|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
1-321 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 619.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 1 MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFDTEI 80
Cdd:PRK10262 1 MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 81 IFDHINSVDLQNRPFRLVGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVE 160
Cdd:PRK10262 81 IFDHINKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 161 EALYLSNIASEVHLIHRRDTFRAEKILINRLMDKVANGNIVLHTHRTLEEVTGDQMGVSGLRLRDTQNADNVESLEVAGL 240
Cdd:PRK10262 161 EALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 241 FVAIGHSPNTAIFEGQLALENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA 320
Cdd:PRK10262 241 FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA 320
|
.
gi 490998305 321 C 321
Cdd:PRK10262 321 K 321
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
8-314 |
2.46e-167 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 467.10 E-value: 2.46e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFDTEIIFDHINS 87
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 88 VDLQNRPFRLV-GDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLS 166
Cdd:TIGR01292 81 VDKSDRPFKVYtGDGKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 167 NIASEVHLIHRRDTFRAEKILINRLMDkvaNGNIVLHTHRTLEEVTGDQmGVSGLRLRDTQNADnVESLEVAGLFVAIGH 246
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLKK---NPKIEFLWNSTVEEIVGDN-KVEGVKIKNTVTGE-EEELEVDGVFIAIGH 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490998305 247 SPNTAIFEGQLAL-ENGYIKVQSGihgnaTQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
Cdd:TIGR01292 236 EPNTELLKGLLELdENGYIVTDEG-----MRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
8-317 |
2.05e-156 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 439.56 E-value: 2.05e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFDTEIIFDHINS 87
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEEVTS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 88 VDLQNRPFRLVGDSG-EYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLS 166
Cdd:COG0492 82 VDKDDGPFRVTTDDGtEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 167 NIASEVHLIHRRDTFRAEKILINRLMdkvANGNIVLHTHRTLEEVTGDQmGVSGLRLRDTQNaDNVESLEVAGLFVAIGH 246
Cdd:COG0492 162 KFASKVTLIHRRDELRASKILVERLR---ANPKIEVLWNTEVTEIEGDG-RVEGVTLKNVKT-GEEKELEVDGVFVAIGL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490998305 247 SPNTAIFEGQ-LAL-ENGYIKVqsgihGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGL 317
Cdd:COG0492 237 KPNTELLKGLgLELdEDGYIVV-----DEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
9-317 |
3.59e-67 |
|
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase homologs is found adjacent to alkylhydroperoxide reductase C subunit predominantly in cases where there is only one C subunit in the genome and that genome is lacking the F subunit partner (also a thioredcxin reductase homolog) that is usually found (TIGR03140).
Pssm-ID: 132187 [Multi-domain] Cd Length: 555 Bit Score: 219.65 E-value: 3.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 9 LLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNdLTGPLLMERMHEHATKFDTEIIFDHINSV 88
Cdd:TIGR03143 7 LIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILN-TTGPELMQEMRQQAQDFGVKFLQAEVLDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 89 DLQNRPFRLVGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNI 168
Cdd:TIGR03143 86 DFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLTRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 169 ASEVHLIHRRDTFRAEKILINRLMdkvANGNIVLHTHRTLEEVTGDQM--------GVSGLRLRDTQNADNveslEVAGL 240
Cdd:TIGR03143 166 ASKVTVIVREPDFTCAKLIAEKVK---NHPKIEVKFNTELKEATGDDGlryakfvnNVTGEITEYKAPKDA----GTFGV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490998305 241 FVAIGHSPNTAIFEGQLAL-ENGYIkvqsgIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGL 317
Cdd:TIGR03143 239 FVFVGYAPSSELFKGVVELdKRGYI-----PTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYVKEL 311
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
10-314 |
5.50e-64 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 210.40 E-value: 5.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 10 LILGSGPAGYTAAVYAARANLQpvliTGM--EK-GGQLTTTTEVENWPGDPnDLTGPLLMERMHEHATKFDTEIIfDHIN 86
Cdd:PRK15317 215 LVVGGGPAGAAAAIYAARKGIR----TGIvaERfGGQVLDTMGIENFISVP-ETEGPKLAAALEEHVKEYDVDIM-NLQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 87 SVDL--QNRPFRLVGDSGE-YTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEAL 163
Cdd:PRK15317 289 ASKLepAAGLIEVELANGAvLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAI 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 164 YLSNIASEVHLIHRRDTFRAEKILINRLMdkvANGNIVLHTHRTLEEVTGDQMGVSGLRLRDtQNADNVESLEVAGLFVA 243
Cdd:PRK15317 369 DLAGIVKHVTVLEFAPELKADQVLQDKLR---SLPNVTIITNAQTTEVTGDGDKVTGLTYKD-RTTGEEHHLELEGVFVQ 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998305 244 IGHSPNTAIFEGQLALEN-GYIKVQSgiHGnatQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
Cdd:PRK15317 445 IGLVPNTEWLKGTVELNRrGEIIVDA--RG---ATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
8-303 |
2.39e-58 |
|
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: 189.84 E-value: 2.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 8 KLLILGSGPAGYTAAVYAARANLQPVLIT--GMEKGGQLTTTTEVENWPGDPNDL-TGPLLMERMHEHATKFDTEIIF-- 82
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdeGTCPYGGCVLSKALLGAAEAPEIAsLWADLYKRKEEVVKKLNNGIEVll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 83 -DHINSVDLQNRPFRL----VGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRN--QKVAVIGGG 155
Cdd:pfam07992 82 gTEVVSIDPGAKKVVLeelvDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLlpKRVVVVGGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 156 NTAVEEALYLSNIASEVHLIHRRDTF--RAEKILINRLMDKVANGNIVLHTHRTLEEVTGDQMGVsglrlrdTQNADNVE 233
Cdd:pfam07992 162 YIGVELAAALAKLGKEVTLIEALDRLlrAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGV-------EVILKDGT 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998305 234 SLEVAGLFVAIGHSPNTAIFE--GQLALENGYIKVQSGIhgnatQTSIPGVFAAGDVMDHIYRQAITSAGTG 303
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEaaGLELDERGGIVVDEYL-----RTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
4-288 |
3.68e-22 |
|
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: 96.31 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 4 TKHSKLLILGSGPAGYTAAVYAARANLQPVLItgmEK---GG------------------QLTTTTEVEN--WPGDPNDL 60
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALV---EKgrlGGtclnvgcipskallhaaeVAHEARHAAEfgISAGAPSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 61 TGPLLMERMHEHATKFDTEIIF-------DHINS----VDlqnrPFRL-VGDSGEYTCDALIIATGASARYLglPSEEAF 128
Cdd:COG1249 78 DWAALMARKDKVVDRLRGGVEEllkkngvDVIRGrarfVD----PHTVeVTGGETLTADHIVIATGSRPRVP--PIPGLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 129 KGRGVsacaTCDGFFYRNQ---KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTF--RAEKILINRLMDKVANGNIVLH 203
Cdd:COG1249 152 EVRVL----TSDEALELEElpkSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpGEDPEISEALEKALEKEGIDIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 204 THRTLEEVTGDQmgvSGLRLRdTQNADNVESLEVAGLFVAIGHSPNTAifegQLALEN--------GYIKVqsgihgNAT 275
Cdd:COG1249 228 TGAKVTSVEKTG---DGVTVT-LEDGGGEEAVEADKVLVATGRRPNTD----GLGLEAagvelderGGIKV------DEY 293
|
330
....*....|....
gi 490998305 276 -QTSIPGVFAAGDV 288
Cdd:COG1249 294 lRTSVPGIYAIGDV 307
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
65-294 |
5.66e-21 |
|
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: 91.41 E-value: 5.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 65 LMERMHEHATKFDTEIIFDH-INSVDLQNRpfRLVGDSGE-YTCDALIIATGASARYL---GLPSEEAFKGRGVSACATC 139
Cdd:COG0446 38 LLVRTPESFERKGIDVRTGTeVTAIDPEAK--TVTLRDGEtLSYDKLVLATGARPRPPpipGLDLPGVFTLRTLDDADAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 140 DGFFYRN--QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTF--RAEKILINRLMDKVANGNIVLHTHRTLEEVTGDq 215
Cdd:COG0446 116 REALKEFkgKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLlgVLDPEMAALLEEELREHGVELRLGETVVAIDGD- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 216 mGVSGLRLRDTqnadnvESLEVAGLFVAIGHSPNTAIFEG-QLAL-ENGYIKVqsgihgNAT-QTSIPGVFAAGDVMDHI 292
Cdd:COG0446 195 -DKVAVTLTDG------EEIPADLVVVAPGVRPNTELAKDaGLALgERGWIKV------DETlQTSDPDVYAAGDCAEVP 261
|
..
gi 490998305 293 YR 294
Cdd:COG0446 262 HP 263
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
103-292 |
9.84e-21 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 92.14 E-value: 9.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 103 EYTCDALIIATGASARYLGLPseeafkgrGVSACATCDGFFYRN---QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD 179
Cdd:PRK06116 129 RYTADHILIATGGRPSIPDIP--------GAEYGITSDGFFALEelpKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 180 TF--RAEKILINRLMDKVANGNIVLHTHRTLEEVTGDQMGVSGLRLrdtqnaDNVESLEVAGLFVAIGHSPNTAifegQL 257
Cdd:PRK06116 201 APlrGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTL------EDGETLTVDCLIWAIGREPNTD----GL 270
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490998305 258 ALEN--------GYIKVQsgihgNATQTSIPGVFAAGDVMDHI 292
Cdd:PRK06116 271 GLENagvklnekGYIIVD-----EYQNTNVPGIYAVGDVTGRV 308
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
9-288 |
2.24e-19 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 88.31 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 9 LLILGSGPAGYTAAVYAARANLQPVLItgmEKGgQLTTT-------------------TEVENWP-----GDPNDLTGPL 64
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALI---EKG-PLGGTclnvgcipskaliaaaeafHEAKHAEefgihADGPKIDFKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 65 LMERMHE---HATKFDTEIIfDHINSVDL---------QNRpfRLVGDSgEYTCDALIIATGAsaRYLGLPSEEAFKGRG 132
Cdd:PRK06292 82 VMARVRRerdRFVGGVVEGL-EKKPKIDKikgtarfvdPNT--VEVNGE-RIEAKNIVIATGS--RVPPIPGVWLILGDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 133 VsacATCDGFFYRN---QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTF-RAEKILINRLMDKVANGNIVLHTHRTL 208
Cdd:PRK06292 156 L---LTSDDAFELDklpKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlPLEDPEVSKQAQKILSKEFKIKLGAKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 209 EEVTGDQmgvsGLRLRDTQNADNVESLEVAGLFVAIGHSPNTAIfegqLALEN--------GYIKVqsgihGNATQTSIP 280
Cdd:PRK06292 233 TSVEKSG----DEKVEELEKGGKTETIEADYVLVATGRRPNTDG----LGLENtgielderGRPVV-----DEHTQTSVP 299
|
....*...
gi 490998305 281 GVFAAGDV 288
Cdd:PRK06292 300 GIYAAGDV 307
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
6-288 |
2.53e-18 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 84.81 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 6 HSKLLILGSGPAGYTAA-VYAARANLQPVLITGMEKGG-----QLttttevenwpgdPNDLTGPLLMERMHEHATKF--- 76
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAeELRKLDPDGEITVIGAEPHPpynrpPL------------SKVLAGETDEEDLLLRPADFyee 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 77 -DTEIIF-DHINSVDLQNRpfRLVGDSGE-YTCDALIIATGASARYLGLPSEEAfkgRGVsacatcdgFFYRN------- 146
Cdd:COG1251 69 nGIDLRLgTRVTAIDRAAR--TVTLADGEtLPYDKLVLATGSRPRVPPIPGADL---PGV--------FTLRTlddadal 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 147 -------QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTfraekiLINRLMDKVA----------NGnIVLHTHRTLE 209
Cdd:COG1251 136 raalapgKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPR------LLPRQLDEEAgallqrlleaLG-VEVRLGTGVT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 210 EVTGDQmGVSGLRLRDTqnadnvESLEVAGLFVAIGHSPNTAifegqLALENGyIKVQSGIHGNAT-QTSIPGVFAAGDV 288
Cdd:COG1251 209 EIEGDD-RVTGVRLADG------EELPADLVVVAIGVRPNTE-----LARAAG-LAVDRGIVVDDYlRTSDPDIYAAGDC 275
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
16-286 |
9.61e-17 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 79.19 E-value: 9.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 16 PAGYTAAVYAARANLQPVLItgMEKG------------GQLTTTTEVENWPGDP------NDLTGPLLMERMH------- 70
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDYLI--LEKGnignsfyrypthMTFFSPSFTSNGFGIPdlnaisPGTSPAFTFNREHpsgneya 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 71 ----EHATKFDTEII-FDHINSVDLQNRPFRLVGDSGEYTCDALIIATG--ASARYLGLPsEEAFKGRGVSACATcdgff 143
Cdd:pfam13738 79 eylrRVADHFELPINlFEEVTSVKKEDDGFVVTTSKGTYQARYVIIATGefDFPNKLGVP-ELPKHYSYVKDFHP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 144 YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTFRAEK---------ILINRLMDKVANGNIVLHTHRTLEEVTGD 214
Cdd:pfam13738 153 YAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDsdpsyslspDTLNRLEELVKNGKIKAHFNAEVKEITEV 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490998305 215 QMGVsglrlrdTQNADNVESLEVAGLFV-AIGHSPNTAIFEGQLAL--ENGYIKVQSgihgnATQ-TSIPGVFAAG 286
Cdd:pfam13738 233 DVSY-------KVHTEDGRKVTSNDDPIlATGYHPDLSFLKKGLFEldEDGRPVLTE-----ETEsTNVPGLFLAG 296
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
8-288 |
1.35e-16 |
|
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: 79.79 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEK-GGQLT------------TTTEVEnwpgdpndltgplLMERMhehAT 74
Cdd:COG0493 123 KVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKpGGLLRygipefrlpkdvLDREIE-------------LIEAL---GV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 75 KFDTEIIFDHINSVD-LQNrpfrlvgdsgEYtcDALIIATGAS-ARYLGLPSEEAfKG--------RGVSACATCDGFFY 144
Cdd:COG0493 187 EFRTNVEVGKDITLDeLLE----------EF--DAVFLATGAGkPRDLGIPGEDL-KGvhsamdflTAVNLGEAPDTILA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 145 RNQKVAVIGGGNTAVE---EALYLSniASEVHLIHRRD----TFRAEKIlinrlMDKVANGnIVLHTHRTLEEVTGDQMG 217
Cdd:COG0493 254 VGKRVVVIGGGNTAMDcarTALRLG--AESVTIVYRRTreemPASKEEV-----EEALEEG-VEFLFLVAPVEIIGDENG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 218 -VSGLRLRDTQNADNVES-----LEVAG---------LFVAIGHSPNTAIFEGQLALE---NGYIKVqsgiHGNATQTSI 279
Cdd:COG0493 326 rVTGLECVRMELGEPDESgrrrpVPIEGseftlpadlVILAIGQTPDPSGLEEELGLEldkRGTIVV----DEETYQTSL 401
|
....*....
gi 490998305 280 PGVFAAGDV 288
Cdd:COG0493 402 PGVFAGGDA 410
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
107-320 |
6.17e-16 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 77.91 E-value: 6.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 107 DALIIATGASA-RYLGLPSEEAfkgRGV-SAC--------ATCDGFFYRNQKVAVIGGGNTA---VEEALYLSniASEVH 173
Cdd:PRK11749 227 DAVFIGTGAGLpRFLGIPGENL---GGVySAVdfltrvnqAVADYDLPVGKRVVVIGGGNTAmdaARTAKRLG--AESVT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 174 LIHRRD----TFRAEKILINRlmdkvANGnIVLHTHRTLEEVTGDQMGVSGLRLRDTQNADNVES-------------LE 236
Cdd:PRK11749 302 IVYRRGreemPASEEEVEHAK-----EEG-VEFEWLAAPVEILGDEGRVTGVEFVRMELGEPDASgrrrvpiegseftLP 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 237 VAGLFVAIGHSPNTAIFEGQLALE---NGYIKVqsgihGNAT-QTSIPGVFAAGDVMdhiyRQA---ITSAGTGCMAALD 309
Cdd:PRK11749 376 ADLVIKAIGQTPNPLILSTTPGLElnrWGTIIA-----DDETgRTSLPGVFAGGDIV----TGAatvVWAVGDGKDAAEA 446
|
250
....*....|.
gi 490998305 310 AERYLDGLADA 320
Cdd:PRK11749 447 IHEYLEGAASA 457
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
148-226 |
1.16e-14 |
|
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: 68.00 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 148 KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTFRA--EKILINRLMDKVANGNIVLHTHRTLEEVTGDQMGVsGLRLRD 225
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPgfDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV-VVVLTD 79
|
.
gi 490998305 226 T 226
Cdd:pfam00070 80 G 80
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
8-288 |
1.52e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 73.63 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVenwPG------DPNDLTGPLLmermhEHATKFDTEII 81
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKKLGGDAEVTLIDPNPYHLFQPLL---PEvaagtlSPDDIAIPLR-----ELLRRAGVRFI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 82 FDHINSVDLQNRpfRLVGDSG-EYTCDALIIATGASARYLGLPSEEAFkgrGVSACATCDGFFYRNQ------------- 147
Cdd:COG1252 75 QGEVTGIDPEAR--TVTLADGrTLSYDYLVIATGSVTNFFGIPGLAEH---ALPLKTLEDALALRERllaaferaerrrl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 148 -KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTFRAEKILINRlMDKVANG----------------NIVLHTHRTLEE 210
Cdd:COG1252 150 lTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDKVRITLVEA-GPRILPGlgeklseaaekelekrGVEVHTGTRVTE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 211 VTGDqmgvsGLRLRDTqnadnvESLEVAGLFVAIGHSPNTAIFEGQLAL-ENGYIKVqsgihgNATQTSI--PGVFAAGD 287
Cdd:COG1252 229 VDAD-----GVTLEDG------EEIPADTVIWAAGVKAPPLLADLGLPTdRRGRVLV------DPTLQVPghPNVFAIGD 291
|
.
gi 490998305 288 V 288
Cdd:COG1252 292 C 292
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
5-316 |
2.34e-14 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 73.13 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 5 KHSKLLILGSGPAGYTAAVYAARANLQPVLITGM-EKGGQLT-------------TTTEVENwpgdpndltgpllmerMH 70
Cdd:PRK12831 139 KGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALhEPGGVLVygipefrlpketvVKKEIEN----------------IK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 71 EHATKFDTEIIFDHINSVD--LQNRPFrlvgdsgeytcDALIIATGAS-ARYLGLPSEEAfkgRGV-SAC---------- 136
Cdd:PRK12831 203 KLGVKIETNVVVGKTVTIDelLEEEGF-----------DAVFIGSGAGlPKFMGIPGENL---NGVfSANefltrvnlmk 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 137 ATCDGF---FYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD----TFRAEKI------------LINR---LMDk 194
Cdd:PRK12831 269 AYKPEYdtpIKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVYRRSeeelPARVEEVhhakeegvifdlLTNPveiLGD- 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 195 vANGNIVLHTHRTLEEVTGDQMGvsglRLRDTQNADNVESLEVAGLFVAIGHSPNTAIFEGQLALE---NGYIKVQSgih 271
Cdd:PRK12831 348 -ENGWVKGMKCIKMELGEPDASG----RRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTKGLKinkRGCIVADE--- 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 490998305 272 gNATQTSIPGVFAAGDvmdhiyrqAITSAGT-------GCMAALDAERYLDG 316
Cdd:PRK12831 420 -ETGLTSKEGVFAGGD--------AVTGAATvilamgaGKKAAKAIDEYLSK 462
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
107-291 |
1.41e-12 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 68.32 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 107 DALIIATGASARYLGLPSEE---AFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTFRA 183
Cdd:TIGR02374 98 DKLILATGSYPFILPIPGADkkgVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMA 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 184 EKI--LINRLM-DKVANGNIVLHTHRTLEEVTGDQMgVSGLRLRDTqnadnvESLEVAGLFVAIGHSPNTaifegQLALE 260
Cdd:TIGR02374 178 KQLdqTAGRLLqRELEQKGLTFLLEKDTVEIVGATK-ADRIRFKDG------SSLEADLIVMAAGIRPND-----ELAVS 245
|
170 180 190
....*....|....*....|....*....|..
gi 490998305 261 NGyIKVQSGIHGN-ATQTSIPGVFAAGDVMDH 291
Cdd:TIGR02374 246 AG-IKVNRGIIVNdSMQTSDPDIYAVGECAEH 276
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
103-294 |
1.63e-12 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 67.50 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 103 EYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQ--KVAVIGGGNTAVEEALYLSNIASEVHLIHRRDT 180
Cdd:PRK13512 103 EESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQvdKALVVGAGYISLEVLENLYERGLHPTLIHRSDK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 181 fraekilINRLMDKVANGNIVlhthrtleevtgDQMGVSGLRLRDTQNADNVESLEV---AG-------LFVAIGHSPNT 250
Cdd:PRK13512 183 -------INKLMDADMNQPIL------------DELDKREIPYRLNEEIDAINGNEVtfkSGkvehydmIIEGVGTHPNS 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490998305 251 AIFEGQLALEN--GYIKVQSGIhgnatQTSIPGVFAAGDVMDHIYR 294
Cdd:PRK13512 244 KFIESSNIKLDdkGFIPVNDKF-----ETNVPNIYAIGDIITSHYR 284
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
107-316 |
3.64e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 66.17 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 107 DALIIATGA-SARYLGLPSEEAfkgRGVsacatCDG--FFYR------------------NQKVAVIGGGNTAV---EEA 162
Cdd:PRK12770 120 DAVLIATGTwKSRKLGIPGEDL---PGV-----YSAleYLFRiraaklgylpwekvppveGKKVVVVGAGLTAVdaaLEA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 163 LYLSniASEVHLIHRRdTFR---AEKILINRLMDKvangNIVLHTHRTLEEVTGDQmGVSGLRLRDTQNADNVES----- 234
Cdd:PRK12770 192 VLLG--AEKVYLAYRR-TINeapAGKYEIERLIAR----GVEFLELVTPVRIIGEG-RVEGVELAKMRLGEPDESgrprp 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 235 ---------LEVAGLFVAIGHSPNTAIFEGQLALEN---GYIKVQsgihgNATQTSIPGVFAAGDVMdHIYRQAITSAGT 302
Cdd:PRK12770 264 vpipgsefvLEADTVVFAIGEIPTPPFAKECLGIELnrkGEIVVD-----EKHMTSREGVFAAGDVV-TGPSKIGKAIKS 337
|
250
....*....|....
gi 490998305 303 GCMAALDAERYLDG 316
Cdd:PRK12770 338 GLRAAQSIHEWLDL 351
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
100-288 |
5.72e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 65.93 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 100 DSGEYTCDALIIATGASARYLGLP----SEEAFKGRGVSACATcdgffyRNQKVAVIGGGNTAVEEALYLSNIASEVHLI 175
Cdd:PRK07251 113 EKIELTAETIVINTGAVSNVLPIPgladSKHVYDSTGIQSLET------LPERLGIIGGGNIGLEFAGLYNKLGSKVTVL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 176 HRRDTF--RAEKILINRLMDKVANGNIVLHTHRTLEEVT--GDQMGVSGlrlrdtqnadNVESLEVAGLFVAIGHSPNTA 251
Cdd:PRK07251 187 DAASTIlpREEPSVAALAKQYMEEDGITFLLNAHTTEVKndGDQVLVVT----------EDETYRFDALLYATGRKPNTE 256
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490998305 252 ifegQLALENGYIKV--QSGIHGNAT-QTSIPGVFAAGDV 288
Cdd:PRK07251 257 ----PLGLENTDIELteRGAIKVDDYcQTSVPGVFAVGDV 292
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
8-289 |
8.81e-12 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 66.12 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 8 KLLILGSGPAGYTAAVYAARANLQPVLITGMEK-GGQLTTTTEVENWPGDPNDLTgpllMERMHEHATKFDTEIIFDHIN 86
Cdd:PRK12775 432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHVvGGVLQYGIPSFRLPRDIIDRE----VQRLVDIGVKIETNKVIGKTF 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 87 SVDlqnrpfRLVGDSGeytCDALIIATGASA-RYLGLPSEeaFKGRGVSA--------CATCDGFFYRN------QKVAV 151
Cdd:PRK12775 508 TVP------QLMNDKG---FDAVFLGVGAGApTFLGIPGE--FAGQVYSAnefltrvnLMGGDKFPFLDtpislgKSVVV 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 152 IGGGNTAVEEALYLSNI-ASEVHLIHRRDTFRAEKiLINRLMDKVANGNIVLHTHRTLEEVTGDQMGVSGLRL------- 223
Cdd:PRK12775 577 IGAGNTAMDCLRVAKRLgAPTVRCVYRRSEAEAPA-RIEEIRHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKVeemelge 655
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998305 224 ------RDTQNADNVESLEVAGLFVAIGHSPNTAIFEGQ--LALEN-GYIKVQSGIHGNATQTSIPGVFAAGDVM 289
Cdd:PRK12775 656 pdekgrRKPMPTGEFKDLECDTVIYALGTKANPIITQSTpgLALNKwGNIAADDGKLESTQSTNLPGVFAGGDIV 730
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
3-178 |
4.06e-11 |
|
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: 63.34 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 3 TTKHSKLLILGSGPAGYTAAVYAARANLQPVLItgmEKGGQL----------TTTTEVENW----PGDPNDLTGPLLMER 68
Cdd:COG2072 3 ATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVL---EKADDVggtwrdnrypGLRLDTPSHlyslPFFPNWSDDPDFPTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 69 ------MHEHATKFD--TEIIFDH-INSVDLQNRP--FRLVGDSGE-YTCDALIIATGA--SARYLGLPSEEAFKGRGVS 134
Cdd:COG2072 80 deilayLEAYADKFGlrRPIRFGTeVTSARWDEADgrWTVTTDDGEtLTARFVVVATGPlsRPKIPDIPGLEDFAGEQLH 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490998305 135 ACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRR 178
Cdd:COG2072 160 SADWRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
8-287 |
1.18e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 61.98 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 8 KLLILGSGPAGYTAAVYAARanLQPVL-ITGMEKggqltttTEVENWPG------------DPNdltgpLLMERMHEHAT 74
Cdd:PRK09564 2 KIIIIGGTAAGMSAAAKAKR--LNKELeITVYEK-------TDIVSFGAcglpyfvggffdDPN-----TMIARTPEEFI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 75 KFDTEIIFDH-INSVDLQNRPFRL----VGDSGEYTCDALIIATGASARylgLPSEEAFKGRGVSACATC-DGFFYR--- 145
Cdd:PRK09564 68 KSGIDVKTEHeVVKVDAKNKTITVknlkTGSIFNDTYDKLMIATGARPI---IPPIKNINLENVYTLKSMeDGLALKell 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 146 ----NQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD-----TFRAE--KILINRLMDKvangNIVLHTHRTLEEVTGD 214
Cdd:PRK09564 145 kdeeIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDrilpdSFDKEitDVMEEELREN----GVELHLNEFVKSLIGE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490998305 215 QmGVSGLRL-RDTQNADNVeslevaglFVAIGHSPNTAIFEGQL--ALENGYIKV-QSGihgnatQTSIPGVFAAGD 287
Cdd:PRK09564 221 D-KVEGVVTdKGEYEADVV--------IVATGVKPNTEFLEDTGlkTLKNGAIIVdEYG------ETSIENIYAAGD 282
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
100-316 |
1.71e-09 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 58.73 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 100 DSGEYtcDALIIATGA-SARYLGLPSEEAfkGRGVSACAtcdgfFYRN----------QKVAVIGGGNTAVE---EALYL 165
Cdd:PRK12771 219 LEGEF--DAVFVAIGAqLGKRLPIPGEDA--AGVLDAVD-----FLRAvgegeppflgKRVVVIGGGNTAMDaarTARRL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 166 SniASEVHLIHRRD-----TFRAEkilinrLMDKVANGnIVLHTHRTLEEVTGDQMGVSGLRL------------RDTQN 228
Cdd:PRK12771 290 G--AEEVTIVYRRTredmpAHDEE------IEEALREG-VEINWLRTPVEIEGDENGATGLRVitvekmeldedgRPSPV 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 229 ADNVESLEVAGLFVAIGHSPNTAIFEGQ--LALENGYIKVQSgihgNATQTSIPGVFAAGDVMDHIyRQAITSAGTGCMA 306
Cdd:PRK12771 361 TGEEETLEADLVVLAIGQDIDSAGLESVpgVEVGRGVVQVDP----NFMMTGRPGVFAGGDMVPGP-RTVTTAIGHGKKA 435
|
250
....*....|
gi 490998305 307 ALDAERYLDG 316
Cdd:PRK12771 436 ARNIDAFLGG 445
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
8-316 |
2.10e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 58.59 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 8 KLLILGSGPAGYTAAVYAAR---------ANLQPvliTGMEKGG--QLTTTTEVENwpgdpNDLTGPLLMERMHEHATKF 76
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLRkghdvtifdANEQA---GGMMRYGipRFRLPESVID-----ADIAPLRAMGAEFRFNTVF 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 77 DTEIIFDhinsvDLQNrpfrlvgdsgEYtcDALIIATGAS-ARYLGLPSEE--------AFKGRGVSACATCDGffyrnQ 147
Cdd:PRK12814 267 GRDITLE-----ELQK----------EF--DAVLLAVGAQkASKMGIPGEElpgvisgiDFLRNVALGTALHPG-----K 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 148 KVAVIGGGNTAVE---EALYLSniASEVHLIHRRDTFR------------AEKILINRLMDKVA----NGNIVLhTHRTL 208
Cdd:PRK12814 325 KVVVIGGGNTAIDaarTALRLG--AESVTILYRRTREEmpanraeieealAEGVSLRELAAPVSiersEGGLEL-TAIKM 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 209 EEVTGDQMG------VSGLRLrdTQNADNVESlevaglfvAIGHSPNTAIFE--GQLALENGYIKVqsgiHGNATQTSIP 280
Cdd:PRK12814 402 QQGEPDESGrrrpvpVEGSEF--TLQADTVIS--------AIGQQVDPPIAEaaGIGTSRNGTVKV----DPETLQTSVA 467
|
330 340 350
....*....|....*....|....*....|....*....
gi 490998305 281 GVFAAGDVM---DhiyrQAITSAGTGCMAALDAERYLDG 316
Cdd:PRK12814 468 GVFAGGDCVtgaD----IAINAVEQGKRAAHAIDLFLNG 502
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
104-290 |
1.74e-08 |
|
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: 55.63 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 104 YTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDT 180
Cdd:TIGR01438 142 YSAERFLIATGERPRYPGIPGAKEL-------CITSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 181 FRA-EKILINRLMDKVANGNIVLHTHRTLEEVTgdQMGVSglRLRDTQNADNVESLEVAGLFVAIGHSPNTAifegQLAL 259
Cdd:TIGR01438 215 LRGfDQDCANKVGEHMEEHGVKFKRQFVPIKVE--QIEAK--VLVEFTDSTNGIEEEYDTVLLAIGRDACTR----KLNL 286
|
170 180 190
....*....|....*....|....*....|....*
gi 490998305 260 ENGYIKV--QSG--IHGNATQTSIPGVFAAGDVMD 290
Cdd:TIGR01438 287 ENVGVKInkKTGkiPADEEEQTNVPYIYAVGDILE 321
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
9-288 |
6.48e-08 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 53.61 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 9 LLILGSGPAGYTAAVYAARANLQPVLITGMEKGGqltttTEVeNWPGDPndlTGPLLM--ERMHE---------HAT--K 75
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGG-----TCL-NRGCIP---SKALLHaaERADEarhsedfgiKAEnvG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 76 FDTEIIFDHINSV------DLQN----------RPF-RLVGD----------SGEYTCDALIIATGASARylGLPSEEaF 128
Cdd:PRK06416 78 IDFKKVQEWKNGVvnrltgGVEGllkknkvdiiRGEaKLVDPntvrvmtedgEQTYTAKNIILATGSRPR--ELPGIE-I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 129 KGRGVsacatcdgFFYRN--------QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD----TFRAE--KILINRLMDK 194
Cdd:PRK06416 155 DGRVI--------WTSDEalnldevpKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPrilpGEDKEisKLAERALKKR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 195 vangNIVLHTHRTLEEVTGDQMGVSgLRLRDTQNadnVESLEVAGLFVAIGHSPNTAifegQLALEN-------GYIKVQ 267
Cdd:PRK06416 227 ----GIKIKTGAKAKKVEQTDDGVT-VTLEDGGK---EETLEADYVLVAVGRRPNTE----NLGLEElgvktdrGFIEVD 294
|
330 340
....*....|....*....|.
gi 490998305 268 SGIHgnatqTSIPGVFAAGDV 288
Cdd:PRK06416 295 EQLR-----TNVPNIYAIGDI 310
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
85-287 |
7.22e-08 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 53.38 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 85 INSVDLQNRpfRLVGDSGEYTCDALIIATGASA---------RYLGLPSEEAFkgrgvsacATCDGFFYRNQKVAVIGGG 155
Cdd:PRK04965 81 VTDIDAEAQ--VVKSQGNQWQYDKLVLATGASAfvppipgreLMLTLNSQQEY--------RAAETQLRDAQRVLVVGGG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 156 NTAVEEALYLSNIASEVHLIHRrdtfrAEKILINRLMDKVAngnivLHTHRTLEevtgdQMGVSgLRLRD-----TQNAD 230
Cdd:PRK04965 151 LIGTELAMDLCRAGKAVTLVDN-----AASLLASLMPPEVS-----SRLQHRLT-----EMGVH-LLLKSqlqglEKTDS 214
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998305 231 NV-------ESLEVAGLFVAIGHSPNTaifegQLALENGyIKVQSGIHGNAT-QTSIPGVFAAGD 287
Cdd:PRK04965 215 GIratldsgRSIEVDAVIAAAGLRPNT-----ALARRAG-LAVNRGIVVDSYlQTSAPDIYALGD 273
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
86-292 |
1.39e-07 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 52.51 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 86 NSVDLQnrpfRLVGDSGEYTCDALIIATGASARYLGLPSEEAfkgrgvsACATCDGFFYRN--QKVAVIGGGNTAVEEAL 163
Cdd:PLN02507 152 NEVEVT----QLDGTKLRYTAKHILIATGSRAQRPNIPGKEL-------AITSDEALSLEElpKRAVVLGGGYIAVEFAS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 164 YLSNIASEVHLIHRRDT----FRAE-KILINRLMDkvaNGNIVLHTHRTLEEVTGDQMGVSGLrlrdtqnADNVESLEVA 238
Cdd:PLN02507 221 IWRGMGATVDLFFRKELplrgFDDEmRAVVARNLE---GRGINLHPRTNLTQLTKTEGGIKVI-------TDHGEEFVAD 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490998305 239 GLFVAIGHSPNTAifegQLALEN--------GYIKVQsgihgNATQTSIPGVFAAGDVMDHI 292
Cdd:PLN02507 291 VVLFATGRAPNTK----RLNLEAvgveldkaGAVKVD-----EYSRTNIPSIWAIGDVTNRI 343
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
150-288 |
1.76e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 52.13 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 150 AVIGGGNTAVEEALYLSNIASEVHLIHRRDTfraekiLINR--------LMDKVANGNIVLHTHRTLEEVTGDQmgvSGL 221
Cdd:PRK06370 175 VIIGGGYIGLEFAQMFRRFGSEVTVIERGPR------LLPRededvaaaVREILEREGIDVRLNAECIRVERDG---DGI 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490998305 222 RLRDTQNADNvESLEVAGLFVAIGHSPNTaifEGqLALE--------NGYIKVQSGIhgnatQTSIPGVFAAGDV 288
Cdd:PRK06370 246 AVGLDCNGGA-PEITGSHILVAVGRVPNT---DD-LGLEaagvetdaRGYIKVDDQL-----RTTNPGIYAAGDC 310
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
9-288 |
2.19e-07 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 52.08 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 9 LLILGSGPAGYTAAVYAARANLQPVLItgmEKGGQL--------T--------TTTEVENW--------PGDPNDLTGPL 64
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVI---ERYRNVgggcthtgTipskalreAVLRLIGFnqnplyssYRVKLRITFAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 65 LMERMHeHATKFDTEII---FDHiNSVDL---------QNRpFRLVGDSGE---YTCDALIIATGAS-ARylglPSEEAF 128
Cdd:PRK05249 85 LLARAD-HVINKQVEVRrgqYER-NRVDLiqgrarfvdPHT-VEVECPDGEvetLTADKIVIATGSRpYR----PPDVDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 129 KGRGV--SacatcDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTFRA--EKILINRLMDKVANGNIV 201
Cdd:PRK05249 158 DHPRIydS-----DSILsldHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSflDDEISDALSYHLRDSGVT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 202 LHTHRTLEEVTGDQMGV-----SGLRLRdtqnADnveslevaGLFVAIGHSPNTAifegQLALEN--------GYIKVqs 268
Cdd:PRK05249 233 IRHNEEVEKVEGGDDGVivhlkSGKKIK----AD--------CLLYANGRTGNTD----GLNLENagleadsrGQLKV-- 294
|
330 340
....*....|....*....|.
gi 490998305 269 gihgNAT-QTSIPGVFAAGDV 288
Cdd:PRK05249 295 ----NENyQTAVPHIYAVGDV 311
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
99-309 |
3.42e-07 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 51.69 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 99 GDSGEYTCDALIIATGASARYLGLP---------SEEAFKGRGVSacatcdgffyrnQKVAVIGGGNTAVEEALYLSNIA 169
Cdd:PRK13748 226 GGERVVAFDRCLIATGASPAVPPIPglketpywtSTEALVSDTIP------------ERLAVIGSSVVALELAQAFARLG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 170 SEVHLIHRR---------------DTFRAE--KILINRLMDKVA--NGNIVLHTHRTleEVTGDQmgvsglrlrdtqnad 230
Cdd:PRK13748 294 SKVTILARStlffredpaigeavtAAFRAEgiEVLEHTQASQVAhvDGEFVLTTGHG--ELRADK--------------- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 231 nveslevagLFVAIGHSPNTAifegQLALENGYIKVQSG---IHGNATQTSIPGVFAAGDVMDH---IYRQAI--TSAG- 301
Cdd:PRK13748 357 ---------LLVATGRAPNTR----SLALDAAGVTVNAQgaiVIDQGMRTSVPHIYAAGDCTDQpqfVYVAAAagTRAAi 423
|
250
....*....|
gi 490998305 302 --TGCMAALD 309
Cdd:PRK13748 424 nmTGGDAALD 433
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
110-288 |
1.33e-06 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 49.54 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 110 IIATGASARYL-GLPseeaFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTF--RAEKI 186
Cdd:PRK06327 150 IIATGSEPRHLpGVP----FDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFlaAADEQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 187 LINRLMDKVANGNIVLHTHRTLEEVTGDQMGVSglrLRDTQNADNVESLEVAGLFVAIGHSPNT----AIFEGQLALENG 262
Cdd:PRK06327 226 VAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVS---VAYTDADGEAQTLEVDKLIVSIGRVPNTdglgLEAVGLKLDERG 302
|
170 180
....*....|....*....|....*.
gi 490998305 263 YIKVQSGIHgnatqTSIPGVFAAGDV 288
Cdd:PRK06327 303 FIPVDDHCR-----TNVPNVYAIGDV 323
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
131-297 |
1.73e-06 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 49.23 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 131 RGVSACATCDGFFY--RNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRD----TFraEKILINRLMDKVANGNIVLHT 204
Cdd:PTZ00058 220 KGKEFTISSDDFFKikEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNrllrKF--DETIINELENDMKKNNINIIT 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 205 HRTLEEVTGDQMGVSGLRLRDTQNADNVESlevagLFVAIGHSPNTAIFEGQ---LALENGYIKVQsgihgNATQTSIPG 281
Cdd:PTZ00058 298 HANVEEIEKVKEKNLTIYLSDGRKYEHFDY-----VIYCVGRSPNTEDLNLKalnIKTPKGYIKVD-----DNQRTSVKH 367
|
170
....*....|....*.
gi 490998305 282 VFAAGDVMDHIYRQAI 297
Cdd:PTZ00058 368 IYAVGDCCMVKKNQEI 383
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
145-292 |
2.11e-06 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 49.10 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 145 RNQKVAVIGGGNTAVEEALYLSNIASEVHLIhrrdtFRAEKILI---NRLMDKVANG----NIVLHTHRTLEEVTGDQMG 217
Cdd:PLN02546 251 KPEKIAIVGGGYIALEFAGIFNGLKSDVHVF-----IRQKKVLRgfdEEVRDFVAEQmslrGIEFHTEESPQAIIKSADG 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 218 VSGLRlrdtQNADNVESLevAGLFVAIGHSPNTAifegQLALE--------NGYIKVQSgihgnATQTSIPGVFAAGDVM 289
Cdd:PLN02546 326 SLSLK----TNKGTVEGF--SHVMFATGRKPNTK----NLGLEevgvkmdkNGAIEVDE-----YSRTSVPSIWAVGDVT 390
|
...
gi 490998305 290 DHI 292
Cdd:PLN02546 391 DRI 393
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
145-307 |
2.11e-06 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 49.45 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 145 RNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRdTFRAEKILINRLMDKVANGnIVLHTHRTLEEVTGDQMG--VSGLR 222
Cdd:PRK12779 446 KGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRR-TKSEMPARVEELHHALEEG-INLAVLRAPREFIGDDHThfVTHAL 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 223 L-------------RDTQNADNVESLEVAGLFVAIGHSPNTAIFEGQLALEN---GYIKVQSGihgnATQTSIPGVFAAG 286
Cdd:PRK12779 524 LdvnelgepdksgrRSPKPTGEIERVPVDLVIMALGNTANPIMKDAEPGLKTnkwGTIEVEKG----SQRTSIKGVYSGG 599
|
170 180
....*....|....*....|....
gi 490998305 287 DVMdhiyR---QAITSAGTGCMAA 307
Cdd:PRK12779 600 DAA----RggsTAIRAAGDGQAAA 619
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
146-248 |
1.18e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 46.78 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 146 NQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDTF--RAEKI------------LINRLMDKV-ANGNIVLHTHRTLEE 210
Cdd:COG1148 140 NKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELggRAAQLhktfpgldcpqcILEPLIAEVeANPNITVYTGAEVEE 219
|
90 100 110
....*....|....*....|....*....|....*...
gi 490998305 211 VTGDqmgVSGLRLRDTQNADNVESLEVAGLFVAIGHSP 248
Cdd:COG1148 220 VSGY---VGNFTVTIKKGPREEIEIEVGAIVLATGFKP 254
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
107-292 |
1.22e-05 |
|
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: 46.50 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 107 DALIIATGASARYLGLPseeafkgrGVSACATCDGFFYRNQ---KVAVIGGGNTAVEEALYLSN---IASEVHLIHRRD- 179
Cdd:TIGR01423 153 EHILLATGSWPQMLGIP--------GIEHCISSNEAFYLDEpprRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNm 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 180 -------TFRAEkiLINRLmdkVANGnIVLHTHRTLEEVTGDQMGVSGLRLRDTQNADnvesleVAGLFVAIGHSPNTai 252
Cdd:TIGR01423 225 ilrgfdsTLRKE--LTKQL---RANG-INIMTNENPAKVTLNADGSKHVTFESGKTLD------VDVVMMAIGRVPRT-- 290
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490998305 253 feGQLALENGYIKV--QSGIHGNA-TQTSIPGVFAAGDVMDHI 292
Cdd:TIGR01423 291 --QTLQLDKVGVELtkKGAIQVDEfSRTNVPNIYAIGDVTDRV 331
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
98-288 |
2.41e-05 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 45.72 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 98 VGDSGEYTCDALIIATGASARYLGLPSEEafkgrGVSacatcdgfFYRN----------QKVAVIGGGNTAVEEALYLSN 167
Cdd:PRK07846 121 TGDGEEITADQVVIAAGSRPVIPPVIADS-----GVR--------YHTSdtimrlpelpESLVIVGGGFIAAEFAHVFSA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 168 IASEVHLIHRRDT-FRAEKILINRLMDKVANGNIVLHTHRTLEEVTGDQMGVSgLRLrdtqnaDNVESLEVAGLFVAIGH 246
Cdd:PRK07846 188 LGVRVTVVNRSGRlLRHLDDDISERFTELASKRWDVRLGRNVVGVSQDGSGVT-LRL------DDGSTVEADVLLVATGR 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490998305 247 SPNTAIFEGQLA----LENGYIKVQSgiHGnatQTSIPGVFAAGDV 288
Cdd:PRK07846 261 VPNGDLLDAAAAgvdvDEDGRVVVDE--YQ---RTSAEGVFALGDV 301
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
99-288 |
2.81e-03 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 39.14 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 99 GDSGEYtcDALIIATGASARYLGLPS---EEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLI 175
Cdd:PRK09754 96 GESWHW--DQLFIATGAAARPLPLLDalgERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490998305 176 HRRDTFRA-------EKILINRLMDKvanGNIVLHTHRTLEEVTGDQMgVSGLRLRDTQNADNVeslevaglFVAIGHSp 248
Cdd:PRK09754 174 ELAATVMGrnapppvQRYLLQRHQQA---GVRILLNNAIEHVVDGEKV-ELTLQSGETLQADVV--------IYGIGIS- 240
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490998305 249 ntaiFEGQLALENGYIKVQSGIHGNATQTSIPGVFAAGDV 288
Cdd:PRK09754 241 ----ANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDV 276
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
9-45 |
3.83e-03 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 38.74 E-value: 3.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 490998305 9 LLILGSGPAGYTAAVYAARANLQPVLItgmEK----GGQLT 45
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLV---ERrgflGGMLT 39
|
|
|