence regions of (probable) bifunctional proteins whose C-terminal sequences are SelD, or selenide,water dikinase, the selenium donor protein necessary for selenium incorporation into protein (as selenocysteine), tRNA (as 2-selenouridine), or both. However, some members of this family occur in species that do not show selenium incorporation, and the function of this protein family is unknown.
Pssm-ID: 274465 Cd Length: 364 Bit Score: 98.81 E-value: 5.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 81 VSDIDADNQVVKSQDR-EWRYDKLVLATGATPFIPPVPGrelmltlnsQREYGAA----------------QSQLRDAKR 143
Cdd:TIGR03169 76 AIGLDLAAKQVICAGRpPIAYDVLSIDIGSTPALPDVPG---------FAEHAIPakplgqfaqrwqrfleRAKPQQPPR 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 144 VLIVGGGLIGCELAMD----FCRAGK--AVTVVDNSASVLSAlMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNAdgir 217
Cdd:TIGR03169 147 IAVIGGGAAGVELALAmahrLRQLGRnaEVTLIDRGNVLLPG-HNARVRRRLERALQERGVTLHLGATVAEVTADA---- 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730651606 218 VTLDRQRTLTVDAVVAAAGLRPETALARhAGLQTHRG--VVVNSQLQT-SHPAIYALGDCA 275
Cdd:TIGR03169 222 VRLEDGQTLPADFTFWATGARPPGWLAE-SGLALDEDgfIRVGPTLQSlSHPDIFAAGDCA 281
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
87-308 |
4.83e-22 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 96.76 E-value: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 87 DNQVVKSQDREWRYDKLVLATGATPFIPPVPGRELMLTLNsqrEYGAAQSQlrdAKRVLIVGGGLIGCELAMDFCRAGKA 166
Cdd:PRK06116 119 DAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSD---GFFALEEL---PKRVAVVGAGYIAVEFAGVLNGLGSE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 167 VTVVDNSASVLSALmPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADG-IRVTLDRQRTLTVDAVVAAAGLRPETA--- 242
Cdd:PRK06116 193 THLFVRGDAPLRGF-DPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGsLTLTLEDGETLTVDCLIWAIGREPNTDglg 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 243 LARhAGLQTH-RG-VVVNSQLQTSHPAIYALGDCA-EINgmvlpfLQPILLSA-MCLGKNLLTQQGELKL 308
Cdd:PRK06116 272 LEN-AGVKLNeKGyIIVDEYQNTNVPGIYAVGDVTgRVE------LTPVAIAAgRRLSERLFNNKPDEKL 334
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
87-285 |
1.42e-21 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 95.63 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 87 DNQVVKSQDREWRYDKLVLATGATpfIPPVPGRELMLtlnSQREYGaaqsqLRDA-------KRVLIVGGGLIGCELAMD 159
Cdd:PRK06292 118 DPNTVEVNGERIEAKNIVIATGSR--VPPIPGVWLIL---GDRLLT-----SDDAfeldklpKSLAVIGGGVIGLELGQA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 160 FCRAGKAVTVVDNSASVLSaLMPPEASSRLQHRLTDMgVDLMLKSQLQSLAQNADGIRVTLDRQ---RTLTVDAVVAAAG 236
Cdd:PRK06292 188 LSRLGVKVTVFERGDRILP-LEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGgktETIEADYVLVATG 265
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1730651606 237 LRPETAL--ARHAGLQT-HRG-VVVNSQLQTSHPAIYALGDcaeINGMvLPFL 285
Cdd:PRK06292 266 RRPNTDGlgLENTGIELdERGrPVVDEHTQTSVPGIYAAGD---VNGK-PPLL 314
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
77-273 |
2.27e-20 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 92.14 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 77 PHT-WVSDIDADNQVVKSqdrewryDKLVLATGATPFIPP-VPgrelmltLNSQREYGAAQ--SQLRDAKRVLIVGGGLI 152
Cdd:PRK05249 121 PHTvEVECPDGEVETLTA-------DKIVIATGSRPYRPPdVD-------FDHPRIYDSDSilSLDHLPRSLIIYGAGVI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 153 GCELAMDFCRAGKAVTVVDNSASVLSaLMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQRTLTVDAVV 232
Cdd:PRK05249 187 GCEYASIFAALGVKVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLL 265
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1730651606 233 AAAGLRPETA---LArHAGLQT-HRG-VVVNSQLQTSHPAIYALGD 273
Cdd:PRK05249 266 YANGRTGNTDglnLE-NAGLEAdSRGqLKVNENYQTAVPHIYAVGD 310
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
101-273 |
6.06e-19 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 87.70 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 101 DKLVLATGATPFIPPVPGrelmltlNSQREYGAAQSQLRDA---KRVLIVGGGLIGCELAMDFCRAGKAVTVVDNSASVL 177
Cdd:PRK07846 130 DQVVIAAGSRPVIPPVIA-------DSGVRYHTSDTIMRLPelpESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 178 SALmppeaSSRLQHRLTDMG---VDLMLKSQLQSLAQNADGIRVTLDRQRTLTVDAVVAAAGLRPETAL--ARHAGLQTH 252
Cdd:PRK07846 203 RHL-----DDDISERFTELAskrWDVRLGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGRVPNGDLldAAAAGVDVD 277
|
170 180
....*....|....*....|...
gi 1730651606 253 RG--VVVNSQLQTSHPAIYALGD 273
Cdd:PRK07846 278 EDgrVVVDEYQRTSAEGVFALGD 300
|
|
| Rbx_binding |
pfam18113 |
Rubredoxin binding C-terminal domain; This is the C-terminal domain found in rubredoxin ... |
305-375 |
6.41e-19 |
|
Rubredoxin binding C-terminal domain; This is the C-terminal domain found in rubredoxin reductase (RdxR) present in Pseudomonas aeruginosa. RdxR are important in prokaryotes as they allow for the metabolism of inert n-alkanes and RdxR is also crucial for archaea and anaerobic bacteria in the response to oxidative stress. This domain is known to recognize and bind to rubredoxin.
Pssm-ID: 436282 Cd Length: 71 Bit Score: 79.98 E-value: 6.41e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730651606 305 ELKLPPMLVKVKTPDLPLHLAGDTRREDLTWHIVAAKDGLVAKGVDAENQLRAFVVSEDRMKDAFALLKQL 375
Cdd:pfam18113 1 AVVYPAMPVIVKTPACPLVVAPPAVGAEGEWQIEGDGEGLTARFYDADGQLLGFALTGEAVAQRMALLKQL 71
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
143-220 |
7.58e-19 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 79.94 E-value: 7.58e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1730651606 143 RVLIVGGGLIGCELAMDFCRAGKAVTVVDNSASVLSAlMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTL 220
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPG-FDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
68-275 |
3.02e-18 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 84.02 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 68 AEQYNLRLFpHTWVSDIDADNQ--VVKSQD-REWRYDKLVLATGATPFIPPVPGRELMLTLN-SqreYGAAQ--SQLRDa 141
Cdd:COG0492 67 AERFGAEIL-LEEVTSVDKDDGpfRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGvS---YCATCdgFFFRG- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 142 KRVLIVGGGLIGCELAMDFCRAGKAVTVVDNSASvlsalmpPEASSRLQHRLTDM-GVDLMLKSQLQSLaqNADGI--RV 218
Cdd:COG0492 142 KDVVVVGGGDSALEEALYLTKFASKVTLIHRRDE-------LRASKILVERLRANpKIEVLWNTEVTEI--EGDGRveGV 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1730651606 219 TLDR-----QRTLTVDAVVAAAGLRPETALARHAGLQTHRG--VVVNSQLQTSHPAIYALGDCA 275
Cdd:COG0492 213 TLKNvktgeEKELEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVR 276
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
5-276 |
8.71e-17 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 81.37 E-value: 8.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 5 IVIIGSGFAARQLVKNIRKQDPNIPLTLIAADSMDEYNKPDLSHVVSRGQNA-DDLTLQTAGEFAEQYNLRLFPHTWVSD 83
Cdd:PRK13512 4 IIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDrKYALAYTPEKFYDRKQITVKTYHEVIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 84 IDADNQVVKSQDR------EWRYDKLVLATGATPFIPPVpGRELMLTLNSQREYGAAQSQLR--DAKRVLIVGGGLIGCE 155
Cdd:PRK13512 84 INDERQTVTVLNRktneqfEESYDKLILSPGASANSLGF-ESDITFTLRNLEDTDAIDQFIKanQVDKALVVGAGYISLE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 156 LAMDFCRAGKAVTVVDNSASVLSaLMPPEASSRLQHRLTDMGVDLMLKSQLQSLaqnaDGIRVTLDRQRTLTVDAVVAAA 235
Cdd:PRK13512 163 VLENLYERGLHPTLIHRSDKINK-LMDADMNQPILDELDKREIPYRLNEEIDAI----NGNEVTFKSGKVEHYDMIIEGV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1730651606 236 GLRPETALARHAGLQTHRG--VVVNSQLQTSHPAIYALGDCAE 276
Cdd:PRK13512 238 GTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIIT 280
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
89-279 |
1.78e-16 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 80.56 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 89 QVVKSQDR-EWRYDKLVLATGATPFIPPVPGrelmlTLNSQREYGAAQSQLRDA--KRVLIVGGGLIGCELAMDFCRAGK 165
Cdd:PRK07251 107 EVQAGDEKiELTAETIVINTGAVSNVLPIPG-----LADSKHVYDSTGIQSLETlpERLGIIGGGNIGLEFAGLYNKLGS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 166 AVTVVDnSASVLSALMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQrTLTVDAVVAAAGLRPETAlar 245
Cdd:PRK07251 182 KVTVLD-AASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKNDGDQVLVVTEDE-TYRFDALLYATGRKPNTE--- 256
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1730651606 246 HAGLQ------THRG-VVVNSQLQTSHPAIYALGDcaeING 279
Cdd:PRK07251 257 PLGLEntdielTERGaIKVDDYCQTSVPGVFAVGD---VNG 294
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
66-273 |
1.29e-14 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 74.66 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 66 EFAEQYNLRLFPhtwvsdidadnqvvKSQDREWRYDKLVLATGATPFIPPVPGreLMLTLNSQREYGAAQSQLRDAkRVL 145
Cdd:PRK08010 100 EFINNHSLRVHR--------------PEGNLEIHGEKIFINTGAQTVVPPIPG--ITTTPGVYDSTGLLNLKELPG-HLG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 146 IVGGGLIGCELAMDFCRAGKAVTVVDNSasvlSALMPPE---ASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDr 222
Cdd:PRK08010 163 ILGGGYIGVEFASMFANFGSKVTILEAA----SLFLPREdrdIADNIATILRDQGVDIILNAHVERISHHENQVQVHSE- 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1730651606 223 QRTLTVDAVVAAAGLRPETA--LARHAGLQTHR--GVVVNSQLQTSHPAIYALGD 273
Cdd:PRK08010 238 HAQLAVDALLIASGRQPATAslHPENAGIAVNErgAIVVDKYLHTTADNIWAMGD 292
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
85-274 |
8.58e-13 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 69.41 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 85 DADNQVVKSQD---REWRYDKLVLATGATPFIPPVPGrelmltLNSQREYGAAQSQLRDA--KRVLIVGGGLIGCELAMD 159
Cdd:PRK13748 215 DDQTLIVRLNDggeRVVAFDRCLIATGASPAVPPIPG------LKETPYWTSTEALVSDTipERLAVIGSSVVALELAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 160 FCRAGKAVTVVdnSASVLSALMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQnADGIRVTLDRQRTLTVDAVVAAAGLRP 239
Cdd:PRK13748 289 FARLGSKVTIL--ARSTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAH-VDGEFVLTTGHGELRADKLLVATGRAP 365
|
170 180 190
....*....|....*....|....*....|....*....
gi 1730651606 240 ETA-LARHA-GLQT--HRGVVVNSQLQTSHPAIYALGDC 274
Cdd:PRK13748 366 NTRsLALDAaGVTVnaQGAIVIDQGMRTSVPHIYAAGDC 404
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
142-275 |
1.31e-12 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 68.80 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 142 KRVLIVGGGLIGCELAMDFCRAGKAVTVVDNSASVLSAlMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTL- 220
Cdd:PRK06327 184 KKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAA-ADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYt 262
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730651606 221 ---DRQRTLTVDAVVAAAGLRPETA--LARHAGLQ-THRG-VVVNSQLQTSHPAIYALGDCA 275
Cdd:PRK06327 263 dadGEAQTLEVDKLIVSIGRVPNTDglGLEAVGLKlDERGfIPVDDHCRTNVPNVYAIGDVV 324
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
101-273 |
2.29e-12 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 68.08 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 101 DKLVLATGATPFIPPVPGRELMLTLNSQREYGAAqsqlrdAKRVLIVGGGLIGCELAMDF----CRAGKaVTVVDNSASV 176
Cdd:TIGR01423 153 EHILLATGSWPQMLGIPGIEHCISSNEAFYLDEP------PRRVLTVGGGFISVEFAGIFnaykPRGGK-VTLCYRNNMI 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 177 LSALmPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIR-VTLDRQRTLTVDAVVAAAGLRPETALAR--HAGLQ-TH 252
Cdd:TIGR01423 226 LRGF-DSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKhVTFESGKTLDVDVVMMAIGRVPRTQTLQldKVGVElTK 304
|
170 180
....*....|....*....|..
gi 1730651606 253 RGVV-VNSQLQTSHPAIYALGD 273
Cdd:TIGR01423 305 KGAIqVDEFSRTNVPNIYAIGD 326
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
102-297 |
2.74e-11 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 64.84 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 102 KLVLATGATPFIPPVPGRELMLTLNSqreygaAQSQLRDAKRVLIVGGGLIGCELAMDFCRAGKAVTVVDNSASVLSAL- 180
Cdd:PLN02507 170 HILIATGSRAQRPNIPGKELAITSDE------ALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFd 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 181 --MPPEASSRLQHRltdmGVDLMLKSQLQSLAQNADGIRVTLDRQRTLTVDAVVAAAGLRPETalaRHAGLQT------H 252
Cdd:PLN02507 244 deMRAVVARNLEGR----GINLHPRTNLTQLTKTEGGIKVITDHGEEFVADVVLFATGRAPNT---KRLNLEAvgveldK 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1730651606 253 RGVV-VNSQLQTSHPAIYALGDCA-EINgmvlpfLQPI-LLSAMCLGK 297
Cdd:PLN02507 317 AGAVkVDEYSRTNIPSIWAIGDVTnRIN------LTPVaLMEGTCFAK 358
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
99-275 |
6.99e-11 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 63.23 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 99 RYDKLVLATGAT-PFIPPVPGREL--------MLTLNSQREYGAAQSQLRdaKRVLIVGGGLIgcelAMDfC-----RAG 164
Cdd:COG0493 206 EFDAVFLATGAGkPRDLGIPGEDLkgvhsamdFLTAVNLGEAPDTILAVG--KRVVVIGGGNT----AMD-CartalRLG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 165 -KAVTVVdnsasvlsALMPPEASSRLQHRLTD---MGVDLMLKSQLQSLAQNADG-------IRVTLD------RQR--- 224
Cdd:COG0493 279 aESVTIV--------YRRTREEMPASKEEVEEaleEGVEFLFLVAPVEIIGDENGrvtglecVRMELGepdesgRRRpvp 350
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730651606 225 ------TLTVDAVVAAAGLRPETA-LARHAGLQ-THRG-VVVNSQ-LQTSHPAIYALGDCA 275
Cdd:COG0493 351 iegsefTLPADLVILAIGQTPDPSgLEEELGLElDKRGtIVVDEEtYQTSLPGVFAGGDAV 411
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
101-274 |
3.01e-10 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 61.41 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 101 DKLVLATGATPFIPP--VPGRELMLTLnsqreygaaqSQLRDAKRV---LIV-GGGLIGCELAMDFCRAGKAVTVVDNSA 174
Cdd:PRK07845 141 DVVLIATGASPRILPtaEPDGERILTW----------RQLYDLDELpehLIVvGSGVTGAEFASAYTELGVKVTLVSSRD 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 175 SVLsalmP---PEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQRTLTVDAVVAAAGLRPETA---LARhAG 248
Cdd:PRK07845 211 RVL----PgedADAAEVLEEVFARRGMTVLKRSRAESVERTGDGVVVTLTDGRTVEGSHALMAVGSVPNTAglgLEE-AG 285
|
170 180
....*....|....*....|....*...
gi 1730651606 249 LQTHRG--VVVNSQLQTSHPAIYALGDC 274
Cdd:PRK07845 286 VELTPSghITVDRVSRTSVPGIYAAGDC 313
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
66-170 |
2.63e-08 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 55.25 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 66 EFAEQYNLR---LFPHTwVSDIDADN-----QVVKSQDREWRYDKLVLATGA--TPFIPPVPGREL--MLTLNSQReYGA 133
Cdd:COG2072 88 AYADKFGLRrpiRFGTE-VTSARWDEadgrwTVTTDDGETLTARFVVVATGPlsRPKIPDIPGLEDfaGEQLHSAD-WRN 165
|
90 100 110
....*....|....*....|....*....|....*..
gi 1730651606 134 AqSQLRDaKRVLIVGGGLIGCELAMDFCRAGKAVTVV 170
Cdd:COG2072 166 P-VDLAG-KRVLVVGTGASAVQIAPELARVAAHVTVF 200
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
83-274 |
3.76e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 54.78 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 83 DIDADnqvvksQDREwRYDKLVLATGAT-PFIPPVPGREL------M--LTLNSQREYGAAQSQLRDA--KRVLIVGGGl 151
Cdd:PRK12810 219 DITAE------ELLA-EYDAVFLGTGAYkPRDLGIPGRDLdgvhfaMdfLIQNTRRVLGDETEPFISAkgKHVVVIGGG- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 152 igcELAMDfC-----RAG-KAVTVVDNSAsvlsalMPPEASSRLQHRLTDM-----------GVDLMLksQLQSLA-QNA 213
Cdd:PRK12810 291 ---DTGMD-CvgtaiRQGaKSVTQRDIMP------MPPSRRNKNNPWPYWPmklevsnaheeGVEREF--NVQTKEfEGE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 214 DG-------IRVTL---DRQ------RTLTVDAVVAAAGLR-PETALARHAGLQTH-RGVVVNSQL--QTSHPAIYALGD 273
Cdd:PRK12810 359 NGkvtgvkvVRTELgegDFEpvegseFVLPADLVLLAMGFTgPEAGLLAQFGVELDeRGRVAAPDNayQTSNPKVFAAGD 438
|
.
gi 1730651606 274 C 274
Cdd:PRK12810 439 M 439
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
81-311 |
4.52e-08 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 54.39 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 81 VSDIDADNQVVK-----------SQDREWRYDKLVLATGATPFIPPVPGRE----LMLTLNSQREYGAAQSQ-------- 137
Cdd:PTZ00318 84 VYDVDFEEKRVKcgvvsksnnanVNTFSVPYDKLVVAHGARPNTFNIPGVEerafFLKEVNHARGIRKRIVQcieraslp 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 138 ---LRDAKRVL---IVGGGLIGCELAM---DFCRAGKA-----------VTVVDNSASVLSALmppeaSSRL----QHRL 193
Cdd:PTZ00318 164 ttsVEERKRLLhfvVVGGGPTGVEFAAelaDFFRDDVRnlnpelveeckVTVLEAGSEVLGSF-----DQALrkygQRRL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 194 TDMGVDLMLKSQL------QSLAQNADGIRVTLdrqrtltvdaVVAAAGLRPETALARHAGLQTHRG-VVVNSQLQTSH- 265
Cdd:PTZ00318 239 RRLGVDIRTKTAVkevldkEVVLKDGEVIPTGL----------VVWSTGVGPGPLTKQLKVDKTSRGrISVDDHLRVKPi 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1730651606 266 PAIYALGDCAEINGMVLPFL-QPILLSAMCLGKNLltqQGELKLPPM 311
Cdd:PTZ00318 309 PNVFALGDCAANEERPLPTLaQVASQQGVYLAKEF---NNELKGKPM 352
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
68-239 |
1.62e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 52.23 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 68 AEQYNLRLFPHTWVSDIDADNQ--VVKSQDREWRYDKLVLATG--ATPFIPPVPgrelmltlnsqrEYGAAQSQLRDA-- 141
Cdd:pfam13738 85 ADHFELPINLFEEVTSVKKEDDgfVVTTSKGTYQARYVIIATGefDFPNKLGVP------------ELPKHYSYVKDFhp 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 142 ---KRVLIVGGGLIGCELAMDFCRAGKAVTVVDNSASVLSALMPPEAS------SRLQHRLTDMGVDLMLKSQLQSLAQN 212
Cdd:pfam13738 153 yagQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSDPSYSlspdtlNRLEELVKNGKIKAHFNAEVKEITEV 232
|
170 180
....*....|....*....|....*...
gi 1730651606 213 ADGIRVTLDRQRTLTV-DAVVAAAGLRP 239
Cdd:pfam13738 233 DVSYKVHTEDGRKVTSnDDPILATGYHP 260
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
49-274 |
4.62e-07 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 51.54 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 49 VVSRGQNADDLTLQTAGEFAEQYNLRLFPHTWVSDIDADNQVVKSQDrewrydkLVLATGATPFIPPVPGRELmlTLNSQ 128
Cdd:PTZ00058 159 LLSENQVLIKKVSQVDGEADESDDDEVTIVSAGVSQLDDGQVIEGKN-------ILIAVGNKPIFPDVKGKEF--TISSD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 129 REYgaaqsQLRDAKRVLIVGGGLIGCELAMDFCRAGKAVTVVDNSASVLSALmPPEASSRLQHRLTDMGVDLMLKSQLQS 208
Cdd:PTZ00058 230 DFF-----KIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKF-DETIINELENDMKKNNINIITHANVEE 303
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1730651606 209 LAQNAD-GIRVTL-DRQRTLTVDAVVAAAGLRPETALARHAGL--QTHRG-VVVNSQLQTSHPAIYALGDC 274
Cdd:PTZ00058 304 IEKVKEkNLTIYLsDGRKYEHFDYVIYCVGRSPNTEDLNLKALniKTPKGyIKVDDNQRTSVKHIYAVGDC 374
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
77-299 |
6.54e-07 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 51.03 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 77 PHTwvsdIDADNQVVKSQDrewrydkLVLATGATPFIPPVPGRELMLtlnsqrEYGAAQSQLRDAKRVLIVGGGLIGCEL 156
Cdd:PLN02546 205 PHT----VDVDGKLYTARN-------ILIAVGGRPFIPDIPGIEHAI------DSDAALDLPSKPEKIAIVGGGYIALEF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 157 AMDFCRAGKAVTVVDNSASVLSALmPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIrVTLDRQRTlTVDA---VVA 233
Cdd:PLN02546 268 AGIFNGLKSDVHVFIRQKKVLRGF-DEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGS-LSLKTNKG-TVEGfshVMF 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730651606 234 AAGLRPETalaRHAGLQT-------HRGVVVNSQLQTSHPAIYALGDCAE-INgmvlpfLQPI-LLSAMCLGKNL 299
Cdd:PLN02546 345 ATGRKPNT---KNLGLEEvgvkmdkNGAIEVDEYSRTSVPSIWAVGDVTDrIN------LTPVaLMEGGALAKTL 410
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
99-275 |
6.90e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 50.95 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 99 RYDKLVLATGAT--PFIPpVPGREL--------MLTLNSQREYgaaQSQLRDAKRVLIVGGGligcELAMDfC-----RA 163
Cdd:PRK11749 225 GYDAVFIGTGAGlpRFLG-IPGENLggvysavdFLTRVNQAVA---DYDLPVGKRVVVIGGG----NTAMD-AartakRL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 164 G-KAVTVV-----DNsasvlsalMPpeASSRLQHRLTDMGVDLMLKSQLQSLAQNADG------IRVTL------DRQR- 224
Cdd:PRK11749 296 GaESVTIVyrrgrEE--------MP--ASEEEVEHAKEEGVEFEWLAAPVEILGDEGRvtgvefVRMELgepdasGRRRv 365
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1730651606 225 -------TLTVDAVVAAAGLRPETALARHA-GLQ-THRG--VVVNSQLQTSHPAIYALGDCA 275
Cdd:PRK11749 366 piegsefTLPADLVIKAIGQTPNPLILSTTpGLElNRWGtiIADDETGRTSLPGVFAGGDIV 427
|
|
| Lys_Orn_oxgnase |
pfam13434 |
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold ... |
96-239 |
5.31e-06 |
|
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold oxidoreductases that catalyze NADPH-dependent hydroxylation and are involved in siderophore biosynthesis. This family includes L-ornithine 5-monooxygenase, which catalyzes the hydroxylation of L-ornithine at the N5 position, and L-lysine 6-monooxygenase, which catalyzes the hydroxylation of lysine at the N6 position (EC:1.14.13.59).
Pssm-ID: 433204 [Multi-domain] Cd Length: 338 Bit Score: 47.97 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 96 REWRYDKLVLATGATPFIPP-VPGRELMLTlNSqrEYGAAQSQLRDAKRVLIVGGGLIGCELAMDFCRAGKAVTVV---- 170
Cdd:pfam13434 144 TTFLARNLVLGTGGEPYIPEcARGGERVFH-SS--EYLERIDRLAAKKRIAVVGSGQSAAEIFRDLLRRGPAYELTwvtr 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 171 -------DNSASVLSALMP---------PE----ASSRLQHRLTDMGVD-----------------------LMLKSQLQ 207
Cdd:pfam13434 221 spnffplDDSPFVNEIFSPeyvdyfyslPEdtrrALLREQKGTNYDGIDpslieeiyrllyeqrvdgdprhrLLPNREVQ 300
|
170 180 190
....*....|....*....|....*....|....*...
gi 1730651606 208 SLAQNADG-IRVTL-----DRQRTLTVDAVVAAAGLRP 239
Cdd:pfam13434 301 SAERVGDGgVELTLrdgeqGREETLETDVVVLATGYRR 338
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
133-274 |
1.62e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 46.65 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 133 AAQSQLRDAKRVLIVGGGLIGCELAMDFCRAG-KAVTVVDNSASvlsALMPPEASsRLQHRLTDmGVDLMLKSQLQSLAQ 211
Cdd:PRK12814 315 ALGTALHPGKKVVVIGGGNTAIDAARTALRLGaESVTILYRRTR---EEMPANRA-EIEEALAE-GVSLRELAAPVSIER 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 212 NADGIRVT--------LD---RQR---------TLTVDAVVAAAGLRPETALARHAGLQTHRG--VVVNSQ-LQTSHPAI 268
Cdd:PRK12814 390 SEGGLELTaikmqqgePDesgRRRpvpvegsefTLQADTVISAIGQQVDPPIAEAAGIGTSRNgtVKVDPEtLQTSVAGV 469
|
....*.
gi 1730651606 269 YALGDC 274
Cdd:PRK12814 470 FAGGDC 475
|
|
| ThiF |
pfam00899 |
ThiF family; This domain is found in ubiquitin activating E1 family and members of the ... |
133-172 |
2.47e-05 |
|
ThiF family; This domain is found in ubiquitin activating E1 family and members of the bacterial ThiF/MoeB/HesA family. It is repeated in Ubiquitin-activating enzyme E1.
Pssm-ID: 459987 [Multi-domain] Cd Length: 238 Bit Score: 45.33 E-value: 2.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1730651606 133 AAQSQLRDAkRVLIVGGGLIGCELAMDFCRAG-KAVTVVDN 172
Cdd:pfam00899 13 DGQEKLRNS-RVLIVGAGGLGSEAAKYLARAGvGKITLVDF 52
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
142-274 |
1.46e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 43.61 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 142 KRVLIVGGGLIGCELAMDFcrAG--KAVTVVDnsasVLSALmppEASSRLQHRLTDMG-VDLMLKSQLQSLaqNADGIRV 218
Cdd:PRK15317 352 KRVAVIGGGNSGVEAAIDL--AGivKHVTVLE----FAPEL---KADQVLQDKLRSLPnVTIITNAQTTEV--TGDGDKV 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1730651606 219 T----LDR----QRTLTVDAVVAAAGLRPETALARHAGLQTHRG-VVVNSQLQTSHPAIYALGDC 274
Cdd:PRK15317 421 TgltyKDRttgeEHHLELEGVFVQIGLVPNTEWLKGTVELNRRGeIIVDARGATSVPGVFAAGDC 485
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
143-272 |
6.03e-04 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 41.61 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 143 RVLIVGGGLIGCELAMDFCRAGKAVTVVD-----------NSASVLSALMPP-----------EASSRLQHRLTDMGVDL 200
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLErgddpgsgasgRNAGLIHPGLRYlepselarlalEALDLWEELEEELGIDC 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730651606 201 MLKSQ--LQsLAQNA--DGIRVTLDRQRTLTVDAVVaaagLRPETALARHAGLQTHRGVVVNSQLQTSHPAIYALG 272
Cdd:pfam01266 81 GFRRCgvLV-LARDEeeEALEKLLAALRRLGVPAEL----LDAEELRELEPLLPGLRGGLFYPDGGHVDPARLLRA 151
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
189-238 |
1.11e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 40.69 E-value: 1.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1730651606 189 LQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQRTLTVDAVVAAAGLR 238
Cdd:COG0654 110 LLEAARALGVELRFGTEVTGLEQDADGVTVTLADGRTLRADLVVGADGAR 159
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
188-253 |
1.23e-03 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 40.34 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1730651606 188 RLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQRTLTVDAVVAAAGLRpeTALARHAGLQTHR 253
Cdd:COG0644 91 WLAEQAEEAGAEVRTGTRVTDVLRDDGRVVVRTGDGEEIRADYVVDADGAR--SLLARKLGLKRRS 154
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
143-253 |
1.89e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.89 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 143 RVLIVGGGLIGC----ELAmdfcRAGKAVTVVD----------NSASVLSALMPPEASSRLqHRLTDMGVDLmlksqLQS 208
Cdd:COG0665 4 DVVVIGGGIAGLstayHLA----RRGLDVTVLErgrpgsgasgRNAGQLRPGLAALADRAL-VRLAREALDL-----WRE 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1730651606 209 LAQNAdGIRVTLDRQRTLTVDAVVA-AAGLRPETALARHAGLQTHR 253
Cdd:COG0665 74 LAAEL-GIDCDFRRTGVLYLARTEAeLAALRAEAEALRALGLPVEL 118
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
102-276 |
2.84e-03 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 39.45 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 102 KLVLATGATPFIPPVPGrelmltlnsQREYGAAQSQL----RDAKRVLIVGGGLIGCELAMDFCRAGKAVTVVdnSASVL 177
Cdd:TIGR01438 146 RFLIATGERPRYPGIPG---------AKELCITSDDLfslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVM--VRSIL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 178 SALMPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQRTLTV---DAVVAAAGLRPETalaRHAGLQThRG 254
Cdd:TIGR01438 215 LRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLVEFTDSTNGIEeeyDTVLLAIGRDACT---RKLNLEN-VG 290
|
170 180 190
....*....|....*....|....*....|.
gi 1730651606 255 VVVNSQL---------QTSHPAIYALGDCAE 276
Cdd:TIGR01438 291 VKINKKTgkipadeeeQTNVPYIYAVGDILE 321
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
142-239 |
3.18e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 39.46 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 142 KRVLIVGGGLIGCELAMDFCRAGKAVTVV--------------------DNSASVLSALMppeasSRLQ-HRLtdmgVDL 200
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVekepelggraaqlhktfpglDCPQCILEPLI-----AEVEaNPN----ITV 211
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1730651606 201 MLKSQLQSLAQNADGIRVTLDR----QRTLTVDAVVAAAGLRP 239
Cdd:COG1148 212 YTGAEVEEVSGYVGNFTVTIKKgpreEIEIEVGAIVLATGFKP 254
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
103-306 |
4.09e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 39.04 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 103 LVLATGATPFIP-PVPG-RELMLTLNSqreygaAQSQLRDAKRVLIVGGGLIGCELAMDFCRAGKAVTVVDNSAsVLSAL 180
Cdd:PTZ00052 148 ILIATGGRPSIPeDVPGaKEYSITSDD------IFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSI-PLRGF 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 181 mPPEASSRLQHRLTDMGVDLMLKSQLQSLAQNADGIRVTLDRQRTLTVDAVVAAAGLRPETAlarhaGLQTHR-GVVVNS 259
Cdd:PTZ00052 221 -DRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDDKIKVLFSDGTTELFDTVLYATGRKPDIK-----GLNLNAiGVHVNK 294
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1730651606 260 QLQ-------TSHPAIYALGDCAEingmVLPFLQPILLSA-MCLGKNLLTQQGEL 306
Cdd:PTZ00052 295 SNKiiapndcTNIPNIFAVGDVVE----GRPELTPVAIKAgILLARRLFKQSNEF 345
|
|
| trkA |
PRK09496 |
Trk system potassium transporter TrkA; |
99-182 |
9.64e-03 |
|
Trk system potassium transporter TrkA;
Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 37.79 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1730651606 99 RYDKLVLATGATPFippVPGRELMLTLNSQ---REYGAAQSQLRDAKRVLIVGGGLIGCELAMDFCRAGKAVTVVDNS-- 173
Cdd:PRK09496 189 RGGRLIIPRGDTVI---EAGDEVYFIGAREhirAVMSEFGRLEKPVKRVMIVGGGNIGYYLAKLLEKEGYSVKLIERDpe 265
|
90
....*....|
gi 1730651606 174 -ASVLSALMP 182
Cdd:PRK09496 266 rAEELAEELP 275
|
|
| |
