|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
80-566 |
0e+00 |
|
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: 940.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 80 YDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKV 159
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 160 EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGI 239
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 240 PGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQ 319
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 320 FVPIKVEQIEAgtpgrlRVVAQSTNSEEIIEGEYNTVLLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIY 399
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 400 AIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLE 479
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 480 WTIPSRDN-NKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSG 558
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
....*...
gi 1331805623 559 ASILQAGC 566
Cdd:TIGR01438 475 QDILQQGC 482
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
79-566 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 524.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 79 SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQ-DSRNYGW 157
Cdd:PTZ00052 3 TFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 158 KVEETvkHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNkGKEKIYSAERFLIATGERPRYL 237
Cdd:PTZ00052 83 KTSSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDN-SQEETITAKYILIATGGRPSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 238 -GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKF 316
Cdd:PTZ00052 160 eDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 317 IRQFVPIKVEQIEAgtpgRLRVVAQSTNSEeiiegEYNTVLLAIGRDACTRKIGLETVGVKINeKTGKIPVTDeEQTNVP 396
Cdd:PTZ00052 240 LEGVVPINIEKMDD----KIKVLFSDGTTE-----LFDTVLYATGRKPDIKGLNLNAIGVHVN-KSNKIIAPN-DCTNIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 397 YIYAIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFW 476
Cdd:PTZ00052 309 NIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 477 PLEWTIPSRD--------------NNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 542
Cdd:PTZ00052 389 TLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHP 468
|
490 500
....*....|....*....|....*
gi 1331805623 543 VCAEVFTTLSVTKRSGAS-ILQAGC 566
Cdd:PTZ00052 469 TDAEVFMNLSVTRRSGESfAAKGGC 493
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
100-551 |
5.33e-140 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 413.01 E-value: 5.33e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 100 AAQYGKKVMVLDfvtptplGTRwgLGGTCVNVGCIPKKLMHQAALLGQALQD-SRNYGWKVEETvKHDWDRMIEAVQNHI 178
Cdd:PRK06116 23 AAMYGAKVALIE-------AKR--LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRDAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 179 GSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKgkekiYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYC 258
Cdd:PRK06116 93 DRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIPDIPG-AEYGITSDGFFALEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 259 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlR 337
Cdd:PRK06116 167 PKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG-----S 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 338 VVAQSTNSEEIiegEYNTVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQ 417
Cdd:PRK06116 242 LTLTLEDGETL---TVDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 418 AGRLLAQRLYAG-STVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNnKCYAKIIC 496
Cdd:PRK06116 317 AGRRLSERLFNNkPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMKLVV 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1331805623 497 NTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 551
Cdd:PRK06116 396 VGKE-EKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
100-551 |
8.67e-118 |
|
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: 356.32 E-value: 8.67e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 100 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDRMIEAVQNHIG 179
Cdd:COG1249 22 AAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGA-PSVDWAALMARKDKVVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 180 SLNWGYRVALREKKVVYENAYGQFIGPHRIKATNnkgkEKIYSAERFLIATGERPRYLGIPG-DKEYCISSDDLFSLPYC 258
Cdd:COG1249 92 RLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTG----GETLTADHIVIATGSRPRVPPIPGlDEVRVLTSDEALELEEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 259 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrLR 337
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG----VT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 338 VVAQSTNSEEIIEGEYntVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPVAIQ 417
Cdd:COG1249 244 VTLEDGGGEEAVEADK--VLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAHVASA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 418 AGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFgeENIEVYHSYFWPLEWTIpSRDNNKCYAKIICN 497
Cdd:COG1249 320 EGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAG--IDVKVGKFPFAANGRAL-ALGETEGFVKLIAD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1331805623 498 tKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 551
Cdd:COG1249 397 -AETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
80-551 |
1.95e-113 |
|
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: 344.87 E-value: 1.95e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 80 YDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFVtptplgtrwglGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGW 157
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 158 KVEEtVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKekiYSAERFLIATGERPRYL 237
Cdd:TIGR01424 70 TVGK-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 238 GIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKF 316
Cdd:TIGR01424 146 ALPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 317 IRQFVPIKVEQIEAGtpgrlRVVAQSTNSEEIIEgeyNTVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVP 396
Cdd:TIGR01424 225 LPEDSITSISKDDDG-----RLKATLSKHEEIVA---DVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 397 YIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFW 476
Cdd:TIGR01424 296 SIYAVGDV-TDRINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331805623 477 PLEWTIPSRdNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 551
Cdd:TIGR01424 373 PMKATFSGR-QEKTLMKLVVDAKD-DKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
100-551 |
1.47e-108 |
|
glutathione-disulfide reductase, animal/bacterial; 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 animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]
Pssm-ID: 273614 [Multi-domain] Cd Length: 450 Bit Score: 332.57 E-value: 1.47e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 100 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIG 179
Cdd:TIGR01421 21 AAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDAYVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 180 SLNWGYRVALREKKVVYENAYGQFIGPHRIKAtnnKGKEkiYSAERFLIATGERPRYL-GIPGdKEYCISSDDLFSLPYC 258
Cdd:TIGR01421 92 RLNGIYQKNLEKNKVDVIFGHARFTKDGTVEV---NGRD--YTAPHILIATGGKPSFPeNIPG-AELGTDSDGFFALEEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 259 PGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlR 337
Cdd:TIGR01421 166 PKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG-----K 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 338 VVAQSTNSEEIIegEYNTVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPVAIQ 417
Cdd:TIGR01421 241 LVIHFEDGKSID--DVDELIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 418 AGRLLAQRLYAGST-VKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRdNNKCYAKIIC 496
Cdd:TIGR01421 317 AGRKLSERLFNGKTdDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSE-KQKCRMKLVC 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1331805623 497 NTKdNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 551
Cdd:TIGR01421 396 AGK-EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
69-560 |
5.36e-107 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 330.24 E-value: 5.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 69 KMNGPEDLPESYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFvtpTPLGTRW--GLGGTCVNVGCIPKKLMHQAAL 144
Cdd:PLN02507 13 KVNADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGIceLPF---HPISSESigGVGGTCVIRGCVPKKILVYGAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 145 LGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKV-VYENAyGQFIGPHRIKATNNKGKEKIYSA 223
Cdd:PLN02507 90 FGGEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVkLYEGE-GKIVGPNEVEVTQLDGTKLRYTA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 224 ERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMA 302
Cdd:PLN02507 169 KHILIATGSRAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 303 NKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrLRVVaqSTNSEEIIEgeyNTVLLAIGRDACTRKIGLETVGVKInEKT 382
Cdd:PLN02507 248 AVVARNLEGRGINLHPRTNLTQLTKTEGG----IKVI--TDHGEEFVA---DVVLFATGRAPNTKRLNLEAVGVEL-DKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 383 GKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEK 462
Cdd:PLN02507 318 GAVKVDEYSRTNIPSIWAIGDV-TNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 463 fGEENIEVYHSYFWPLEWTIPSRdNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 542
Cdd:PLN02507 397 -AKGDILVFTSSFNPMKNTISGR-QEKTVMKLIVDAET-DKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHP 473
|
490
....*....|....*....
gi 1331805623 543 VCAEVFTTL-SVTKRSGAS 560
Cdd:PLN02507 474 SAAEEFVTMrSVTRRVTAK 492
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
1-556 |
1.47e-101 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 317.97 E-value: 1.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 1 MPAMLPTGSHSAVLPP--SHCSTAPPSTSQEPSSSADPklcLSLPTSDGRQERNVQFGLAYQEGRLQKLLKMNGPEDlPE 78
Cdd:PLN02546 1 AAATLPSTSKLTSSPSlqTLYRKLPLRLPLPSSSSSSH---LPLPKTLTRLSSPRPLSHHHRRRSVSRAAAPNGAES-ER 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 79 SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFVTPTPlGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYG 156
Cdd:PLN02546 77 HYDFDLFTIGAGSGGVRASRFASNFGASAAVceLPFATISS-DTLGGVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 157 WKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNnkgkeKIYSAERFLIATGERPRY 236
Cdd:PLN02546 156 WKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDG-----KLYTARNILIAVGGRPFI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 237 LGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIK 315
Cdd:PLN02546 231 PDIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAEQMSLRGIE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 316 FIRQFVPIKVEQIEAGTpgrlrvVAQSTNsEEIIEGeYNTVLLAIGRDACTRKIGLETVGVKINeKTGKIPVTDEEQTNV 395
Cdd:PLN02546 310 FHTEESPQAIIKSADGS------LSLKTN-KGTVEG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 396 PYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYF 475
Cdd:PLN02546 381 PSIWAVGDV-TDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD--VDVFTANF 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 476 WPLEWTIpSRDNNKCYAKIICNTKDNeRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTK 555
Cdd:PLN02546 458 RPLKATL-SGLPDRVFMKLIVCAKTN-KVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMRTPT 535
|
.
gi 1331805623 556 R 556
Cdd:PLN02546 536 R 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
124-552 |
2.28e-87 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 281.12 E-value: 2.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 124 LGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVkhDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQF 203
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 204 IGPHR--IKATNNKGKE----------------------KIYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYcP 259
Cdd:PTZ00058 160 LSENQvlIKKVSQVDGEadesdddevtivsagvsqlddgQVIEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 260 GKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEagTPGRLRV 338
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVK--EKNLTIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 339 VAQSTNSEeiiegEYNTVLLAIGRDACTRKIGLEtvGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDK---------- 408
Cdd:PTZ00058 316 LSDGRKYE-----HFDYVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 409 -----------------------VELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGE 465
Cdd:PTZ00058 389 lklyneepylkkkentsgesyynVQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGK 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 466 ENIEVYHSYFWPLEWTI----PSrDNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIH 541
Cdd:PTZ00058 469 ENVKIYESRFTNLFFSVydmdPA-QKEKTYLKLVCVGKE-ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIH 546
|
490
....*....|.
gi 1331805623 542 PVCAEVFTTLS 552
Cdd:PTZ00058 547 PTAAEEFVTMA 557
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
100-546 |
1.01e-80 |
|
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: 261.45 E-value: 1.01e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 100 AAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVE-ETVKHDWDRMIEAVQNHI 178
Cdd:TIGR01423 23 ATLYKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDrSSVKANWKALIAAKNKAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 179 GSLNWGYRVALREKK-VVYENAYGQFIGPHRIKA-----TNNKGKEKIySAERFLIATGERPRYLGIPGDkEYCISSDDL 252
Cdd:TIGR01423 103 LDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVresadPKSAVKERL-QAEHILLATGSWPQMLGIPGI-EHCISSNEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 253 FSLPYCPGKTLVVGASYVALECAGFLAG---IGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQi 328
Cdd:TIGR01423 181 FYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 329 eaGTPGRLRVVAQSTNseeiiEGEYNTVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDK 408
Cdd:TIGR01423 260 --NADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKK-GAIQVDEFSRTNVPNIYAIGDV-TDR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 409 VELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFgeENIEVYHSYFWPLEWTIPSRDNN 488
Cdd:TIGR01423 331 VMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYK 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331805623 489 KCYAKIICNTKDNErVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAE 546
Cdd:TIGR01423 409 KFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
99-547 |
2.59e-71 |
|
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: 236.00 E-value: 2.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 99 EAAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKK-LMHQAALLGQALQdSRNYGWKVeETVKHDWDRMIEAVQNH 177
Cdd:TIGR01350 19 RAAQLGLKVALVE---------KEYLGGTCLNVGCIPTKaLLHSAEVYDEIKH-AKDLGIEV-ENVSVDWEKMQKRKNKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 178 IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKiYSAERFLIATGERPRYLGIP--GDKEYCISSDDLFSL 255
Cdd:TIGR01350 88 VKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLPGPfdFDGKVVITSTGALNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 256 PYCPGKTLVVGASYVALECAGFLAGIGLDVTV--MVRSIlLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTp 333
Cdd:TIGR01350 167 EEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQV- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 334 grlrVVAQSTNSEEIIEGEYntVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEdKVELTP 413
Cdd:TIGR01350 245 ----TYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIG-GPMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 414 VAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAvekfGEENIEVYHSYFwplewtiPSRDNNK---- 489
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF-------PFAANGKalal 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331805623 490 ----CYAKIICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 547
Cdd:TIGR01350 386 getdGFVKIIAD-KKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
100-547 |
3.95e-63 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 214.24 E-value: 3.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 100 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDrmieAVQNH-- 177
Cdd:PRK06416 23 AAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAEN-VGIDFK----KVQEWkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 178 --IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGkEKIYSAERFLIATGERPRYL-GIPGDKEYCISSDDLFS 254
Cdd:PRK06416 89 gvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDG-EQTYTAKNIILATGSRPRELpGIEIDGRVIWTSDEALN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 255 LPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRsiLLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEAG 331
Cdd:PRK06416 168 LDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALKKRGIKIK---TGAKAKKVEQT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 332 TPGrLRVVAQSTNSEEIIEGEYntVLLAIGRDACTRKIGLETVGVKINEktGKIPVTDEEQTNVPYIYAIGDILEdKVEL 411
Cdd:PRK06416 243 DDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIVG-GPML 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 412 TPVAIQAGRLLAQRLyAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFwplewtipsRDNNKCY 491
Cdd:PRK06416 317 AHKASAEGIIAAEAI-AGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVVKFPF---------AGNGKAL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331805623 492 A--------KIICNTKDNErVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 547
Cdd:PRK06416 385 AlgetdgfvKLIFDKKDGE-VLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
99-550 |
2.03e-61 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 209.65 E-value: 2.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 99 EAAQYGKKVMVLDfvtPTPLGtrwglgGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDRMIEAVQNHI 178
Cdd:PRK06292 21 RAAKLGKKVALIE---KGPLG------GTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADG-PKIDFKKVMARVRRER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 179 GSLNWGYRVALREK-KVVYENAYGQFIGPHRIKAtnnkgKEKIYSAERFLIATGER-PRYLGI-PGDKEYCISSDDLFSL 255
Cdd:PRK06292 91 DRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRvPPIPGVwLILGDRLLTSDDAFEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 256 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIrqfVPIKVEQIEAGtPG 334
Cdd:PRK06292 166 DKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-FKIK---LGAKVTSVEKS-GD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 335 RLRVVAQSTNSEEIIEGEYntVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPV 414
Cdd:PRK06292 241 EKVEELEKGGKTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSVPGIYAAGDVN-GKPPLLHE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 415 AIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEWTIPSR--DNNKCYA 492
Cdd:PRK06292 317 AADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEV-----PFEAQGRARvmGKNDGFV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331805623 493 KIICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTT 550
Cdd:PRK06292 392 KVYAD-KKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRT 448
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
99-546 |
2.90e-61 |
|
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: 209.20 E-value: 2.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 99 EAAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVkhDWDRMIEAVQNHI 178
Cdd:TIGR02053 18 KAAELGASVAMVE---------RGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATVAV--DFGELLEGKREVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 179 GSL-NWGYRVALREKKVVYENAYGQFIGPHRIKAtnNKGKEkIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSL 255
Cdd:TIGR02053 87 EELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGRE-VRGAKRFLIATGARPAIPPIPGLKEagY-LTSEEALAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 256 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQfVPIKVEQIEAgtpG 334
Cdd:TIGR02053 163 DRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTS-AQVKAVSVRG---G 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 335 RLRVVAQSTNSEEIIEGEYntVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPV 414
Cdd:TIGR02053 239 GKIITVEKPGGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDER-GGILVDETLRTSNPGIYAAGDVT-GGLQLEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 415 AIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIpsrDNNKCYAKI 494
Cdd:TIGR02053 315 AAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARIN---RDTRGFIKL 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1331805623 495 IC--NTKdneRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAE 546
Cdd:TIGR02053 392 VAepGTG---KVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
124-551 |
2.55e-54 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 190.80 E-value: 2.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 124 LGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDW----DRMIEAVQN-HIGSLNWgyrvaLREKK---VV 195
Cdd:PRK06370 39 LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFkavmARKRRIRARsRHGSEQW-----LRGLEgvdVF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 196 YENAygQFIGPHRIKATNnkgkeKIYSAERFLIATGERPRYLGIPG--DKEYcISSDDLFSLPYCPGKTLVVGASYVALE 273
Cdd:PRK06370 114 RGHA--RFESPNTVRVGG-----ETLRAKRIFINTGARAAIPPIPGldEVGY-LTNETIFSLDELPEHLVIIGGGYIGLE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 274 CAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQieagTPGRLRVVAQSTNSEEIIEGE 352
Cdd:PRK06370 186 FAQMFRRFGSEVTVIERGpRLLPREDEDVAAAVREILEREGIDVRLNAECIRVER----DGDGIAVGLDCNGGAPEITGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 353 YntVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTV 432
Cdd:PRK06370 262 H--ILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRGAFTHTAYNDARIVAANLLDGGRR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 433 KCDYENVPTTVFTPLEYGACGLSEEKAVEKfGeENIEVYhsyfwplewTIPSRD--------NNKCYAKIICNtKDNERV 504
Cdd:PRK06370 338 KVSDRIVPYATYTDPPLARVGMTEAEARKS-G-RRVLVG---------TRPMTRvgravekgETQGFMKVVVD-ADTDRI 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1331805623 505 VGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 551
Cdd:PRK06370 406 LGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
98-419 |
3.50e-54 |
|
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: 185.60 E-value: 3.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 98 KEAAQYGKKVMVLdfvtptplgtrwGLGGTCVNVGCIPKKLMHQAAllgqalqdsrnygwKVEETVKHDWDRMiEAVQNH 177
Cdd:pfam07992 17 LTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAA--------------EAPEIASLWADLY-KRKEEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 178 IGSLNWGYRVALREKKVVYENAYGQFIGPHrikatNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYC------ISSDD 251
Cdd:pfam07992 70 VKKLNNGIEVLLGTEVVSIDPGAKKVVLEE-----LVDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtLDSAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 252 LFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEa 330
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGVEVR---LGTSVKEII- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 331 GTPGRLRVVaqsTNSEEIIEGEynTVLLAIGRDACTRkiGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDILEDKVE 410
Cdd:pfam07992 221 GDGDGVEVI---LKDGTEIDAD--LVVVAIGRRPNTE--LLEAAGLELDE-RGGIVVDEYLRTSVPGIYAAGDCRVGGPE 292
|
....*....
gi 1331805623 411 LTPVAIQAG 419
Cdd:pfam07992 293 LAQNAVAQG 301
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
125-547 |
3.62e-44 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 162.82 E-value: 3.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 125 GGTCVNVGCIPKKLMHQAALLGQALQDSRNYGwkVEETVKH-DWDRMIEAVQNHIGSLNWG---YRVALREKKVVYENAY 200
Cdd:PRK07846 34 GGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIAAGgeeYRGRDTPNIDVYRGHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 201 gQFIGPHRIKAtnnkGKEKIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSLPYCPGKTLVVGASYVALECAGFL 278
Cdd:PRK07846 112 -RFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSGvrY-HTSDTIMRLPELPESLVIVGGGFIAAEFAHVF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 279 AGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIRQFVPIKVEQIEAGtpgrlrvVAQSTNSEEIIEGEynTVL 357
Cdd:PRK07846 186 SALGVRVTVVNRSgRLLRHLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSG-------VTLRLDDGSTVEAD--VLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 358 LAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAG-STVKCDY 436
Cdd:PRK07846 256 VATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV-SSPYQLKHVANHEARVVQHNLLHPdDLIASDH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 437 ENVPTTVFTPLEYGACGLSEEKAVEKfgEENIEVYH------SYFWPLEWTipsrdnnKCYAKIICNtKDNERVVGFHVL 510
Cdd:PRK07846 334 RFVPAAVFTHPQIASVGLTENEARAA--GLDITVKVqnygdvAYGWAMEDT-------TGFVKLIAD-RDTGRLLGAHII 403
|
410 420 430
....*....|....*....|....*....|....*...
gi 1331805623 511 GPNAGEVTQGFAAALKCGLTKKQL-DSTIGIHPVCAEV 547
Cdd:PRK07846 404 GPQASTLIQPLIQAMSFGLDAREMaRGQYWIHPALPEV 441
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
78-557 |
2.95e-42 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 158.16 E-value: 2.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 78 ESYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRwgLGGTCVNVGCIPKK-LMHQAALLGQALQDSRNYG 156
Cdd:PRK06327 1 MSKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNPKGKPA--LGGTCLNVGCIPSKaLLASSEEFENAGHHFADHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 157 WKVEEtVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIG----PHRIKATnNKGKEKIySAERFLIATGE 232
Cdd:PRK06327 79 IHVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGktdaGYEIKVT-GEDETVI-TAKHVIIATGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 233 RPRYL-GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHME 310
Cdd:PRK06327 156 EPRHLpGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 311 EHGIKFIrqfVPIKVEQIEAGTPGrLRVVAQSTNSEEIIEgEYNTVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDE 390
Cdd:PRK06327 236 KQGLDIH---LGVKIGEIKTGGKG-VSVAYTDADGEAQTL-EVDKLIVSIGRVPNTDGLGLEAVGLKLDER-GFIPVDDH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 391 EQTNVPYIYAIGDILEdKVELTPVAIQAGRLLAQRLyAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVekfgEENIEV 470
Cdd:PRK06327 310 CRTNVPNVYAIGDVVR-GPMLAHKAEEEGVAVAERI-AGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLK----AEGVEY 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 471 YHSYFwplewtiPSRDNNKC--------YAKIICNTKdNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 542
Cdd:PRK06327 384 KAGKF-------PFMANGRAlamgepdgFVKIIADAK-TDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHP 455
|
490
....*....|....*..
gi 1331805623 543 VCAEVF--TTLSVTKRS 557
Cdd:PRK06327 456 TLSEVWheAALAVDKRP 472
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
125-547 |
1.72e-39 |
|
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: 149.91 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 125 GGTCVNVGCIPKKLMHQAALLGQALQDSRNYGwkVEETVKH-DWDRMIEAVQNH----IGSLNWGYRVALREKKVVYENA 199
Cdd:TIGR03452 35 GGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRVFGDridpIAAGGEDYRRGDETPNIDVYDG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 200 YGQFIGPHRIKAtnnkGKEKIYSAERFLIATGERPR---YLGIPGDKEYciSSDDLFSLPYCPGKTLVVGASYVALECAG 276
Cdd:TIGR03452 113 HARFVGPRTLRT----GDGEEITGDQIVIAAGSRPYippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGYIAAEFAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 277 FLAGIGLDVTVMVRS-ILLRGFDQDMANKIGE----HMEEHGIKFIrqfvpIKVEQIEAGtpgrlrvVAQSTNSEEIIEG 351
Cdd:TIGR03452 187 VFSALGTRVTIVNRStKLLRHLDEDISDRFTEiakkKWDIRLGRNV-----TAVEQDGDG-------VTLTLDDGSTVTA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 352 EynTVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDkVELTPVAIQAGRLLAQRL-YAGS 430
Cdd:TIGR03452 255 D--VLLVATGRVPNGDLLDAEAAGVEVDED-GRIKVDEYGRTSARGVWALGDVSSP-YQLKHVANAEARVVKHNLlHPND 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 431 TVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYH----SYFWPLEWTipsrdnnKCYAKIICNtKDNERVVG 506
Cdd:TIGR03452 331 LRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIQNygdvAYGWAMEDT-------TGFCKLIAD-RDTGKLLG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1331805623 507 FHVLGPNAGEVTQGFAAALKCGLTKKQL-DSTIGIHPVCAEV 547
Cdd:TIGR03452 403 AHIIGPQASSLIQPLITAMAFGLDAREMaRKQYWIHPALPEV 444
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
439-551 |
8.59e-37 |
|
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: 132.29 E-value: 8.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 439 VPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFWPLEWTIPSRDNnKCYAKIICNtKDNERVVGFHVLGPNAGEVT 518
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDT-DGFVKLVAD-RETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 1331805623 519 QGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 551
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
100-534 |
3.79e-36 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 142.21 E-value: 3.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 100 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQaLQDSRNYGWKVEETVKH-DWDRMIEAVQNhi 178
Cdd:PRK13748 117 AVEQGARVTLIE---------RGTIGGTCVNVGCVPSKIMIRAAHIAH-LRRESPFDGGIAATVPTiDRSRLLAQQQA-- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 179 gslnwgyRV-ALREKKvvYEN------------AYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKE- 244
Cdd:PRK13748 185 -------RVdELRHAK--YEGildgnpaitvlhGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKEt 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 245 -YCISSDDLFSlPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLrgFDQDMAnkIGEHM----EEHGIKFIrq 319
Cdd:PRK13748 256 pYWTSTEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLF--FREDPA--IGEAVtaafRAEGIEVL-- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 320 fvpikvEQIEAGTpgrlrvVAQStNSEEIIEGEYNTV-----LLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTN 394
Cdd:PRK13748 329 ------EHTQASQ------VAHV-DGEFVLTTGHGELradklLVATGRAPNTRSLALDAAGVTVNAQ-GAIVIDQGMRTS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 395 VPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTvKCDYENVPTTVFTPLEYGACGLSEEKAvekfGEENIEVyHSY 474
Cdd:PRK13748 395 VPHIYAAGDC-TDQPQFVYVAAAAGTRAAINMTGGDA-ALDLTAMPAVVFTDPQVATVGYSEAEA----HHDGIET-DSR 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331805623 475 FWPLEwTIPSRDNN---KCYAKIICNTKDNeRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQL 534
Cdd:PRK13748 468 TLTLD-NVPRALANfdtRGFIKLVIEEGSG-RLIGVQAVAPEAGELIQTAALAIRNRMTVQEL 528
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
77-516 |
3.02e-35 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 137.98 E-value: 3.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 77 PESYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDfvtptplgTRWGLGGTCVNVGCIPKKLMHQAAL-LGQALQDS--R 153
Cdd:PRK05249 1 MHMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlyS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 154 NYGWKVEETVKHDWDRMIEAVQNHIGSLnwgyRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGER 233
Cdd:PRK05249 73 SYRVKLRITFADLLARADHVINKQVEVR----RGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 234 P-RYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEE 311
Cdd:PRK05249 149 PyRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 312 HGIKFI-RQfvpiKVEQIEAGTPGRLRVVAqstnSEEIIEGEynTVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDE 390
Cdd:PRK05249 229 SGVTIRhNE----EVEKVEGGDDGVIVHLK----SGKKIKAD--CLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNEN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 391 EQTNVPYIYAIGDiledkV----ELTPVAIQAGRLLAQRLYaGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVekfgEE 466
Cdd:PRK05249 298 YQTAVPHIYAVGD-----VigfpSLASASMDQGRIAAQHAV-GEATAHLIEDIPTGIYTIPEISSVGKTEQELT----AA 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331805623 467 NI--EVYHSYFWPLewtipSR-----DNNKCYaKIICNTKDnERVVGFHVLGPNAGE 516
Cdd:PRK05249 368 KVpyEVGRARFKEL-----ARaqiagDNVGML-KILFHRET-LEILGVHCFGERATE 417
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
125-546 |
5.75e-30 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 122.55 E-value: 5.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 125 GGTCVNVGCIPKKLMHQAAllgqalqdsrNYGWKVEETVKHDwdrmiEAVQNHIGSLNWGyrvALREKKVVYENAYGQFI 204
Cdd:PRK07251 40 GGTCINIGCIPTKTLLVAA----------EKNLSFEQVMATK-----NTVTSRLRGKNYA---MLAGSGVDLYDAEAHFV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 205 GPHRIKATnnKGKEKI-YSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGI 281
Cdd:PRK07251 102 SNKVIEVQ--AGDEKIeLTAETIVINTGAVSNVLPIPGlaDSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 282 GLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpIKVEQIEAGTPGrlrvVAQSTNSEEIIegeYNTVLLAI 360
Cdd:PRK07251 180 GSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLN---AHTTEVKNDGDQ----VLVVTEDETYR---FDALLYAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 361 GRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKC-DYENV 439
Cdd:PRK07251 250 GRKPNTEPLGLENTDIELTER-GAIKVDDYCQTSVPGVFAVGDV-NGGPQFTYISLDDFRIVFGYLTGDGSYTLeDRGNV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 440 PTTVFTPLEYGACGLSEEKAVEKFGEenievYHSYFWPLEWTIPSRDNN--KCYAKIICNTKDNErVVGFHVLGPNAGEV 517
Cdd:PRK07251 328 PTTMFITPPLSQVGLTEKEAKEAGLP-----YAVKELLVAAMPRAHVNNdlRGAFKVVVNTETKE-ILGATLFGEGSQEI 401
|
410 420
....*....|....*....|....*....
gi 1331805623 518 TQGFAAALKCGLTKKQLDSTIGIHPVCAE 546
Cdd:PRK07251 402 INLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
125-551 |
1.28e-28 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 118.73 E-value: 1.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 125 GGTCVNVGCIP-KKLMHQAALlgqalqdsrnygwkveetvKHDWDRMIeAVQNHIGSLnwgyrvaLREK---------KV 194
Cdd:NF040477 40 GGTCINIGCIPtKTLVHDAEQ-------------------HQDFSTAM-QRKSSVVGF-------LRDKnyhnladldNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 195 VYENAYGQFIGPHRIKATNNKGKEKIYsAERFLIATGERPRYLGIPGDKEY--CISSDDLFSLPYCPGKTLVVGASYVAL 272
Cdd:NF040477 93 DVINGRAEFIDNHTLRVFQADGEQELR-GEKIFINTGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 273 ECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEAgTPGRLRVVAQstnseeiiEG 351
Cdd:NF040477 172 EFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVELI---LNAQVQRVSS-HEGEVQLETA--------EG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 352 EY--NTVLLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLY-A 428
Cdd:NF040477 240 VLtvDALLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLgE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 429 GSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEwTIPSrdnnkcyAKIICNTK--------- 499
Cdd:NF040477 318 GKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTL-----PVA-AIPR-------ARVMNDTRgvlkavvdn 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1331805623 500 DNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 551
Cdd:NF040477 385 KTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDL 436
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
100-550 |
1.66e-26 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 114.24 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 100 AAQYGKKVMVLDfvtptplGTRWGLGGTCVNVGCIPKKLMHQAA----------------LLGQALQDSRNYGWK----V 159
Cdd:PTZ00153 135 AMERGLKVIIFT-------GDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVErnqlV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 160 EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPH-RIKATNNKGKEK---IYSAERFLIATGERPR 235
Cdd:PTZ00153 208 ADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYERgHIVDKNTIKSEKsgkEFKVKNIIIATGSTPN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 236 Y-LGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANkigeHMEEHG 313
Cdd:PTZ00153 288 IpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLLPLLDADVAK----YFERVF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 314 IKF--IRQFVPIKVEQIEAGTPGRLRVVAQS-----------TNSEEIIEGEYNTVLLAIGRDACTRKIGLETVGVKINE 380
Cdd:PTZ00153 364 LKSkpVRVHLNTLIEYVRAGKGNQPVIIGHSerqtgesdgpkKNMNDIKETYVDSCLVATGRKPNTNNLGLDKLKIQMKR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 381 ktGKIPVTD------EEQTNVPYIYAIGD-----ILEDKVELTPVAI------QAGRLLAQRLYAGSTVKCDYENVPTTV 443
Cdd:PTZ00153 444 --GFVSVDEhlrvlrEDQEVYDNIFCIGDangkqMLAHTASHQALKVvdwiegKGKENVNINVENWASKPIIYKNIPSVC 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 444 FTPLEYGACGLSEEKAVEKFGEENIEVYHSYF-------WPLEWTIPSRDNNKCYAKIICNT-------------KDNER 503
Cdd:PTZ00153 522 YTTPELAFIGLTEKEAKELYPPDNVGVEISFYkanskvlCENNISFPNNSKNNSYNKGKYNTvdntegmvkivylKDTKE 601
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1331805623 504 VVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTT 550
Cdd:PTZ00153 602 ILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
100-542 |
8.22e-24 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 104.56 E-value: 8.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 100 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDrmIEAVQNHIG 179
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEARVD--LPAVNARVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 180 SL----NWGYRVALREKKVVYENAYGQFI----GPHRIKATNNKGKEKIYSAERFLIATGERPRYLgiPG---DKEYCIS 248
Cdd:PRK07845 89 ALaaaqSADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGASPRIL--PTaepDGERILT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 249 SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQ 327
Cdd:PRK07845 167 WRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 328 IEAGtpgrlrVVAQSTNSEEiIEGEYntVLLAIGRDACTRKIGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDIlED 407
Cdd:PRK07845 247 TGDG------VVVTLTDGRT-VEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIYAAGDC-TG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 408 KVELTPVAIQAGRL-LAQRLyaGSTVK-CDYENVPTTVFTPLEYGACGLSeEKAVEKfGEENIEVYhsyfwplewTIPSR 485
Cdd:PRK07845 316 VLPLASVAAMQGRIaMYHAL--GEAVSpLRLKTVASNVFTRPEIATVGVS-QAAIDS-GEVPARTV---------MLPLA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331805623 486 DNNKC--------YAKIICnTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 542
Cdd:PRK07845 383 TNPRAkmsglrdgFVKLFC-RPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYP 446
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
125-551 |
2.24e-23 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 103.17 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 125 GGTCVNVGCIPKKLMhqaallgqaLQDSRNYGwkveetvkhDWDRMIE---AVQNHIGSLNWGYRVALREKKVVYENAyg 201
Cdd:PRK08010 40 GGTCINIGCIPTKTL---------VHDAQQHT---------DFVRAIQrknEVVNFLRNKNFHNLADMPNIDVIDGQA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 202 QFIGPHRIKaTNNKGKEKIYSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLA 279
Cdd:PRK08010 100 EFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIPGitTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 280 GIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpikvEQIEAGTPGRLRVVAQSTNSEEIIEGeyntVLL 358
Cdd:PRK08010 179 NFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILN------AHVERISHHENQVQVHSEHAQLAVDA----LLI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 359 AIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYA-GSTVKCDYE 437
Cdd:PRK08010 249 ASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNIWAMGDV-TGGLQFTYISLDDYRIVRDELLGeGKRSTDDRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 438 NVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEWTIPSR--DNNKCYAKIICNTKdNERVVGFHVLGPNAG 515
Cdd:PRK08010 327 NVPYSVFMTPPLSRVGMTEEQARESGADIQVVTL-----PVAAIPRARvmNDTRGVLKAIVDNK-TQRILGASLLCVDSH 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 1331805623 516 EVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 551
Cdd:PRK08010 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
205-421 |
2.81e-22 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 97.50 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 205 GPHRIKATNnkgkEKIYSAERFLIATGERPRYLGIPGDKE-------YCISSDdlfsLPYCPGKT-LVVGASYVALECAG 276
Cdd:COG0492 87 GPFRVTTDD----GTEYEAKAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEAL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 277 FLAGIGLDVTVMVRSILLRGfDQDMANKIGEHmeeHGIKFIRQFVPIKVEqieaGTPGRLRVVAQSTNSEEIIEGEYNTV 356
Cdd:COG0492 159 YLTKFASKVTLIHRRDELRA-SKILVERLRAN---PKIEVLWNTEVTEIE----GDGRVEGVTLKNVKTGEEKELEVDGV 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331805623 357 LLAIGRDACTRkiGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRL 421
Cdd:COG0492 231 FVAIGLKPNTE--LLKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAI 292
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
227-443 |
1.85e-21 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 95.26 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 227 LIATGERPRYLGIPGdkeycISSDDLFSL------PYC--------PGKTLVVGASYVALECAGFLAGIGLDVTVMVRS- 291
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddaDALrealkefkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 292 ILLRGFDQDMANKIGEHMEEHGIKFIRQFvpiKVEQIEAGTpgrlRVVAQSTNSEEIiegEYNTVLLAIG--------RD 363
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGE---TVVAIDGDD----KVAVTLTDGEEI---PADLVVVAPGvrpntelaKD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 364 ActrkigletvGVKINEkTGKIPVTDEEQTNVPYIYAIGDILE---------DKVELTPVAIQAGRLLAQRLyAGSTVKc 434
Cdd:COG0446 228 A----------GLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtgktVYIPLASAANKQGRVAAENI-LGGPAP- 294
|
....*....
gi 1331805623 435 dYENVPTTV 443
Cdd:COG0446 295 -FPGLGTFI 302
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
261-337 |
1.02e-19 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 83.41 E-value: 1.02e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331805623 261 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLR 337
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDrLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
227-426 |
1.02e-18 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 88.27 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 227 LIATGERPRYLGIPG-DKEYCI---SSDDLFSL-PYCPGKT--LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGF 297
Cdd:COG1251 103 VLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 298 DQDMANKIGEHMEEHGIKFIRQfvpIKVEQIEaGTPGRLRVVaqsTNSEEIIEGEynTVLLAIG---RDACTRKIGLETV 374
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVRLG---TGVTEIE-GDDRVTGVR---LADGEELPAD--LVVVAIGvrpNTELARAAGLAVD 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331805623 375 -GVKINEKTgkipvtdeeQTNVPYIYAIGDILE--------DKVELTPVAIQAGRLLAQRL 426
Cdd:COG1251 254 rGIVVDDYL---------RTSDPDIYAAGDCAEhpgpvygrRVLELVAPAYEQARVAAANL 305
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
261-406 |
2.51e-13 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 72.12 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 261 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIkfirqfvPIKVEQIEAGTPGRLrVV 339
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREI-------PYRLNEEIDAINGNE-VT 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331805623 340 AQSTNSEEiiegeYNTVLLAIGRDACTRKIglETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILE 406
Cdd:PRK13512 222 FKSGKVEH-----YDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIIT 280
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
263-534 |
7.56e-11 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 64.29 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 263 LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGFDQDMANKIGEHMEEHGIKFirqFVPIKVEQIEagtpGRLRVVA 340
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVEL---HLNEFVKSLI----GEDKVEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 341 QSTNseeiiEGEYNT--VLLAIGRDACTRKI---GLETVgvkineKTGKIPVTDEEQTNVPYIYAIGD------ILEDKV 409
Cdd:PRK09564 226 VVTD-----KGEYEAdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKN 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 410 ELTPVAIQA---GRLLAQRLyAGSTVKcdyenVPTT-------VFTpLEYGACGLSEEKAVEKfgeeNIEVY-------- 471
Cdd:PRK09564 295 VYVPLATTAnklGRMVGENL-AGRHVS-----FKGTlgsacikVLD-LEAARTGLTEEEAKKL----GIDYKtvfikdkn 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331805623 472 HSYFWPlewtipsrDNNKCYAKIICNtKDNERVVGFHVLGPNaGEV--TQGFAAALKCGLTKKQL 534
Cdd:PRK09564 364 HTNYYP--------GQEDLYVKLIYE-ADTKVILGGQIIGKK-GAVlrIDALAVAIYAKLTTQEL 418
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
228-460 |
8.18e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 64.00 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 228 IATGERPRYLGIPGDKEYCI---SSDDLFSL------------PYCPGKTLVVGASYVALECAGFLA----------GIG 282
Cdd:COG1252 103 IATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAellrkllrypGID 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 283 LD------VTVMVRsiLLRGFDQDMANKIGEHMEEHGIKFIRQFvpiKVEQIEAGTpgrlrvvAQSTNSEEIiegEYNTV 356
Cdd:COG1252 183 PDkvritlVEAGPR--ILPGLGEKLSEAAEKELEKRGVEVHTGT---RVTEVDADG-------VTLEDGEEI---PADTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 357 LLAIGRDA--CTRKIGLETvgvkinEKTGKIPVTDEEQT-NVPYIYAIGDI--LEDKVELT-----PVAIQAGRLLAQRL 426
Cdd:COG1252 248 IWAAGVKAppLLADLGLPT------DRRGRVLVDPTLQVpGHPNVFAIGDCaaVPDPDGKPvpktaQAAVQQAKVLAKNI 321
|
250 260 270
....*....|....*....|....*....|....*
gi 1331805623 427 YAgstvkcDYENVPTTVFTPLEYGA-CGLSEEKAV 460
Cdd:COG1252 322 AA------LLRGKPLKPFRYRDKGClASLGRGAAV 350
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
227-404 |
1.46e-09 |
|
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: 60.15 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 227 LIATG-ERPRYLGIPG-DKEYCIS----------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIG-LDVTVMVRsil 293
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 294 lRGFDqDMANKIGE--HMEEHGIKFIRQFVP-------------IKVEQIEAGTP---GRLRVVAqSTNSEEIIEGEynT 355
Cdd:COG0493 288 -RTRE-EMPASKEEveEALEEGVEFLFLVAPveiigdengrvtgLECVRMELGEPdesGRRRPVP-IEGSEFTLPAD--L 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1331805623 356 VLLAIGRDACTRKIgLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDI 404
Cdd:COG0493 363 VILAIGQTPDPSGL-EEELGLELDKR-GTI-VVDEEtyQTSLPGVFAGGDA 410
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
227-426 |
1.36e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 56.92 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 227 LIATGE-RPRYLGIPG-DKEYCISS-DDLFS-----LPYCP---------GKTLVVGASYVALECA--GFLAGiGLDVTV 287
Cdd:PRK12770 123 LIATGTwKSRKLGIPGeDLPGVYSAlEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAAleAVLLG-AEKVYL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 288 MVRsillRGFDQDMANKIG-EHMEEHGIKFIRQFVP--------------IKVEQIEAGTPGRLRVVAQsTNSEEIIegE 352
Cdd:PRK12770 202 AYR----RTINEAPAGKYEiERLIARGVEFLELVTPvriigegrvegvelAKMRLGEPDESGRPRPVPI-PGSEFVL--E 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331805623 353 YNTVLLAIGRDAcTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDKVELTPvAIQAGRLLAQRL 426
Cdd:PRK12770 275 ADTVVFAIGEIP-TPPFAKECLGIELNRK-GEIVVDEKHMTSREGVFAAGDVVTGPSKIGK-AIKSGLRAAQSI 345
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
217-404 |
4.56e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 55.79 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 217 KEKIYSAerFLIATGE-RPRYLGIPGdkeycISSDDLFSL-----------PYCPG---------KTLVVGASYVALECA 275
Cdd:PRK12831 225 EEEGFDA--VFIGSGAgLPKFMGIPG-----ENLNGVFSAnefltrvnlmkAYKPEydtpikvgkKVAVVGGGNVAMDAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 276 GFLAGIGLDVTVMVRsillRGfDQDMANKIGE--HMEEHGIKFIRQFVPI-------------KVEQIEAGTP---GRLR 337
Cdd:PRK12831 298 RTALRLGAEVHIVYR----RS-EEELPARVEEvhHAKEEGVIFDLLTNPVeilgdengwvkgmKCIKMELGEPdasGRRR 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331805623 338 VVaQSTNSEEIIegEYNTVLLAIGRDAcTRKIGLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDI 404
Cdd:PRK12831 373 PV-EIEGSEFVL--EVDTVIMSLGTSP-NPLISSTTKGLKINKR-GCI-VADEEtgLTSKEGVFAGGDA 435
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
227-424 |
5.53e-08 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 55.19 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 227 LIATG-ERPRYLGIPGDK--------EYCISS---DDLFSLPycPGKTLVV-GASYVALECAGFLAGIG-LDVTVMVRsi 292
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDFLTRVnqaVADYDLP--VGKRVVViGGGNTAMDAARTAKRLGaESVTIVYR-- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 293 llRGFDqDMANKIGE--HMEEHGIKFIRQFVPIKVEQIEAGTPG------RLRVVAQSTNSEEIIEGEY-----NTVLLA 359
Cdd:PRK11749 306 --RGRE-EMPASEEEveHAKEEGVEFEWLAAPVEILGDEGRVTGvefvrmELGEPDASGRRRVPIEGSEftlpaDLVIKA 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331805623 360 IGRDAcTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDIL--EDkveLTPVAIQAGRLLAQ 424
Cdd:PRK11749 383 IGQTP-NPLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVtgAA---TVVWAVGDGKDAAE 445
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
219-406 |
6.67e-08 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 55.60 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 219 KIYSAERFLIATGERPRYLGIPG-DKEYCI---SSDDLFSLPYCPGKTL---VVGASYVALECAGFLAGIGLDVTV--MV 289
Cdd:TIGR02374 93 RTLSYDKLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMDVSVihHA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 290 RSILLRGFDQDMANKIGEHMEEHGIKFIRQfvPIKVEQIEAGTPGRLRVvaqsTNSEEIiegEYNTVLLAIG---RDACT 366
Cdd:TIGR02374 173 PGLMAKQLDQTAGRLLQRELEQKGLTFLLE--KDTVEIVGATKADRIRF----KDGSSL---EADLIVMAAGirpNDELA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1331805623 367 RKIGLetvgvKINektGKIPVTDEEQTNVPYIYAIGDILE 406
Cdd:TIGR02374 244 VSAGI-----KVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
223-404 |
8.00e-08 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 55.13 E-value: 8.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 223 AERF---LIATGE-RPRYLGIPGDKEYCISS--------------DDLFSLPYCPGK-TLVVGASYVALECAGFLAGIGL 283
Cdd:PRK12778 515 EEGFkgiFIASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGKkVAVVGGGNTAMDSARTAKRLGA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 284 DvTVMvrsILLRGFDQDMANKIGE--HMEEHGIKFIRQFVPIK--------VEQI-----EAGTP---GRLRVVAqSTNS 345
Cdd:PRK12778 595 E-RVT---IVYRRSEEEMPARLEEvkHAKEEGIEFLTLHNPIEyladekgwVKQVvlqkmELGEPdasGRRRPVA-IPGS 669
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 346 EEIIEgeYNTVLLAIGRDActRKIGLETV-GVKINEKtGKIPVTDEEQTNVPYIYAIGDI 404
Cdd:PRK12778 670 TFTVD--VDLVIVSVGVSP--NPLVPSSIpGLELNRK-GTIVVDEEMQSSIPGIYAGGDI 724
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
213-428 |
8.71e-08 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 55.33 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 213 NNKGKEKIysaerFLIATGERPRYLGIPGDKEYCISSDDLF---------------SLPYCPGKTLVV-GASYVALECAG 276
Cdd:PRK12775 514 NDKGFDAV-----FLGVGAGAPTFLGIPGEFAGQVYSANEFltrvnlmggdkfpflDTPISLGKSVVViGAGNTAMDCLR 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 277 FLAGIGldvTVMVRSILLRGfDQDMANKIGE--HMEEHGIKFIRQFVPI-------------KVEQIEAGTP---GRLRV 338
Cdd:PRK12775 589 VAKRLG---APTVRCVYRRS-EAEAPARIEEirHAKEEGIDFFFLHSPVeiyvdaegsvrgmKVEEMELGEPdekGRRKP 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 339 VAqstnSEEIIEGEYNTVLLAIGRDAcTRKIGLETVGVKINeKTGKIPVTDE-----EQTNVPYIYAIGDILEDKVELTp 413
Cdd:PRK12775 665 MP----TGEFKDLECDTVIYALGTKA-NPIITQSTPGLALN-KWGNIAADDGklestQSTNLPGVFAGGDIVTGGATVI- 737
|
250
....*....|....*
gi 1331805623 414 VAIQAGRLLAQRLYA 428
Cdd:PRK12775 738 LAMGAGRRAARSIAT 752
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
221-402 |
5.48e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 51.46 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 221 YSAERFLIATGE--RPRYLGIPgdkEYCISSDDLFSL-PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGF 297
Cdd:pfam13738 117 YQARYVIIATGEfdFPNKLGVP---ELPKHYSYVKDFhPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 298 DQDMA--------NKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlrVVAQSTNSEEIIegEYNTVLLAIGRDaCTRKI 369
Cdd:pfam13738 194 DSDPSyslspdtlNRLEELVKNGKIKAHFNAEVKEITEVDVS------YKVHTEDGRKVT--SNDDPILATGYH-PDLSF 264
|
170 180 190
....*....|....*....|....*....|....
gi 1331805623 370 gLETVGVKINEKtGKIPVTDE-EQTNVPYIYAIG 402
Cdd:pfam13738 265 -LKKGLFELDED-GRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
221-406 |
1.13e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 47.75 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 221 YSAERFLIATGERPRYLGIPGDKEY-------CISSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL 293
Cdd:PRK10262 104 YTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 294 LRGfDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPG-RLRVVAQSTNSEEIiegEYNTVLLAIGRDACTR----K 368
Cdd:PRK10262 181 FRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGvRLRDTQNSDNIESL---DVAGLFVAIGHSPNTAifegQ 256
|
170 180 190
....*....|....*....|....*....|....*...
gi 1331805623 369 IGLETVGVKINEKTGKipvtDEEQTNVPYIYAIGDILE 406
Cdd:PRK10262 257 LELENGYIKVQSGIHG----NATQTSIPGVFAAGDVMD 290
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
323-403 |
5.88e-03 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 39.38 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331805623 323 IKVEQIEAGTPGRLRVvaqsTNSEEIIEGEYntVLLAIGRDACTRKIgLETVGVKINEKtGKIPVTDEE-QTNVPYIYAI 401
Cdd:PRK12810 365 VKVVRTELGEGDFEPV----EGSEFVLPADL--VLLAMGFTGPEAGL-LAQFGVELDER-GRVAAPDNAyQTSNPKVFAA 436
|
..
gi 1331805623 402 GD 403
Cdd:PRK12810 437 GD 438
|
|
| |
