|
Name |
Accession |
Description |
Interval |
E-value |
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
2-491 |
8.70e-158 |
|
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: 456.09 E-value: 8.70e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 2 SEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDaTVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVNGIDF 81
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKG-RLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAPSVDW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 82 GTLRDYRLRVVKTMVGGLAGLLAHRGITVFRANAAFhadetapaTSNHIVHLvpspdqsdiltyhkadvpepSGPTMdLT 161
Cdd:COG1249 80 AALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARF--------VDPHTVEV--------------------TGGET-LT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 162 TTNIVIATGAKPRPLPGNPFAGALI-DSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDRR 240
Cdd:COG1249 131 ADHIVIATGSRPRVPPIPGLDEVRVlTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 241 AGTTLTRELKRHGVNIITRASVTHVDTGANlGATVHYtrEGQDGEQSVWGEIALVAIGRDPITD----PAWGVTIDDHGH 316
Cdd:COG1249 211 ISEALEKALEKEGIDILTGAKVTSVEKTGD-GVTVTL--EDGGGEEAVEADKVLVATGRRPNTDglglEAAGVELDERGG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 317 VATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFPEAASVGLTveQAQAREDL 396
Cdd:COG1249 288 IKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLT--EEEAREAG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 397 IEIKETNYPMLANARMLMSG-TAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLVHPHP 475
Cdd:COG1249 366 IDVKVGKFPFAANGRALALGeTEGFVKLI-----ADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHP 440
|
490
....*....|....*.
gi 2796464736 476 TFSETLGEALLKADGR 491
Cdd:COG1249 441 TLSEALKEAALALLGR 456
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
1-495 |
6.39e-151 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 438.81 E-value: 6.39e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 1 MSEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDaTVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVNGID 80
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKE-KLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 81 FGTLRDYRLRVVKTMVGGLAGLLAHRGITVFRANAAFHADetapatsnhivhlvpspdqsdiltyHKADVPEPSGPTmDL 160
Cdd:PRK06416 80 FKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDP-------------------------NTVRVMTEDGEQ-TY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 161 TTTNIVIATGAKPRPLPGNPFAGALI-DSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDR 239
Cdd:PRK06416 134 TAKNIILATGSRPRELPGIEIDGRVIwTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDK 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 240 RAGTTLTRELKRHGVNIITRASVTHVDTGANlGATVHYtrEGQDGEQSVWGEIALVAIGRDPITD----PAWGVTIDdHG 315
Cdd:PRK06416 214 EISKLAERALKKRGIKIKTGAKAKKVEQTDD-GVTVTL--EDGGKEETLEADYVLVAVGRRPNTEnlglEELGVKTD-RG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 316 HVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGlNPKPVDEATVPQIVFSFPEAASVGLTveQAQARED 395
Cdd:PRK06416 290 FIEVDEQLRTNVPNIYAIGDIVGGPMLAHKASAEGIIAAEAIAG-NPHPIDYRGIPAVTYTHPEVASVGLT--EAKAKEE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 396 LIEIKETNYPMLANARML-MSGTAGSLTIVSgcdaaNPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLVHPH 474
Cdd:PRK06416 367 GFDVKVVKFPFAGNGKALaLGETDGFVKLIF-----DKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPH 441
|
490 500
....*....|....*....|.
gi 2796464736 475 PTFSETLGEALLKADGRPLHT 495
Cdd:PRK06416 442 PTLSEALGEAALAAAGKPLHA 462
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
5-494 |
2.47e-137 |
|
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: 403.95 E-value: 2.47e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIERDaTVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVNGIDFGTL 84
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVEKE-YLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVENVSVDWEKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 85 RDYRLRVVKTMVGGLAGLLAHRGITVFRANAAFHadetapatsnhivhlvpSPDQSDILTyhkadvpepSGPTMDLTTTN 164
Cdd:TIGR01350 81 QKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFL-----------------DPGTVSVTG---------ENGEETLEAKN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 165 IVIATGAKPRPLPG-NPFAGALI-DSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDRRAG 242
Cdd:TIGR01350 135 IIIATGSRPRSLPGpFDFDGKVViTSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 243 TTLTRELKRHGVNIITRASVTHVDTGanlGATVHYTREGQDGEqSVWGEIALVAIGRDPITDP----AWGVTIDDHGHVA 318
Cdd:TIGR01350 215 KVLQKALKKKGVKILTNTKVTAVEKN---DDQVTYENKGGETE-TLTGEKVLVAVGRKPNTEGlgleKLGVELDERGRIV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 319 TDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFPEAASVGLTveQAQAREDLIE 398
Cdd:TIGR01350 291 VDEYMRTNVPGIYAIGDVIGGPMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLT--EEQAKEAGYD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 399 IKETNYPMLANARML-MSGTAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLVHPHPTF 477
Cdd:TIGR01350 369 VKIGKFPFAANGKALaLGETDGFVKII-----ADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTL 443
|
490
....*....|....*..
gi 2796464736 478 SETLGEALLKADGRPLH 494
Cdd:TIGR01350 444 SEAIKEAALAALGKPIH 460
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
1-494 |
3.09e-120 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 360.78 E-value: 3.09e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 1 MSEQFDLVIIGAGPGGYSTALRAAELGMKVALIER------DATVGGTCLNRGCIPSKALITATHTIDTV-HRAAELGVN 73
Cdd:PRK06327 1 MSKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAwknpkgKPALGGTCLNVGCIPSKALLASSEEFENAgHHFADHGIH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 74 ASVNGIDFGTLRDYRLRVVKTMVGGLAGLLAHRGITVFRANAAFhadetapatsnhivhlVPSPDQSDILTYHKADvpep 153
Cdd:PRK06327 81 VDGVKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSF----------------VGKTDAGYEIKVTGED---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 154 sgpTMDLTTTNIVIATGAKPRPLPGNPFAGALI-DSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDR 232
Cdd:PRK06327 141 ---ETVITAKHVIIATGSEPRHLPGVPFDNKIIlDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 233 VLSAWDRRAGTTLTRELKRHGVNIITRASVTHVDTGANlGATVHYTrEGQDGEQSVWGEIALVAIGRDPITD----PAWG 308
Cdd:PRK06327 218 FLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGK-GVSVAYT-DADGEAQTLEVDKLIVSIGRVPNTDglglEAVG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 309 VTIDDHGHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKpVDEATVPQIVFSFPEAASVGLTVE 388
Cdd:PRK06327 296 LKLDERGFIPVDDHCRTNVPNVYAIGDVVRGPMLAHKAEEEGVAVAERIAGQKGH-IDYNTIPWVIYTSPEIAWVGKTEQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 389 QAQAREdlIEIKETNYPMLANARML-MSGTAGSLTIVSgcDAanpDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADA 467
Cdd:PRK06327 375 QLKAEG--VEYKAGKFPFMANGRALaMGEPDGFVKIIA--DA---KTDEILGVHVIGPNASELIAEAVVAMEFKASSEDI 447
|
490 500
....*....|....*....|....*..
gi 2796464736 468 ARLVHPHPTFSETLGEALLKADGRPLH 494
Cdd:PRK06327 448 ARICHAHPTLSEVWHEAALAVDKRPLH 474
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
3-494 |
4.06e-113 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 342.16 E-value: 4.06e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 3 EQFDLVIIGAGPGGYSTALRAAELGMKVALIERDaTVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVNGIDFG 82
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKG-PLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKIDFK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 83 TLRDYRLRVVKTMVGG-LAGLLAHRGITVFRANAAFhadetapaTSNHIVhlvpspdqsdiltyhKADVPEpsgptmdLT 161
Cdd:PRK06292 81 KVMARVRRERDRFVGGvVEGLEKKPKIDKIKGTARF--------VDPNTV---------------EVNGER-------IE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 162 TTNIVIATGAKPRPLPG--NPFAGALIDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDR 239
Cdd:PRK06292 131 AKNIVIATGSRVPPIPGvwLILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 240 RAGTTLTRELKRHgVNIITRASVTHVDTGANLGATVhytREGQDGEQSVWGEIALVAIGRDPITD----PAWGVTIDDHG 315
Cdd:PRK06292 211 EVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEE---LEKGGKTETIEADYVLVATGRRPNTDglglENTGIELDERG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 316 HVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFPEAASVGLTVEQAQAREd 395
Cdd:PRK06292 287 RPVVDEHTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAG- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 396 lIEIKETNYPMLANAR-MLMSGTAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLVHPH 474
Cdd:PRK06292 366 -IDYVVGEVPFEAQGRaRVMGKNDGFVKVY-----ADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYH 439
|
490 500
....*....|....*....|
gi 2796464736 475 PTFSETLGEALLKADGRPLH 494
Cdd:PRK06292 440 PTLSEGLRTALRDLFSKLIH 459
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
1-485 |
4.44e-82 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 262.06 E-value: 4.44e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 1 MSEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDAtVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVN-GI 79
Cdd:PRK06370 2 PAQRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGL-LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPvSV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 80 DFGTLRDYRLRVVKTMVGGLAGLLAH-RGITVFRANAAFhadetapaTSNHIVHLvpspdqsdiltyhkadvpepSGPTm 158
Cdd:PRK06370 81 DFKAVMARKRRIRARSRHGSEQWLRGlEGVDVFRGHARF--------ESPNTVRV--------------------GGET- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 159 dLTTTNIVIATGAKPR--PLPGNPFAGALIDSTqALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSA 236
Cdd:PRK06370 132 -LRAKRIFINTGARAAipPIPGLDEVGYLTNET-IFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 237 WDRRAGTTLTRELKRHGVNIITRASVTHVDTGANlGATVHYTREGqdGEQSVWGEIALVAIGRDPITDP----AWGVTID 312
Cdd:PRK06370 210 EDEDVAAAVREILEREGIDVRLNAECIRVERDGD-GIAVGLDCNG--GAPEITGSHILVAVGRVPNTDDlgleAAGVETD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 313 DHGHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFPEAASVGLTveQAQA 392
Cdd:PRK06370 287 ARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMT--EAEA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 393 REDLIEIKETNYPMLANARMLMSG-TAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLV 471
Cdd:PRK06370 365 RKSGRRVLVGTRPMTRVGRAVEKGeTQGFMKVV-----VDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAI 439
|
490
....*....|....*..
gi 2796464736 472 HPHPTFSE---TLGEAL 485
Cdd:PRK06370 440 HIHPTVSElipTLAQAL 456
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
5-481 |
1.66e-74 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 242.33 E-value: 1.66e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIERdATVGGTCLNRGCIPSKALITATHTIDTVhRAAELGVNASVNGIDFGTL 84
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVER-GPLGGTCVNVGCVPSKMLLRAAEVAHYA-RKPPFGGLAATVAVDFGEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 85 RDYRLRVVKTM-VGGLAGLLAHRGITVFRANAAFHADETAPAtsnhivhlvpspDQSDILTYHKAdvpepsgptmdlttt 163
Cdd:TIGR02053 79 LEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV------------DLGREVRGAKR--------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 164 nIVIATGAKPR--PLPGNPFAGALiDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDRRA 241
Cdd:TIGR02053 132 -FLIATGARPAipPIPGLKEAGYL-TSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 242 GTTLTRELKRHGVNIITRASVTHVDTGanlGATVHYTREGQDGEQSVWGEIALVAIGRDPITDP----AWGVTIDDHGHV 317
Cdd:TIGR02053 210 SAAVEEALAEEGIEVVTSAQVKAVSVR---GGGKIITVEKPGGQGEVEADELLVATGRRPNTDGlgleKAGVKLDERGGI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 318 ATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFPEAASVGLTVEQAQarEDLI 397
Cdd:TIGR02053 287 LVDETLRTSNPGIYAAGDVTGGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQ--KAGI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 398 EIKETNYPMLANARMLMSG-TAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLVHPHPT 476
Cdd:TIGR02053 365 ECDCRTLPLTNVPRARINRdTRGFIKLV-----AEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPT 439
|
....*
gi 2796464736 477 FSETL 481
Cdd:TIGR02053 440 MAEGL 444
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
1-479 |
2.51e-74 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 241.60 E-value: 2.51e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 1 MSEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDAtVGGTCLNRGCIPSKALITATHTIDTVHR-AAELGVNASVNGI 79
Cdd:PRK06116 1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKR-LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 80 DFGTLRDYRLRVVKTMVGGLAGLLAHRGITVFRANAAFHADETAPATSNHIvhlvpspdqsdiltyhkadvpepsgptmd 159
Cdd:PRK06116 80 DWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERY----------------------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 160 lTTTNIVIATGAKPRP--LPGNPFAgalIDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAW 237
Cdd:PRK06116 131 -TADHILIATGGRPSIpdIPGAEYG---ITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGF 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 238 DRRAGTTLTRELKRHGVNIITRASVTHVDTGANLGATVHYtregQDGEQSVWGEIaLVAIGRDPITD----PAWGVTIDD 313
Cdd:PRK06116 207 DPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTL----EDGETLTVDCL-IWAIGREPNTDglglENAGVKLNE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 314 HGHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPK-PVDEATVPQIVFSFPEAASVGLTVEQAQA 392
Cdd:PRK06116 282 KGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRRLSERLFNNKPDeKLDYSNIPTVVFSHPPIGTVGLTEEEARE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 393 R--EDLIEIKETNY-PM---LANAR--MLMSgtagslTIVSGcdaanpDTPRVLGVHMVSQMASDIIaeaeQLVGnhVPL 464
Cdd:PRK06116 362 QygEDNVKVYRSSFtPMytaLTGHRqpCLMK------LVVVG------KEEKVVGLHGIGFGADEMI----QGFA--VAI 423
|
490 500
....*....|....*....|.
gi 2796464736 465 ------ADAARLVHPHPTFSE 479
Cdd:PRK06116 424 kmgatkADFDNTVAIHPTAAE 444
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
4-451 |
6.34e-63 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 211.94 E-value: 6.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 4 QFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVNGIDFGT 83
Cdd:PRK05249 5 DYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHTGTIPSKALREAVLRLIGFNQNPLYSSYRVKLRITFAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 84 LRDYRLRVVKTMVGGLAGLLAHRGITVFRANAAFhADEtapatsnhivhlvpspdqsdiltyHKADVPEPSGPTMDLTTT 163
Cdd:PRK05249 85 LLARADHVINKQVEVRRGQYERNRVDLIQGRARF-VDP------------------------HTVEVECPDGEVETLTAD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 164 NIVIATGAKPRPLPGNPFAGALI-DSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDRRAG 242
Cdd:PRK05249 140 KIVIATGSRPYRPPDVDFDHPRIyDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEIS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 243 TTLTRELKRHGVNIITRASVTHVDTGANlGATVHYtregQDGEQsVWGEIALVAIGRDPITD----PAWGVTIDDHGHVA 318
Cdd:PRK05249 220 DALSYHLRDSGVTIRHNEEVEKVEGGDD-GVIVHL----KSGKK-IKADCLLYANGRTGNTDglnlENAGLEADSRGQLK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 319 TDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGL-NPKPVDEatVPQIVFSFPEAASVGLTVEQAQAREDLI 397
Cdd:PRK05249 294 VNENYQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQHAVGEaTAHLIED--IPTGIYTIPEISSVGKTEQELTAAKVPY 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 398 EI-----KETnypmlanARMLMSG-TAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDII 451
Cdd:PRK05249 372 EVgrarfKEL-------ARAQIAGdNVGMLKIL-----FHRETLEILGVHCFGERATEII 419
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
5-490 |
5.34e-62 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 209.04 E-value: 5.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELgmKVALIErDATVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVNGIDFGTL 84
Cdd:PRK07846 2 YDLIIIGTGSGNSILDERFADK--RIAIVE-KGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAELDGVRWPDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 85 RDyrlRVVKTMVGGLAGLLAHRG-----ITVFRANAAFHADETAPATSNHIVhlvpspdqsdiltyhkadvpepsgptmd 159
Cdd:PRK07846 79 VS---RVFGRIDPIAAGGEEYRGrdtpnIDVYRGHARFIGPKTLRTGDGEEI---------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 160 lTTTNIVIATGAKPRpLPGNPFAGALIDSTQA--LEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAW 237
Cdd:PRK07846 128 -TADQVVIAAGSRPV-IPPVIADSGVRYHTSDtiMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHL 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 238 DRRAGTTLTrELKRHGVNIITRASVTHVDTGANlGATVHYtregqDGEQSVWGEIALVAIGRDPITD----PAWGVTIDD 313
Cdd:PRK07846 206 DDDISERFT-ELASKRWDVRLGRNVVGVSQDGS-GVTLRL-----DDGSTVEADVLLVATGRVPNGDlldaAAAGVDVDE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 314 HGHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIA-GLNPKPVDEATVPQIVFSFPEAASVGLTVEQAQA 392
Cdd:PRK07846 279 DGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVVQHNLLhPDDLIASDHRFVPAAVFTHPQIASVGLTENEARA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 393 REDLIEIKETNYPMLANArMLMSGTAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLVH 472
Cdd:PRK07846 359 AGLDITVKVQNYGDVAYG-WAMEDTTGFVKLI-----ADRDTGRLLGAHIIGPQASTLIQPLIQAMSFGLDAREMARGQY 432
|
490
....*....|....*....
gi 2796464736 473 -PHPTFSETLGEALLKADG 490
Cdd:PRK07846 433 wIHPALPEVVENALLGLDL 451
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
5-350 |
2.40e-60 |
|
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: 200.24 E-value: 2.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIErdatVGGTCLNRGCIPSKALITATHTIDTVHRAAELgvnasvngidfgtl 84
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPYGGCVLSKALLGAAEAPEIASLWADL-------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 85 RDYRLRVVKTMVGGLAGLLAHRGITVFRANAAFHadetapatsnhivhlvpspdqsdiltyhkaDVPEPSGPTMDLTTTN 164
Cdd:pfam07992 63 YKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVV------------------------------LEELVDGDGETITYDR 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 165 IVIATGAKPRPLP------GNPFAGALIDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWD 238
Cdd:pfam07992 113 LVIATGARPRLPPipgvelNVGFLVRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFD 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 239 RRAGTTLTRELKRHGVNIITRASVTHVDtganlGATVHYTREGQDGeQSVWGEIALVAIGRDPITDPA--WGVTIDDHGH 316
Cdd:pfam07992 193 EEISAALEKALEKNGVEVRLGTSVKEII-----GDGDGVEVILKDG-TEIDADLVVVAIGRRPNTELLeaAGLELDERGG 266
|
330 340 350
....*....|....*....|....*....|....*
gi 2796464736 317 VATDAYGRTDKPGVWAVGDVTAGH-ALAHRAFEQG 350
Cdd:pfam07992 267 IVVDEYLRTSVPGIYAAGDCRVGGpELAQNAVAQG 301
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
5-481 |
5.14e-60 |
|
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]
Pssm-ID: 213618 [Multi-domain] Cd Length: 446 Bit Score: 203.89 E-value: 5.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIERDaTVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVNGIDFGTL 84
Cdd:TIGR01424 3 YDLFVIGAGSGGVRAARLAAALGAKVAIAEEF-RVGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVGKARFDWKKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 85 rdyrLRVVKTMVGGLAGLlaHRGitvFRANAAFHADET-APATSNHIVHLVPSPDqsdilTYhkadvpepsgptmdlTTT 163
Cdd:TIGR01424 82 ----LAAKDQEIARLSGL--YRK---GLANAGAELLDGrAELVGPNTVEVLASGK-----TY---------------TAE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 164 NIVIATGAKP-RP-LPGNPFAgalIDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDRRA 241
Cdd:TIGR01424 133 KILIAVGGRPpKPaLPGHELG---ITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 242 GTTLTRELKRHGVNIITRASVTHV---DTGANLGATVHytregqdgEQSVWGEIALVAIGRDPITD----PAWGVTIDDH 314
Cdd:TIGR01424 210 RRGLAAALEERGIRILPEDSITSIskdDDGRLKATLSK--------HEEIVADVVLFATGRSPNTNglglEAAGVRLNDL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 315 GHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFPEAASVGLTVEQAQARE 394
Cdd:TIGR01424 282 GAIAVDEYSRTSTPSIYAVGDVTDRINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 395 DLIEIKETNY-PMLANARMLMSGTAGSLTIvsgcdaaNPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLVHP 473
Cdd:TIGR01424 362 GDIEVYRAEFrPMKATFSGRQEKTLMKLVV-------DAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAV 434
|
....*...
gi 2796464736 474 HPTFSETL 481
Cdd:TIGR01424 435 HPTSAEEL 442
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
5-451 |
2.10e-53 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 187.33 E-value: 2.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIE---------RDATVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNas 75
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpisseSIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWE-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 76 VNG-IDFG--TLRDYRLRVVKTMVGGLAGLLAHRGITVFRANAAfhadetapatsnhivhlvpspdqsdILTYHKADVPE 152
Cdd:PLN02507 104 INEkVDFNwkKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGK-------------------------IVGPNEVEVTQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 153 PSGPTMDLTTTNIVIATGAKPRPL--PGNPFAgalIDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRK 230
Cdd:PLN02507 159 LDGTKLRYTAKHILIATGSRAQRPniPGKELA---ITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 231 DRVLSAWDRRAGTTLTRELKRHGVNIITRASVTHVDTGANlGATVhYTREGQDgeqsVWGEIALVAIGRDPITD----PA 306
Cdd:PLN02507 236 ELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEG-GIKV-ITDHGEE----FVADVVLFATGRAPNTKrlnlEA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 307 WGVTIDDHGHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFPEAASVGLT 386
Cdd:PLN02507 310 VGVELDKAGAVKVDEYSRTNIPSIWAIGDVTNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLS 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796464736 387 VEQA--QAREDLIEIKETNYPMLANARMLMSGTAGSLTIVSGCDaanpdtpRVLGVHMVSQMASDII 451
Cdd:PLN02507 390 EEEAveQAKGDILVFTSSFNPMKNTISGRQEKTVMKLIVDAETD-------KVLGASMCGPDAPEIM 449
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
2-481 |
1.25e-51 |
|
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: 182.48 E-value: 1.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 2 SEQFDLVIIGAGPGGYSTALRAAEL-GMKVALIERD--------ATVGGTCLNRGCIPSKALITATHTIDTVHRAAELG- 71
Cdd:TIGR01423 1 SKAFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQthhgppfyAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 72 -VNASVNGIDFGTLRDYRLRVVKTMVGGLAGLLAH-RGITVFRANAAFHadetapatSNHIVHLVPSPDQsdiltyhKAD 149
Cdd:TIGR01423 81 eFDRSSVKANWKALIAAKNKAVLDINKSYEGMFADtEGLTFFLGWGALE--------DKNVVLVRESADP-------KSA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 150 VPEpsgptmDLTTTNIVIATGAKPRpLPGNPFAGALIDSTQALEVNEFPSSAVIIGAGAIALEFASMWNA---AGSKVTL 226
Cdd:TIGR01423 146 VKE------RLQAEHILLATGSWPQ-MLGIPGIEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 227 LIRKDRVLSAWDRRAGTTLTRELKRHGVNIITRASVTHVDTGANlgATVHYTRE-GQDGEQSVwgeiALVAIGRDPITD- 304
Cdd:TIGR01423 219 CYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNAD--GSKHVTFEsGKTLDVDV----VMMAIGRVPRTQt 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 305 ---PAWGVTIDDHGHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFPEAA 381
Cdd:TIGR01423 293 lqlDKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 382 SVGLTVEQAQAREDLIEIKETNY-PMLANarmlMSGTAGSLTIVSgcDAANPDTPRVLGVHMVSQMASDIIAEAEQLVGN 460
Cdd:TIGR01423 373 TCGLVEEDAAKKFEKVAVYESSFtPLMHN----ISGSKYKKFVAK--IVTNHADGTVLGVHLLGDSSPEIIQAVGICLKL 446
|
490 500
....*....|....*....|.
gi 2796464736 461 HVPLADAARLVHPHPTFSETL 481
Cdd:TIGR01423 447 NAKISDFYNTIGVHPTSAEEL 467
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
7-496 |
2.76e-51 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 180.83 E-value: 2.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 7 LVIIGAGPGGYSTALRAAELGMKVALIERDAtVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVNG---IDFGT 83
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDG-LGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGearVDLPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 84 LRDYRLRVVKTMVGGLAGLLAHRGITVFRANAAFHADETAPatsnhivhlvpspdqsdiltyHKADVPEPSGPTMDLTTT 163
Cdd:PRK07845 83 VNARVKALAAAQSADIRARLEREGVRVIAGRGRLIDPGLGP---------------------HRVKVTTADGGEETLDAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 164 NIVIATGAKPRPLPGNPFAGALI-DSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDRRAG 242
Cdd:PRK07845 142 VVLIATGASPRILPTAEPDGERIlTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 243 TTLTRELKRHGVNIITRA---SVTHVDTganlGATVHYTregqDGeQSVWGEIALVAIGRDPITD----PAWGVTIDDHG 315
Cdd:PRK07845 222 EVLEEVFARRGMTVLKRSraeSVERTGD----GVVVTLT----DG-RTVEGSHALMAVGSVPNTAglglEEAGVELTPSG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 316 HVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFPEAASVGLTveQAQARED 395
Cdd:PRK07845 293 HITVDRVSRTSVPGIYAAGDCTGVLPLASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVS--QAAIDSG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 396 LIEIKETNYPMLANARMLMSGTA-GSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLVHPH 474
Cdd:PRK07845 371 EVPARTVMLPLATNPRAKMSGLRdGFVKLF-----CRPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVY 445
|
490 500
....*....|....*....|..
gi 2796464736 475 PTFSETLGEAllkadGRPLHTR 496
Cdd:PRK07845 446 PSLSGSITEA-----ARRLMAH 462
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
3-486 |
1.59e-50 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 178.80 E-value: 1.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 3 EQFDLVIIGAGPGgySTALRAAELGMKVALIERdATVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVNGIDFg 82
Cdd:TIGR03452 1 RHYDLIIIGTGSG--NSIPDPRFADKRIAIVEK-GTFGGTCLNVGCIPTKMFVYAAEVAQSIGESARLGIDAEIDSVRW- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 83 tlRDYRLRVVKTMVGGLA--GLLAHRG-----ITVFRANAAFHADETapatsnhivhlvpspdqsdiltyhkadVPEPSG 155
Cdd:TIGR03452 77 --PDIVSRVFGDRIDPIAagGEDYRRGdetpnIDVYDGHARFVGPRT---------------------------LRTGDG 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 156 PTmdLTTTNIVIATGAKPRPLPgnpfagALIDSTQALEVN-------EFPSSAVIIGAGAIALEFASMWNAAGSKVTLLI 228
Cdd:TIGR03452 128 EE--ITGDQIVIAAGSRPYIPP------AIADSGVRYHTNedimrlpELPESLVIVGGGYIAAEFAHVFSALGTRVTIVN 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 229 RKDRVLSAWDRRAGTTLTrELKRHGVNIITRASVTHVDTGANlGATVhytrEGQDGEqSVWGEIALVAIGRDPITD---- 304
Cdd:TIGR03452 200 RSTKLLRHLDEDISDRFT-EIAKKKWDIRLGRNVTAVEQDGD-GVTL----TLDDGS-TVTADVLLVATGRVPNGDllda 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 305 PAWGVTIDDHGHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIagLNP---KPVDEATVPQIVFSFPEAA 381
Cdd:TIGR03452 273 EAAGVEVDEDGRIKVDEYGRTSARGVWALGDVSSPYQLKHVANAEARVVKHNL--LHPndlRKMPHDFVPSAVFTHPQIA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 382 SVGLTVEQAQAREDLIEIKETNYPMLANArMLMSGTAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNH 461
Cdd:TIGR03452 351 TVGLTEQEAREAGHDITVKIQNYGDVAYG-WAMEDTTGFCKLI-----ADRDTGKLLGAHIIGPQASSLIQPLITAMAFG 424
|
490 500
....*....|....*....|....*.
gi 2796464736 462 VPLADAARLVH-PHPTFSETLGEALL 486
Cdd:TIGR03452 425 LDAREMARKQYwIHPALPEVVENALL 450
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
3-494 |
3.48e-49 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 178.95 E-value: 3.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 3 EQFDLVIIGAGPGGYSTALRAAELGMKVALIERDA-TVGGTCLNRGCIPSKALITATHTIDTVHRAAEL---GV--NASV 76
Cdd:PTZ00153 115 EEYDVGIIGCGVGGHAAAINAMERGLKVIIFTGDDdSIGGTCVNVGCIPSKALLYATGKYRELKNLAKLytyGIytNAFK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 77 NG----------------IDFGTLRDYRLRVVKTMVGGLAGLLAHRGITVFRAnaafhadetapatsnhivHLVPSPDQS 140
Cdd:PTZ00153 195 NGkndpvernqlvadtvqIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSE------------------HVQVIYERG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 141 DILTYHKADVPEpSGPTmdLTTTNIVIATGAKPRpLPGNPFAG--ALIDSTQALEVNEFPSSAVIIGAGAIALEFASMWN 218
Cdd:PTZ00153 257 HIVDKNTIKSEK-SGKE--FKVKNIIIATGSTPN-IPDNIEVDqkSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYT 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 219 AAGSKVTLLIRKDRVLSAWDRRAGTTLTRE-LKRHGVNIITRASVTHVDTGANLGATVHYTREGQDGEQSVWGEIA---- 293
Cdd:PTZ00153 333 ALGSEVVSFEYSPQLLPLLDADVAKYFERVfLKSKPVRVHLNTLIEYVRAGKGNQPVIIGHSERQTGESDGPKKNMndik 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 294 -------LVAIGRDPITDpawGVTIDD------HGHVATDAYGRTDKP------GVWAVGDVTAGHALAHRAFEQGIVIA 354
Cdd:PTZ00153 413 etyvdscLVATGRKPNTN---NLGLDKlkiqmkRGFVSVDEHLRVLREdqevydNIFCIGDANGKQMLAHTASHQALKVV 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 355 ETIAG------------LNPKPVDEATVPQIVFSFPEAASVGLTVEQAQAREDLIEI-KETNYpMLANARMLMSGTAgSL 421
Cdd:PTZ00153 490 DWIEGkgkenvninvenWASKPIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVgVEISF-YKANSKVLCENNI-SF 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 422 TIVSGCDAANP-------------------DTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLVHPHPTFSETLG 482
Cdd:PTZ00153 568 PNNSKNNSYNKgkyntvdntegmvkivylkDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLD 647
|
570
....*....|..
gi 2796464736 483 EALLKADGRPLH 494
Cdd:PTZ00153 648 AAFKAIAGVRTH 659
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
3-481 |
1.53e-47 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 170.32 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 3 EQFDLVIIGAGPGGYSTALRAAELGMKVALIER-DATVGGTCLNRGCIPSKALITAthtidtvhraAElgvnasvNGIDF 81
Cdd:PRK07251 2 LTYDLIVIGFGKAGKTLAAKLASAGKKVALVEEsKAMYGGTCINIGCIPTKTLLVA----------AE-------KNLSF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 82 GTLRDYRLRVVKTMVGGLAGLLAHRGITVFRANAAFhadetapaTSNHIVHLVPSPDQsdiltyhkadvpepsgptMDLT 161
Cdd:PRK07251 65 EQVMATKNTVTSRLRGKNYAMLAGSGVDLYDAEAHF--------VSNKVIEVQAGDEK------------------IELT 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 162 TTNIVIATGAKPR--PLPGNPFAGALIDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDR 239
Cdd:PRK07251 119 AETIVINTGAVSNvlPIPGLADSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEP 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 240 RAGTTLTRELKRHGVNIITRASVTHVdtgANLGATVHYTREGQDGEqsvwGEIALVAIGRDPITDPAW----GVTIDDHG 315
Cdd:PRK07251 199 SVAALAKQYMEEDGITFLLNAHTTEV---KNDGDQVLVVTEDETYR----FDALLYATGRKPNTEPLGlentDIELTERG 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 316 HVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAG---LNPKpvDEATVPQIVFSFPEAASVGLTVEQAqa 392
Cdd:PRK07251 272 AIKVDDYCQTSVPGVFAVGDVNGGPQFTYISLDDFRIVFGYLTGdgsYTLE--DRGNVPTTMFITPPLSQVGLTEKEA-- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 393 redlieiKETNYPMLANaRMLMSGTA---------GSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVP 463
Cdd:PRK07251 348 -------KEAGLPYAVK-ELLVAAMPrahvnndlrGAFKVV-----VNTETKEILGATLFGEGSQEIINLITMAMDNKIP 414
|
490
....*....|....*...
gi 2796464736 464 LADAARLVHPHPTFSETL 481
Cdd:PRK07251 415 YTYFKKQIFTHPTMAENL 432
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
5-479 |
2.45e-43 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 161.20 E-value: 2.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIE-------RDAT--VGGTCLNRGCIPSKALITATHTIDTVHRAAELG-VNA 74
Cdd:PLN02546 80 FDLFTIGAGSGGVRASRFASNFGASAAVCElpfatisSDTLggVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGwKYE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 75 SVNGIDFGTLRDYRLRVVKTMVGGLAGLLAHRGITVFRAnaafhadetapatsnhivhlvpspdQSDILTYHKADVpepS 154
Cdd:PLN02546 160 TEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEG-------------------------RGKIVDPHTVDV---D 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 155 GPTMdlTTTNIVIATGAKP-RP-LPGNPFAgalIDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDR 232
Cdd:PLN02546 212 GKLY--TARNILIAVGGRPfIPdIPGIEHA---IDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 233 VLSAWDRRAGTTLTRELKRHGVNIITRASVTHVDTGANLGATVHYTREGQDGEQSVwgeiaLVAIGRDPITD----PAWG 308
Cdd:PLN02546 287 VLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKGTVEGFSHV-----MFATGRKPNTKnlglEEVG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 309 VTIDDHGHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFPEAASVGLTVE 388
Cdd:PLN02546 362 VKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 389 QAQAREDLIEIKETNY-PMLANARMLMSGTAGSLtIVSGcdaanpDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADA 467
Cdd:PLN02546 442 QAIEEYGDVDVFTANFrPLKATLSGLPDRVFMKL-IVCA------KTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADF 514
|
490
....*....|..
gi 2796464736 468 ARLVHPHPTFSE 479
Cdd:PLN02546 515 DATVGIHPTAAE 526
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
4-483 |
2.14e-41 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 153.63 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 4 QFDLVIIGAGPGGYSTALRAAELGMKVALIERDATV-GGTCLNRGCIPSKALitathtidtVHRAAELGvnasvngiDFG 82
Cdd:PRK08010 3 KYQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNAMyGGTCINIGCIPTKTL---------VHDAQQHT--------DFV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 83 TLRDYRLRVVKtmvgglagllahrgitvFRANAAFH--ADetapatsnhivhlVPSPD----QSDILTYHKADVPEPSGp 156
Cdd:PRK08010 66 RAIQRKNEVVN-----------------FLRNKNFHnlAD-------------MPNIDvidgQAEFINNHSLRVHRPEG- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 157 TMDLTTTNIVIATGAKP--RPLPGNPFAGALIDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVL 234
Cdd:PRK08010 115 NLEIHGEKIFINTGAQTvvPPIPGITTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 235 SAWDRRAGTTLTRELKRHGVNIITRASVTHVDTGANlGATVHyTREGQDGEQSVwgeiaLVAIGRDPITDPAW----GVT 310
Cdd:PRK08010 195 PREDRDIADNIATILRDQGVDIILNAHVERISHHEN-QVQVH-SEHAQLAVDAL-----LIASGRQPATASLHpenaGIA 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 311 IDDHGHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPV-DEATVPQIVFSFPEAASVGLTVEQ 389
Cdd:PRK08010 268 VNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGKRSTdDRKNVPYSVFMTPPLSRVGMTEEQ 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 390 AQAREDLIEIKETNYPMLANARmLMSGTAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAAR 469
Cdd:PRK08010 348 ARESGADIQVVTLPVAAIPRAR-VMNDTRGVLKAI-----VDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRD 421
|
490
....*....|....
gi 2796464736 470 LVHPHPTFSETLGE 483
Cdd:PRK08010 422 QIFTHPSMSESLND 435
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
2-481 |
2.87e-40 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 152.61 E-value: 2.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 2 SEQFDLVIIGAGPGGYSTALRAAELGMKVALIERdATVGGTCLNRGCIPSKALITATHtIDTVHRAA--ELGVNASVNGI 79
Cdd:PRK13748 96 ERPLHVAVIGSGGAAMAAALKAVEQGARVTLIER-GTIGGTCVNVGCVPSKIMIRAAH-IAHLRRESpfDGGIAATVPTI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 80 DFGTL------RDYRLRVVKTMvGGLAGLLAhrgITVFRANAAFHADETapatsnhivhlvpspdqsdiLTYHKADvpep 153
Cdd:PRK13748 174 DRSRLlaqqqaRVDELRHAKYE-GILDGNPA---ITVLHGEARFKDDQT--------------------LIVRLND---- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 154 sGPTMDLTTTNIVIATGAKPR--PLPG---NPFAgaliDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLI 228
Cdd:PRK13748 226 -GGERVVAFDRCLIATGASPAvpPIPGlkeTPYW----TSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 229 RkDRVLSAWDRRAGTTLTRELKRHGVNII--TRAS-VTHVDtganlGATVHYTREGQdgeqsVWGEIALVAIGRDPITDP 305
Cdd:PRK13748 301 R-STLFFREDPAIGEAVTAAFRAEGIEVLehTQASqVAHVD-----GEFVLTTGHGE-----LRADKLLVATGRAPNTRS 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 306 ----AWGVTIDDHGHVATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKpVDEATVPQIVFSFPEAA 381
Cdd:PRK13748 370 laldAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGDAA-LDLTAMPAVVFTDPQVA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 382 SVGLTveQAQAREDLIEIKETNYPMLANARMLMS-GTAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGN 460
Cdd:PRK13748 449 TVGYS--EAEAHHDGIETDSRTLTLDNVPRALANfDTRGFIKLV-----IEEGSGRLIGVQAVAPEAGELIQTAALAIRN 521
|
490 500
....*....|....*....|.
gi 2796464736 461 HVPLADAARLVHPHPTFSETL 481
Cdd:PRK13748 522 RMTVQELADQLFPYLTMVEGL 542
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
4-483 |
7.38e-40 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 149.54 E-value: 7.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 4 QFDLVIIGAGPGGYSTALRAAELGMKVALIERDATV-GGTCLNRGCIPSKALItatHTIDTvHRAAELGVNASVNGIDFG 82
Cdd:NF040477 3 HYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQSAQMyGGTCINIGCIPTKTLV---HDAEQ-HQDFSTAMQRKSSVVGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 83 TLRDYRLrvvktmvggLAGLlahRGITVFRANAAFhadetapatsnhivhlvpspdqsdiLTYHKADVPEPSGpTMDLTT 162
Cdd:NF040477 79 RDKNYHN---------LADL---DNVDVINGRAEF-------------------------IDNHTLRVFQADG-EQELRG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 163 TNIVIATGAKPR--PLPGNPFAGALIDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDRR 240
Cdd:NF040477 121 EKIFINTGAQSVlpPIPGLTTTPGVYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAELFLPREDRD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 241 AGTTLTRELKRHGVNIITRASVTHVDTGANlgaTVHYtrEGQDGEQSVwgEIALVAIGRDPITD----PAWGVTIDDHGH 316
Cdd:NF040477 201 IAQAIATILQDQGVELILNAQVQRVSSHEG---EVQL--ETAEGVLTV--DALLVASGRKPATAglqlQNAGVAVNERGA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 317 VATDAYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETIAGLNPKPV-DEATVPQIVFSFPEAASVGLTVEQAQARED 395
Cdd:NF040477 274 IVVDKYLRTTADNIWAMGDVTGGLQFTYISLDDFRIVRDSLLGEGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARASGA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 396 LIEIKETNYPMLANARmLMSGTAGSLTIVsgcdaANPDTPRVLGVHMVSQMASDIIAEAEQLVGNHVPLADAARLVHPHP 475
Cdd:NF040477 354 DIQVVTLPVAAIPRAR-VMNDTRGVLKAV-----VDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHP 427
|
....*...
gi 2796464736 476 TFSETLGE 483
Cdd:NF040477 428 TMSESLND 435
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
5-479 |
1.20e-37 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 145.14 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIERDaTVGGTCLNRGCIPSKALITATHTIDTVHRAAELGVNASVNgIDFGTL 84
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKD-YLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFS-FNLPLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 85 RDYRLRVVKTMVGGLAGLLAHRGITVFRANAAFHADETAPATSNHIVHLVPSPDQSDILTYHKADVPEPSGPTMdLTTTN 164
Cdd:PTZ00058 127 VERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKVSQVDGEADESDDDEVTIVSAGVSQLDDGQV-IEGKN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 165 IVIATGAKPR--PLPGNPFAgalIDSTQALEVNEfPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDRRAG 242
Cdd:PTZ00058 206 ILIAVGNKPIfpDVKGKEFT---ISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETII 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 243 TTLTRELKRHGVNIITRASVTHVDTGANLGATVHYTregqDGEQSVWGEIALVAIGRDPITDPAWGVTIDD---HGHVAT 319
Cdd:PTZ00058 282 NELENDMKKNNINIITHANVEEIEKVKEKNLTIYLS----DGRKYEHFDYVIYCVGRSPNTEDLNLKALNIktpKGYIKV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 320 DAYGRTDKPGVWAVGDV-----------------------------TAGHA-----LAHRAFEQGIVIAETIAGLNPKPV 365
Cdd:PTZ00058 358 DDNQRTSVKHIYAVGDCcmvkknqeiedlnllklyneepylkkkenTSGESyynvqLTPVAINAGRLLADRLFGPFSRTT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 366 DEATVPQIVFSFPEAASVGLTVEQAQAR--EDLIEIKETNYPMLANARMLMSGTAGSLTIVSGCDAANPDtpRVLGVHMV 443
Cdd:PTZ00058 438 NYKLIPSVIFSHPPIGTIGLSEQEAIDIygKENVKIYESRFTNLFFSVYDMDPAQKEKTYLKLVCVGKEE--LIKGLHIV 515
|
490 500 510
....*....|....*....|....*....|....*.
gi 2796464736 444 SQMASDIIAEAEQLVGNHVPLADAARLVHPHPTFSE 479
Cdd:PTZ00058 516 GLNADEILQGFAVALKMNATKADFDETIPIHPTAAE 551
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
5-399 |
1.67e-33 |
|
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: 132.28 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIerDAT----------VGGTCLNRGCIPSKALitathtidtvHRAAELGV-- 72
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLL--DFVtptplgtrwgIGGTCVNVGCIPKKLM----------HQAALLGQal 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 73 ----NASVNGIDfgTLRDYRLRVVKTMVGGLAGL-------LAHRGITVFRANAAFHADETAPATSNhivhlvpspdqsd 141
Cdd:TIGR01438 71 kdsrNYGWKVEE--TVKHDWKRLVEAVQNHIGSLnwgyrvaLREKKVKYENAYAEFVDKHRIKATNK------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 142 iltyhkadvpepSGPTMDLTTTNIVIATGAKPRpLPGNPFAGAL-IDSTQALEVNEFPSSAVIIGAGAIALEFASMWNAA 220
Cdd:TIGR01438 136 ------------KGKEKIYSAERFLIATGERPR-YPGIPGAKELcITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGI 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 221 GSKVTLLIRKdRVLSAWDRRAGTTLTRELKRHGVNIITRASVTHVDT-GANLGATVHYTREGQDGEQsvwgEIALVAIGR 299
Cdd:TIGR01438 203 GLDVTVMVRS-ILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQiEAKVLVEFTDSTNGIEEEY----DTVLLAIGR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 300 DPITD----PAWGVTIDDH-GHVATDAYGRTDKPGVWAVGDVTAGHA-LAHRAFEQGIVIAETIAGLNPKPVDEATVPQI 373
Cdd:TIGR01438 278 DACTRklnlENVGVKINKKtGKIPADEEEQTNVPYIYAVGDILEDKPeLTPVAIQAGRLLAQRLFKGSTVICDYENVPTT 357
|
410 420
....*....|....*....|....*...
gi 2796464736 374 VFSFPEAASVGLTVEQAQAR--EDLIEI 399
Cdd:TIGR01438 358 VFTPLEYGACGLSEEKAVEKfgEENVEV 385
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
166-384 |
2.63e-30 |
|
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: 120.30 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 166 VIATGAKPR--PLPGNPFAGAL----IDSTQAL--EVNEF-PSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSA 236
Cdd:COG0446 83 VLATGARPRppPIPGLDLPGVFtlrtLDDADALreALKEFkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 237 WDRRAGTTLTRELKRHGVNIITRASVTHVDTGANLGATVhytregQDGEqSVWGEIALVAIGRDPITDPAW--GVTIDDH 314
Cdd:COG0446 163 LDPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTL------TDGE-EIPADLVVVAPGVRPNTELAKdaGLALGER 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 315 GHVATDAYGRTDKPGVWAVGDV----------TAGHALAHRAFEQGIVIAETIAGLNPKPVDEATVPQIVFSFpEAASVG 384
Cdd:COG0446 236 GWIKVDETLQTSDPDVYAAGDCaevphpvtgkTVYIPLASAANKQGRVAAENILGGPAPFPGLGTFISKVFDL-CIASTG 314
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
5-340 |
2.93e-27 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 111.37 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIERDAtVGGTClnrgcipskaliTATHTIDTVhraaeLGVNASVNGIDFGT- 83
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQL------------ATTKEIENY-----PGFPEGISGPELAEr 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 84 ----LRDYRLRVVKTMVgglagllahrgITVFRANAAFHadetapatsnhiVHLvpspdqSDILTYHkADVpepsgptmd 159
Cdd:COG0492 63 lreqAERFGAEILLEEV-----------TSVDKDDGPFR------------VTT------DDGTEYE-AKA--------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 160 ltttnIVIATGAKPRPL--PG-NPFAGALIDSTQALEVNEFPSSAV-IIGAGAIALEFASMWNAAGSKVTLLIRKDrvls 235
Cdd:COG0492 104 -----VIIATGAGPRKLglPGeEEFEGRGVSYCATCDGFFFRGKDVvVVGGGDSALEEALYLTKFASKVTLIHRRD---- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 236 awDRRAGTTLTRELKRH-GVNIITRASVTHVDTGANL-GATVhytREGQDGEQSvwgEIA----LVAIGRDPITDPA--W 307
Cdd:COG0492 175 --ELRASKILVERLRANpKIEVLWNTEVTEIEGDGRVeGVTL---KNVKTGEEK---ELEvdgvFVAIGLKPNTELLkgL 246
|
330 340 350
....*....|....*....|....*....|...
gi 2796464736 308 GVTIDDHGHVATDAYGRTDKPGVWAVGDVTAGH 340
Cdd:COG0492 247 GLELDEDGYIVVDEDMETSVPGVFAAGDVRDYK 279
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
5-482 |
2.37e-23 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 102.98 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIE--RDAT------VGGTCLNRGCIPSKALITAT--------------HTID 62
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvKPSTqgtkwgLGGTCVNVGCVPKKLMHYAAnigsifhhdsqmygWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 63 TVHRAAEL--GVNASVNGIDFGTLRDYRLRVVKTMvGGLAGLlahrgitvfranaafhADEtapatsnhivHLVPSPDQS 140
Cdd:PTZ00052 86 SSFNWGKLvtTVQNHIRSLNFSYRTGLRSSKVEYI-NGLAKL----------------KDE----------HTVSYGDNS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 141 DILTYhkadvpepsgptmdlTTTNIVIATGAKPRPLPGNPFAGAL-IDSTQALEVNEFPSSAVIIGAGAIALEFASMWNA 219
Cdd:PTZ00052 139 QEETI---------------TAKYILIATGGRPSIPEDVPGAKEYsITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 220 AGSKVTLLIRKdRVLSAWDRRAGTTLTRELKRHGV---NIITRASVTHVDTGANLGATVHYTREgqdgeqsvwGEIALVA 296
Cdd:PTZ00052 204 LGFDVTVAVRS-IPLRGFDRQCSEKVVEYMKEQGTlflEGVVPINIEKMDDKIKVLFSDGTTEL---------FDTVLYA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 297 IGRDPITD----PAWGVTIDDHGH-VATDAYgrTDKPGVWAVGDVTAGHA-LAHRAFEQGIVIAETIAGLNPKPVDEATV 370
Cdd:PTZ00052 274 TGRKPDIKglnlNAIGVHVNKSNKiIAPNDC--TNIPNIFAVGDVVEGRPeLTPVAIKAGILLARRLFKQSNEFIDYTFI 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 371 PQIVFSFPEAASVGLTVEQAQAR--EDLIE--IKETNYPMLA--------NARMLMSGTAGSLTIVSGCDAANPDTPRVL 438
Cdd:PTZ00052 352 PTTIFTPIEYGACGYSSEAAIAKygEDDIEeyLQEFNTLEIAavhrekheRARKDEYDFDVSSNCLAKLVCVKSEDNKVV 431
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2796464736 439 GVHMVSQMASDIIAEAEQLVGNHVPLADAARLVHPHPTFSETLG 482
Cdd:PTZ00052 432 GFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVFM 475
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
166-359 |
5.04e-23 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 100.99 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 166 VIATGAKPR--PLPGNPFAGAL----IDSTQAL-EVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAW- 237
Cdd:COG1251 103 VLATGSRPRvpPIPGADLPGVFtlrtLDDADALrAALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQl 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 238 DRRAGTTLTRELKRHGVNIITRASVTHVdTGANLGATVHYTregqDGEQsVWGEIALVAIGRDPITDPAWGVTID-DHGh 316
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVRLGTGVTEI-EGDDRVTGVRLA----DGEE-LPADLVVVAIGVRPNTELARAAGLAvDRG- 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2796464736 317 VATDAYGRTDKPGVWAVGDVTA-------GHALAHR--AFEQGIVIAETIAG 359
Cdd:COG1251 256 IVVDDYLRTSDPDIYAAGDCAEhpgpvygRRVLELVapAYEQARVAAANLAG 307
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
370-484 |
4.03e-22 |
|
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: 91.08 E-value: 4.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 370 VPQIVFSFPEAASVGLTveQAQAREDLIEIKETNYPMLANARMLMSG-TAGSLTIVsgcdaANPDTPRVLGVHMVSQMAS 448
Cdd:pfam02852 1 IPSVVFTDPEIASVGLT--EEEAKEKGGEVKVGKFPFAANGRALAYGdTDGFVKLV-----ADRETGKILGAHIVGPNAG 73
|
90 100 110
....*....|....*....|....*....|....*.
gi 2796464736 449 DIIAEAEQLVGNHVPLADAARLVHPHPTFSETLGEA 484
Cdd:pfam02852 74 ELIQEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
200-280 |
2.14e-17 |
|
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: 76.86 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 200 SAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDRRAGTTLTRELKRHGVNIITRASVTHVDTGANlGATVHYTR 279
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGD-GVVVVLTD 79
|
.
gi 2796464736 280 E 280
Cdd:pfam00070 80 G 80
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
165-404 |
2.11e-15 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 78.16 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 165 IVIATGAKP--RPLPGNPFAG--ALIDSTQALEVNEF-----PSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLS 235
Cdd:PRK09564 107 LMIATGARPiiPPIKNINLENvyTLKSMEDGLALKELlkdeeIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 236 -AWDRRAGTTLTRELKRHGVNIITRASVTHVDTGANLGATVhyTREGQdgeqsVWGEIALVAIGRDPITDPAWGVTID-- 312
Cdd:PRK09564 187 dSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVV--TDKGE-----YEADVVIVATGVKPNTEFLEDTGLKtl 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 313 DHGHVATDAYGRTDKPGVWAVGDVTAGH----------ALAHRAFEQGIVIAETIAGLNPKPVDEATVPQI-VFSFpEAA 381
Cdd:PRK09564 260 KNGAIIVDEYGETSIENIYAAGDCATIYnivsnknvyvPLATTANKLGRMVGENLAGRHVSFKGTLGSACIkVLDL-EAA 338
|
250 260
....*....|....*....|....*....
gi 2796464736 382 SVGLTVEQAQARE---DLIEIKE---TNY 404
Cdd:PRK09564 339 RTGLTEEEAKKLGidyKTVFIKDknhTNY 367
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
6-337 |
2.30e-11 |
|
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: 64.57 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 6 DLVIIGAGPGGYSTALRAAELGMKVALIERdATVGGTclnrgcipskalITATHTID------TVHRAAELGVNASVNGI 79
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEG-MEPGGQ------------LTTTTEVEnypgfpEGISGPELMEKMKEQAV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 80 DFGTlrDYRLRVVktmvgglagllahrgITVFRANAAFhadetapatsnhIVHLvpspdqSDILTYhkadvpepsgptmd 159
Cdd:TIGR01292 68 KFGA--EIIYEEV---------------IKVDKSDRPF------------KVYT------GDGKEY-------------- 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 160 lTTTNIVIATGAKPRPL--PG-NPFAGALIDSTQALEVNEFPSSAVI-IGAGAIALEFASMWNAAGSKVTLLIRKDRVls 235
Cdd:TIGR01292 99 -TAKAVIIATGASARKLgiPGeDEFWGRGVSYCATCDGPFFKNKEVAvVGGGDSAIEEALYLTRIAKKVTLVHRRDKF-- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 236 awdRRAGTTLTRELKRHGVNIITRASVTHV--DTGANlGATVHYTREGQDGEQSVWGeiALVAIGRDPITDPAWG-VTID 312
Cdd:TIGR01292 176 ---RAEKILLDRLKKNPKIEFLWNSTVEEIvgDNKVE-GVKIKNTVTGEEEELEVDG--VFIAIGHEPNTELLKGlLELD 249
|
330 340
....*....|....*....|....*
gi 2796464736 313 DHGHVATDAYGRTDKPGVWAVGDVT 337
Cdd:TIGR01292 250 ENGYIVTDEGMRTSVPGVFAAGDVR 274
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
9-357 |
3.12e-10 |
|
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: 62.07 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 9 IIGAGPGGYSTALRAAELGMKVALIERDATVGGtcLNRGCIPskalitathtidtvhraaelgvnasvngidfgtlrDYR 88
Cdd:COG0493 126 VVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG--LLRYGIP-----------------------------------EFR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 89 L--RVVKTMVGGLAGLlahrGITvFRANAAFHADETApatsnhivhlvpspdqSDILTYHKAdvpepsgptmdltttnIV 166
Cdd:COG0493 169 LpkDVLDREIELIEAL----GVE-FRTNVEVGKDITL----------------DELLEEFDA----------------VF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 167 IATGA-KPRPLP-----------GNPFagaLIDSTQALEVNEFPS---SAVIIGAGAIALefasmwNAAGS-------KV 224
Cdd:COG0493 212 LATGAgKPRDLGipgedlkgvhsAMDF---LTAVNLGEAPDTILAvgkRVVVIGGGNTAM------DCARTalrlgaeSV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 225 TLLIRKDRV-LSAWDRRagttlTRELKRHGVNIITRASVTHVDTGAN---LGATVHYTREGQDGE------QSVWGE--- 291
Cdd:COG0493 283 TIVYRRTREeMPASKEE-----VEEALEEGVEFLFLVAPVEIIGDENgrvTGLECVRMELGEPDEsgrrrpVPIEGSeft 357
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2796464736 292 ----IALVAIGRDPITDP---AWGVTIDDHGHVATDA-YGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETI 357
Cdd:COG0493 358 lpadLVILAIGQTPDPSGleeELGLELDKRGTIVVDEeTYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAI 431
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
166-358 |
3.67e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 61.69 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 166 VIATGAKPR--PLPG-NPFAGALIDSTQALE----VNEFPSSA--------VIIGAGA----IALEFASMWNAAGS---- 222
Cdd:COG1252 102 VIATGSVTNffGIPGlAEHALPLKTLEDALAlrerLLAAFERAerrrlltiVVVGGGPtgveLAGELAELLRKLLRypgi 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 223 -----KVTLLIRKDRVLSAWDRRAGTTLTRELKRHGVNIITRASVTHVDTGanlgaTVHYTregqDGEQ-----SVW-GE 291
Cdd:COG1252 182 dpdkvRITLVEAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDAD-----GVTLE----DGEEipadtVIWaAG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 292 IALVAIGRDpitdpaWGVTIDDHGHVATDAYGRT-DKPGVWAVGDVTA------------GHAlAHRafeQGIVIAETIA 358
Cdd:COG1252 253 VKAPPLLAD------LGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAvpdpdgkpvpktAQA-AVQ---QAKVLAKNIA 322
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
165-336 |
4.32e-10 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 61.48 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 165 IVIATGAKPRPLP------GNPFAGALIDSTQAL-EVNEFPSSAVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSaw 237
Cdd:PRK09754 104 LFIATGAAARPLPlldalgERCFTLRHAGDAARLrEVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMG-- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 238 dRRAGTTLTRE-LKRH---GVNIITRASVTHVDTGANLGATVhytregQDGEqSVWGEIALVAIGRDPITDPAWGVTIDD 313
Cdd:PRK09754 182 -RNAPPPVQRYlLQRHqqaGVRILLNNAIEHVVDGEKVELTL------QSGE-TLQADVVIYGIGISANDQLAREANLDT 253
|
170 180
....*....|....*....|...
gi 2796464736 314 HGHVATDAYGRTDKPGVWAVGDV 336
Cdd:PRK09754 254 ANGIVIDEACRTCDPAIFAGGDV 276
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
9-357 |
4.41e-10 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 61.73 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 9 IIGAGPGGYSTALRAAELGMKVALIERDATVGGtcLNRGCIPSkalitathtidtvhraaelgvnasvngidfgtlrdYR 88
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLRYGIPE-----------------------------------FR 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 89 L--RVVKTMVGGLAGLlahrGITvFRANAAFHADETApatsnhivhlvpspdqSDILTYHKAdvpepsgptmdltttnIV 166
Cdd:PRK11749 188 LpkDIVDREVERLLKL----GVE-IRTNTEVGRDITL----------------DELRAGYDA----------------VF 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 167 IATGA-KPRPL--PGNPFAG--------ALIDSTQALEVNEFPSSAVIIGAGAIALEfasmwnAA------GSK-VTLLI 228
Cdd:PRK11749 231 IGTGAgLPRFLgiPGENLGGvysavdflTRVNQAVADYDLPVGKRVVVIGGGNTAMD------AArtakrlGAEsVTIVY 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 229 RKDRV-LSAwdRRagttltREL---KRHGVNIITRASVT--HVDTGANLGATVHYTREGQ---DGEQSVWGE-------- 291
Cdd:PRK11749 305 RRGREeMPA--SE------EEVehaKEEGVEFEWLAAPVeiLGDEGRVTGVEFVRMELGEpdaSGRRRVPIEgseftlpa 376
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796464736 292 -IALVAIGRDPITDPAWGVT---IDDHGHVATD-AYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETI 357
Cdd:PRK11749 377 dLVIKAIGQTPNPLILSTTPgleLNRWGTIIADdETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAI 447
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
201-407 |
1.53e-09 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 59.80 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 201 AVIIGAGAIALEFASMWNAAGSKVTLLIRKDRVLSAWDRRAGTTLTRELKRHGVNIITRASVTHVDtganlGATVHYTre 280
Cdd:PRK13512 151 ALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAIN-----GNEVTFK-- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 281 gqDGEQSVWgEIALVAIGRDPITD--PAWGVTIDDHGHVATDAYGRTDKPGVWAVGDVTAGH----------ALAHRAFE 348
Cdd:PRK13512 224 --SGKVEHY-DMIIEGVGTHPNSKfiESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHyrhvdlpasvPLAWGAHR 300
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 349 QGIVIAETIAGLNPKPVDEATVPQIVFSFPEA-ASVGLTVEqaqaredliEIKETNYPML 407
Cdd:PRK13512 301 AASIVAEQIAGNDTIEFKGFLGNNIVKFFDYTfASVGVKPN---------ELKQFDYKMV 351
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
3-42 |
1.55e-07 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 53.68 E-value: 1.55e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2796464736 3 EQFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGT 42
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGH 41
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
2-42 |
4.08e-07 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 52.43 E-value: 4.08e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2796464736 2 SEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGT 42
Cdd:PRK12843 14 DAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT 54
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
3-41 |
1.82e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 50.23 E-value: 1.82e-06
10 20 30
....*....|....*....|....*....|....*....
gi 2796464736 3 EQFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGG 41
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
6-42 |
2.50e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 49.91 E-value: 2.50e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2796464736 6 DLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGT 42
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGM 37
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
1-43 |
5.15e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 48.73 E-value: 5.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2796464736 1 MSEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGTC 43
Cdd:PRK07208 1 MTNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGIS 43
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
6-35 |
1.08e-05 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 47.80 E-value: 1.08e-05
10 20 30
....*....|....*....|....*....|
gi 2796464736 6 DLVIIGAGPGGYSTALRAAELGMKVALIER 35
Cdd:COG2509 32 DVVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
6-42 |
1.44e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 47.41 E-value: 1.44e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2796464736 6 DLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGT 42
Cdd:PRK06134 14 DVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGGT 50
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
166-335 |
2.92e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 46.06 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 166 VIATGAKP--RPLPGN----------PFAGALIDSTQALEVnefpssaVIIGAGAIALEFASMWNAAGSKVTLLIRKDRV 233
Cdd:PRK04965 104 VLATGASAfvPPIPGRelmltlnsqqEYRAAETQLRDAQRV-------LVVGGGLIGTELAMDLCRAGKAVTLVDNAASL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 234 LSAW-DRRAGTTLTRELKRHGVNIITRASVTHVD-TGANLGATVHytregqDGeQSVWGEIALVAIGRDPITDPAWGVTI 311
Cdd:PRK04965 177 LASLmPPEVSSRLQHRLTEMGVHLLLKSQLQGLEkTDSGIRATLD------SG-RSIEVDAVIAAAGLRPNTALARRAGL 249
|
170 180
....*....|....*....|....
gi 2796464736 312 DDHGHVATDAYGRTDKPGVWAVGD 335
Cdd:PRK04965 250 AVNRGIVVDSYLQTSAPDIYALGD 273
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
6-42 |
3.30e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 46.13 E-value: 3.30e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2796464736 6 DLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGT 42
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGA 37
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
6-43 |
5.02e-05 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 45.59 E-value: 5.02e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2796464736 6 DLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGTC 43
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
6-42 |
6.94e-05 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 45.45 E-value: 6.94e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2796464736 6 DLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGT 42
Cdd:PRK12842 11 DVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGGT 47
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
5-35 |
7.64e-05 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 44.62 E-value: 7.64e-05
10 20 30
....*....|....*....|....*....|.
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIER 35
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEK 31
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1-42 |
1.16e-04 |
|
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: 44.47 E-value: 1.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2796464736 1 MSEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGT 42
Cdd:COG2072 3 ATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
9-43 |
1.22e-04 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 40.21 E-value: 1.22e-04
10 20 30
....*....|....*....|....*....|....*
gi 2796464736 9 IIGAGPGGYSTALRAAELGMKVALIERDATVGGTC 43
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
5-40 |
3.04e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 42.95 E-value: 3.04e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIERDATVG 40
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
9-41 |
3.68e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 42.92 E-value: 3.68e-04
10 20 30
....*....|....*....|....*....|...
gi 2796464736 9 IIGAGPGGYSTALRAAELGMKVALIERDATVGG 41
Cdd:COG1148 145 VIGGGIAGMTAALELAEQGYEVYLVEKEPELGG 177
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
5-33 |
4.77e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 42.53 E-value: 4.77e-04
10 20
....*....|....*....|....*....
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALI 33
Cdd:PRK05329 3 FDVLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
189-360 |
5.41e-04 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 42.45 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 189 TQALEVNEFPSSAVIIGAGAIALEFASMWNAAGS--------------KVTLLIRKDRVLSAWDRRAGTTLTRELKRHGV 254
Cdd:PTZ00318 164 TTSVEERKRLLHFVVVGGGPTGVEFAAELADFFRddvrnlnpelveecKVTVLEAGSEVLGSFDQALRKYGQRRLRRLGV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 255 NIITRASVTHVDTGANLgatvhytreGQDGEQSVWGEIALVA-IGRDPIT-------DPAWGVTIDDHGHVAtdaygrtD 326
Cdd:PTZ00318 244 DIRTKTAVKEVLDKEVV---------LKDGEVIPTGLVVWSTgVGPGPLTkqlkvdkTSRGRISVDDHLRVK-------P 307
|
170 180 190
....*....|....*....|....*....|....*....
gi 2796464736 327 KPGVWAVGDVTAGH-----ALAHRAFEQGIVIAETIAGL 360
Cdd:PTZ00318 308 IPNVFALGDCAANEerplpTLAQVASQQGVYLAKEFNNE 346
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
3-42 |
5.62e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 42.20 E-value: 5.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2796464736 3 EQFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGT 42
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGA 40
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
8-41 |
5.88e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 42.18 E-value: 5.88e-04
10 20 30
....*....|....*....|....*....|....
gi 2796464736 8 VIIGAGPGGYSTALRAAELGMKVALIERDATVGG 41
Cdd:PRK07233 3 AIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
6-41 |
6.21e-04 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 42.00 E-value: 6.21e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2796464736 6 DLVIIGAGPGGYSTALRAAELGMKVALIERDATVGG 41
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
5-35 |
6.93e-04 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 41.85 E-value: 6.93e-04
10 20 30
....*....|....*....|....*....|.
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVALIER 35
Cdd:PRK09126 4 SDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
1-44 |
7.05e-04 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 42.13 E-value: 7.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2796464736 1 MSEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGTCL 44
Cdd:PRK06481 58 LKDKYDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAGGNTM 101
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
1-69 |
1.58e-03 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 41.17 E-value: 1.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796464736 1 MSEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGTCLNRGC---IPSKALITATHTIDTVHRAAE 69
Cdd:PRK07843 4 TVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGGSTARSGGgvwIPNNEVLKRAGVPDTPEAART 75
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
2-37 |
1.75e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 40.31 E-value: 1.75e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2796464736 2 SEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDA 37
Cdd:COG0654 1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAP 36
|
|
| PLN02697 |
PLN02697 |
lycopene epsilon cyclase |
2-36 |
2.41e-03 |
|
lycopene epsilon cyclase
Pssm-ID: 215375 [Multi-domain] Cd Length: 529 Bit Score: 40.57 E-value: 2.41e-03
10 20 30
....*....|....*....|....*....|....*
gi 2796464736 2 SEQFDLVIIGAGPGGYSTALRAAELGMKVALIERD 36
Cdd:PLN02697 106 DGTLDLVVIGCGPAGLALAAESAKLGLNVGLIGPD 140
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
201-354 |
2.43e-03 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 40.53 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 201 AVIiGAG------AIALefasmwnaAG--SKVTLL-----IRKDRVLSawdRRAgttltRELKRhgVNIITRASVTHVdT 267
Cdd:PRK15317 355 AVI-GGGnsgveaAIDL--------AGivKHVTVLefapeLKADQVLQ---DKL-----RSLPN--VTIITNAQTTEV-T 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 268 GANLGAT-VHYTREGQDGEQSVWGEIALVAIGRDPITDpaW---GVTIDDHGHVATDAYGRTDKPGVWAVGDVTAGhala 343
Cdd:PRK15317 415 GDGDKVTgLTYKDRTTGEEHHLELEGVFVQIGLVPNTE--WlkgTVELNRRGEIIVDARGATSVPGVFAAGDCTTV---- 488
|
170
....*....|.
gi 2796464736 344 hrAFEQgIVIA 354
Cdd:PRK15317 489 --PYKQ-IIIA 496
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
296-371 |
3.01e-03 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 40.10 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 296 AIGR--DPITDPAWGVTIDDHGHVATD-AYGRTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETI-AGLNPKPVDEATVP 371
Cdd:PRK12814 432 AIGQqvDPPIAEAAGIGTSRNGTVKVDpETLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIdLFLNGKPVTAPVQP 511
|
|
| PRK12845 |
PRK12845 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
6-68 |
3.16e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237226 [Multi-domain] Cd Length: 564 Bit Score: 40.13 E-value: 3.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796464736 6 DLVIIGAGPGgYSTALRAAELGMKVALIERDATVGGTCLNRG---CIPSKALITATHTIDTVHRAA 68
Cdd:PRK12845 18 DLLVVGSGTG-MAAALAAHELGLSVLIVEKSSYVGGSTARSGgafWLPASPVLDEAGAGDTLERAR 82
|
|
| PLN02464 |
PLN02464 |
glycerol-3-phosphate dehydrogenase |
2-42 |
5.11e-03 |
|
glycerol-3-phosphate dehydrogenase
Pssm-ID: 215257 [Multi-domain] Cd Length: 627 Bit Score: 39.38 E-value: 5.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2796464736 2 SEQFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGT 42
Cdd:PLN02464 69 AEPLDVLVVGGGATGAGVALDAATRGLRVGLVEREDFSSGT 109
|
|
| PLN02463 |
PLN02463 |
lycopene beta cyclase |
2-34 |
5.40e-03 |
|
lycopene beta cyclase
Pssm-ID: 178082 [Multi-domain] Cd Length: 447 Bit Score: 39.31 E-value: 5.40e-03
10 20 30
....*....|....*....|....*....|...
gi 2796464736 2 SEQFDLVIIGAGPGGYSTALRAAELGMKVALIE 34
Cdd:PLN02463 26 SRVVDLVVVGGGPAGLAVAQQVSEAGLSVCCID 58
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
8-40 |
6.07e-03 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 39.08 E-value: 6.07e-03
10 20 30
....*....|....*....|....*....|...
gi 2796464736 8 VIIGAGPGGYSTALRAAELGMKVALIERDATVG 40
Cdd:PRK08132 27 VVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLS 59
|
|
| PTZ00139 |
PTZ00139 |
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional |
5-75 |
7.51e-03 |
|
Succinate dehydrogenase [ubiquinone] flavoprotein subunit; Provisional
Pssm-ID: 240286 [Multi-domain] Cd Length: 617 Bit Score: 38.95 E-value: 7.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796464736 5 FDLVIIGAGPGGYSTALRAAELGMKVAlierdatvggtclnrgCIpSKALITATHTIdtvhrAAELGVNAS 75
Cdd:PTZ00139 30 YDAVVVGAGGAGLRAALGLVELGYKTA----------------CI-SKLFPTRSHTV-----AAQGGINAA 78
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
6-49 |
8.62e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 38.63 E-value: 8.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2796464736 6 DLVIIGAGPGGYSTALRAAELGMKVALIERDATVGG-TCLNRGCI 49
Cdd:PRK12835 13 DVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHFGGsTALSGGGI 57
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
3-69 |
9.35e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 38.58 E-value: 9.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 3 EQFDLVIIGAGPGGYSTALRAAELGMKVALIERDATVGGTCLNRGC---IPSKALITATHTIDTVHRAAE 69
Cdd:PRK12844 5 ETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGSTAMSGGvlwLPNNPLMKAAGVPDSHEDALA 74
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
9-357 |
9.42e-03 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 38.61 E-value: 9.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 9 IIGAGPGGYSTALRAAELGMKVALIERDATVGGtcLNRGCIPS----KALITathtidtvhraaelgvnasvngidfgtl 84
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHKVTVFERADRIGG--LLRYGIPDfkleKEVID---------------------------- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 85 rdyrlRVVKTMVGGlagllahrGITvFRANAAFHADETApatsnhivhlvpspdqSDILTYHKAdvpepsgptmdltttn 164
Cdd:PRK12810 198 -----RRIELMEAE--------GIE-FRTNVEVGKDITA----------------EELLAEYDA---------------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 165 IVIATGA-KPR--PLPGNPFAGA------LIDSTQAL--EVNEFPSSA-----VIIGAG---------AIALEFAS---- 215
Cdd:PRK12810 232 VFLGTGAyKPRdlGIPGRDLDGVhfamdfLIQNTRRVlgDETEPFISAkgkhvVVIGGGdtgmdcvgtAIRQGAKSvtqr 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796464736 216 --MwNAAGSKVTllirKDRVLSAWDRRAGTTLTRElkrHGVNIITRASVT--HVDTGANLGATVHYTREGQDGEQSVWGE 291
Cdd:PRK12810 312 diM-PMPPSRRN----KNNPWPYWPMKLEVSNAHE---EGVEREFNVQTKefEGENGKVTGVKVVRTELGEGDFEPVEGS 383
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796464736 292 -------IALVAIGRDPiTDPAW----GVTIDDHGHVATDAYG-RTDKPGVWAVGDVTAGHALAHRAFEQGIVIAETI 357
Cdd:PRK12810 384 efvlpadLVLLAMGFTG-PEAGLlaqfGVELDERGRVAAPDNAyQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAI 460
|
|
| |
