|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
1-320 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 546.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 1 MGTAKHSKLLILGSGPAGYTAAVYAARANLSPVLITGMEQGGQLTTTTEVENWPGDAEGLTGPALMERMREHAEKFQTEI 80
Cdd:PRK10262 1 MGTTKHSKLLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNDLTGPLLMERMHEHATKFETEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 81 VFDHINSVDLQQRPFRLFGDSGEYSCDALIIATGASARYLGLPSEDAFKGKGVSACATCDGFFYRNQKVAVVGGGNTAVE 160
Cdd:PRK10262 81 IFDHINKVDLQNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 161 EALYLSNIAAEVHLIHRRDSFRSEKILIDRLMEKVKSGNIVLHTDHTLDEVLGDEMGVTGVRIRSTKAENETRELELAGV 240
Cdd:PRK10262 161 EALYLSNIASEVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLDVAGL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 241 FIAIGHSPNTGIFGGQLELENGYIKVQSGIHGNATQTTIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGIAGA 320
Cdd:PRK10262 241 FVAIGHSPNTAIFEGQLELENGYIKVQSGIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA 320
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
8-314 |
2.24e-166 |
|
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: 464.41 E-value: 2.24e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 8 KLLILGSGPAGYTAAVYAARANLSPVLITGMEQGGQLTTTTEVENWPGDAEGLTGPALMERMREHAEKFQTEIVFDHINS 87
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 88 VDLQQRPFRLF-GDSGEYSCDALIIATGASARYLGLPSEDAFKGKGVSACATCDGFFYRNQKVAVVGGGNTAVEEALYLS 166
Cdd:TIGR01292 81 VDKSDRPFKVYtGDGKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 167 NIAAEVHLIHRRDSFRSEKILIDRLMEKvksGNIVLHTDHTLDEVLGDEmGVTGVRIRSTKaENETRELELAGVFIAIGH 246
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLKKN---PKIEFLWNSTVEEIVGDN-KVEGVKIKNTV-TGEEEELEVDGVFIAIGH 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725096556 247 SPNTGIFGGQLEL-ENGYIKVQSGihgnaTQTTIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
Cdd:TIGR01292 236 EPNTELLKGLLELdENGYIVTDEG-----MRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
8-317 |
1.93e-159 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 447.26 E-value: 1.93e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 8 KLLILGSGPAGYTAAVYAARANLSPVLITGMEQGGQLTTTTEVENWPGDAEGLTGPALMERMREHAEKFQTEIVFDHINS 87
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPEGISGPELAERLREQAERFGAEILLEEVTS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 88 VDLQQRPFRLFGDSG-EYSCDALIIATGASARYLGLPSEDAFKGKGVSACATCDGFFYRNQKVAVVGGGNTAVEEALYLS 166
Cdd:COG0492 82 VDKDDGPFRVTTDDGtEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 167 NIAAEVHLIHRRDSFRSEKILIDRLMEKVKsgnIVLHTDHTLDEVLGDEmGVTGVRIRSTKaENETRELELAGVFIAIGH 246
Cdd:COG0492 162 KFASKVTLIHRRDELRASKILVERLRANPK---IEVLWNTEVTEIEGDG-RVEGVTLKNVK-TGEEKELEVDGVFVAIGL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725096556 247 SPNTGIFGGQ-LEL-ENGYIKVqsgihGNATQTTIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGI 317
Cdd:COG0492 237 KPNTELLKGLgLELdEDGYIVV-----DEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
9-316 |
1.60e-64 |
|
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: 212.72 E-value: 1.60e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 9 LLILGSGPAGYTAAVYAARANLSPVLITGMEQGGQLTTTTEVENWPGDAEgLTGPALMERMREHAEKFQTEIVFDHINSV 88
Cdd:TIGR03143 7 LIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILN-TTGPELMQEMRQQAQDFGVKFLQAEVLDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 89 DLQQRPFRLFGDSGEYSCDALIIATGASARYLGLPSEDAFKGKGVSACATCDGFFYRNQKVAVVGGGNTAVEEALYLSNI 168
Cdd:TIGR03143 86 DFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLTRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 169 AAEVHLIHRRDSFRSEKILIDRLMEKVKsgnIVLHTDHTLDEVLGDEM--------GVTGVRIR-STKAENETrelelAG 239
Cdd:TIGR03143 166 ASKVTVIVREPDFTCAKLIAEKVKNHPK---IEVKFNTELKEATGDDGlryakfvnNVTGEITEyKAPKDAGT-----FG 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1725096556 240 VFIAIGHSPNTGIFGGQLEL-ENGYIkvqsgIHGNATQTTIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDG 316
Cdd:TIGR03143 238 VFVFVGYAPSSELFKGVVELdKRGYI-----PTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYVKE 310
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
10-314 |
5.97e-62 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 205.01 E-value: 5.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 10 LILGSGPAGYTAAVYAARANLSpvliTGM--EQ-GGQLTTTTEVENWPGDAEgLTGPALMERMREHAEKFQTEIvFDHIN 86
Cdd:PRK15317 215 LVVGGGPAGAAAAIYAARKGIR----TGIvaERfGGQVLDTMGIENFISVPE-TEGPKLAAALEEHVKEYDVDI-MNLQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 87 SVDLQQ--RPFRLFGDSGE-YSCDALIIATGASARYLGLPSEDAFKGKGVSACATCDGFFYRNQKVAVVGGGNTAVEEAL 163
Cdd:PRK15317 289 ASKLEPaaGLIEVELANGAvLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAI 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 164 YLSNIAAEVHLIHRRDSFRSEKILIDRLmekvKS-GNIVLHTDHTLDEVLGDEMGVTGVRI--RSTkaeNETRELELAGV 240
Cdd:PRK15317 369 DLAGIVKHVTVLEFAPELKADQVLQDKL----RSlPNVTIITNAQTTEVTGDGDKVTGLTYkdRTT---GEEHHLELEGV 441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1725096556 241 FIAIGHSPNTGIFGGQLELEN-GYIKVQSgiHGnatQTTIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
Cdd:PRK15317 442 FVQIGLVPNTEWLKGTVELNRrGEIIVDA--RG---ATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
8-303 |
6.80e-55 |
|
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: 180.98 E-value: 6.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 8 KLLILGSGPAGYTAAVYAARANLSPVLIT--GMEQGGQLTTTTEVENWPGDAEGL-TGPALMERMREHAEKFQTEIVF-- 82
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEdeGTCPYGGCVLSKALLGAAEAPEIAsLWADLYKRKEEVVKKLNNGIEVll 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 83 -DHINSVDLQQRPFRL----FGDSGEYSCDALIIATGASARYLGLPSEDAFKGKGVSACATCDGFFYRN--QKVAVVGGG 155
Cdd:pfam07992 82 gTEVVSIDPGAKKVVLeelvDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLlpKRVVVVGGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 156 NTAVEEALYLSNIAAEVHLIHRRD--SFRSEKILIDRLMEKVKSGNIVLHTDHTLDEVLGDEMGVTGVrirstkaENETR 233
Cdd:pfam07992 162 YIGVELAAALAKLGKEVTLIEALDrlLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVI-------LKDGT 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1725096556 234 ELELAGVFIAIGHSPNT-GIFGGQLEL-ENGYIKVQSGIhgnatQTTIPGVFAAGDVMDHIYRQAITSAGTG 303
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTeLLEAAGLELdERGGIVVDEYL-----RTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
9-288 |
6.43e-23 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 98.33 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 9 LLILGSGPAGYTAAVYAARANLSPVLItgmeQGGQLTTT-------------------TEVENWP-----GDAEGLTGPA 64
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALI----EKGPLGGTclnvgcipskaliaaaeafHEAKHAEefgihADGPKIDFKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 65 LMERMREHAEKFQTEIV--FDHINSVDLQQ---RpfrlFGDSG-------EYSCDALIIATGAsaRYLGLPSEDAFKGKG 132
Cdd:PRK06292 82 VMARVRRERDRFVGGVVegLEKKPKIDKIKgtaR----FVDPNtvevngeRIEAKNIVIATGS--RVPPIPGVWLILGDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 133 VsacATCDGFFYRN---QKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSF-RSEKILIDRLMEKVKSGNIVLHTDHTL 208
Cdd:PRK06292 156 L---LTSDDAFELDklpKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlPLEDPEVSKQAQKILSKEFKIKLGAKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 209 DEVLGDEmgvtGVRIRSTKAENETRELELAGVFIAIGHSPNTGIFG---GQLEL-ENGYIKVqsgihGNATQTTIPGVFA 284
Cdd:PRK06292 233 TSVEKSG----DEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGlenTGIELdERGRPVV-----DEHTQTSVPGIYA 303
|
....
gi 1725096556 285 AGDV 288
Cdd:PRK06292 304 AGDV 307
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
64-294 |
2.45e-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: 92.18 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 64 ALMERMREHAEKFQTEIVFDH-INSVDLQQRpfRLFGDSGE-YSCDALIIATGASARYL---GLPSEDAFKGKGVSACAT 138
Cdd:COG0446 37 DLLVRTPESFERKGIDVRTGTeVTAIDPEAK--TVTLRDGEtLSYDKLVLATGARPRPPpipGLDLPGVFTLRTLDDADA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 139 CDGFFYRN--QKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSF--RSEKILIDRLMEKVKSGNIVLHTDHTLDEVLGD 214
Cdd:COG0446 115 LREALKEFkgKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLlgVLDPEMAALLEEELREHGVELRLGETVVAIDGD 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 215 EmgvtGVRIRSTkaenETRELELAGVFIAIGHSPNTGIFGG-QLEL-ENGYIKVqsgihgNAT-QTTIPGVFAAGDVMDH 291
Cdd:COG0446 195 D----KVAVTLT----DGEEIPADLVVVAPGVRPNTELAKDaGLALgERGWIKV------DETlQTSDPDVYAAGDCAEV 260
|
...
gi 1725096556 292 IYR 294
Cdd:COG0446 261 PHP 263
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
9-288 |
2.61e-21 |
|
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: 93.61 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 9 LLILGSGPAGYTAAVYAARANLSPVLITGMEQGG------------------QLTTTTEVEN--WPGDAEGLTGPALMER 68
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGtclnvgcipskallhaaeVAHEARHAAEfgISAGAPSVDWAALMAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 69 MREHAEKFQTEIVF-------DHI---------NSVDLQqrpfrlfgDSGEYSCDALIIATGASARYLGLPSEDafkGKG 132
Cdd:COG1249 86 KDKVVDRLRGGVEEllkkngvDVIrgrarfvdpHTVEVT--------GGETLTADHIVIATGSRPRVPPIPGLD---EVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 133 VSacaTCDGFFYRNQ---KVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSF--RSEKILIDRLMEKVKSGNIVLHTDHT 207
Cdd:COG1249 155 VL---TSDEALELEElpkSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpGEDPEISEALEKALEKEGIDILTGAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 208 LDEVLGDEmgvTGVRIRsTKAENETRELELAGVFIAIGHSPNTGIFGgqLE------LENGYIKVqsgihgNAT-QTTIP 280
Cdd:COG1249 232 VTSVEKTG---DGVTVT-LEDGGGEEAVEADKVLVATGRRPNTDGLG--LEaagvelDERGGIKV------DEYlRTSVP 299
|
....*...
gi 1725096556 281 GVFAAGDV 288
Cdd:COG1249 300 GIYAIGDV 307
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
5-316 |
2.34e-19 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 88.15 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 5 KHSKLLILGSGPAGYTAAVYAARANLSPVLITGM-EQGGQLTTttevenwpGDAE-GLTGPALMERMREHAEKFQTEIVF 82
Cdd:PRK12831 139 KGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALhEPGGVLVY--------GIPEfRLPKETVVKKEIENIKKLGVKIET 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 83 DHI--NSVDLQQrpfrLFGDSGeysCDALIIATGASA-RYLGLPSEDAfkgKGV-SAC----------ATCDGF---FYR 145
Cdd:PRK12831 211 NVVvgKTVTIDE----LLEEEG---FDAVFIGSGAGLpKFMGIPGENL---NGVfSANefltrvnlmkAYKPEYdtpIKV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 146 NQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRrdsfRSEKILIDRLME--KVKSGNIVLHTDHTLDEVLGDEMG-VTGV- 221
Cdd:PRK12831 281 GKKVAVVGGGNVAMDAARTALRLGAEVHIVYR----RSEEELPARVEEvhHAKEEGVIFDLLTNPVEILGDENGwVKGMk 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 222 -------------RIRSTKAENETRELELAGVFIAIGHSPNTGIFGGQLELE---NGYIKVQSgihgNATQTTIPGVFAA 285
Cdd:PRK12831 357 cikmelgepdasgRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTKGLKinkRGCIVADE----ETGLTSKEGVFAG 432
|
330 340 350
....*....|....*....|....*....|....*...
gi 1725096556 286 GDvmdhiyrqAITSAGT-------GCMAALDAERYLDG 316
Cdd:PRK12831 433 GD--------AVTGAATvilamgaGKKAAKAIDEYLSK 462
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
16-286 |
3.50e-18 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 83.04 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 16 PAGYTAAVYAARANLSPVLItgMEQG------------GQLTTTTEVEN-----------------WPGDAEGLTGPALM 66
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDYLI--LEKGnignsfyrypthMTFFSPSFTSNgfgipdlnaispgtspaFTFNREHPSGNEYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 67 ERMREHAEKFQTEIV-FDHINSVDLQQRPFRLFGDSGEYSCDALIIATGasarYLGLPSEDAFKGKGVSACATCDGFFYR 145
Cdd:pfam13738 79 EYLRRVADHFELPINlFEEVTSVKKEDDGFVVTTSKGTYQARYVIIATG----EFDFPNKLGVPELPKHYSYVKDFHPYA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 146 NQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSFRSEK---------ILIDRLMEKVKSGNIVLHTDHTLDEVlgDEM 216
Cdd:pfam13738 155 GQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDsdpsyslspDTLNRLEELVKNGKIKAHFNAEVKEI--TEV 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1725096556 217 GVtGVRIRStkaeNETRELELAGVFI-AIGHSPNTGIFGGQL--ELENGYIKVQSgihgnATQ-TTIPGVFAAG 286
Cdd:pfam13738 233 DV-SYKVHT----EDGRKVTSNDDPIlATGYHPDLSFLKKGLfeLDEDGRPVLTE-----ETEsTNVPGLFLAG 296
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
107-288 |
9.82e-18 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 83.30 E-value: 9.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 107 DALIIATGASA-RYLGLPSEDAfkgKGV-SAC--------ATCDGFFYRNQKVAVVGGGNTA---VEEALYLSniAAEVH 173
Cdd:PRK11749 227 DAVFIGTGAGLpRFLGIPGENL---GGVySAVdfltrvnqAVADYDLPVGKRVVVIGGGNTAmdaARTAKRLG--AESVT 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 174 LIHRRDsfRSEKILIDRLMEKVKSGNIVLHTDHTLDEVLGDEMGVTGVRI-------------RSTKAENETRELELAGV 240
Cdd:PRK11749 302 IVYRRG--REEMPASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFvrmelgepdasgrRRVPIEGSEFTLPADLV 379
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1725096556 241 FIAIGHSPNTGIFGGQLELE---NGYIKVqsgihGNAT-QTTIPGVFAAGDV 288
Cdd:PRK11749 380 IKAIGQTPNPLILSTTPGLElnrWGTIIA-----DDETgRTSLPGVFAGGDI 426
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
8-288 |
1.65e-17 |
|
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: 82.49 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 8 KLLILGSGPAGYTAAVYAARANLSPVLITGMEQ-GGQLTTttevenwpG-----------DAEgltgpalMERMREHAEK 75
Cdd:COG0493 123 KVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKpGGLLRY--------GipefrlpkdvlDRE-------IELIEALGVE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 76 FQTEIVFDHINSVDlqqrpfRLFGdsgEYscDALIIATGAS-ARYLGLPSEDAfkgKGV-SA---------CATCDGFFY 144
Cdd:COG0493 188 FRTNVEVGKDITLD------ELLE---EF--DAVFLATGAGkPRDLGIPGEDL---KGVhSAmdfltavnlGEAPDTILA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 145 RNQKVAVVGGGNTAVE---EALYLSniAAEVHLIHRRD----SFRSEKIlidrlmEKVKSGNIVLHTDHTLDEVLGDEMG 217
Cdd:COG0493 254 VGKRVVVIGGGNTAMDcarTALRLG--AESVTIVYRRTreemPASKEEV------EEALEEGVEFLFLVAPVEIIGDENG 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 218 -VTGVRIRSTKA--------------ENETRELELAGVFIAIGHSPNTGIFGGQLELE---NGYIKVqsgiHGNATQTTI 279
Cdd:COG0493 326 rVTGLECVRMELgepdesgrrrpvpiEGSEFTLPADLVILAIGQTPDPSGLEEELGLEldkRGTIVV----DEETYQTSL 401
|
....*....
gi 1725096556 280 PGVFAAGDV 288
Cdd:COG0493 402 PGVFAGGDA 410
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
103-292 |
2.12e-17 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 82.13 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 103 EYSCDALIIATGASARYLGLPsedafkgkGVSACATCDGFFYRN---QKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRD 179
Cdd:PRK06116 129 RYTADHILIATGGRPSIPDIP--------GAEYGITSDGFFALEelpKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGD 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 180 SF-RS-EKILIDRLMEKVKSGNIVLHTDHTLDEVLGDEMGVTGVRIRStkaeneTRELELAGVFIAIGHSPNTGIFGgqL 257
Cdd:PRK06116 201 APlRGfDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTLED------GETLTVDCLIWAIGREPNTDGLG--L 272
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1725096556 258 E------LENGYIKVQsgihgNATQTTIPGVFAAGDVMDHI 292
Cdd:PRK06116 273 EnagvklNEKGYIIVD-----EYQNTNVPGIYAVGDVTGRV 308
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
6-288 |
2.25e-15 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 75.95 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 6 HSKLLILGSGPAGYTAA-VYAARANLSPVLITGMEQGG-----QLTtttevenwpgdaEGLTGPALMERMREHAEKFQTE 79
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAeELRKLDPDGEITVIGAEPHPpynrpPLS------------KVLAGETDEEDLLLRPADFYEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 80 --IVF---DHINSVDLQQRpfRLFGDSGE-YSCDALIIATGASARYLGLPSEDAfkgKGVsacatcdgFFYRN------- 146
Cdd:COG1251 69 ngIDLrlgTRVTAIDRAAR--TVTLADGEtLPYDKLVLATGSRPRVPPIPGADL---PGV--------FTLRTlddadal 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 147 -------QKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSF-------RSEKILIDRLMEKvksgNIVLHTDHTLDEVL 212
Cdd:COG1251 136 raalapgKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlprqldeEAGALLQRLLEAL----GVEVRLGTGVTEIE 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1725096556 213 GDEmGVTGVRIRSTkaenetRELELAGVFIAIGHSPNTGIfggqleLENGYIKVQSGIHGNAT-QTTIPGVFAAGDV 288
Cdd:COG1251 212 GDD-RVTGVRLADG------EELPADLVVVAIGVRPNTEL------ARAAGLAVDRGIVVDDYlRTSDPDIYAAGDC 275
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
8-314 |
3.61e-13 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 70.16 E-value: 3.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 8 KLLILGSGPAGYTAAVYAARANLSPVLITGM-EQGGQLTTTTEVENWPG---DAEgltgpalMERMREHAEKFQTEIVFD 83
Cdd:PRK12778 433 KVAVIGSGPAGLSFAGDLAKRGYDVTVFEALhEIGGVLKYGIPEFRLPKkivDVE-------IENLKKLGVKFETDVIVG 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 84 HINSVDlqqrpfrlfgDSGEYSCDALIIATGAS-ARYLGLPSE------------------DAFKGKGVSACATcdgffy 144
Cdd:PRK12778 506 KTITIE----------ELEEEGFKGIFIASGAGlPNFMNIPGEnsngvmssneyltrvnlmDAASPDSDTPIKF------ 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 145 rNQKVAVVGGGNTAVEEALYLSNIAAE-VHLIHRrdsfRSEKILIDRLME--KVKSGNIVLHTDHTLDEVLGDEMG-VTG 220
Cdd:PRK12778 570 -GKKVAVVGGGNTAMDSARTAKRLGAErVTIVYR----RSEEEMPARLEEvkHAKEEGIEFLTLHNPIEYLADEKGwVKQ 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 221 V--------------RIRSTKAENETRELELAGVFIAIGHSPNTGIFGGQLELE---NGYIKVQsgihgNATQTTIPGVF 283
Cdd:PRK12778 645 VvlqkmelgepdasgRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSIPGLElnrKGTIVVD-----EEMQSSIPGIY 719
|
330 340 350
....*....|....*....|....*....|....
gi 1725096556 284 AAGDvmdhIYRQA---ITSAGTGCMAALDAERYL 314
Cdd:PRK12778 720 AGGD----IVRGGatvILAMGDGKRAAAAIDEYL 749
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
107-316 |
6.47e-13 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 68.48 E-value: 6.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 107 DALIIATGA-SARYLGLPSEDAfkgKGVsacatCDG--FFYR------------------NQKVAVVGGGNTAV---EEA 162
Cdd:PRK12770 120 DAVLIATGTwKSRKLGIPGEDL---PGV-----YSAleYLFRiraaklgylpwekvppveGKKVVVVGAGLTAVdaaLEA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 163 LYLSniAAEVHLIHRRDsfRSE----KILIDRLMEKvksgNIVLHTDHTLDEVLGDEmGVTGVRIRSTKA---------- 228
Cdd:PRK12770 192 VLLG--AEKVYLAYRRT--INEapagKYEIERLIAR----GVEFLELVTPVRIIGEG-RVEGVELAKMRLgepdesgrpr 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 229 ----ENETRELELAGVFIAIGHSPNTGIFGGQLELEN---GYIKVQsgihgNATQTTIPGVFAAGDVMdHIYRQAITSAG 301
Cdd:PRK12770 263 pvpiPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELnrkGEIVVD-----EKHMTSREGVFAAGDVV-TGPSKIGKAIK 336
|
250
....*....|....*
gi 1725096556 302 TGCMAALDAERYLDG 316
Cdd:PRK12770 337 SGLRAAQSIHEWLDL 351
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
148-221 |
7.07e-13 |
|
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: 62.99 E-value: 7.07e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1725096556 148 KVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSFRS--EKILIDRLMEKVKSGNIVLHTDHTLDEVLGDEMGVTGV 221
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPgfDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVV 76
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
103-294 |
5.06e-12 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 66.34 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 103 EYSCDALIIATGASARYLGLPSEDAFKGKGVSACATCDGFFYRNQ--KVAVVGGGNTAVEEALYLSNIAAEVHLIHrrds 180
Cdd:PRK13512 103 EESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQvdKALVVGAGYISLEVLENLYERGLHPTLIH---- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 181 fRSEKI--LIDRLMEKV-----KSGNIVLHTDHTLDEVLGDEmgvtgVRIRSTKAENETRELElagvfiAIGHSPNTG-I 252
Cdd:PRK13512 179 -RSDKInkLMDADMNQPildelDKREIPYRLNEEIDAINGNE-----VTFKSGKVEHYDMIIE------GVGTHPNSKfI 246
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1725096556 253 FGGQLELEN-GYIKVQSGIhgnatQTTIPGVFAAGDVMDHIYR 294
Cdd:PRK13512 247 ESSNIKLDDkGFIPVNDKF-----ETNVPNIYAIGDIITSHYR 284
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
70-288 |
8.74e-12 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 65.15 E-value: 8.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 70 REHAEKFQTEIVFDHINSVDLQQRpfRLFGDSG-EYSCDALIIATGASARYLGLP--SEDAFKGKGVSACATC----DGF 142
Cdd:COG1252 63 RELLRRAGVRFIQGEVTGIDPEAR--TVTLADGrTLSYDYLVIATGSVTNFFGIPglAEHALPLKTLEDALALrerlLAA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 143 FYRNQ-----KVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSFRSEKILI---DRLM----EKV--------KSGNIVL 202
Cdd:COG1252 141 FERAErrrllTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPDKVRITLVeagPRILpglgEKLseaaekelEKRGVEV 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 203 HTDHTLDEVLGDemgvtGVRIRStkaeneTRELELAGVFIAIGHSPNTgiFGGQLELE---NGYIKVqsgihgNATQTTI 279
Cdd:COG1252 221 HTGTRVTEVDAD-----GVTLED------GEEIPADTVIWAAGVKAPP--LLADLGLPtdrRGRVLV------DPTLQVP 281
|
250
....*....|.
gi 1725096556 280 --PGVFAAGDV 288
Cdd:COG1252 282 ghPNVFAIGDC 292
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
8-289 |
9.50e-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: 65.73 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 8 KLLILGSGPAGYTAAVYAARANLSPVLITGME-QGGQLTTTTEVENWPG---DAEgltgpalMERMREHAEKFQTEIVFD 83
Cdd:PRK12775 432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHvVGGVLQYGIPSFRLPRdiiDRE-------VQRLVDIGVKIETNKVIG 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 84 HINSVDlqqrpfRLFGDSGeysCDALIIATGASA-RYLGLPSEdaFKGKGVSA--------CATCDGFFYRN------QK 148
Cdd:PRK12775 505 KTFTVP------QLMNDKG---FDAVFLGVGAGApTFLGIPGE--FAGQVYSAnefltrvnLMGGDKFPFLDtpislgKS 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 149 VAVVGGGNTAVEEALYLSNI-AAEVHLIHRRdsfrSEKILIDRLME--KVKSGNIVLHTDHTLDEVLGDEMG-VTGVRI- 223
Cdd:PRK12775 574 VVVIGAGNTAMDCLRVAKRLgAPTVRCVYRR----SEAEAPARIEEirHAKEEGIDFFFLHSPVEIYVDAEGsVRGMKVe 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 224 ------------RSTKAENETRELELAGVFIAIGHSPNTGIfgGQ----LELEN-GYIKVQSGIHGNATQTTIPGVFAAG 286
Cdd:PRK12775 650 emelgepdekgrRKPMPTGEFKDLECDTVIYALGTKANPII--TQstpgLALNKwGNIAADDGKLESTQSTNLPGVFAGG 727
|
...
gi 1725096556 287 DVM 289
Cdd:PRK12775 728 DIV 730
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
107-287 |
5.12e-11 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 63.14 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 107 DALIIATGASARylgLPSEDAFKGKGVSACATC-DGFFYR-------NQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRR 178
Cdd:PRK09564 105 DKLMIATGARPI---IPPIKNINLENVYTLKSMeDGLALKellkdeeIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 179 D-----SFRSEkiLIDRLMEKVKSGNIVLHTDHTLDEVLGDEmGVTGVRirstkaeNETRELELAGVFIAIGHSPNTGIF 253
Cdd:PRK09564 182 DrilpdSFDKE--ITDVMEEELRENGVELHLNEFVKSLIGED-KVEGVV-------TDKGEYEADVVIVATGVKPNTEFL 251
|
170 180 190
....*....|....*....|....*....|....*..
gi 1725096556 254 GGQ-LE-LENGYIKV-QSGihgnatQTTIPGVFAAGD 287
Cdd:PRK09564 252 EDTgLKtLKNGAIIVdEYG------ETSIENIYAAGD 282
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
100-288 |
3.63e-10 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 60.53 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 100 DSGEYSCDALIIATGASARYLGLP----SEDAFKGKGVSACATcdgffyRNQKVAVVGGGNTAVEEALYLSNIAAEVHLI 175
Cdd:PRK07251 113 EKIELTAETIVINTGAVSNVLPIPgladSKHVYDSTGIQSLET------LPERLGIIGGGNIGLEFAGLYNKLGSKVTVL 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 176 HRRDSF--RSEKILIDRLMEKVKSGNIVLHTDHTLDEVL--GDEMGVTgvrirstkAENETRELELagVFIAIGHSPNTG 251
Cdd:PRK07251 187 DAASTIlpREEPSVAALAKQYMEEDGITFLLNAHTTEVKndGDQVLVV--------TEDETYRFDA--LLYATGRKPNTE 256
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1725096556 252 ifggQLELENGYIKV--QSGIHGNAT-QTTIPGVFAAGDV 288
Cdd:PRK07251 257 ----PLGLENTDIELteRGAIKVDDYcQTSVPGVFAVGDV 292
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
100-316 |
3.73e-10 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 60.66 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 100 DSGEYscDALIIATGA-SARYLGLPSEDAfkGKGVSACAtcdgfFYRN----------QKVAVVGGGNTAVE---EALYL 165
Cdd:PRK12771 219 LEGEF--DAVFVAIGAqLGKRLPIPGEDA--AGVLDAVD-----FLRAvgegeppflgKRVVVIGGGNTAMDaarTARRL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 166 SniAAEVHLIHRRD-----SFRSEkiLIDRLMEKVKsgnivLHTDHTLDEVLGDEMGVTGVRI------------RSTKA 228
Cdd:PRK12771 290 G--AEEVTIVYRRTredmpAHDEE--IEEALREGVE-----INWLRTPVEIEGDENGATGLRVitvekmeldedgRPSPV 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 229 ENETRELELAGVFIAIGHSPNTGIFGGQ--LELENGYIKVQSgihgNATQTTIPGVFAAGDVMDHIyRQAITSAGTGCMA 306
Cdd:PRK12771 361 TGEEETLEADLVVLAIGQDIDSAGLESVpgVEVGRGVVQVDP----NFMMTGRPGVFAGGDMVPGP-RTVTTAIGHGKKA 435
|
250
....*....|
gi 1725096556 307 ALDAERYLDG 316
Cdd:PRK12771 436 ARNIDAFLGG 445
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
10-178 |
1.57e-09 |
|
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: 58.34 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 10 LILGSGPAGYTAAVYAARANLSPVLItgmEQGGQ------------LTTTTE--------VENWPGDAEGLTGPALMERM 69
Cdd:COG2072 10 VVIGAGQAGLAAAYHLRRAGIDFVVL---EKADDvggtwrdnrypgLRLDTPshlyslpfFPNWSDDPDFPTGDEILAYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 70 REHAEKFQ--TEIVFDH-INSV--DLQQRPFRLFGDSGE-YSCDALIIATGA--SARYLGLPSEDAFKGKGVSACATCDG 141
Cdd:COG2072 87 EAYADKFGlrRPIRFGTeVTSArwDEADGRWTVTTDDGEtLTARFVVVATGPlsRPKIPDIPGLEDFAGEQLHSADWRNP 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1725096556 142 FFYRNQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRR 178
Cdd:COG2072 167 VDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
86-292 |
2.02e-08 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 55.21 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 86 NSVDLQQrpfrLFGDSGEYSCDALIIATGASARYLGLPSEDAfkgkgvsACATCDGFFYRN--QKVAVVGGGNTAVEEAL 163
Cdd:PLN02507 152 NEVEVTQ----LDGTKLRYTAKHILIATGSRAQRPNIPGKEL-------AITSDEALSLEElpKRAVVLGGGYIAVEFAS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 164 YLSNIAAEVHLIHRRD----SFRSE-KILIDRLMEkvkSGNIVLHTDHTLDEVLGDEmgvTGVRIRSTKAEnetrELELA 238
Cdd:PLN02507 221 IWRGMGATVDLFFRKElplrGFDDEmRAVVARNLE---GRGINLHPRTNLTQLTKTE---GGIKVITDHGE----EFVAD 290
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1725096556 239 GVFIAIGHSPNTGIFGGQ---LELEN-GYIKVQsgihgNATQTTIPGVFAAGDVMDHI 292
Cdd:PLN02507 291 VVLFATGRAPNTKRLNLEavgVELDKaGAVKVD-----EYSRTNIPSIWAIGDVTNRI 343
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
9-290 |
2.92e-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: 54.86 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 9 LLILGSGPAGYTAAVYAARANLSPVLITGMEQGGQLT------TTTEVENWPGD---AEGLTGPAL---------MERMR 70
Cdd:TIGR01438 5 LIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTrwgiggTCVNVGCIPKKlmhQAALLGQALkdsrnygwkVEETV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 71 EHAEKFQTEIVFDHINS------VDLQQRPFRLFGDSGE------------------YSCDALIIATGASARYLGLPSED 126
Cdd:TIGR01438 85 KHDWKRLVEAVQNHIGSlnwgyrVALREKKVKYENAYAEfvdkhrikatnkkgkekiYSAERFLIATGERPRYPGIPGAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 127 AFkgkgvsaCATCDGFF---YRNQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSFRS-EKILIDRLMEKVKSGNIVL 202
Cdd:TIGR01438 165 EL-------CITSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGfDQDCANKVGEHMEEHGVKF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 203 hTDHTLDEVLgDEMGvTGVRIRSTKAENETRElELAGVFIAIGHSPNTGifggQLELENGYIKV--QSG--IHGNATQTT 278
Cdd:TIGR01438 238 -KRQFVPIKV-EQIE-AKVLVEFTDSTNGIEE-EYDTVLLAIGRDACTR----KLNLENVGVKInkKTGkiPADEEEQTN 309
|
330
....*....|..
gi 1725096556 279 IPGVFAAGDVMD 290
Cdd:TIGR01438 310 VPYIYAVGDILE 321
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
4-288 |
2.54e-07 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 51.74 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 4 AKHSKLLILGSGPAGYTAAVYAARANLSPVLItgmEQG---------GQLTTTTEVEN-------WPGDAEGLTGP---- 63
Cdd:PRK06370 3 AQRYDAIVIGAGQAGPPLAARAAGLGMKVALI---ERGllggtcvntGCVPTKTLIASaraahlaRRAAEYGVSVGgpvs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 64 ----ALMERMREHAEKFQT--EIVFDHINSVDLQQ------RPFRLFGDSGEYSCDALIIATGASARYLGLPsedafkgk 131
Cdd:PRK06370 80 vdfkAVMARKRRIRARSRHgsEQWLRGLEGVDVFRgharfeSPNTVRVGGETLRAKRIFINTGARAAIPPIP-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 132 GVSACA--TCDGFF---YRNQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRrdsfrSEKIL--IDR-----LMEKVKSGN 199
Cdd:PRK06370 152 GLDEVGylTNETIFsldELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIER-----GPRLLprEDEdvaaaVREILEREG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 200 IVLHTDhtlDEVLGDEMGVTGVRIRSTKAENEtRELELAGVFIAIGHSPNTGIFGgqLEL------ENGYIKVQSGIhgn 273
Cdd:PRK06370 227 IDVRLN---AECIRVERDGDGIAVGLDCNGGA-PEITGSHILVAVGRVPNTDDLG--LEAagvetdARGYIKVDDQL--- 297
|
330
....*....|....*
gi 1725096556 274 atQTTIPGVFAAGDV 288
Cdd:PRK06370 298 --RTTNPGIYAAGDC 310
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
8-316 |
3.83e-07 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 51.65 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 8 KLLILGSGPAGYTAAVYAARanlspvlitgmeqGGQLTTTTEVENWPGdaeGLtgpalmerMREHAEKFQ-TEIVFDhin 86
Cdd:PRK12814 195 KVAIIGAGPAGLTAAYYLLR-------------KGHDVTIFDANEQAG---GM--------MRYGIPRFRlPESVID--- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 87 sVDLQqrPFRLFGdsGEYSC-----------------DALIIATGAS-ARYLGLPSEDAfkgKGVsacaTCDGFFYRN-- 146
Cdd:PRK12814 248 -ADIA--PLRAMG--AEFRFntvfgrditleelqkefDAVLLAVGAQkASKMGIPGEEL---PGV----ISGIDFLRNva 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 147 --------QKVAVVGGGNTAVEEALYLSNIAAE-VHLIHRR------------DSFRSEKILIDRL-----MEKVKSGNI 200
Cdd:PRK12814 316 lgtalhpgKKVVVIGGGNTAIDAARTALRLGAEsVTILYRRtreempanraeiEEALAEGVSLRELaapvsIERSEGGLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 201 VLHTDHTLDEVlgDEMGvtgvRIRSTKAENETRELELAGVFIAIGH------SPNTGIFGGQleleNGYIKVqsgiHGNA 274
Cdd:PRK12814 396 LTAIKMQQGEP--DESG----RRRPVPVEGSEFTLQADTVISAIGQqvdppiAEAAGIGTSR----NGTVKV----DPET 461
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1725096556 275 TQTTIPGVFAAGDVM---DhiyrQAITSAGTGCMAALDAERYLDG 316
Cdd:PRK12814 462 LQTSVAGVFAGGDCVtgaD----IAINAVEQGKRAAHAIDLFLNG 502
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
107-292 |
4.20e-07 |
|
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: 51.13 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 107 DALIIATGASARYLGLPsedafkgkGVSACATCDGFFYRNQ---KVAVVGGGNTAVEEALYLSN---IAAEVHLIHRRD- 179
Cdd:TIGR01423 153 EHILLATGSWPQMLGIP--------GIEHCISSNEAFYLDEpprRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNm 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 180 ---SFRSEkiLIDRLMEKVKSGNIVLHTDHTLDEVLGDEMGVTGVRIRSTKaenetrELELAGVFIAIGHSPNTgifgGQ 256
Cdd:TIGR01423 225 ilrGFDST--LRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESGK------TLDVDVVMMAIGRVPRT----QT 292
|
170 180 190
....*....|....*....|....*....|....*....
gi 1725096556 257 LELENGYIKV--QSGIHGNA-TQTTIPGVFAAGDVMDHI 292
Cdd:TIGR01423 293 LQLDKVGVELtkKGAIQVDEfSRTNVPNIYAIGDVTDRV 331
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
131-297 |
4.62e-07 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 51.15 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 131 KGVSACATCDGFFY--RNQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSF--RSEKILIDRLMEKVKSGNIVLHTDH 206
Cdd:PTZ00058 220 KGKEFTISSDDFFKikEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLlrKFDETIINELENDMKKNNINIITHA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 207 TLDEVLGDEMgvTGVrirSTKAENETRELELAGVFIAIGHSPNT---GIFGGQLELENGYIKVQsgihgNATQTTIPGVF 283
Cdd:PTZ00058 300 NVEEIEKVKE--KNL---TIYLSDGRKYEHFDYVIYCVGRSPNTedlNLKALNIKTPKGYIKVD-----DNQRTSVKHIY 369
|
170
....*....|....
gi 1725096556 284 AAGDVMDHIYRQAI 297
Cdd:PTZ00058 370 AVGDCCMVKKNQEI 383
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
145-292 |
8.81e-07 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 50.26 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 145 RNQKVAVVGGGNTAVEEALYLSNIAAEVHLIhrrdsFRSEKIL-------IDRLMEKVKSGNIVLHTDHTLDEVLGDEMG 217
Cdd:PLN02546 251 KPEKIAIVGGGYIALEFAGIFNGLKSDVHVF-----IRQKKVLrgfdeevRDFVAEQMSLRGIEFHTEESPQAIIKSADG 325
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1725096556 218 VTgvrirSTKAENETRElELAGVFIAIGHSPNTGIFG----GQLELENGYIKVQSgihgnATQTTIPGVFAAGDVMDHI 292
Cdd:PLN02546 326 SL-----SLKTNKGTVE-GFSHVMFATGRKPNTKNLGleevGVKMDKNGAIEVDE-----YSRTSVPSIWAVGDVTDRI 393
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
71-287 |
1.40e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 49.14 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 71 EHAEKFQTEIvFDH--INSVDLQQRpfRLFGDSGEYSCDALIIATGASA---------RYLGLPSEDAFkgkgvsacATC 139
Cdd:PRK04965 66 EFAEQFNLRL-FPHtwVTDIDAEAQ--VVKSQGNQWQYDKLVLATGASAfvppipgreLMLTLNSQQEY--------RAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 140 DGFFYRNQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSFRSEKI---LIDRLMEKVKSGNIVLHTDHTLDEVlgdEM 216
Cdd:PRK04965 135 ETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMppeVSSRLQHRLTEMGVHLLLKSQLQGL---EK 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1725096556 217 GVTGVRIRSTKAenetRELELAGVFIAIGHSPNTgifggQLELENGyIKVQSGIHGNAT-QTTIPGVFAAGD 287
Cdd:PRK04965 212 TDSGIRATLDSG----RSIEVDAVIAAAGLRPNT-----ALARRAG-LAVNRGIVVDSYlQTSAPDIYALGD 273
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
107-287 |
6.86e-06 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 47.47 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 107 DALIIATGAS-ARYLGLPSEDAfkgKGV--------SACATCDGFFY------RNQKVAVVGGGNTA---VEEALYLSni 168
Cdd:PRK12810 230 DAVFLGTGAYkPRDLGIPGRDL---DGVhfamdfliQNTRRVLGDETepfisaKGKHVVVIGGGDTGmdcVGTAIRQG-- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 169 AAEVHlihRRD------SFRSEKILIDR--LMEKVKSG-----NIVLHTDhTLdEVLGDEMGVTGVRIRSTKA------- 228
Cdd:PRK12810 305 AKSVT---QRDimpmppSRRNKNNPWPYwpMKLEVSNAheegvEREFNVQ-TK-EFEGENGKVTGVKVVRTELgegdfep 379
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1725096556 229 -ENETRELELAGVFIAIGHSPNTGIFGGQLELE---NGYIKVQSGIHgnatQTTIPGVFAAGD 287
Cdd:PRK12810 380 vEGSEFVLPADLVLLAMGFTGPEAGLLAQFGVEldeRGRVAAPDNAY----QTSNPKVFAAGD 438
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
145-307 |
7.39e-06 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 47.52 E-value: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 145 RNQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDsfRSE-KILIDRLMEKVKSGnIVLHTDHTLDEVLGDEMG--VTGV 221
Cdd:PRK12779 446 KGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRRT--KSEmPARVEELHHALEEG-INLAVLRAPREFIGDDHThfVTHA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 222 RI-------------RSTKAENETRELELAGVFIAIGHSPNTGIFGGQLELEN---GYIKVQSGihgnATQTTIPGVFAA 285
Cdd:PRK12779 523 LLdvnelgepdksgrRSPKPTGEIERVPVDLVIMALGNTANPIMKDAEPGLKTnkwGTIEVEKG----SQRTSIKGVYSG 598
|
170 180
....*....|....*....|....*
gi 1725096556 286 GDVMdhiyR---QAITSAGTGCMAA 307
Cdd:PRK12779 599 GDAA----RggsTAIRAAGDGQAAA 619
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
9-288 |
2.47e-05 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 45.53 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 9 LLILGSGPAGYTAAVYAARANLSPVLItgmEQGGQL--------T--------TTTEVENW--------PGDAEGLTGPA 64
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVI---ERYRNVgggcthtgTipskalreAVLRLIGFnqnplyssYRVKLRITFAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 65 LMERMREHAEKfQTEIV---FDHiNSVDLQQ-----------RPFRLFGDSGEYSCDALIIATGAS-ARylglPSEDAFK 129
Cdd:PRK05249 85 LLARADHVINK-QVEVRrgqYER-NRVDLIQgrarfvdphtvEVECPDGEVETLTADKIVIATGSRpYR----PPDVDFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 130 GKGV--SacatcDGFF---YRNQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSFRS--EKILIDRLMEKVKSGNIVL 202
Cdd:PRK05249 159 HPRIydS-----DSILsldHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSflDDEISDALSYHLRDSGVTI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 203 HTDHTLDEVLGDEMGVT-----GVRIRSTKaenetrelelagVFIAIGHSPNTGifggQLELEN--------GYIKVqsg 269
Cdd:PRK05249 234 RHNEEVEKVEGGDDGVIvhlksGKKIKADC------------LLYANGRTGNTD----GLNLENagleadsrGQLKV--- 294
|
330 340
....*....|....*....|
gi 1725096556 270 ihgNAT-QTTIPGVFAAGDV 288
Cdd:PRK05249 295 ---NENyQTAVPHIYAVGDV 311
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
110-288 |
5.34e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 44.53 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 110 IIATGASARYL-GLPsedaFKGKGVSACATCDGFFYRNQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSFRS---EK 185
Cdd:PRK06327 150 IIATGSEPRHLpGVP----FDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAaadEQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 186 ILIDRLMEKVKSGnIVLHTDHTLDEVlgdEMGVTGVRIRSTKAENETRELELAGVFIAIGHSPNTGIFGGQ---LEL-EN 261
Cdd:PRK06327 226 VAKEAAKAFTKQG-LDIHLGVKIGEI---KTGGKGVSVAYTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEavgLKLdER 301
|
170 180
....*....|....*....|....*..
gi 1725096556 262 GYIKVQSGIHgnatqTTIPGVFAAGDV 288
Cdd:PRK06327 302 GFIPVDDHCR-----TNVPNVYAIGDV 323
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
146-248 |
7.15e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 44.47 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 146 NQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDSF--------------RSEKILIDRLMEKVKS-GNIVLHTDHTLDE 210
Cdd:COG1148 140 NKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELggraaqlhktfpglDCPQCILEPLIAEVEAnPNITVYTGAEVEE 219
|
90 100 110
....*....|....*....|....*....|....*...
gi 1725096556 211 VLGdEMGVTGVRIRstKAENETRELELAGVFIAIGHSP 248
Cdd:COG1148 220 VSG-YVGNFTVTIK--KGPREEIEIEVGAIVLATGFKP 254
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
4-288 |
2.47e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 42.83 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 4 AKHSKLLILGSGPAGYTAAVYAARAnlspvlitgmeqgGQLTTTTEVENWPGDAEGLTGPalmeRMREHAEKFQTEIVFD 83
Cdd:PRK13984 281 KKNKKVAIVGSGPAGLSAAYFLATM-------------GYEVTVYESLSKPGGVMRYGIP----SYRLPDEALDKDIAFI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 84 -------HINSVDLQQRPFRLFGDsgEYscDALIIATGAS-ARYLGLPS---EDAFKG----KGVSACATCDG-FFYRNQ 147
Cdd:PRK13984 344 ealgvkiHLNTRVGKDIPLEELRE--KH--DAVFLSTGFTlGRSTRIPGtdhPDVIQAlpllREIRDYLRGEGpKPKIPR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 148 KVAVVGGGNTAVEEALYLSNI------AAEVHLIHRRDSFrsEKILIDrlMEKVKSG---NIVLHTDHTLDEVLGDEMGV 218
Cdd:PRK13984 420 SLVVIGGGNVAMDIARSMARLqkmeygEVNVKVTSLERTF--EEMPAD--MEEIEEGleeGVVIYPGWGPMEVVIENDKV 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 219 TGVRIRSTKA-------------ENETRELELAGVFIAIGHSPNTGIFG----GQLELENGYIKVQsgihgNATQTTIPG 281
Cdd:PRK13984 496 KGVKFKKCVEvfdeegrfnpkfdESDQIIVEADMVVEAIGQAPDYSYLPeelkSKLEFVRGRILTN-----EYGQTSIPW 570
|
....*..
gi 1725096556 282 VFAAGDV 288
Cdd:PRK13984 571 LFAGGDI 577
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
9-84 |
9.95e-04 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 40.67 E-value: 9.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 9 LLILGSGPAGYTAAVYAARANLSPVLI-TGMEQGGQLTT---TTEVENWPGDAEGLTGPA--LMERMRE------HAEKF 76
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVeRRGFLGGMLTSglvGPDMGFYLNKEQVVGGIAreFRQRLRArgglpgPYGLR 81
|
....*...
gi 1725096556 77 QTEIVFDH 84
Cdd:pfam12831 82 GGWVPFDP 89
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
9-288 |
1.38e-03 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 40.13 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 9 LLILGSGPAGYTAAVYAARANLSPVLITGMEQGG-----------QLTTTTEVENWPGDAEGL----TGPAL-MERMREH 72
Cdd:PRK06416 7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGtclnrgcipskALLHAAERADEARHSEDFgikaENVGIdFKKVQEW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 73 A---------------EKFQTEIV-----FDHINSVDLQQRpfrlfGDSGEYSCDALIIATGASARYL-GLP-------- 123
Cdd:PRK06416 87 KngvvnrltggvegllKKNKVDIIrgeakLVDPNTVRVMTE-----DGEQTYTAKNIILATGSRPRELpGIEidgrviwt 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 124 SEDAFKGKGVSacatcdgffyrnQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRDS----FRSEkilIDRLMEKV-KSG 198
Cdd:PRK06416 162 SDEALNLDEVP------------KSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRilpgEDKE---ISKLAERAlKKR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 199 NIVLHTDHTLDEVLGDEMGVTgVRIrSTKAENETRELELagVFIAIGHSPNTGIFG----GqLELENGYIKVQSGIHgna 274
Cdd:PRK06416 227 GIKIKTGAKAKKVEQTDDGVT-VTL-EDGGKEETLEADY--VLVAVGRRPNTENLGleelG-VKTDRGFIEVDEQLR--- 298
|
330
....*....|....
gi 1725096556 275 tqTTIPGVFAAGDV 288
Cdd:PRK06416 299 --TNVPNIYAIGDI 310
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
9-61 |
2.68e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 39.33 E-value: 2.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1725096556 9 LLILGSGPAGYTAAVYAARANLSPVLITGMEQGGQLTTTTEVENW-PGDAEGLT 61
Cdd:PRK12843 19 VIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGTTATSAGTTWiPGTRHGLA 72
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
145-244 |
7.17e-03 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 37.85 E-value: 7.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1725096556 145 RNQKVAVVGGGNTAVEEALYLSNIAAEVHLIHRRD-----------SFRSEKILIDRLMEKVKSGNIVLHTDH------T 207
Cdd:PRK11749 139 TGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDkaggllrygipEFRLPKDIVDREVERLLKLGVEIRTNTevgrdiT 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1725096556 208 LDEvLGDE-------MGVTGVRIRSTKAENetreleLAGVFIAI 244
Cdd:PRK11749 219 LDE-LRAGydavfigTGAGLPRFLGIPGEN------LGGVYSAV 255
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
8-54 |
7.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 37.94 E-value: 7.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1725096556 8 KLLILGSGPAGYTAAVYAARANLSPVLITGMEQGGQLTTTTEVENWP 54
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFEFGGLP 47
|
|
|