|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
1-438 |
0e+00 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 866.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 1 MPKIVVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYVIGEVVEDRKYALAYTPEKFYDRKQITVKTYHE 80
Cdd:PRK13512 1 MPKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYALAYTPEKFYDRKQITVKTYHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 81 VIAINDERQTVTVLNRKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVS 160
Cdd:PRK13512 81 VIAINDERQTVTVLNRKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVDKALVVGAGYIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 161 LEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTINGNEITFKSGKVEHYDMIIEGVGTH 240
Cdd:PRK13512 161 LEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGNEVTFKSGKVEHYDMIIEGVGTH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 241 PNSKFIESSNIKIDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGF 320
Cdd:PRK13512 241 PNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 321 LGNNIVKFFDYTFASVGVKPNELKQFDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNHQILRAAAVGKEGADKRIDVLS 400
Cdd:PRK13512 321 LGNNIVKFFDYTFASVGVKPNELKQFDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNRKILRAAAVGKEGADKRIDVLS 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 447047256 401 MAMMNQLTVDELTEFEVAYAPPYSHPKDLINMIGYKAK 438
Cdd:PRK13512 401 MAMMNQLTVDELTEFEVAYAPPYSHPKDLINMIGYKAK 438
|
|
| CoA_CoA_reduc |
TIGR03385 |
CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1. ... |
15-434 |
0e+00 |
|
CoA-disulfide reductase; Members of this protein family are CoA-disulfide reductase (EC 1.8.1.14), as characterized in Staphylococcus aureus, Pyrococcus horikoshii, and Borrelia burgdorferi, and inferred in several other species on the basis of high levels of CoA and an absence of glutathione as a protective thiol. [Cellular processes, Detoxification]
Pssm-ID: 163244 [Multi-domain] Cd Length: 427 Bit Score: 663.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 15 TCASQIRRLDKESDIIIFEKDRDMSFANCALPYVIGEVVEDRKYALAYTPEKFYDRKQITVKTYHEVIAINDERQTVTVL 94
Cdd:TIGR03385 1 SAASRVRRLDKESDIIVFEKTEDVSFANCGLPYVIGGVIDDRNKLLAYTPEVFIKKRGIDVKTNHEVIEVNDERQTVVVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 95 NRKTNEQFEESYDKLILSPGASANSLGFES---DITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVSLEVLENLYERG 171
Cdd:TIGR03385 81 NNKTNETYEESYDYLILSPGASPIVPNIEGinlDIVFTLRNLEDTDAIKQYIDKNKVENVVIIGGGYIGIEMAEALRERG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 172 LHPTLIHRSDKI-NKLMDADMNQPILDELDKREIPYRLNEEIDTINGNEI--TFKSGKVEHYDMIIEGVGTHPNSKFIES 248
Cdd:TIGR03385 161 KNVTLIHRSERIlNKLFDEEMNQIVEEELKKHEINLRLNEEVDSIEGEERvkVFTSGGVYQADMVILATGIKPNSELAKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 249 SNIKIDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDtIEFKGFLGNNIVKF 328
Cdd:TIGR03385 241 SGLKLGETGAIWVNEKFQTSVPNIYAAGDVAESHNIITKKPAWVPLAWGANKMGRIAGENIAGND-IEFKGVLGTNITKF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 329 FDYTFASVGVKPNELK--QFDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNHQILRAAAVGKEGADKRIDVLSMAMMNQ 406
Cdd:TIGR03385 320 FDLTIASTGVTENEAKklNIDYKTVFVKAKTHANYYPGNSPLHLKLIYEKDTRRILGAQAVGKEGADKRIDVLAAAIMAG 399
|
410 420
....*....|....*....|....*...
gi 447047256 407 LTVDELTEFEVAYAPPYSHPKDLINMIG 434
Cdd:TIGR03385 400 LTVKDLFFFELAYAPPYSRVWDPLNMAG 427
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
22-337 |
1.84e-100 |
|
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: 302.50 E-value: 1.84e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 22 RLDKESDIIIFEKDRDMSFANCALPYVIGEVVEDRKYALAYTPEKFyDRKQITVKTYHEVIAINDERQTVTVlnrKTNEq 101
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESF-ERKGIDVRTGTEVTAIDPEAKTVTL---RDGE- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 102 fEESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVSLEVLENLYERGLHPTLIH 178
Cdd:COG0446 76 -TLSYDKLVLATGARPRPPpipGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 179 RSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTINGNE---ITFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKIDR 255
Cdd:COG0446 155 RAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGDDkvaVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 256 KGFIPVNDKFETNVPNIYAIGDIATSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDtIEFKGfLGNNIVKFFDYTFAS 335
Cdd:COG0446 235 RGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGP-APFPG-LGTFISKVFDLCIAS 312
|
..
gi 447047256 336 VG 337
Cdd:COG0446 313 TG 314
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
17-438 |
2.97e-93 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 288.48 E-value: 2.97e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 17 ASQIRRLDKESDIIIFEKDRDMSFANCALPYVIGEVVEDRKYALAYTPEKFyDRKQITVKTYHEVIAINDERQTVTVLNR 96
Cdd:PRK09564 16 AAKAKRLNKELEITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEF-IKSGIDVKTEHEVVKVDAKNKTITVKNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 97 KTNEQFEESYDKLILSPGASA---NSLGFESDITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVSLEVLENLYERGLH 173
Cdd:PRK09564 95 KTGSIFNDTYDKLMIATGARPiipPIKNINLENVYTLKSMEDGLALKELLKDEEIKNIVIIGAGFIGLEAVEAAKHLGKN 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 174 PTLIHRSDKI-NKLMDADMNQPILDELDKREIPYRLNEEIDTINGNE-----ITFKsGKVEhYDMIIEGVGTHPNSKFIE 247
Cdd:PRK09564 175 VRIIQLEDRIlPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDkvegvVTDK-GEYE-ADVVIVATGVKPNTEFLE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 248 SSNIKIDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTiEFKGFLGNNIVK 327
Cdd:PRK09564 253 DTGLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGRMVGENLAGRHV-SFKGTLGSACIK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 328 FFDYTFASVGVKPNELKQ--FDYKMVEVTQGAHANYYPGNSPLHLRVYYDTSNHQILRAAAVGKEGADKRIDVLSMAMMN 405
Cdd:PRK09564 332 VLDLEAARTGLTEEEAKKlgIDYKTVFIKDKNHTNYYPGQEDLYVKLIYEADTKVILGGQIIGKKGAVLRIDALAVAIYA 411
|
410 420 430
....*....|....*....|....*....|...
gi 447047256 406 QLTVDELTEFEVAYAPPYSHPKDLINMIGYKAK 438
Cdd:PRK09564 412 KLTTQELGMMDFCYAPPFARTWDALNVAGNVAK 444
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
9-337 |
4.84e-55 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 187.66 E-value: 4.84e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 9 AVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYVI-GEVVEDRkyaLAYTPEKFYDRKQITVKTYHEVIAINDE 87
Cdd:COG1251 9 AGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLaGETDEED---LLLRPADFYEENGIDLRLGTRVTAIDRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 88 RQTVTvlnrkTNEQFEESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIDQFIKanQVDKVLVVGAGYVSLEVL 164
Cdd:COG1251 86 ARTVT-----LADGETLPYDKLVLATGSRPRVPpipGADLPGVFTLRTLDDADALRAALA--PGKRVVVIGGGLIGLEAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 165 ENLYERGLHPTLIHRSDKI-NKLMDADMNQPILDELDKREIPYRLNEEIDTINGNE----ITFKSGKVEHYDMIIEGVGT 239
Cdd:COG1251 159 AALRKRGLEVTVVERAPRLlPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDrvtgVRLADGEELPADLVVVAIGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 240 HPNSKFIESSNIKIDRkGfIPVNDKFETNVPNIYAIGDIATSHYRHVDLP--ASVPLAWgahRAASIVAEQIAGNDTiEF 317
Cdd:COG1251 239 RPNTELARAAGLAVDR-G-IVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRvlELVAPAY---EQARVAAANLAGGPA-AY 312
|
330 340
....*....|....*....|
gi 447047256 318 KGFLGNNIVKFFDYTFASVG 337
Cdd:COG1251 313 EGSVPSTKLKVFGVDVASAG 332
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
15-286 |
2.96e-48 |
|
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: 167.11 E-value: 2.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 15 TCASQIRRLDKEsdIIIFEKDRDMSFANCALPYVIGEVVEDRKYALayTPEKFYDRKQITVKTY---------HEVIAIN 85
Cdd:pfam07992 14 AAALTLAQLGGK--VTLIEDEGTCPYGGCVLSKALLGAAEAPEIAS--LWADLYKRKEEVVKKLnngievllgTEVVSID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 86 DERQTVTVLNRKTNEQFEESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIDQFIKANqvdKVLVVGAGYVSLE 162
Cdd:pfam07992 90 PGAKKVVLEELVDGDGETITYDRLVIATGARPRLPpipGVELNVGFLVRTLDSAEALRLKLLPK---RVVVVGGGYIGVE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 163 VLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTINGN----EITFKSGKVEHYDMIIEGVG 238
Cdd:pfam07992 167 LAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDgdgvEVILKDGTEIDADLVVVAIG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447047256 239 THPNSKFIESSNIKIDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHV 286
Cdd:pfam07992 247 RRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELA 294
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
107-426 |
2.64e-30 |
|
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: 121.73 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 107 DKLILSPGASANSLGFEsditftlrNLEDTDAI--DQFIKANQV-DKVLVVGAGYVSLE---VLENLyerGLHPTLIHRS 180
Cdd:COG1249 132 DHIVIATGSRPRVPPIP--------GLDEVRVLtsDEALELEELpKSLVVIGGGYIGLEfaqIFARL---GSEVTLVERG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 181 DKINKLMDADMNQPILDELDKREIPYRLNEEIDTI----NGNEITFKSGKVEH---YDMIIEGVGTHPNSKFI--ESSNI 251
Cdd:COG1249 201 DRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVektgDGVTVTLEDGGGEEaveADKVLVATGRRPNTDGLglEAAGV 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 252 KIDRKGFIPVNDKFETNVPNIYAIGDIAtshyrhvdlpASVPLAWGAHRAASIVAEQIAGNDtiefkgflgnniVKFFDY 331
Cdd:COG1249 281 ELDERGGIKVDEYLRTSVPGIYAIGDVT----------GGPQLAHVASAEGRVAAENILGKK------------PRPVDY 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 332 ------TF-----ASVGVKPNELKQFDYKMVEVTQGAHANYYP---GNSPLHLRVYYDTSNHQILRAAAVGkEGADKRID 397
Cdd:COG1249 339 raipsvVFtdpeiASVGLTEEEAREAGIDVKVGKFPFAANGRAlalGETEGFVKLIADAETGRILGAHIVG-PHAGELIH 417
|
330 340
....*....|....*....|....*....
gi 447047256 398 VLSMAMMNQLTVDELTEFevayapPYSHP 426
Cdd:COG1249 418 EAALAMEMGLTVEDLADT------IHAHP 440
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
15-320 |
2.67e-28 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 115.23 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 15 TCASQIRR-LDKESDIIIFEKDRDMSFANcALPYVIGEVVEDRKYALAYtpEKFYDRKQITVKTyHEVIAINDERQTVTv 93
Cdd:COG1252 15 EAARRLRKkLGGDAEVTLIDPNPYHLFQP-LLPEVAAGTLSPDDIAIPL--RELLRRAGVRFIQ-GEVTGIDPEARTVT- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 94 lnrkTNEQFEESYDKLILSPGASANSLGFE--SDITFTLRNLEDTDAI-----DQFIKANQVDK--VLVVGAGYVSLEVL 164
Cdd:COG1252 90 ----LADGRTLSYDYLVIATGSVTNFFGIPglAEHALPLKTLEDALALrerllAAFERAERRRLltIVVVGGGPTGVELA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 165 --------ENLYERGLHP-----TLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTINGNEITFKSGKVEHYD 231
Cdd:COG1252 166 gelaellrKLLRYPGIDPdkvriTLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDADGVTLEDGEEIPAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 232 MIIEGVGTHPNSkFIESSNIKIDRKGFIPVNDKFET-NVPNIYAIGDIAtsHYRHVDLPASVPLAWGAHRAASIVAEQIA 310
Cdd:COG1252 246 TVIWAAGVKAPP-LLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCA--AVPDPDGKPVPKTAQAAVQQAKVLAKNIA 322
|
330
....*....|....
gi 447047256 311 ----GNDTIEFKGF 320
Cdd:COG1252 323 allrGKPLKPFRYR 336
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
149-426 |
6.10e-26 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 109.50 E-value: 6.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 149 DKVLVVGAGYVSLE---VLENLyerGLHPTLIHRSDKINKLMDADMNQPILDELDKrEIPYRLN---EEIDTINGNEITF 222
Cdd:PRK06292 170 KSLAVIGGGVIGLElgqALSRL---GVKVTVFERGDRILPLEDPEVSKQAQKILSK-EFKIKLGakvTSVEKSGDEKVEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 223 --KSGKVE--HYDMIIEGVGTHPNSKF--IESSNIKIDRKGFIPVNDKFETNVPNIYAIGDIATSHyrhvdlpasvPLAW 296
Cdd:PRK06292 246 leKGGKTEtiEADYVLVATGRRPNTDGlgLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKP----------PLLH 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 297 GAHRAASIVAEQIAGNDTIEFKGFLGNNIVkffdYTF---ASVGVKPNELKQ--FDYKMVEV---TQG-AHANyypGNSP 367
Cdd:PRK06292 316 EAADEGRIAAENAAGDVAGGVRYHPIPSVV----FTDpqiASVGLTEEELKAagIDYVVGEVpfeAQGrARVM---GKND 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447047256 368 LHLRVYYDTSNHQILRAAAVGkEGADKRIDVLSMAMMNQLTVDELTEFevayapPYSHP 426
Cdd:PRK06292 389 GFVKVYADKKTGRLLGAHIIG-PDAEHLIHLLAWAMQQGLTVEDLLRM------PFYHP 440
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
78-313 |
3.50e-24 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 101.74 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 78 YHEVIAINDERQTVTVlnrKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQvdKVLVVGAG 157
Cdd:COG0492 76 LEEVTSVDKDDGPFRV---TTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGK--DVVVVGGG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 158 YVSLEVLENLYERGLHPTLIHRSDKinkLMDADMNQPILDELDKreIPYRLNEEIDTINGNE----ITFKSGKV-EHYDM 232
Cdd:COG0492 151 DSALEEALYLTKFASKVTLIHRRDE---LRASKILVERLRANPK--IEVLWNTEVTEIEGDGrvegVTLKNVKTgEEKEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 233 IIEGV----GTHPNSKFIESSNIKIDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHVdlpasvplAWGAHRAAsivaeq 308
Cdd:COG0492 226 EVDGVfvaiGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQA--------ATAAGEGA------ 291
|
....*
gi 447047256 309 IAGND 313
Cdd:COG0492 292 IAALS 296
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
16-319 |
2.60e-23 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 102.98 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 16 CASQIRRLDKES-DIIIFEKDRDMSFANCALPYVIgEVVEDRKyALAYTPEKFYDRKQITVKTYHEVIAINDERQTVTVL 94
Cdd:TIGR02374 13 CIEEVLKLNRHMfEITIFGEEPHPNYNRILLSSVL-QGEADLD-DITLNSKDWYEKHGITLYTGETVIQIDTDQKQVITD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 95 NRKTneqfeESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIDQfiKANQVDKVLVVGAGYVSLEVLENLYERG 171
Cdd:TIGR02374 91 AGRT-----LSYDKLILATGSYPFILpipGADKKGVYVFRTIEDLDAIMA--MAQRFKKAAVIGGGLLGLEAAVGLQNLG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 172 LHPTLIHRSDKI-NKLMDADMNQPILDELDKREIPYRLNEEIDTINGNE----ITFKSGKVEHYDMIIEGVGTHPNSKFI 246
Cdd:TIGR02374 164 MDVSVIHHAPGLmAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATkadrIRFKDGSSLEADLIVMAAGIRPNDELA 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447047256 247 ESSNIKIDRKgfIPVNDKFETNVPNIYAIGDIATSHYRHVDLPAsvPLawgaHRAASIVAEQIAGNDTIEFKG 319
Cdd:TIGR02374 244 VSAGIKVNRG--IIVNDSMQTSDPDIYAVGECAEHNGRVYGLVA--PL----YEQAKVLADHICGVECEEYEG 308
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
89-412 |
2.34e-22 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 99.06 E-value: 2.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 89 QTVTVLNRKTNEQFEesYDKLILSPGASANSL-GFESD--ITFTlrnleDTDAI--DQFIKanqvdKVLVVGAGYVSLE- 162
Cdd:PRK06416 120 NTVRVMTEDGEQTYT--AKNIILATGSRPRELpGIEIDgrVIWT-----SDEALnlDEVPK-----SLVVIGGGYIGVEf 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 163 --VLENLyerGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLN----EEIDTINGNEITFKSGKVEHY---DMI 233
Cdd:PRK06416 188 asAYASL---GAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGakakKVEQTDDGVTVTLEDGGKEETleaDYV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 234 IEGVGTHPNSKFI--ESSNIKIDRkGFIPVNDKFETNVPNIYAIGDIatshyrhvdlpasVPLAWGAHRA---ASIVAEQ 308
Cdd:PRK06416 265 LVAVGRRPNTENLglEELGVKTDR-GFIEVDEQLRTNVPNIYAIGDI-------------VGGPMLAHKAsaeGIIAAEA 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 309 IAGNDT-IEFKGFLGnniVKFFDYTFASVGVKPNELKQFDYKMVEVTqgahanyYP--GNS-PLHL-------RVYYDTS 377
Cdd:PRK06416 331 IAGNPHpIDYRGIPA---VTYTHPEVASVGLTEAKAKEEGFDVKVVK-------FPfaGNGkALALgetdgfvKLIFDKK 400
|
330 340 350
....*....|....*....|....*....|....*
gi 447047256 378 NHQILRAAAVGKEGADkRIDVLSMAMMNQLTVDEL 412
Cdd:PRK06416 401 DGEVLGAHMVGARASE-LIQEAQLAINWEATPEDL 434
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
90-412 |
1.84e-20 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 93.09 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 90 TVTVLNRKTNEQFEesYDKLILSPGASANSLGFESDitftlrnlEDTDAI---DQFIKANQV-DKVLVVGAGYVSLEvLE 165
Cdd:TIGR01350 118 TVSVTGENGEETLE--AKNIIIATGSRPRSLPGPFD--------FDGKVVitsTGALNLEEVpESLVIIGGGVIGIE-FA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 166 NLYER-GLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTINGN----EITFKSGKVE--HYDMIIEGVG 238
Cdd:TIGR01350 187 SIFASlGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNddqvTYENKGGETEtlTGEKVLVAVG 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 239 THPNSKFI--ESSNIKIDRKGFIPVNDKFETNVPNIYAIGDIAtshyrhvdlpASVPLAWGAHRAASIVAEQIAGNDTIE 316
Cdd:TIGR01350 267 RKPNTEGLglEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVI----------GGPMLAHVASHEGIVAAENIAGKEPAH 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 317 FKGFLGNNIVkffdYTF---ASVGVKPNELKQ--FDYKMVEV-------------TQGahanyypgnsplHLRVYYDTSN 378
Cdd:TIGR01350 337 IDYDAVPSVI----YTDpevASVGLTEEQAKEagYDVKIGKFpfaangkalalgeTDG------------FVKIIADKKT 400
|
330 340 350
....*....|....*....|....*....|....
gi 447047256 379 HQILRAAAVGKEGADkRIDVLSMAMMNQLTVDEL 412
Cdd:TIGR01350 401 GEILGAHIIGPHATE-LISEAALAMELEGTVEEL 433
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
19-279 |
2.72e-18 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 86.12 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 19 QIRRLDKESDIIIFEKDRDMSFANCALPYVI--GEVVED--RKYAlaytpEKFYDRKQITVKTYHEVIAINDERQTVTVl 94
Cdd:PRK04965 20 NIRKQDAHIPITLITADSGDEYNKPDLSHVFsqGQRADDltRQSA-----GEFAEQFNLRLFPHTWVTDIDAEAQVVKS- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 95 nrkTNEQFeeSYDKLILSPGASANSLGFESD-ITFTLRNLEDTDAIDQfiKANQVDKVLVVGAGYVSLEVLENLYERGLH 173
Cdd:PRK04965 94 ---QGNQW--QYDKLVLATGASAFVPPIPGReLMLTLNSQQEYRAAET--QLRDAQRVLVVGGGLIGTELAMDLCRAGKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 174 PTLIHRSDKI-NKLMDADMNQPILDELDKREIPYRLNEEIDTINGNE----ITFKSGKVEHYDMIIEGVGTHPNSKFIES 248
Cdd:PRK04965 167 VTLVDNAASLlASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDsgirATLDSGRSIEVDAVIAAAGLRPNTALARR 246
|
250 260 270
....*....|....*....|....*....|.
gi 447047256 249 SNIKIDRKgfIPVNDKFETNVPNIYAIGDIA 279
Cdd:PRK04965 247 AGLAVNRG--IVVDSYLQTSAPDIYALGDCA 275
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
152-414 |
5.21e-18 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 86.02 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 152 LVVGAGYVSLEvLENLYER-GLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTI----NGNEITFKSGK 226
Cdd:PRK06370 175 VIIGGGYIGLE-FAQMFRRfGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVerdgDGIAVGLDCNG 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 227 VEHY---DMIIEGVGTHPNSKFI--ESSNIKIDRKGFIPVNDKFETNVPNIYAIGDIaTSHYR--HVdlpasvplawgAH 299
Cdd:PRK06370 254 GAPEitgSHILVAVGRVPNTDDLglEAAGVETDARGYIKVDDQLRTTNPGIYAAGDC-NGRGAftHT-----------AY 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 300 RAASIVAEQIAGNDTIEfkgfLGNNIVKFFDYT---FASVGVKPNELKQFDYK-------MVEV--------TQGahany 361
Cdd:PRK06370 322 NDARIVAANLLDGGRRK----VSDRIVPYATYTdppLARVGMTEAEARKSGRRvlvgtrpMTRVgravekgeTQG----- 392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447047256 362 ypgnsplHLRVYYDTSNHQILRAAAVGkEGADKRIDVLSMAMMNQLTVDELTE 414
Cdd:PRK06370 393 -------FMKVVVDADTDRILGATILG-VHGDEMIHEILDAMYAGAPYTTLSR 437
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
150-278 |
6.60e-18 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 85.59 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 150 KVLVVGAGYVSLE---VLENLyerGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTINGNE-----IT 221
Cdd:PRK06116 169 RVAVVGAGYIAVEfagVLNGL---GSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNAdgsltLT 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 447047256 222 FKSGKVEHYDMIIEGVGTHPNSKFI--ESSNIKIDRKGFIPVNDKFETNVPNIYAIGDI 278
Cdd:PRK06116 246 LEDGETLTVDCLIWAIGREPNTDGLglENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
150-345 |
2.51e-17 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 83.82 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 150 KVLVVGAGYVSLEvLENLYER-GLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTI----NGNEITFKS 224
Cdd:PRK06327 185 KLAVIGAGVIGLE-LGSVWRRlGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIktggKGVSVAYTD 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 225 GK----VEHYDMIIEGVGTHPNSKFI--ESSNIKIDRKGFIPVNDKFETNVPNIYAIGDIatshyrhvdlpasVPLAWGA 298
Cdd:PRK06327 264 ADgeaqTLEVDKLIVSIGRVPNTDGLglEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDV-------------VRGPMLA 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 447047256 299 HRA---ASIVAEQIAGNdtiefKGFLGNNIVKFFDYTF---ASVGVKPNELKQ 345
Cdd:PRK06327 331 HKAeeeGVAVAERIAGQ-----KGHIDYNTIPWVIYTSpeiAWVGKTEQQLKA 378
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-225 |
3.89e-16 |
|
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: 73.01 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 150 KVLVVGAGYVSLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTINGNE----ITFKSG 225
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGdgvvVVLTDG 80
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
150-278 |
5.32e-16 |
|
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: 80.02 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 150 KVLVVGAGYVSLEV--LENLYE-RGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNE-----EIDTINGNEIT 221
Cdd:TIGR01423 189 RVLTVGGGFISVEFagIFNAYKpRGGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNEnpakvTLNADGSKHVT 268
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 447047256 222 FKSGKVEHYDMIIEGVGTHPNSKFIESSN--IKIDRKGFIPVNDKFETNVPNIYAIGDI 278
Cdd:TIGR01423 269 FESGKTLDVDVVMMAIGRVPRTQTLQLDKvgVELTKKGAIQVDEFSRTNVPNIYAIGDV 327
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
17-311 |
5.93e-15 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 76.12 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 17 ASQIRRLDKESDIIIFEKDRDMSFANCALP--YVIgEVVEDRKYALaytPEKFYDRKQITVKTyheviaindeRQTVTVL 94
Cdd:PRK09754 19 AASLRQQGFTGELHLFSDERHLPYERPPLSksMLL-EDSPQLQQVL---PANWWQENNVHLHS----------GVTIKTL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 95 NRKTNEQFEES-----YDKLILSPGASANSLGFESDI---TFTLRNLEDTDAIDQFIKANQvdKVLVVGAGYVSLEVLEN 166
Cdd:PRK09754 85 GRDTRELVLTNgeswhWDQLFIATGAAARPLPLLDALgerCFTLRHAGDAARLREVLQPER--SVVIVGAGTIGLELAAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 167 LYERGLHPTLIHRSDKInklMDADMNQPILDELDKRE----IPYRLNEEIDTI-NGNEI--TFKSGKVEHYDMIIEGVGT 239
Cdd:PRK09754 163 ATQRRCKVTVIELAATV---MGRNAPPPVQRYLLQRHqqagVRILLNNAIEHVvDGEKVelTLQSGETLQADVVIYGIGI 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447047256 240 HPNSKFIESSNikIDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHVDLPASVplAW-GAHRAASIVAEQIAG 311
Cdd:PRK09754 240 SANDQLAREAN--LDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCE--SWeNANNQAQIAAAAMLG 308
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
52-337 |
4.38e-14 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 73.65 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 52 VVEDRKYALAYTPEKFYDRKqitvktyheVIAINDERQTVTVLNRKTNEQ-----FEESYDKLILSPGASANSLGFES-- 124
Cdd:PTZ00318 64 ICEPVRPALAKLPNRYLRAV---------VYDVDFEEKRVKCGVVSKSNNanvntFSVPYDKLVVAHGARPNTFNIPGve 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 125 DITFTLRNLEDTDAIDQ-----FIKANQVD----------KVLVVGAGYVSLEVLENLYE------RGLHP--------T 175
Cdd:PTZ00318 135 ERAFFLKEVNHARGIRKrivqcIERASLPTtsveerkrllHFVVVGGGPTGVEFAAELADffrddvRNLNPelveeckvT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 176 LIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTINGNEITFKSGKVEHYDMII--EGVGTHPNSKfiessNIKI 253
Cdd:PTZ00318 215 VLEAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVVLKDGEVIPTGLVVwsTGVGPGPLTK-----QLKV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 254 DRK--GFIPVNDKFET-NVPNIYAIGDIATSHYRhvDLPasvPLAWGAHRAASIVAEQIAGNdtiefkgFLGNNIVKFFD 330
Cdd:PTZ00318 290 DKTsrGRISVDDHLRVkPIPNVFALGDCAANEER--PLP---TLAQVASQQGVYLAKEFNNE-------LKGKPMSKPFV 357
|
330
....*....|.
gi 447047256 331 YTF----ASVG 337
Cdd:PTZ00318 358 YRSlgslAYLG 368
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
87-315 |
3.70e-13 |
|
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: 71.04 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 87 ERQTVTVLNRKTNEQFEeSYDKLILSPGASANSLGFESDITFTLrnleDTDaiDQFIKANQVDKVLVVGAGYVSLEVLEN 166
Cdd:TIGR01438 126 DKHRIKATNKKGKEKIY-SAERFLIATGERPRYPGIPGAKELCI----TSD--DLFSLPYCPGKTLVVGASYVALECAGF 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 167 LYERGLHPTLIHRSDKInKLMDADMNQPILDELDKREIPYR---LNEEIDTINGNEITFKSGK----VEHYDMIIEGVGT 239
Cdd:TIGR01438 199 LAGIGLDVTVMVRSILL-RGFDQDCANKVGEHMEEHGVKFKrqfVPIKVEQIEAKVLVEFTDStngiEEEYDTVLLAIGR 277
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447047256 240 HPNSKFI--ESSNIKIDRK-GFIPVNDKFETNVPNIYAIGDIATshyrhvDLPASVPLAWgahRAASIVAEQIAGNDTI 315
Cdd:TIGR01438 278 DACTRKLnlENVGVKINKKtGKIPADEEEQTNVPYIYAVGDILE------DKPELTPVAI---QAGRLLAQRLFKGSTV 347
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
126-277 |
2.81e-12 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 68.49 E-value: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 126 ITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVSLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKRE-- 203
Cdd:PTZ00058 215 IFPDVKGKEFTISSDDFFKIKEAKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELENDMKKNNin 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447047256 204 -IPYRLNEEIDTINGNEITF---KSGKVEHYDMIIEGVGTHPNSKFIESSNIKI-DRKGFIPVNDKFETNVPNIYAIGD 277
Cdd:PTZ00058 295 iITHANVEEIEKVKEKNLTIylsDGRKYEHFDYVIYCVGRSPNTEDLNLKALNIkTPKGYIKVDDNQRTSVKHIYAVGD 373
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
150-278 |
2.18e-11 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 65.56 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 150 KVLVVGAGYVSLE---VLENLyerGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTI----NGNEITF 222
Cdd:PRK05249 177 SLIIYGAGVIGCEyasIFAAL---GVKVTLINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVeggdDGVIVHL 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 447047256 223 KSGKVEHYDMIIEGVGTHPNSKF--IESSNIKIDRKGFIPVNDKFETNVPNIYAIGDI 278
Cdd:PRK05249 254 KSGKKIKADCLLYANGRTGNTDGlnLENAGLEADSRGQLKVNENYQTAVPHIYAVGDV 311
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
60-319 |
2.96e-11 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 65.52 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 60 LAYTPEKFYDRKQITVKTYHEVIAINDERQTVtvlnrKTNEQFEESYDKLILSPGAS---ANSLGFESDITFTLRNLEDT 136
Cdd:PRK14989 61 LSLVREGFYEKHGIKVLVGERAITINRQEKVI-----HSSAGRTVFYDKLIMATGSYpwiPPIKGSETQDCFVYRTIEDL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 137 DAIDQfiKANQVDKVLVVGAGYVSLEVLENLYERGLHPTLIHRSDkinKLMDADMNQPILDELdKREIPyRLNEEIDTI- 215
Cdd:PRK14989 136 NAIEA--CARRSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAP---MLMAEQLDQMGGEQL-RRKIE-SMGVRVHTSk 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 216 NGNEIT-----------FKSGKVEHYDMIIEGVGTHPNSKFIESSNIKIDRKGFIPVNDKFETNVPNIYAIGDIATSHYR 284
Cdd:PRK14989 209 NTLEIVqegvearktmrFADGSELEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGECASWNNR 288
|
250 260 270
....*....|....*....|....*....|....*
gi 447047256 285 HVDLPASvplawgAHRAASIVAEQIAGNDTiEFKG 319
Cdd:PRK14989 289 VFGLVAP------GYKMAQVAVDHLLGSEN-AFEG 316
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
149-276 |
2.26e-10 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 61.47 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 149 DKVLVVGAGYVSLEVLENLYERGLHPTLIHRSDKINKlMDADM-------NQPILDEL-DKREIPYRLNEEIDTI----N 216
Cdd:pfam13738 156 QKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWED-RDSDPsyslspdTLNRLEELvKNGKIKAHFNAEVKEItevdV 234
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447047256 217 GNEITFKSG-KVEHYDMIIEGVGTHPNSKFIESSNIKIDRKGFIPVNDK-FETNVPNIYAIG 276
Cdd:pfam13738 235 SYKVHTEDGrKVTSNDDPILATGYHPDLSFLKKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
151-286 |
2.57e-09 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 58.81 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 151 VLVVGAGYVSLE---VLENLyerGLHPTLIHRSDKINKLMDADMNQPILdELDKREIPYRLNEEI----DTINGNEITFK 223
Cdd:PRK07846 169 LVIVGGGFIAAEfahVFSAL---GVRVTVVNRSGRLLRHLDDDISERFT-ELASKRWDVRLGRNVvgvsQDGSGVTLRLD 244
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447047256 224 SGKVEHYDMIIEGVGTHPNSKFI--ESSNIKIDRKGFIPVnDKFE-TNVPNIYAIGDIATSH-YRHV 286
Cdd:PRK07846 245 DGSTVEADVLLVATGRVPNGDLLdaAAAGVDVDEDGRVVV-DEYQrTSAEGVFALGDVSSPYqLKHV 310
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
150-333 |
3.61e-09 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 58.68 E-value: 3.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 150 KVLVVGAGYVSLEVLENLYERGLHPTLIHRSDKInKLMDADMNQPILDELDKREIPYR---LNEEIDTINGN-EITFKSG 225
Cdd:PTZ00052 184 KTLIVGASYIGLETAGFLNELGFDVTVAVRSIPL-RGFDRQCSEKVVEYMKEQGTLFLegvVPINIEKMDDKiKVLFSDG 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 226 KVEHYDMIIEGVGTHPNSKFI--ESSNIKIDRKGFIPVNDKfETNVPNIYAIGDIAtshyrhVDLPASVPLAWgahRAAS 303
Cdd:PTZ00052 263 TTELFDTVLYATGRKPDIKGLnlNAIGVHVNKSNKIIAPND-CTNIPNIFAVGDVV------EGRPELTPVAI---KAGI 332
|
170 180 190
....*....|....*....|....*....|
gi 447047256 304 IVAEQIAGNDTiefkgflgnnivKFFDYTF 333
Cdd:PTZ00052 333 LLARRLFKQSN------------EFIDYTF 350
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
96-285 |
6.28e-09 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 56.99 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 96 RKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQvdKVLVVGAGYVSLEVLENLYERGLHPT 175
Cdd:PRK10262 96 RLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQ--KVAVIGGGNTAVEEALYLSNIASEVH 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 176 LIHRSDKINKlmDADMNQPILDELDKREIPYRLNEEIDTINGNEI---------TFKSGKVEHYDM--IIEGVGTHPNSK 244
Cdd:PRK10262 174 LIHRRDGFRA--EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMgvtgvrlrdTQNSDNIESLDVagLFVAIGHSPNTA 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 447047256 245 FIESsNIKIDrKGFIPVN-----DKFETNVPNIYAIGDIATSHYRH 285
Cdd:PRK10262 252 IFEG-QLELE-NGYIKVQsgihgNATQTSIPGVFAAGDVMDHIYRQ 295
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
326-424 |
9.65e-09 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 52.94 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 326 VKFFDYTFASVGVKPNELKQ----FDYKMVEVTQGAHANYYPGNSPlHLRVYYDTSNHQILRAAAVGKEGADkRIDVLSM 401
Cdd:pfam02852 4 VVFTDPEIASVGLTEEEAKEkggeVKVGKFPFAANGRALAYGDTDG-FVKLVADRETGKILGAHIVGPNAGE-LIQEAAL 81
|
90 100
....*....|....*....|...
gi 447047256 402 AMMNQLTVDELTEfEVAYAPPYS 424
Cdd:pfam02852 82 AIKMGATVEDLAN-TIHIHPTLS 103
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
100-407 |
4.33e-08 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 55.14 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 100 EQFEESYDKLILSPGASANSLGFeSDITfTLRNLEDTDAIDQFikANQVDKVLVVGAGYVSLEvLENLYER-GLHPTLIH 178
Cdd:PRK07251 113 EKIELTAETIVINTGAVSNVLPI-PGLA-DSKHVYDSTGIQSL--ETLPERLGIIGGGNIGLE-FAGLYNKlGSKVTVLD 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 179 RSDKINKLMDADMNQPILDELDKREIPYRLN---EEIDTINGNEITFKSGKVEHYDMIIEGVGTHPNSKFI--ESSNIKI 253
Cdd:PRK07251 188 AASTILPREEPSVAALAKQYMEEDGITFLLNahtTEVKNDGDQVLVVTEDETYRFDALLYATGRKPNTEPLglENTDIEL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 254 DRKGFIPVNDKFETNVPNIYAIGDI-ATSHYRHVDLPASvplawgahraaSIVAEQIAGNDTIEFKGFLGNNIVKFFDYT 332
Cdd:PRK07251 268 TERGAIKVDDYCQTSVPGVFAVGDVnGGPQFTYISLDDF-----------RIVFGYLTGDGSYTLEDRGNVPTTMFITPP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 333 FASVGVKPNELKQ--FDYK----MVEVTQGAHANyypGNSPLHLRVYYDTSNHQILRAAAVGkEGADKRIDVLSMAMMNQ 406
Cdd:PRK07251 337 LSQVGLTEKEAKEagLPYAvkelLVAAMPRAHVN---NDLRGAFKVVVNTETKEILGATLFG-EGSQEIINLITMAMDNK 412
|
.
gi 447047256 407 L 407
Cdd:PRK07251 413 I 413
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
150-278 |
7.21e-08 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 54.44 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 150 KVLVVGAGYVSLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYR----LNEEIDTINGNEITFKSG 225
Cdd:PLN02507 205 RAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHprtnLTQLTKTEGGIKVITDHG 284
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 447047256 226 KVEHYDMIIEGVGTHPNSKFI--ESSNIKIDRKGFIPVNDKFETNVPNIYAIGDI 278
Cdd:PLN02507 285 EEFVADVVLFATGRAPNTKRLnlEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV 339
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
149-278 |
4.04e-07 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 52.19 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 149 DKVLVVGAGYVSLEV--LENLYERGLHptLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTI---NGNEITFK 223
Cdd:PLN02546 253 EKIAIVGGGYIALEFagIFNGLKSDVH--VFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIiksADGSLSLK 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 447047256 224 SGK--VEHYDMIIEGVGTHPNSKFI--ESSNIKIDRKGFIPVNDKFETNVPNIYAIGDI 278
Cdd:PLN02546 331 TNKgtVEGFSHVMFATGRKPNTKNLglEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDV 389
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
231-312 |
7.63e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 51.67 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 231 DMIIEGVGTHPNsKFIESS--NIKIDRKGFIPVNDKFETNVPNIYAIGDIATShyrhvdlPASVPLAWGA-HRAASIVAE 307
Cdd:PRK12778 676 DLVIVSVGVSPN-PLVPSSipGLELNRKGTIVVDEEMQSSIPGIYAGGDIVRG-------GATVILAMGDgKRAAAAIDE 747
|
....*
gi 447047256 308 QIAGN 312
Cdd:PRK12778 748 YLSSK 752
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
231-280 |
5.96e-06 |
|
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: 48.21 E-value: 5.96e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 447047256 231 DMIIEGVGTHPNSKFIESS-NIKIDRKGFIPVNDK-FETNVPNIYAIGDIAT 280
Cdd:COG0493 361 DLVILAIGQTPDPSGLEEElGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVR 412
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
206-280 |
8.19e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 47.87 E-value: 8.19e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447047256 206 YRLNEEIDTINGNEITFKSGKVEHYDMIIEGVGTHPNSKFIESSN-IKIDRKGFIPVNDK-FETNVPNIYAIGDIAT 280
Cdd:PRK11749 352 MELGEPDASGRRRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTPgLELNRWGTIIADDEtGRTSLPGVFAGGDIVT 428
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
150-280 |
4.71e-05 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 45.37 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 150 KVLVVGAGYVSLEV-LENLYERGLHPTLIHR---------SDKINKLMDA-----DMNQP--ILDElDKRE----IPYRL 208
Cdd:PRK12770 174 KVVVVGAGLTAVDAaLEAVLLGAEKVYLAYRrtineapagKYEIERLIARgveflELVTPvrIIGE-GRVEgvelAKMRL 252
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447047256 209 NEEIDTING-NEITFKSGKVEHYDMIIEGVGTHPNSKF-IESSNIKIDRKGFIPVNDKFETNVPNIYAIGDIAT 280
Cdd:PRK12770 253 GEPDESGRPrPVPIPGSEFVLEADTVVFAIGEIPTPPFaKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVT 326
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
231-302 |
1.06e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 44.24 E-value: 1.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447047256 231 DMIIEGVGTHPNsKFIESS--NIKIDRKGFIPVN-DKFETNVPNIYAIGDIATShyrhvdlPASVPLAWGAHRAA 302
Cdd:PRK12831 386 DTVIMSLGTSPN-PLISSTtkGLKINKRGCIVADeETGLTSKEGVFAGGDAVTG-------AATVILAMGAGKKA 452
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
153-278 |
4.19e-04 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 42.31 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447047256 153 VVGAGYVSLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDTINGNE--ITFKSGKVEH- 229
Cdd:PRK08010 163 ILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISHHEnqVQVHSEHAQLa 242
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 447047256 230 YDMIIEGVGTHPNSKFIESSN--IKIDRKGFIPVNDKFETNVPNIYAIGDI 278
Cdd:PRK08010 243 VDALLIASGRQPATASLHPENagIAVNERGAIVVDKYLHTTADNIWAMGDV 293
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
217-277 |
9.88e-04 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 41.29 E-value: 9.88e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447047256 217 GNEITFKSGKVE-HYDMIIEGVGTHPNSKFI--ESSNIKIDRKGFIPVNDKFETNVPNIYAIGD 277
Cdd:PRK13748 340 DGEFVLTTGHGElRADKLLVATGRAPNTRSLalDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGD 403
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
234-277 |
1.74e-03 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 40.61 E-value: 1.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 447047256 234 IEG------VGTHPNSKFI--ESSNIKIDRKGFIPVNDKFETNVPNIYAIGD 277
Cdd:PRK07845 261 VEGshalmaVGSVPNTAGLglEEAGVELTPSGHITVDRVSRTSVPGIYAAGD 312
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
218-283 |
3.27e-03 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 39.76 E-value: 3.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447047256 218 NEITFK---SGKVEHYDmiIEGV----GTHPNSKFIESSnIKIDRKGFIPVNDKFETNVPNIYAIGDIATSHY 283
Cdd:PRK15317 421 TGLTYKdrtTGEEHHLE--LEGVfvqiGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCTTVPY 490
|
|
| |
