|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
61-549 |
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: 938.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 61 YDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKV 140
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 141 EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGI 220
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 221 PGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQ 300
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 301 FVPIKVEQIEAgtpgrlRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIY 380
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 381 AIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLE 460
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 461 WTIPSRDN-NKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSG 539
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 387598068 540 ASILQAGCUG 549
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
60-549 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 526.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 60 SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQ-DSRNYGW 138
Cdd:PTZ00052 3 TFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 139 KVEETvkHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNkGKEKIYSAERFLIATGERPRYL 218
Cdd:PTZ00052 83 KTSSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDN-SQEETITAKYILIATGGRPSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 219 -GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKF 297
Cdd:PTZ00052 160 eDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 298 IRQFVPIKVEQIEAgtpgRLRVVAQSTNSEeiiegEYNTVMLAIGRDACTRKIGLETVGVKINeKTGKIPVTDeEQTNVP 377
Cdd:PTZ00052 240 LEGVVPINIEKMDD----KIKVLFSDGTTE-----LFDTVLYATGRKPDIKGLNLNAIGVHVN-KSNKIIAPN-DCTNIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 378 YIYAIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFW 457
Cdd:PTZ00052 309 NIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 458 PLEWTIPSRD--------------NNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 523
Cdd:PTZ00052 389 TLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHP 468
|
490 500
....*....|....*....|....*.
gi 387598068 524 VCAEVFTTLSVTKRSGASILQAGCUG 549
Cdd:PTZ00052 469 TDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
81-532 |
1.16e-138 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 408.78 E-value: 1.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 81 AAQYGKKVMVLDfvtptplGTRwgLGGTCVNVGCIPKKLMHQAALLGQALQD-SRNYGWKVEETvKHDWDRMIEAVQNHI 159
Cdd:PRK06116 23 AAMYGAKVALIE-------AKR--LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRDAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 160 GSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKgkekiYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYC 239
Cdd:PRK06116 93 DRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIPDIPG-AEYGITSDGFFALEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 240 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlR 318
Cdd:PRK06116 167 PKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG-----S 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 319 VVAQSTNSEEIiegEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQ 398
Cdd:PRK06116 242 LTLTLEDGETL---TVDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 399 AGRLLAQRLYAG-STVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNnKCYAKIIC 477
Cdd:PRK06116 317 AGRRLSERLFNNkPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMKLVV 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 387598068 478 NTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 532
Cdd:PRK06116 396 VGKE-EKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
81-532 |
5.56e-115 |
|
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: 348.61 E-value: 5.56e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 81 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDRMIEAVQNHIG 160
Cdd:COG1249 22 AAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGA-PSVDWAALMARKDKVVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 161 SLNWGYRVALREKKVVYENAYGQFIGPHRIKATNnkgkEKIYSAERFLIATGERPRYLGIPG-DKEYCISSDDLFSLPYC 239
Cdd:COG1249 92 RLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTG----GETLTADHIVIATGSRPRVPPIPGlDEVRVLTSDEALELEEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 240 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrLR 318
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG----VT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 319 VVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPVAIQ 398
Cdd:COG1249 244 VTLEDGGGEEAVEADK--VLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAHVASA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 399 AGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFgeENIEVYHSYFWPLEWTIpSRDNNKCYAKIICN 478
Cdd:COG1249 320 EGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAG--IDVKVGKFPFAANGRAL-ALGETEGFVKLIAD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 387598068 479 tKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 532
Cdd:COG1249 397 -AETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
61-532 |
1.87e-112 |
|
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: 341.79 E-value: 1.87e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 61 YDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFVtptplgtrwglGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGW 138
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 139 KVEEtVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKekiYSAERFLIATGERPRYL 218
Cdd:TIGR01424 70 TVGK-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 219 GIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKF 297
Cdd:TIGR01424 146 ALPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 298 IRQFVPIKVEQIEAGtpgrlRVVAQSTNSEEIIEgeyNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVP 377
Cdd:TIGR01424 225 LPEDSITSISKDDDG-----RLKATLSKHEEIVA---DVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 378 YIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFW 457
Cdd:TIGR01424 296 SIYAVGDV-TDRINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 387598068 458 PLEWTIPSRdNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 532
Cdd:TIGR01424 373 PMKATFSGR-QEKTLMKLVVDAKD-DKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
81-532 |
5.09e-107 |
|
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: 327.95 E-value: 5.09e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 81 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIG 160
Cdd:TIGR01421 21 AAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDAYVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 161 SLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKgkekiYSAERFLIATGERPRYL-GIPGdKEYCISSDDLFSLPYC 239
Cdd:TIGR01421 92 RLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIPG-AELGTDSDGFFALEEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 240 PGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlR 318
Cdd:TIGR01421 166 PKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG-----K 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 319 VVAQSTNSEEIIegEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPVAIQ 398
Cdd:TIGR01421 241 LVIHFEDGKSID--DVDELIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 399 AGRLLAQRLYAGST-VKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRdNNKCYAKIIC 477
Cdd:TIGR01421 317 AGRKLSERLFNGKTdDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSE-KQKCRMKLVC 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 387598068 478 NTKdNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 532
Cdd:TIGR01421 396 AGK-EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
50-541 |
1.02e-105 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 326.00 E-value: 1.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 50 KMNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFvtpTPLGTRW--GLGGTCVNVGCIPKKLMHQAAL 125
Cdd:PLN02507 13 KVNADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGIceLPF---HPISSESigGVGGTCVIRGCVPKKILVYGAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 126 LGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKV-VYENAyGQFIGPHRIKATNNKGKEKIYSA 204
Cdd:PLN02507 90 FGGEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVkLYEGE-GKIVGPNEVEVTQLDGTKLRYTA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 205 ERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMA 283
Cdd:PLN02507 169 KHILIATGSRAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 284 NKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrLRVVaqSTNSEEIIEgeyNTVMLAIGRDACTRKIGLETVGVKInEKT 363
Cdd:PLN02507 248 AVVARNLEGRGINLHPRTNLTQLTKTEGG----IKVI--TDHGEEFVA---DVVLFATGRAPNTKRLNLEAVGVEL-DKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 364 GKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEK 443
Cdd:PLN02507 318 GAVKVDEYSRTNIPSIWAIGDV-TNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 444 fGEENIEVYHSYFWPLEWTIPSRdNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 523
Cdd:PLN02507 397 -AKGDILVFTSSFNPMKNTISGR-QEKTVMKLIVDAET-DKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHP 473
|
490
....*....|....*....
gi 387598068 524 VCAEVFTTL-SVTKRSGAS 541
Cdd:PLN02507 474 SAAEEFVTMrSVTRRVTAK 492
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
52-537 |
2.77e-101 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 316.82 E-value: 2.77e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 52 NGPEDlPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFVTPTPlGTRWGLGGTCVNVGCIPKKLMHQAALLGQA 129
Cdd:PLN02546 70 NGAES-ERHYDFDLFTIGAGSGGVRASRFASNFGASAAVceLPFATISS-DTLGGVGGTCVLRGCVPKKLLVYASKYSHE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 130 LQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNnkgkeKIYSAERFLI 209
Cdd:PLN02546 148 FEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDG-----KLYTARNILI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 210 ATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGE 288
Cdd:PLN02546 223 AVGGRPFIPDIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 289 HMEEHGIKFIRQFVPIKVEQIEAGTpgrlrvVAQSTNsEEIIEGeYNTVMLAIGRDACTRKIGLETVGVKINeKTGKIPV 368
Cdd:PLN02546 302 QMSLRGIEFHTEESPQAIIKSADGS------LSLKTN-KGTVEG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 369 TDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEen 448
Cdd:PLN02546 373 DEYSRTSVPSIWAVGDV-TDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD-- 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 449 IEVYHSYFWPLEWTIpSRDNNKCYAKIICNTKDNeRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 528
Cdd:PLN02546 450 VDVFTANFRPLKATL-SGLPDRVFMKLIVCAKTN-KVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEE 527
|
....*....
gi 387598068 529 FTTLSVTKR 537
Cdd:PLN02546 528 FVTMRTPTR 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
105-533 |
1.14e-86 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 278.81 E-value: 1.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 105 LGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVkhDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQF 184
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 185 IGPHR--IKATNNKGKE----------------------KIYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYcP 240
Cdd:PTZ00058 160 LSENQvlIKKVSQVDGEadesdddevtivsagvsqlddgQVIEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 241 GKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEagTPGRLRV 319
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVK--EKNLTIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 320 VAQSTNSEeiiegEYNTVMLAIGRDACTRKIGLEtvGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDK---------- 389
Cdd:PTZ00058 316 LSDGRKYE-----HFDYVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 390 -----------------------VELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGE 446
Cdd:PTZ00058 389 lklyneepylkkkentsgesyynVQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGK 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 447 ENIEVYHSYFWPLEWTI----PSrDNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIH 522
Cdd:PTZ00058 469 ENVKIYESRFTNLFFSVydmdPA-QKEKTYLKLVCVGKE-ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIH 546
|
490
....*....|.
gi 387598068 523 PVCAEVFTTLS 533
Cdd:PTZ00058 547 PTAAEEFVTMA 557
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
81-527 |
1.05e-81 |
|
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: 263.37 E-value: 1.05e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 81 AAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVE-ETVKHDWDRMIEAVQNHI 159
Cdd:TIGR01423 23 ATLYKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDrSSVKANWKALIAAKNKAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 160 GSLNWGYRVALREKK-VVYENAYGQFIGPHRIKA-----TNNKGKEKIySAERFLIATGERPRYLGIPGDkEYCISSDDL 233
Cdd:TIGR01423 103 LDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVresadPKSAVKERL-QAEHILLATGSWPQMLGIPGI-EHCISSNEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 234 FSLPYCPGKTLVVGASYVALECAGFLAG---IGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQi 309
Cdd:TIGR01423 181 FYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 310 eaGTPGRLRVVAQSTNseeiiEGEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDK 389
Cdd:TIGR01423 260 --NADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKK-GAIQVDEFSRTNVPNIYAIGDV-TDR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 390 VELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFgeENIEVYHSYFWPLEWTIPSRDNN 469
Cdd:TIGR01423 331 VMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYK 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 387598068 470 KCYAKIICNTKDNErVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAE 527
Cdd:TIGR01423 409 KFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
80-528 |
2.02e-69 |
|
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: 230.61 E-value: 2.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 80 EAAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKK-LMHQAALLGQALQdSRNYGWKVeETVKHDWDRMIEAVQNH 158
Cdd:TIGR01350 19 RAAQLGLKVALVE---------KEYLGGTCLNVGCIPTKaLLHSAEVYDEIKH-AKDLGIEV-ENVSVDWEKMQKRKNKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 159 IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKiYSAERFLIATGERPRYLGIP--GDKEYCISSDDLFSL 236
Cdd:TIGR01350 88 VKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLPGPfdFDGKVVITSTGALNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 237 PYCPGKTLVVGASYVALECAGFLAGIGLDVTV--MVRSIlLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTp 314
Cdd:TIGR01350 167 EEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQV- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 315 grlrVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEdKVELTP 394
Cdd:TIGR01350 245 ----TYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIG-GPMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 395 VAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAvekfGEENIEVYHSYFwplewtiPSRDNNK---- 470
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF-------PFAANGKalal 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387598068 471 ----CYAKIICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 528
Cdd:TIGR01350 386 getdGFVKIIAD-KKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
81-528 |
3.32e-61 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 208.85 E-value: 3.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 81 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDrmieAVQNH-- 158
Cdd:PRK06416 23 AAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAEN-VGIDFK----KVQEWkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 159 --IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGkEKIYSAERFLIATGERPRYL-GIPGDKEYCISSDDLFS 235
Cdd:PRK06416 89 gvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDG-EQTYTAKNIILATGSRPRELpGIEIDGRVIWTSDEALN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 236 LPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRsiLLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEAG 312
Cdd:PRK06416 168 LDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALKKRGIKIK---TGAKAKKVEQT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 313 TPGrLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEktGKIPVTDEEQTNVPYIYAIGDILEdKVEL 392
Cdd:PRK06416 243 DDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIVG-GPML 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 393 TPVAIQAGRLLAQRLyAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFwplewtipsRDNNKCY 472
Cdd:PRK06416 317 AHKASAEGIIAAEAI-AGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVVKFPF---------AGNGKAL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387598068 473 A--------KIICNTKDNErVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 528
Cdd:PRK06416 385 AlgetdgfvKLIFDKKDGE-VLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
80-527 |
8.49e-60 |
|
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: 204.96 E-value: 8.49e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 80 EAAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVkhDWDRMIEAVQNHI 159
Cdd:TIGR02053 18 KAAELGASVAMVE---------RGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATVAV--DFGELLEGKREVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 160 GSL-NWGYRVALREKKVVYENAYGQFIGPHRIKAtnNKGKEkIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSL 236
Cdd:TIGR02053 87 EELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGRE-VRGAKRFLIATGARPAIPPIPGLKEagY-LTSEEALAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 237 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQfVPIKVEQIEAgtpG 315
Cdd:TIGR02053 163 DRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTS-AQVKAVSVRG---G 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 316 RLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPV 395
Cdd:TIGR02053 239 GKIITVEKPGGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDER-GGILVDETLRTSNPGIYAAGDVT-GGLQLEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 396 AIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIpsrDNNKCYAKI 475
Cdd:TIGR02053 315 AAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARIN---RDTRGFIKL 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 387598068 476 ICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAE 527
Cdd:TIGR02053 392 VAE-PGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
80-531 |
2.52e-59 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 203.49 E-value: 2.52e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 80 EAAQYGKKVMVLDfvtPTPLGtrwglgGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDRMIEAVQNHI 159
Cdd:PRK06292 21 RAAKLGKKVALIE---KGPLG------GTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADG-PKIDFKKVMARVRRER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 160 GSLNWGYRVALREK-KVVYENAYGQFIGPHRIKAtnnkgKEKIYSAERFLIATGER-PRYLGI-PGDKEYCISSDDLFSL 236
Cdd:PRK06292 91 DRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRvPPIPGVwLILGDRLLTSDDAFEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 237 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIrqfVPIKVEQIEAGtPG 315
Cdd:PRK06292 166 DKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-FKIK---LGAKVTSVEKS-GD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 316 RLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPV 395
Cdd:PRK06292 241 EKVEELEKGGKTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSVPGIYAAGDVN-GKPPLLHE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 396 AIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEWTIPSR--DNNKCYA 473
Cdd:PRK06292 317 AADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEV-----PFEAQGRARvmGKNDGFV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 387598068 474 KIICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTT 531
Cdd:PRK06292 392 KVYAD-KKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRT 448
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
105-532 |
1.54e-52 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 185.41 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 105 LGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDW----DRMIEAVQN-HIGSLNWgyrvaLREKK---VV 176
Cdd:PRK06370 39 LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFkavmARKRRIRARsRHGSEQW-----LRGLEgvdVF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 177 YENAygQFIGPHRIKATNnkgkeKIYSAERFLIATGERPRYLGIPG--DKEYcISSDDLFSLPYCPGKTLVVGASYVALE 254
Cdd:PRK06370 114 RGHA--RFESPNTVRVGG-----ETLRAKRIFINTGARAAIPPIPGldEVGY-LTNETIFSLDELPEHLVIIGGGYIGLE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 255 CAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQieagTPGRLRVVAQSTNSEEIIEGE 333
Cdd:PRK06370 186 FAQMFRRFGSEVTVIERGpRLLPREDEDVAAAVREILEREGIDVRLNAECIRVER----DGDGIAVGLDCNGGAPEITGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 334 YntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTV 413
Cdd:PRK06370 262 H--ILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRGAFTHTAYNDARIVAANLLDGGRR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 414 KCDYENVPTTVFTPLEYGACGLSEEKAVEKfGeENIEVYhsyfwplewTIPSRD--------NNKCYAKIICNtKDNERV 485
Cdd:PRK06370 338 KVSDRIVPYATYTDPPLARVGMTEAEARKS-G-RRVLVG---------TRPMTRvgravekgETQGFMKVVVD-ADTDRI 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 387598068 486 VGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 532
Cdd:PRK06370 406 LGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
79-400 |
9.18e-52 |
|
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: 179.05 E-value: 9.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 79 KEAAQYGKKVMVLDfvtptplgtrwgLGGTCVNVGCIPKKLMHQAAllgqalqdsrnygwKVEETVKHDWDRMiEAVQNH 158
Cdd:pfam07992 17 LTLAQLGGKVTLIE------------DEGTCPYGGCVLSKALLGAA--------------EAPEIASLWADLY-KRKEEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 159 IGSLNWGYRVALREKKVVYENAYGQFIGPHrikatNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYC------ISSDD 232
Cdd:pfam07992 70 VKKLNNGIEVLLGTEVVSIDPGAKKVVLEE-----LVDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtLDSAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 233 LFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEa 311
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGVEVR---LGTSVKEII- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 312 GTPGRLRVVaqsTNSEEIIEGEynTVMLAIGRDACTRkiGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDILEDKVE 391
Cdd:pfam07992 221 GDGDGVEVI---LKDGTEIDAD--LVVVAIGRRPNTE--LLEAAGLELDE-RGGIVVDEYLRTSVPGIYAAGDCRVGGPE 292
|
....*....
gi 387598068 392 LTPVAIQAG 400
Cdd:pfam07992 293 LAQNAVAQG 301
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
106-528 |
1.69e-43 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 160.50 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 106 GGTCVNVGCIPKKLMHQAALLGQALQDSRNYGwkVEETVKH-DWDRMIEAVQNHIGSLNWG---YRVALREKKVVYENAY 181
Cdd:PRK07846 34 GGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIAAGgeeYRGRDTPNIDVYRGHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 182 gQFIGPHRIKAtnnkGKEKIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSLPYCPGKTLVVGASYVALECAGFL 259
Cdd:PRK07846 112 -RFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSGvrY-HTSDTIMRLPELPESLVIVGGGFIAAEFAHVF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 260 AGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIRQFVPIKVEQIEAGtpgrlrvVAQSTNSEEIIEGEynTVM 338
Cdd:PRK07846 186 SALGVRVTVVNRSgRLLRHLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSG-------VTLRLDDGSTVEAD--VLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 339 LAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAG-STVKCDY 417
Cdd:PRK07846 256 VATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV-SSPYQLKHVANHEARVVQHNLLHPdDLIASDH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 418 ENVPTTVFTPLEYGACGLSEEKAVEKfgEENIEVYH------SYFWPLEWTipsrdnnKCYAKIICNtKDNERVVGFHVL 491
Cdd:PRK07846 334 RFVPAAVFTHPQIASVGLTENEARAA--GLDITVKVqnygdvAYGWAMEDT-------TGFVKLIAD-RDTGRLLGAHII 403
|
410 420 430
....*....|....*....|....*....|....*...
gi 387598068 492 GPNAGEVTQGFAAALKCGLTKKQL-DSTIGIHPVCAEV 528
Cdd:PRK07846 404 GPQASTLIQPLIQAMSFGLDAREMaRGQYWIHPALPEV 441
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
60-538 |
7.80e-41 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 153.93 E-value: 7.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 60 SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRwgLGGTCVNVGCIPKK-LMHQAALLGQALQDSRNYGW 138
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNPKGKPA--LGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 139 KVEEtVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIG----PHRIKATnNKGKEKIySAERFLIATGER 214
Cdd:PRK06327 80 HVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGktdaGYEIKVT-GEDETVI-TAKHVIIATGSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 215 PRYL-GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEE 292
Cdd:PRK06327 157 PRHLpGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 293 HGIKFIrqfVPIKVEQIEAGTPGrLRVVAQSTNSEEIIEgEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEE 372
Cdd:PRK06327 237 QGLDIH---LGVKIGEIKTGGKG-VSVAYTDADGEAQTL-EVDKLIVSIGRVPNTDGLGLEAVGLKLDER-GFIPVDDHC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 373 QTNVPYIYAIGDILEdKVELTPVAIQAGRLLAQRLyAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVekfgEENIEVY 452
Cdd:PRK06327 311 RTNVPNVYAIGDVVR-GPMLAHKAEEEGVAVAERI-AGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLK----AEGVEYK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 453 HSYFwplewtiPSRDNNKC--------YAKIICNTKdNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPV 524
Cdd:PRK06327 385 AGKF-------PFMANGRAlamgepdgFVKIIADAK-TDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPT 456
|
490
....*....|....*.
gi 387598068 525 CAEVF--TTLSVTKRS 538
Cdd:PRK06327 457 LSEVWheAALAVDKRP 472
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
106-528 |
8.82e-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: 147.60 E-value: 8.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 106 GGTCVNVGCIPKKLMHQAALLGQALQDSRNYGwkVEETVKH-DWDRMIEAVQNH----IGSLNWGYRVALREKKVVYENA 180
Cdd:TIGR03452 35 GGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRVFGDridpIAAGGEDYRRGDETPNIDVYDG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 181 YGQFIGPHRIKAtnnkGKEKIYSAERFLIATGERPR---YLGIPGDKEYciSSDDLFSLPYCPGKTLVVGASYVALECAG 257
Cdd:TIGR03452 113 HARFVGPRTLRT----GDGEEITGDQIVIAAGSRPYippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGYIAAEFAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 258 FLAGIGLDVTVMVRS-ILLRGFDQDMANKIGE----HMEEHGIKFIrqfvpIKVEQIEAGtpgrlrvVAQSTNSEEIIEG 332
Cdd:TIGR03452 187 VFSALGTRVTIVNRStKLLRHLDEDISDRFTEiakkKWDIRLGRNV-----TAVEQDGDG-------VTLTLDDGSTVTA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 333 EynTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDkVELTPVAIQAGRLLAQRL-YAGS 411
Cdd:TIGR03452 255 D--VLLVATGRVPNGDLLDAEAAGVEVDED-GRIKVDEYGRTSARGVWALGDVSSP-YQLKHVANAEARVVKHNLlHPND 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 412 TVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYH----SYFWPLEWTipsrdnnKCYAKIICNtKDNERVVG 487
Cdd:TIGR03452 331 LRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIQNygdvAYGWAMEDT-------TGFCKLIAD-RDTGKLLG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 387598068 488 FHVLGPNAGEVTQGFAAALKCGLTKKQL-DSTIGIHPVCAEV 528
Cdd:TIGR03452 403 AHIIGPQASSLIQPLITAMAFGLDAREMaRKQYWIHPALPEV 444
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
420-532 |
2.70e-36 |
|
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: 130.75 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 420 VPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFWPLEWTIPSRDNnKCYAKIICNtKDNERVVGFHVLGPNAGEVT 499
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDT-DGFVKLVAD-RETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 387598068 500 QGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 532
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
81-515 |
1.23e-35 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 140.29 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 81 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQaLQDSRNYGWKVEETVKH-DWDRMIEAVQNhi 159
Cdd:PRK13748 117 AVEQGARVTLIE---------RGTIGGTCVNVGCVPSKIMIRAAHIAH-LRRESPFDGGIAATVPTiDRSRLLAQQQA-- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 160 gslnwgyRV-ALREKKvvYEN------------AYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKE- 225
Cdd:PRK13748 185 -------RVdELRHAK--YEGildgnpaitvlhGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKEt 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 226 -YCISSDDLFSlPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLrgFDQDMAnkIGEHM----EEHGIKFIrq 300
Cdd:PRK13748 256 pYWTSTEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLF--FREDPA--IGEAVtaafRAEGIEVL-- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 301 fvpikvEQIEAGTpgrlrvVAQStNSEEIIEGEYNTV-----MLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTN 375
Cdd:PRK13748 329 ------EHTQASQ------VAHV-DGEFVLTTGHGELradklLVATGRAPNTRSLALDAAGVTVNAQ-GAIVIDQGMRTS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 376 VPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTvKCDYENVPTTVFTPLEYGACGLSEEKAvekfGEENIEVyHSY 455
Cdd:PRK13748 395 VPHIYAAGDC-TDQPQFVYVAAAAGTRAAINMTGGDA-ALDLTAMPAVVFTDPQVATVGYSEAEA----HHDGIET-DSR 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 387598068 456 FWPLEwTIPSRDNN---KCYAKIICNTKDNeRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQL 515
Cdd:PRK13748 468 TLTLD-NVPRALANfdtRGFIKLVIEEGSG-RLIGVQAVAPEAGELIQTAALAIRNRMTVQEL 528
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
58-497 |
6.53e-35 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 136.82 E-value: 6.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 58 PKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDfvtptplgTRWGLGGTCVNVGCIPKKLMHQAAL-LGQALQDS--R 134
Cdd:PRK05249 1 MHMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlyS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 135 NYGWKVEETVKHDWDRMIEAVQNHIGSLnwgyRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGER 214
Cdd:PRK05249 73 SYRVKLRITFADLLARADHVINKQVEVR----RGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 215 P-RYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEE 292
Cdd:PRK05249 149 PyRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 293 HGIKFI-RQfvpiKVEQIEAGTPGRLRVVAqstnSEEIIEGEynTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDE 371
Cdd:PRK05249 229 SGVTIRhNE----EVEKVEGGDDGVIVHLK----SGKKIKAD--CLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNEN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 372 EQTNVPYIYAIGDiledkV----ELTPVAIQAGRLLAQRLYaGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVekfgEE 447
Cdd:PRK05249 298 YQTAVPHIYAVGD-----VigfpSLASASMDQGRIAAQHAV-GEATAHLIEDIPTGIYTIPEISSVGKTEQELT----AA 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 387598068 448 NI--EVYHSYFWPLewtipSR-----DNNKCYaKIICNTKDnERVVGFHVLGPNAGE 497
Cdd:PRK05249 368 KVpyEVGRARFKEL-----ARaqiagDNVGML-KILFHRET-LEILGVHCFGERATE 417
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
106-527 |
5.47e-29 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 119.47 E-value: 5.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 106 GGTCVNVGCIPKKLMHQAAllgqalqdsrNYGWKVEETVKHDwdrmiEAVQNHIGSLNWGyrvALREKKVVYENAYGQFI 185
Cdd:PRK07251 40 GGTCINIGCIPTKTLLVAA----------EKNLSFEQVMATK-----NTVTSRLRGKNYA---MLAGSGVDLYDAEAHFV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 186 GPHRIKATnnKGKEKI-YSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGI 262
Cdd:PRK07251 102 SNKVIEVQ--AGDEKIeLTAETIVINTGAVSNVLPIPGlaDSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 263 GLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpIKVEQIEAGTPGrlrvVAQSTNSEEIIegeYNTVMLAI 341
Cdd:PRK07251 180 GSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLN---AHTTEVKNDGDQ----VLVVTEDETYR---FDALLYAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 342 GRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKC-DYENV 420
Cdd:PRK07251 250 GRKPNTEPLGLENTDIELTER-GAIKVDDYCQTSVPGVFAVGDV-NGGPQFTYISLDDFRIVFGYLTGDGSYTLeDRGNV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 421 PTTVFTPLEYGACGLSEEKAVEKFGEenievYHSYFWPLEWTIPSRDNN--KCYAKIICNTKDNErVVGFHVLGPNAGEV 498
Cdd:PRK07251 328 PTTMFITPPLSQVGLTEKEAKEAGLP-----YAVKELLVAAMPRAHVNNdlRGAFKVVVNTETKE-ILGATLFGEGSQEI 401
|
410 420
....*....|....*....|....*....
gi 387598068 499 TQGFAAALKCGLTKKQLDSTIGIHPVCAE 527
Cdd:PRK07251 402 INLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
106-532 |
3.54e-28 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 117.19 E-value: 3.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 106 GGTCVNVGCIP-KKLMHQAALlgqalqdsrnygwkveetvKHDWDRMIeAVQNHIGSLnwgyrvaLREK---------KV 175
Cdd:NF040477 40 GGTCINIGCIPtKTLVHDAEQ-------------------HQDFSTAM-QRKSSVVGF-------LRDKnyhnladldNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 176 VYENAYGQFIGPHRIKATNNKGKEKIYsAERFLIATGERPRYLGIPGDKEY--CISSDDLFSLPYCPGKTLVVGASYVAL 253
Cdd:NF040477 93 DVINGRAEFIDNHTLRVFQADGEQELR-GEKIFINTGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 254 ECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEAgTPGRLRVVAQstnseeiiEG 332
Cdd:NF040477 172 EFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVELI---LNAQVQRVSS-HEGEVQLETA--------EG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 333 EY--NTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLY-A 409
Cdd:NF040477 240 VLtvDALLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLgE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 410 GSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEwTIPSrdnnkcyAKIICNTK--------- 480
Cdd:NF040477 318 GKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTL-----PVA-AIPR-------ARVMNDTRgvlkavvdn 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 387598068 481 DNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 532
Cdd:NF040477 385 KTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDL 436
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
81-531 |
5.37e-26 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 112.31 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 81 AAQYGKKVMVLDfvtptplGTRWGLGGTCVNVGCIPKKLMHQAA----------------LLGQALQDSRNYGWK----V 140
Cdd:PTZ00153 135 AMERGLKVIIFT-------GDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVErnqlV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 141 EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPH-RIKATNNKGKEK---IYSAERFLIATGERPR 216
Cdd:PTZ00153 208 ADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYERgHIVDKNTIKSEKsgkEFKVKNIIIATGSTPN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 217 Y-LGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANkigeHMEEHG 294
Cdd:PTZ00153 288 IpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLLPLLDADVAK----YFERVF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 295 IKF--IRQFVPIKVEQIEAGTPGRLRVVAQS-----------TNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINE 361
Cdd:PTZ00153 364 LKSkpVRVHLNTLIEYVRAGKGNQPVIIGHSerqtgesdgpkKNMNDIKETYVDSCLVATGRKPNTNNLGLDKLKIQMKR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 362 ktGKIPVTD------EEQTNVPYIYAIGD-----ILEDKVELTPVAI------QAGRLLAQRLYAGSTVKCDYENVPTTV 424
Cdd:PTZ00153 444 --GFVSVDEhlrvlrEDQEVYDNIFCIGDangkqMLAHTASHQALKVvdwiegKGKENVNINVENWASKPIIYKNIPSVC 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 425 FTPLEYGACGLSEEKAVEKFGEENIEVYHSYF-------WPLEWTIPSRDNNKCYAKIICNT-------------KDNER 484
Cdd:PTZ00153 522 YTTPELAFIGLTEKEAKELYPPDNVGVEISFYkanskvlCENNISFPNNSKNNSYNKGKYNTvdntegmvkivylKDTKE 601
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 387598068 485 VVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTT 531
Cdd:PTZ00153 602 ILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
106-532 |
4.31e-23 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 102.01 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 106 GGTCVNVGCIPKKLMhqaallgqaLQDSRNYGwkveetvkhDWDRMIE---AVQNHIGSLNWGYRVALREKKVVYENAyg 182
Cdd:PRK08010 40 GGTCINIGCIPTKTL---------VHDAQQHT---------DFVRAIQrknEVVNFLRNKNFHNLADMPNIDVIDGQA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 183 QFIGPHRIKaTNNKGKEKIYSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLA 260
Cdd:PRK08010 100 EFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIPGitTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 261 GIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpikvEQIEAGTPGRLRVVAQSTNSEEIIEGeyntVML 339
Cdd:PRK08010 179 NFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILN------AHVERISHHENQVQVHSEHAQLAVDA----LLI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 340 AIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYA-GSTVKCDYE 418
Cdd:PRK08010 249 ASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNIWAMGDV-TGGLQFTYISLDDYRIVRDELLGeGKRSTDDRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 419 NVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEWTIPSR--DNNKCYAKIICNTKdNERVVGFHVLGPNAG 496
Cdd:PRK08010 327 NVPYSVFMTPPLSRVGMTEEQARESGADIQVVTL-----PVAAIPRARvmNDTRGVLKAIVDNK-TQRILGASLLCVDSH 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 387598068 497 EVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 532
Cdd:PRK08010 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
81-523 |
8.51e-23 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 101.48 E-value: 8.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 81 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDrmIEAVQNHIG 160
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEARVD--LPAVNARVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 161 SL----NWGYRVALREKKVVYENAYGQFI----GPHRIKATNNKGKEKIYSAERFLIATGERPRYLgiPG---DKEYCIS 229
Cdd:PRK07845 89 ALaaaqSADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGASPRIL--PTaepDGERILT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 230 SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQ 308
Cdd:PRK07845 167 WRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 309 IEAGtpgrlrVVAQSTNSEEiIEGEYntVMLAIGRDACTRKIGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDIlED 388
Cdd:PRK07845 247 TGDG------VVVTLTDGRT-VEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIYAAGDC-TG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 389 KVELTPVAIQAGRL-LAQRLyaGSTVK-CDYENVPTTVFTPLEYGACGLSeEKAVEKfGEENIEVYhsyfwplewTIPSR 466
Cdd:PRK07845 316 VLPLASVAAMQGRIaMYHAL--GEAVSpLRLKTVASNVFTRPEIATVGVS-QAAIDS-GEVPARTV---------MLPLA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 387598068 467 DNNKC--------YAKIICnTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 523
Cdd:PRK07845 383 TNPRAkmsglrdgFVKLFC-RPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYP 446
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
186-402 |
6.70e-21 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 93.26 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 186 GPHRIKATNnkgkEKIYSAERFLIATGERPRYLGIPGDKE-------YCISSDdlfsLPYCPGKT-LVVGASYVALECAG 257
Cdd:COG0492 87 GPFRVTTDD----GTEYEAKAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEAL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 258 FLAGIGLDVTVMVRSILLRGfDQDMANKIGEHmeeHGIKFIRQFVPIKVEqieaGTPGRLRVVAQSTNSEEIIEGEYNTV 337
Cdd:COG0492 159 YLTKFASKVTLIHRRDELRA-SKILVERLRAN---PKIEVLWNTEVTEIE----GDGRVEGVTLKNVKTGEEKELEVDGV 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 387598068 338 MLAIGRDACTRkiGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRL 402
Cdd:COG0492 231 FVAIGLKPNTE--LLKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAI 292
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
208-407 |
8.47e-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: 93.34 E-value: 8.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 208 LIATGERPRYLGIPGdkeycISSDDLFSL--------------PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS- 272
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddadalrealkEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 273 ILLRGFDQDMANKIGEHMEEHGIKFIRQFvpiKVEQIEAGTpgrlRVVAQSTNSEEIiegEYNTVMLAIG--------RD 344
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGE---TVVAIDGDD----KVAVTLTDGEEI---PADLVVVAPGvrpntelaKD 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 387598068 345 ActrkigletvGVKINEkTGKIPVTDEEQTNVPYIYAIGDILE---------DKVELTPVAIQAGRLLAQRL 407
Cdd:COG0446 228 A----------GLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtgktVYIPLASAANKQGRVAAENI 288
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
242-318 |
7.28e-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: 81.10 E-value: 7.28e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 387598068 242 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLR 318
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDrLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
208-407 |
1.96e-17 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 84.42 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 208 LIATGERPRYLGIPG-DKEYCI---SSDDLFSL-PYCPGKT--LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGF 278
Cdd:COG1251 103 VLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 279 DQDMANKIGEHMEEHGIKFIRQfvpIKVEQIEaGTPGRLRVVaqsTNSEEIIEGEynTVMLAIG---RDACTRKIGLETV 355
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVRLG---TGVTEIE-GDDRVTGVR---LADGEELPAD--LVVVAIGvrpNTELARAAGLAVD 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 387598068 356 -GVKINEKTgkipvtdeeQTNVPYIYAIGDILE--------DKVELTPVAIQAGRLLAQRL 407
Cdd:COG1251 254 rGIVVDDYL---------RTSDPDIYAAGDCAEhpgpvygrRVLELVAPAYEQARVAAANL 305
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
242-387 |
2.69e-13 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 72.12 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 242 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIkfirqfvPIKVEQIEAGTPGRLrVV 320
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREI-------PYRLNEEIDAINGNE-VT 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387598068 321 AQSTNSEEiiegeYNTVMLAIGRDACTRKIglETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILE 387
Cdd:PRK13512 222 FKSGKVEH-----YDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIIT 280
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
209-441 |
1.06e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 63.61 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 209 IATGERPRYLGIPGDKEYCI---SSDDLFSL------------PYCPGKTLVVGASYVALECAGFLA----------GIG 263
Cdd:COG1252 103 IATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAellrkllrypGID 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 264 LD------VTVMVRsiLLRGFDQDMANKIGEHMEEHGIKFIRQFvpiKVEQIEAGTpgrlrvvAQSTNSEEIiegEYNTV 337
Cdd:COG1252 183 PDkvritlVEAGPR--ILPGLGEKLSEAAEKELEKRGVEVHTGT---RVTEVDADG-------VTLEDGEEI---PADTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 338 MLAIGRDA--CTRKIGLETvgvkinEKTGKIPVTDEEQT-NVPYIYAIGDI--LEDKVELT-----PVAIQAGRLLAQRL 407
Cdd:COG1252 248 IWAAGVKAppLLADLGLPT------DRRGRVLVDPTLQVpGHPNVFAIGDCaaVPDPDGKPvpktaQAAVQQAKVLAKNI 321
|
250 260 270
....*....|....*....|....*....|....*
gi 387598068 408 YAgstvkcDYENVPTTVFTPLEYGA-CGLSEEKAV 441
Cdd:COG1252 322 AA------LLRGKPLKPFRYRDKGClASLGRGAAV 350
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
244-515 |
4.40e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 61.98 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 244 LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGFDQDMANKIGEHMEEHGIKFirqFVPIKVEQIEagtpGRLRVVA 321
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVEL---HLNEFVKSLI----GEDKVEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 322 QSTNseeiiEGEYNT--VMLAIGRDACTRKI---GLETVgvkineKTGKIPVTDEEQTNVPYIYAIGD------ILEDKV 390
Cdd:PRK09564 226 VVTD-----KGEYEAdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKN 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 391 ELTPVAIQA---GRLLAQRLyAGSTVKcdyenVPTT-------VFTpLEYGACGLSEEKAVEKfgeeNIEVY-------- 452
Cdd:PRK09564 295 VYVPLATTAnklGRMVGENL-AGRHVS-----FKGTlgsacikVLD-LEAARTGLTEEEAKKL----GIDYKtvfikdkn 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 387598068 453 HSYFWPlewtipsrDNNKCYAKIICNtKDNERVVGFHVLGPNaGEV--TQGFAAALKCGLTKKQL 515
Cdd:PRK09564 364 HTNYYP--------GQEDLYVKLIYE-ADTKVILGGQIIGKK-GAVlrIDALAVAIYAKLTTQEL 418
|
|
| GRX_GRXh_1_2_like |
cd03419 |
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ... |
1-48 |
2.89e-09 |
|
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.
Pssm-ID: 239511 [Multi-domain] Cd Length: 82 Bit Score: 53.70 E-value: 2.89e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 387598068 1 MEDGRALEGTLSELAAETDLPVVFVKQRKIGGHGPTLKAYQEGRLQKL 48
Cdd:cd03419 35 HEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLVKL 82
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
208-385 |
3.17e-08 |
|
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: 55.91 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 208 LIATG-ERPRYLGIPG-DKEYCIS----------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIG-LDVTVMVRsil 274
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 275 lRGFDqDMANKIGE--HMEEHGIKFIRQFVP-------------IKVEQIEAGTP---GRLRVVAqSTNSEEIIEGEynT 336
Cdd:COG0493 288 -RTRE-EMPASKEEveEALEEGVEFLFLVAPveiigdengrvtgLECVRMELGEPdesGRRRPVP-IEGSEFTLPAD--L 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 387598068 337 VMLAIGRDACTRKIgLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDI 385
Cdd:COG0493 363 VILAIGQTPDPSGL-EEELGLELDKR-GTI-VVDEEtyQTSLPGVFAGGDA 410
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
208-407 |
7.73e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 54.61 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 208 LIATGE-RPRYLGIPG-DKEYCISS-DDLFS-----LPYCP---------GKTLVVGASYVALECA--GFLAGiGLDVTV 268
Cdd:PRK12770 123 LIATGTwKSRKLGIPGeDLPGVYSAlEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAAleAVLLG-AEKVYL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 269 MVRsillRGFDQDMANKIG-EHMEEHGIKFIRQFVP--------------IKVEQIEAGTPGRLRVVAQsTNSEEIIegE 333
Cdd:PRK12770 202 AYR----RTINEAPAGKYEiERLIARGVEFLELVTPvriigegrvegvelAKMRLGEPDESGRPRPVPI-PGSEFVL--E 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 387598068 334 YNTVMLAIGRDAcTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDKVELTPvAIQAGRLLAQRL 407
Cdd:PRK12770 275 ADTVVFAIGEIP-TPPFAKECLGIELNRK-GEIVVDEKHMTSREGVFAAGDVVTGPSKIGK-AIKSGLRAAQSI 345
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
200-387 |
1.09e-07 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 54.83 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 200 KIYSAERFLIATGERPRYLGIPG-DKEYCI---SSDDLFSLPYCPGKTL---VVGASYVALECAGFLAGIGLDVTV--MV 270
Cdd:TIGR02374 93 RTLSYDKLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMDVSVihHA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 271 RSILLRGFDQDMANKIGEHMEEHGIKFIRQfvPIKVEQIEAGTPGRLRVvaqsTNSEEIiegEYNTVMLAIG---RDACT 347
Cdd:TIGR02374 173 PGLMAKQLDQTAGRLLQRELEQKGLTFLLE--KDTVEIVGATKADRIRF----KDGSSL---EADLIVMAAGirpNDELA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 387598068 348 RKIGLetvgvKINektGKIPVTDEEQTNVPYIYAIGDILE 387
Cdd:TIGR02374 244 VSAGI-----KVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
194-409 |
1.22e-07 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 54.56 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 194 NNKGKEKIysaerFLIATGERPRYLGIPGDKEYCISSDDLF---------------SLPYCPGKTLVV-GASYVALECAG 257
Cdd:PRK12775 514 NDKGFDAV-----FLGVGAGAPTFLGIPGEFAGQVYSANEFltrvnlmggdkfpflDTPISLGKSVVViGAGNTAMDCLR 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 258 FLAGIGldvTVMVRSILLRGfDQDMANKIGE--HMEEHGIKFIRQFVPI-------------KVEQIEAGTP---GRLRV 319
Cdd:PRK12775 589 VAKRLG---APTVRCVYRRS-EAEAPARIEEirHAKEEGIDFFFLHSPVeiyvdaegsvrgmKVEEMELGEPdekGRRKP 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 320 VAqstnSEEIIEGEYNTVMLAIGRDAcTRKIGLETVGVKINeKTGKIPVTDE-----EQTNVPYIYAIGDILEDKVELTp 394
Cdd:PRK12775 665 MP----TGEFKDLECDTVIYALGTKA-NPIITQSTPGLALN-KWGNIAADDGklestQSTNLPGVFAGGDIVTGGATVI- 737
|
250
....*....|....*
gi 387598068 395 VAIQAGRLLAQRLYA 409
Cdd:PRK12775 738 LAMGAGRRAARSIAT 752
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
198-385 |
1.37e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 53.87 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 198 KEKIYSAerFLIATGE-RPRYLGIPGdkeycISSDDLFSL-----------PYCPG---------KTLVVGASYVALECA 256
Cdd:PRK12831 225 EEEGFDA--VFIGSGAgLPKFMGIPG-----ENLNGVFSAnefltrvnlmkAYKPEydtpikvgkKVAVVGGGNVAMDAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 257 GFLAGIGLDVTVMVRsillRGfDQDMANKIGE--HMEEHGIKFIRQFVPI-------------KVEQIEAGTP---GRLR 318
Cdd:PRK12831 298 RTALRLGAEVHIVYR----RS-EEELPARVEEvhHAKEEGVIFDLLTNPVeilgdengwvkgmKCIKMELGEPdasGRRR 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 387598068 319 VVaQSTNSEEIIegEYNTVMLAIGRDAcTRKIGLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDI 385
Cdd:PRK12831 373 PV-EIEGSEFVL--EVDTVIMSLGTSP-NPLISSTTKGLKINKR-GCI-VADEEtgLTSKEGVFAGGDA 435
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
204-385 |
1.96e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 53.98 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 204 AERF---LIATGE-RPRYLGIPGDKEYCISS--------------DDLFSLPYCPGK-TLVVGASYVALECAGFLAGIGL 264
Cdd:PRK12778 515 EEGFkgiFIASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGKkVAVVGGGNTAMDSARTAKRLGA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 265 DvTVMvrsILLRGFDQDMANKIGE--HMEEHGIKF----------------IRQFVPIKVEQIEAGTPGRLRVVAqSTNS 326
Cdd:PRK12778 595 E-RVT---IVYRRSEEEMPARLEEvkHAKEEGIEFltlhnpieyladekgwVKQVVLQKMELGEPDASGRRRPVA-IPGS 669
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 327 EEIIEgeYNTVMLAIGRDActRKIGLETV-GVKINEKtGKIPVTDEEQTNVPYIYAIGDI 385
Cdd:PRK12778 670 TFTVD--VDLVIVSVGVSP--NPLVPSSIpGLELNRK-GTIVVDEEMQSSIPGIYAGGDI 724
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
208-405 |
2.52e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 53.26 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 208 LIATG-ERPRYLGIPGDK--------EYCISS---DDLFSLPycPGKTLVV-GASYVALECAGFLAGIG-LDVTVMVRsi 273
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDFLTRVnqaVADYDLP--VGKRVVViGGGNTAMDAARTAKRLGaESVTIVYR-- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 274 llRGFDqDMANKIGE--HMEEHGIKFIRQFVPIKVEQIEAGTPG------RLRVVAQSTNSEEIIEGEY-----NTVMLA 340
Cdd:PRK11749 306 --RGRE-EMPASEEEveHAKEEGVEFEWLAAPVEILGDEGRVTGvefvrmELGEPDASGRRRVPIEGSEftlpaDLVIKA 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 387598068 341 IGRDAcTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDIL--EDkveLTPVAIQAGRLLAQ 405
Cdd:PRK11749 383 IGQTP-NPLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVtgAA---TVVWAVGDGKDAAE 445
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
202-383 |
9.67e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 50.69 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 202 YSAERFLIATGE--RPRYLGIPgdkEYCISSDDLFSL-PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGF 278
Cdd:pfam13738 117 YQARYVIIATGEfdFPNKLGVP---ELPKHYSYVKDFhPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 279 DQDMA--------NKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlrVVAQSTNSEEIIegEYNTVMLAIGRDaCTRKI 350
Cdd:pfam13738 194 DSDPSyslspdtlNRLEELVKNGKIKAHFNAEVKEITEVDVS------YKVHTEDGRKVT--SNDDPILATGYH-PDLSF 264
|
170 180 190
....*....|....*....|....*....|....
gi 387598068 351 gLETVGVKINEKtGKIPVTDE-EQTNVPYIYAIG 383
Cdd:pfam13738 265 -LKKGLFELDED-GRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
202-387 |
1.45e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 47.36 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 202 YSAERFLIATGERPRYLGIPGDKEY-------CISSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL 274
Cdd:PRK10262 104 YTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 387598068 275 LRGfDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPG-RLRVVAQSTNSEEIiegEYNTVMLAIGRDACTR----K 349
Cdd:PRK10262 181 FRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGvRLRDTQNSDNIESL---DVAGLFVAIGHSPNTAifegQ 256
|
170 180 190
....*....|....*....|....*....|....*...
gi 387598068 350 IGLETVGVKINEKTGKipvtDEEQTNVPYIYAIGDILE 387
Cdd:PRK10262 257 LELENGYIKVQSGIHG----NATQTSIPGVFAAGDVMD 290
|
|
| |
