|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
25-513 |
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: 937.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 25 YDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKV 104
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 105 EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGI 184
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 185 PGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQ 264
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 265 FVPIKVEQIEAgtpgrlRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIY 344
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 345 AIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLE 424
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 425 WTIPSRDN-NKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSG 503
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
2ZZ0_A 504 ASILQAGCCG 513
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
24-513 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 526.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 24 SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQ-DSRNYGW 102
Cdd:PTZ00052 3 TFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 103 KVEETvkHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNkGKEKIYSAERFLIATGERPRYL 182
Cdd:PTZ00052 83 KTSSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDN-SQEETITAKYILIATGGRPSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 183 -GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKF 261
Cdd:PTZ00052 160 eDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 262 IRQFVPIKVEQIEAgtpgRLRVVAQSTNSEeiiegEYNTVMLAIGRDACTRKIGLETVGVKINeKTGKIPVTDeEQTNVP 341
Cdd:PTZ00052 240 LEGVVPINIEKMDD----KIKVLFSDGTTE-----LFDTVLYATGRKPDIKGLNLNAIGVHVN-KSNKIIAPN-DCTNIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 342 YIYAIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFW 421
Cdd:PTZ00052 309 NIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 422 PLEWTIPSRD--------------NNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 487
Cdd:PTZ00052 389 TLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHP 468
|
490 500
....*....|....*....|....*.
2ZZ0_A 488 VCAEVFTTLSVTKRSGASILQAGCCG 513
Cdd:PTZ00052 469 TDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
45-496 |
3.52e-139 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 408.78 E-value: 3.52e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 45 AAQYGKKVMVLDfvtptplGTRwgLGGTCVNVGCIPKKLMHQAALLGQALQD-SRNYGWKVEETvKHDWDRMIEAVQNHI 123
Cdd:PRK06116 23 AAMYGAKVALIE-------AKR--LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRDAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 124 GSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKgkekiYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYC 203
Cdd:PRK06116 93 DRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIPDIPG-AEYGITSDGFFALEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 204 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlR 282
Cdd:PRK06116 167 PKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG-----S 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 283 VVAQSTNSEEIiegEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQ 362
Cdd:PRK06116 242 LTLTLEDGETL---TVDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 363 AGRLLAQRLYAG-STVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNnKCYAKIIC 441
Cdd:PRK06116 317 AGRRLSERLFNNkPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMKLVV 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
2ZZ0_A 442 NTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 496
Cdd:PRK06116 396 VGKE-EKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
45-496 |
7.94e-116 |
|
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: 349.39 E-value: 7.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 45 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDRMIEAVQNHIG 124
Cdd:COG1249 22 AAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGA-PSVDWAALMARKDKVVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 125 SLNWGYRVALREKKVVYENAYGQFIGPHRIKATNnkgkEKIYSAERFLIATGERPRYLGIPG-DKEYCISSDDLFSLPYC 203
Cdd:COG1249 92 RLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTG----GETLTADHIVIATGSRPRVPPIPGlDEVRVLTSDEALELEEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 204 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrLR 282
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG----VT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 283 VVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPVAIQ 362
Cdd:COG1249 244 VTLEDGGGEEAVEADK--VLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAHVASA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 363 AGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFgeENIEVYHSYFWPLEWTIpSRDNNKCYAKIICN 442
Cdd:COG1249 320 EGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAG--IDVKVGKFPFAANGRAL-ALGETEGFVKLIAD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
2ZZ0_A 443 tKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 496
Cdd:COG1249 397 -AETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
25-496 |
2.63e-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: 342.56 E-value: 2.63e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 25 YDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFVtptplgtrwglGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGW 102
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 103 KVEEtVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKekiYSAERFLIATGERPRYL 182
Cdd:TIGR01424 70 TVGK-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 183 GIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKF 261
Cdd:TIGR01424 146 ALPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 262 IRQFVPIKVEQIEAGtpgrlRVVAQSTNSEEIIEgeyNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVP 341
Cdd:TIGR01424 225 LPEDSITSISKDDDG-----RLKATLSKHEEIVA---DVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 342 YIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFW 421
Cdd:TIGR01424 296 SIYAVGDV-TDRINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2ZZ0_A 422 PLEWTIPSRdNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 496
Cdd:TIGR01424 373 PMKATFSGR-QEKTLMKLVVDAKD-DKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
45-496 |
1.63e-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: 1.63e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 45 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIG 124
Cdd:TIGR01421 21 AAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDAYVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 125 SLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKgkekiYSAERFLIATGERPRYL-GIPGdKEYCISSDDLFSLPYC 203
Cdd:TIGR01421 92 RLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIPG-AELGTDSDGFFALEEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 204 PGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlR 282
Cdd:TIGR01421 166 PKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG-----K 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 283 VVAQSTNSEEIIegEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPVAIQ 362
Cdd:TIGR01421 241 LVIHFEDGKSID--DVDELIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 363 AGRLLAQRLYAGST-VKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRdNNKCYAKIIC 441
Cdd:TIGR01421 317 AGRKLSERLFNGKTdDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSE-KQKCRMKLVC 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
2ZZ0_A 442 NTKdNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 496
Cdd:TIGR01421 396 AGK-EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
14-505 |
1.46e-106 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 327.16 E-value: 1.46e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 14 KMNGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFvtpTPLGTRW--GLGGTCVNVGCIPKKLMHQAAL 89
Cdd:PLN02507 13 KVNADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGIceLPF---HPISSESigGVGGTCVIRGCVPKKILVYGAT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 90 LGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKV-VYENAyGQFIGPHRIKATNNKGKEKIYSA 168
Cdd:PLN02507 90 FGGEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVkLYEGE-GKIVGPNEVEVTQLDGTKLRYTA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 169 ERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMA 247
Cdd:PLN02507 169 KHILIATGSRAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 248 NKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrLRVVaqSTNSEEIIEgeyNTVMLAIGRDACTRKIGLETVGVKInEKT 327
Cdd:PLN02507 248 AVVARNLEGRGINLHPRTNLTQLTKTEGG----IKVI--TDHGEEFVA---DVVLFATGRAPNTKRLNLEAVGVEL-DKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 328 GKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEK 407
Cdd:PLN02507 318 GAVKVDEYSRTNIPSIWAIGDV-TNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 408 fGEENIEVYHSYFWPLEWTIPSRdNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 487
Cdd:PLN02507 397 -AKGDILVFTSSFNPMKNTISGR-QEKTVMKLIVDAET-DKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHP 473
|
490
....*....|....*....
2ZZ0_A 488 VCAEVFTTL-SVTKRSGAS 505
Cdd:PLN02507 474 SAAEEFVTMrSVTRRVTAK 492
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
16-501 |
9.23e-102 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 316.82 E-value: 9.23e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 16 NGPEDlPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFVTPTPlGTRWGLGGTCVNVGCIPKKLMHQAALLGQA 93
Cdd:PLN02546 70 NGAES-ERHYDFDLFTIGAGSGGVRASRFASNFGASAAVceLPFATISS-DTLGGVGGTCVLRGCVPKKLLVYASKYSHE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 94 LQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNnkgkeKIYSAERFLI 173
Cdd:PLN02546 148 FEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDG-----KLYTARNILI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 174 ATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGE 252
Cdd:PLN02546 223 AVGGRPFIPDIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 253 HMEEHGIKFIRQFVPIKVEQIEAGTpgrlrvVAQSTNsEEIIEGeYNTVMLAIGRDACTRKIGLETVGVKINeKTGKIPV 332
Cdd:PLN02546 302 QMSLRGIEFHTEESPQAIIKSADGS------LSLKTN-KGTVEG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 333 TDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEen 412
Cdd:PLN02546 373 DEYSRTSVPSIWAVGDV-TDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD-- 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 413 IEVYHSYFWPLEWTIpSRDNNKCYAKIICNTKDNeRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 492
Cdd:PLN02546 450 VDVFTANFRPLKATL-SGLPDRVFMKLIVCAKTN-KVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEE 527
|
....*....
2ZZ0_A 493 FTTLSVTKR 501
Cdd:PLN02546 528 FVTMRTPTR 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
69-497 |
4.05e-87 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 278.81 E-value: 4.05e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 69 LGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVkhDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQF 148
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 149 IGPHR--IKATNNKGKE----------------------KIYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYcP 204
Cdd:PTZ00058 160 LSENQvlIKKVSQVDGEadesdddevtivsagvsqlddgQVIEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 205 GKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEagTPGRLRV 283
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVK--EKNLTIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 284 VAQSTNSEeiiegEYNTVMLAIGRDACTRKIGLEtvGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDK---------- 353
Cdd:PTZ00058 316 LSDGRKYE-----HFDYVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 354 -----------------------VELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGE 410
Cdd:PTZ00058 389 lklyneepylkkkentsgesyynVQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGK 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 411 ENIEVYHSYFWPLEWTI----PSrDNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIH 486
Cdd:PTZ00058 469 ENVKIYESRFTNLFFSVydmdPA-QKEKTYLKLVCVGKE-ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIH 546
|
490
....*....|.
2ZZ0_A 487 PVCAEVFTTLS 497
Cdd:PTZ00058 547 PTAAEEFVTMA 557
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
45-491 |
3.92e-82 |
|
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: 3.92e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 45 AAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVE-ETVKHDWDRMIEAVQNHI 123
Cdd:TIGR01423 23 ATLYKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDrSSVKANWKALIAAKNKAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 124 GSLNWGYRVALREKK-VVYENAYGQFIGPHRIKA-----TNNKGKEKIySAERFLIATGERPRYLGIPGDkEYCISSDDL 197
Cdd:TIGR01423 103 LDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVresadPKSAVKERL-QAEHILLATGSWPQMLGIPGI-EHCISSNEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 198 FSLPYCPGKTLVVGASYVALECAGFLAG---IGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQi 273
Cdd:TIGR01423 181 FYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 274 eaGTPGRLRVVAQSTNseeiiEGEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDK 353
Cdd:TIGR01423 260 --NADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKK-GAIQVDEFSRTNVPNIYAIGDV-TDR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 354 VELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFgeENIEVYHSYFWPLEWTIPSRDNN 433
Cdd:TIGR01423 331 VMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYK 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
2ZZ0_A 434 KCYAKIICNTKDNErVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAE 491
Cdd:TIGR01423 409 KFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
44-492 |
6.15e-70 |
|
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: 6.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 44 EAAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKK-LMHQAALLGQALQdSRNYGWKVeETVKHDWDRMIEAVQNH 122
Cdd:TIGR01350 19 RAAQLGLKVALVE---------KEYLGGTCLNVGCIPTKaLLHSAEVYDEIKH-AKDLGIEV-ENVSVDWEKMQKRKNKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 123 IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKiYSAERFLIATGERPRYLGIP--GDKEYCISSDDLFSL 200
Cdd:TIGR01350 88 VKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLPGPfdFDGKVVITSTGALNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 201 PYCPGKTLVVGASYVALECAGFLAGIGLDVTV--MVRSIlLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTp 278
Cdd:TIGR01350 167 EEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQV- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 279 grlrVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEdKVELTP 358
Cdd:TIGR01350 245 ----TYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIG-GPMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 359 VAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAvekfGEENIEVYHSYFwplewtiPSRDNNK---- 434
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF-------PFAANGKalal 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
2ZZ0_A 435 ----CYAKIICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 492
Cdd:TIGR01350 386 getdGFVKIIAD-KKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
45-492 |
8.63e-62 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 209.23 E-value: 8.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 45 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDrmieAVQNH-- 122
Cdd:PRK06416 23 AAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAEN-VGIDFK----KVQEWkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 123 --IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGkEKIYSAERFLIATGERPRYL-GIPGDKEYCISSDDLFS 199
Cdd:PRK06416 89 gvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDG-EQTYTAKNIILATGSRPRELpGIEIDGRVIWTSDEALN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 200 LPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRsiLLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEAG 276
Cdd:PRK06416 168 LDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALKKRGIKIK---TGAKAKKVEQT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 277 TPGrLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEktGKIPVTDEEQTNVPYIYAIGDILEdKVEL 356
Cdd:PRK06416 243 DDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIVG-GPML 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 357 TPVAIQAGRLLAQRLyAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFwplewtipsRDNNKCY 436
Cdd:PRK06416 317 AHKASAEGIIAAEAI-AGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVVKFPF---------AGNGKAL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
2ZZ0_A 437 A--------KIICNTKDNErVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 492
Cdd:PRK06416 385 AlgetdgfvKLIFDKKDGE-VLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
44-491 |
2.16e-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: 205.73 E-value: 2.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 44 EAAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVkhDWDRMIEAVQNHI 123
Cdd:TIGR02053 18 KAAELGASVAMVE---------RGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATVAV--DFGELLEGKREVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 124 GSL-NWGYRVALREKKVVYENAYGQFIGPHRIKAtnNKGKEkIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSL 200
Cdd:TIGR02053 87 EELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGRE-VRGAKRFLIATGARPAIPPIPGLKEagY-LTSEEALAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 201 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQfVPIKVEQIEAgtpG 279
Cdd:TIGR02053 163 DRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTS-AQVKAVSVRG---G 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 280 RLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPV 359
Cdd:TIGR02053 239 GKIITVEKPGGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDER-GGILVDETLRTSNPGIYAAGDVT-GGLQLEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 360 AIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIpsrDNNKCYAKI 439
Cdd:TIGR02053 315 AAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARIN---RDTRGFIKL 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
2ZZ0_A 440 IC--NTKdneRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAE 491
Cdd:TIGR02053 392 VAepGTG---KVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
44-495 |
6.92e-60 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 204.26 E-value: 6.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 44 EAAQYGKKVMVLDfvtPTPLGtrwglgGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDRMIEAVQNHI 123
Cdd:PRK06292 21 RAAKLGKKVALIE---KGPLG------GTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADG-PKIDFKKVMARVRRER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 124 GSLNWGYRVALREK-KVVYENAYGQFIGPHRIKAtnnkgKEKIYSAERFLIATGER-PRYLGI-PGDKEYCISSDDLFSL 200
Cdd:PRK06292 91 DRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRvPPIPGVwLILGDRLLTSDDAFEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 201 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIrqfVPIKVEQIEAGtPG 279
Cdd:PRK06292 166 DKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-FKIK---LGAKVTSVEKS-GD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 280 RLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPV 359
Cdd:PRK06292 241 EKVEELEKGGKTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSVPGIYAAGDVN-GKPPLLHE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 360 AIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEWTIPSR--DNNKCYA 437
Cdd:PRK06292 317 AADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEV-----PFEAQGRARvmGKNDGFV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
2ZZ0_A 438 KIICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTT 495
Cdd:PRK06292 392 KVYAD-KKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRT 448
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
69-496 |
5.86e-53 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 185.79 E-value: 5.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 69 LGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDW----DRMIEAVQN-HIGSLNWgyrvaLREKK---VV 140
Cdd:PRK06370 39 LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFkavmARKRRIRARsRHGSEQW-----LRGLEgvdVF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 141 YENAygQFIGPHRIKATNnkgkeKIYSAERFLIATGERPRYLGIPG--DKEYcISSDDLFSLPYCPGKTLVVGASYVALE 218
Cdd:PRK06370 114 RGHA--RFESPNTVRVGG-----ETLRAKRIFINTGARAAIPPIPGldEVGY-LTNETIFSLDELPEHLVIIGGGYIGLE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 219 CAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQieagTPGRLRVVAQSTNSEEIIEGE 297
Cdd:PRK06370 186 FAQMFRRFGSEVTVIERGpRLLPREDEDVAAAVREILEREGIDVRLNAECIRVER----DGDGIAVGLDCNGGAPEITGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 298 YntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTV 377
Cdd:PRK06370 262 H--ILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRGAFTHTAYNDARIVAANLLDGGRR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 378 KCDYENVPTTVFTPLEYGACGLSEEKAVEKfGeENIEVYhsyfwplewTIPSRD--------NNKCYAKIICNtKDNERV 449
Cdd:PRK06370 338 KVSDRIVPYATYTDPPLARVGMTEAEARKS-G-RRVLVG---------TRPMTRvgravekgETQGFMKVVVD-ADTDRI 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
2ZZ0_A 450 VGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 496
Cdd:PRK06370 406 LGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
43-364 |
2.99e-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: 179.44 E-value: 2.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 43 KEAAQYGKKVMVLDfvtptplgtrwgLGGTCVNVGCIPKKLMHQAAllgqalqdsrnygwKVEETVKHDWDRMiEAVQNH 122
Cdd:pfam07992 17 LTLAQLGGKVTLIE------------DEGTCPYGGCVLSKALLGAA--------------EAPEIASLWADLY-KRKEEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 123 IGSLNWGYRVALREKKVVYENAYGQFIGPHrikatNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYC------ISSDD 196
Cdd:pfam07992 70 VKKLNNGIEVLLGTEVVSIDPGAKKVVLEE-----LVDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtLDSAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 197 LFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEa 275
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGVEVR---LGTSVKEII- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 276 GTPGRLRVVaqsTNSEEIIEGEynTVMLAIGRDACTRkiGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDILEDKVE 355
Cdd:pfam07992 221 GDGDGVEVI---LKDGTEIDAD--LVVVAIGRRPNTE--LLEAAGLELDE-RGGIVVDEYLRTSVPGIYAAGDCRVGGPE 292
|
....*....
2ZZ0_A 356 LTPVAIQAG 364
Cdd:pfam07992 293 LAQNAVAQG 301
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
70-492 |
9.25e-44 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 160.50 E-value: 9.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 70 GGTCVNVGCIPKKLMHQAALLGQALQDSRNYGwkVEETVKH-DWDRMIEAVQNHIGSLNWG---YRVALREKKVVYENAY 145
Cdd:PRK07846 34 GGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIAAGgeeYRGRDTPNIDVYRGHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 146 gQFIGPHRIKAtnnkGKEKIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSLPYCPGKTLVVGASYVALECAGFL 223
Cdd:PRK07846 112 -RFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSGvrY-HTSDTIMRLPELPESLVIVGGGFIAAEFAHVF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 224 AGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIRQFVPIKVEQIEAGtpgrlrvVAQSTNSEEIIEGEynTVM 302
Cdd:PRK07846 186 SALGVRVTVVNRSgRLLRHLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSG-------VTLRLDDGSTVEAD--VLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 303 LAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAG-STVKCDY 381
Cdd:PRK07846 256 VATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV-SSPYQLKHVANHEARVVQHNLLHPdDLIASDH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 382 ENVPTTVFTPLEYGACGLSEEKAVEKfgEENIEVYH------SYFWPLEWTipsrdnnKCYAKIICNtKDNERVVGFHVL 455
Cdd:PRK07846 334 RFVPAAVFTHPQIASVGLTENEARAA--GLDITVKVqnygdvAYGWAMEDT-------TGFVKLIAD-RDTGRLLGAHII 403
|
410 420 430
....*....|....*....|....*....|....*...
2ZZ0_A 456 GPNAGEVTQGFAAALKCGLTKKQL-DSTIGIHPVCAEV 492
Cdd:PRK07846 404 GPQASTLIQPLIQAMSFGLDAREMaRGQYWIHPALPEV 441
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
24-502 |
3.46e-41 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 153.93 E-value: 3.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 24 SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRwgLGGTCVNVGCIPKK-LMHQAALLGQALQDSRNYGW 102
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNPKGKPA--LGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 103 KVEEtVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIG----PHRIKATnNKGKEKIySAERFLIATGER 178
Cdd:PRK06327 80 HVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGktdaGYEIKVT-GEDETVI-TAKHVIIATGSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 179 PRYL-GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEE 256
Cdd:PRK06327 157 PRHLpGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 257 HGIKFIrqfVPIKVEQIEAGTPGrLRVVAQSTNSEEIIEgEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEE 336
Cdd:PRK06327 237 QGLDIH---LGVKIGEIKTGGKG-VSVAYTDADGEAQTL-EVDKLIVSIGRVPNTDGLGLEAVGLKLDER-GFIPVDDHC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 337 QTNVPYIYAIGDILEdKVELTPVAIQAGRLLAQRLyAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVekfgEENIEVY 416
Cdd:PRK06327 311 RTNVPNVYAIGDVVR-GPMLAHKAEEEGVAVAERI-AGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLK----AEGVEYK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 417 HSYFwplewtiPSRDNNKC--------YAKIICNTKdNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPV 488
Cdd:PRK06327 385 AGKF-------PFMANGRAlamgepdgFVKIIADAK-TDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPT 456
|
490
....*....|....*.
2ZZ0_A 489 CAEVF--TTLSVTKRS 502
Cdd:PRK06327 457 LSEVWheAALAVDKRP 472
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
70-492 |
4.79e-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: 4.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 70 GGTCVNVGCIPKKLMHQAALLGQALQDSRNYGwkVEETVKH-DWDRMIEAVQNH----IGSLNWGYRVALREKKVVYENA 144
Cdd:TIGR03452 35 GGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRVFGDridpIAAGGEDYRRGDETPNIDVYDG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 145 YGQFIGPHRIKAtnnkGKEKIYSAERFLIATGERPR---YLGIPGDKEYciSSDDLFSLPYCPGKTLVVGASYVALECAG 221
Cdd:TIGR03452 113 HARFVGPRTLRT----GDGEEITGDQIVIAAGSRPYippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGYIAAEFAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 222 FLAGIGLDVTVMVRS-ILLRGFDQDMANKIGE----HMEEHGIKFIrqfvpIKVEQIEAGtpgrlrvVAQSTNSEEIIEG 296
Cdd:TIGR03452 187 VFSALGTRVTIVNRStKLLRHLDEDISDRFTEiakkKWDIRLGRNV-----TAVEQDGDG-------VTLTLDDGSTVTA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 297 EynTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDkVELTPVAIQAGRLLAQRL-YAGS 375
Cdd:TIGR03452 255 D--VLLVATGRVPNGDLLDAEAAGVEVDED-GRIKVDEYGRTSARGVWALGDVSSP-YQLKHVANAEARVVKHNLlHPND 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 376 TVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYH----SYFWPLEWTipsrdnnKCYAKIICNtKDNERVVG 451
Cdd:TIGR03452 331 LRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIQNygdvAYGWAMEDT-------TGFCKLIAD-RDTGKLLG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
2ZZ0_A 452 FHVLGPNAGEVTQGFAAALKCGLTKKQL-DSTIGIHPVCAEV 492
Cdd:TIGR03452 403 AHIIGPQASSLIQPLITAMAFGLDAREMaRKQYWIHPALPEV 444
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
384-496 |
1.95e-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: 1.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 384 VPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFWPLEWTIPSRDNnKCYAKIICNtKDNERVVGFHVLGPNAGEVT 463
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDT-DGFVKLVAD-RETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
2ZZ0_A 464 QGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 496
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
45-479 |
7.58e-36 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 140.29 E-value: 7.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 45 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQaLQDSRNYGWKVEETVKH-DWDRMIEAVQNhi 123
Cdd:PRK13748 117 AVEQGARVTLIE---------RGTIGGTCVNVGCVPSKIMIRAAHIAH-LRRESPFDGGIAATVPTiDRSRLLAQQQA-- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 124 gslnwgyRV-ALREKKvvYEN------------AYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKE- 189
Cdd:PRK13748 185 -------RVdELRHAK--YEGildgnpaitvlhGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKEt 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 190 -YCISSDDLFSlPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLrgFDQDMAnkIGEHM----EEHGIKFIrq 264
Cdd:PRK13748 256 pYWTSTEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLF--FREDPA--IGEAVtaafRAEGIEVL-- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 265 fvpikvEQIEAGTpgrlrvVAQStNSEEIIEGEYNTV-----MLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTN 339
Cdd:PRK13748 329 ------EHTQASQ------VAHV-DGEFVLTTGHGELradklLVATGRAPNTRSLALDAAGVTVNAQ-GAIVIDQGMRTS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 340 VPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTvKCDYENVPTTVFTPLEYGACGLSEEKAvekfGEENIEVyHSY 419
Cdd:PRK13748 395 VPHIYAAGDC-TDQPQFVYVAAAAGTRAAINMTGGDA-ALDLTAMPAVVFTDPQVATVGYSEAEA----HHDGIET-DSR 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
2ZZ0_A 420 FWPLEwTIPSRDNN---KCYAKIICNTKDNeRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQL 479
Cdd:PRK13748 468 TLTLD-NVPRALANfdtRGFIKLVIEEGSG-RLIGVQAVAPEAGELIQTAALAIRNRMTVQEL 528
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
22-461 |
3.44e-35 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 137.21 E-value: 3.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 22 PKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDfvtptplgTRWGLGGTCVNVGCIPKKLMHQAAL-LGQALQDS--R 98
Cdd:PRK05249 1 MHMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlyS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 99 NYGWKVEETVKHDWDRMIEAVQNHIGSLnwgyRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGER 178
Cdd:PRK05249 73 SYRVKLRITFADLLARADHVINKQVEVR----RGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 179 P-RYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEE 256
Cdd:PRK05249 149 PyRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 257 HGIKFI-RQfvpiKVEQIEAGTPGRLRVVAqstnSEEIIEGEynTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDE 335
Cdd:PRK05249 229 SGVTIRhNE----EVEKVEGGDDGVIVHLK----SGKKIKAD--CLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNEN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 336 EQTNVPYIYAIGDiledkV----ELTPVAIQAGRLLAQRLYaGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVekfgEE 411
Cdd:PRK05249 298 YQTAVPHIYAVGD-----VigfpSLASASMDQGRIAAQHAV-GEATAHLIEDIPTGIYTIPEISSVGKTEQELT----AA 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
2ZZ0_A 412 NI--EVYHSYFWPLewtipSR-----DNNKCYaKIICNTKDnERVVGFHVLGPNAGE 461
Cdd:PRK05249 368 KVpyEVGRARFKEL-----ARaqiagDNVGML-KILFHRET-LEILGVHCFGERATE 417
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
70-491 |
3.31e-29 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 119.47 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 70 GGTCVNVGCIPKKLMHQAAllgqalqdsrNYGWKVEETVKHDwdrmiEAVQNHIGSLNWGyrvALREKKVVYENAYGQFI 149
Cdd:PRK07251 40 GGTCINIGCIPTKTLLVAA----------EKNLSFEQVMATK-----NTVTSRLRGKNYA---MLAGSGVDLYDAEAHFV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 150 GPHRIKATnnKGKEKI-YSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGI 226
Cdd:PRK07251 102 SNKVIEVQ--AGDEKIeLTAETIVINTGAVSNVLPIPGlaDSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 227 GLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpIKVEQIEAGTPGrlrvVAQSTNSEEIIegeYNTVMLAI 305
Cdd:PRK07251 180 GSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLN---AHTTEVKNDGDQ----VLVVTEDETYR---FDALLYAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 306 GRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKC-DYENV 384
Cdd:PRK07251 250 GRKPNTEPLGLENTDIELTER-GAIKVDDYCQTSVPGVFAVGDV-NGGPQFTYISLDDFRIVFGYLTGDGSYTLeDRGNV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 385 PTTVFTPLEYGACGLSEEKAVEKFGEenievYHSYFWPLEWTIPSRDNN--KCYAKIICNTKDNErVVGFHVLGPNAGEV 462
Cdd:PRK07251 328 PTTMFITPPLSQVGLTEKEAKEAGLP-----YAVKELLVAAMPRAHVNNdlRGAFKVVVNTETKE-ILGATLFGEGSQEI 401
|
410 420
....*....|....*....|....*....
2ZZ0_A 463 TQGFAAALKCGLTKKQLDSTIGIHPVCAE 491
Cdd:PRK07251 402 INLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
70-496 |
2.56e-28 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 117.19 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 70 GGTCVNVGCIP-KKLMHQAALlgqalqdsrnygwkveetvKHDWDRMIeAVQNHIGSLnwgyrvaLREK---------KV 139
Cdd:NF040477 40 GGTCINIGCIPtKTLVHDAEQ-------------------HQDFSTAM-QRKSSVVGF-------LRDKnyhnladldNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 140 VYENAYGQFIGPHRIKATNNKGKEKIYsAERFLIATGERPRYLGIPGDKEY--CISSDDLFSLPYCPGKTLVVGASYVAL 217
Cdd:NF040477 93 DVINGRAEFIDNHTLRVFQADGEQELR-GEKIFINTGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 218 ECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEAgTPGRLRVVAQstnseeiiEG 296
Cdd:NF040477 172 EFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVELI---LNAQVQRVSS-HEGEVQLETA--------EG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 297 EY--NTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLY-A 373
Cdd:NF040477 240 VLtvDALLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLgE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 374 GSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEwTIPSrdnnkcyAKIICNTK--------- 444
Cdd:NF040477 318 GKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTL-----PVA-AIPR-------ARVMNDTRgvlkavvdn 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
2ZZ0_A 445 DNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 496
Cdd:NF040477 385 KTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDL 436
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
45-495 |
4.64e-26 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 112.31 E-value: 4.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 45 AAQYGKKVMVLDfvtptplGTRWGLGGTCVNVGCIPKKLMHQAA----------------LLGQALQDSRNYGWK----V 104
Cdd:PTZ00153 135 AMERGLKVIIFT-------GDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVErnqlV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 105 EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPH-RIKATNNKGKEK---IYSAERFLIATGERPR 180
Cdd:PTZ00153 208 ADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYERgHIVDKNTIKSEKsgkEFKVKNIIIATGSTPN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 181 Y-LGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANkigeHMEEHG 258
Cdd:PTZ00153 288 IpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLLPLLDADVAK----YFERVF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 259 IKF--IRQFVPIKVEQIEAGTPGRLRVVAQS-----------TNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINE 325
Cdd:PTZ00153 364 LKSkpVRVHLNTLIEYVRAGKGNQPVIIGHSerqtgesdgpkKNMNDIKETYVDSCLVATGRKPNTNNLGLDKLKIQMKR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 326 ktGKIPVTD------EEQTNVPYIYAIGD-----ILEDKVELTPVAI------QAGRLLAQRLYAGSTVKCDYENVPTTV 388
Cdd:PTZ00153 444 --GFVSVDEhlrvlrEDQEVYDNIFCIGDangkqMLAHTASHQALKVvdwiegKGKENVNINVENWASKPIIYKNIPSVC 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 389 FTPLEYGACGLSEEKAVEKFGEENIEVYHSYF-------WPLEWTIPSRDNNKCYAKIICNT-------------KDNER 448
Cdd:PTZ00153 522 YTTPELAFIGLTEKEAKELYPPDNVGVEISFYkanskvlCENNISFPNNSKNNSYNKGKYNTvdntegmvkivylKDTKE 601
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
2ZZ0_A 449 VVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTT 495
Cdd:PTZ00153 602 ILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
70-496 |
3.46e-23 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 102.01 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 70 GGTCVNVGCIPKKLMhqaallgqaLQDSRNYGwkveetvkhDWDRMIE---AVQNHIGSLNWGYRVALREKKVVYENAyg 146
Cdd:PRK08010 40 GGTCINIGCIPTKTL---------VHDAQQHT---------DFVRAIQrknEVVNFLRNKNFHNLADMPNIDVIDGQA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 147 QFIGPHRIKaTNNKGKEKIYSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLA 224
Cdd:PRK08010 100 EFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIPGitTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 225 GIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpikvEQIEAGTPGRLRVVAQSTNSEEIIEGeyntVML 303
Cdd:PRK08010 179 NFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILN------AHVERISHHENQVQVHSEHAQLAVDA----LLI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 304 AIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYA-GSTVKCDYE 382
Cdd:PRK08010 249 ASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNIWAMGDV-TGGLQFTYISLDDYRIVRDELLGeGKRSTDDRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 383 NVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEWTIPSR--DNNKCYAKIICNTKdNERVVGFHVLGPNAG 460
Cdd:PRK08010 327 NVPYSVFMTPPLSRVGMTEEQARESGADIQVVTL-----PVAAIPRARvmNDTRGVLKAIVDNK-TQRILGASLLCVDSH 400
|
410 420 430
....*....|....*....|....*....|....*.
2ZZ0_A 461 EVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 496
Cdd:PRK08010 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
45-487 |
4.16e-23 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 101.86 E-value: 4.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 45 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDrmIEAVQNHIG 124
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEARVD--LPAVNARVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 125 SL----NWGYRVALREKKVVYENAYGQFI----GPHRIKATNNKGKEKIYSAERFLIATGERPRYLgiPG---DKEYCIS 193
Cdd:PRK07845 89 ALaaaqSADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGASPRIL--PTaepDGERILT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 194 SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQ 272
Cdd:PRK07845 167 WRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 273 IEAGtpgrlrVVAQSTNSEEiIEGEYntVMLAIGRDACTRKIGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDIlED 352
Cdd:PRK07845 247 TGDG------VVVTLTDGRT-VEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIYAAGDC-TG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 353 KVELTPVAIQAGRL-LAQRLyaGSTVK-CDYENVPTTVFTPLEYGACGLSeEKAVEKfGEENIEVYhsyfwplewTIPSR 430
Cdd:PRK07845 316 VLPLASVAAMQGRIaMYHAL--GEAVSpLRLKTVASNVFTRPEIATVGVS-QAAIDS-GEVPARTV---------MLPLA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
2ZZ0_A 431 DNNKC--------YAKIICnTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 487
Cdd:PRK07845 383 TNPRAkmsglrdgFVKLFC-RPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYP 446
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
150-366 |
4.60e-21 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 93.65 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 150 GPHRIKATNnkgkEKIYSAERFLIATGERPRYLGIPGDKE-------YCISSDdlfsLPYCPGKT-LVVGASYVALECAG 221
Cdd:COG0492 87 GPFRVTTDD----GTEYEAKAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEAL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 222 FLAGIGLDVTVMVRSILLRGfDQDMANKIGEHmeeHGIKFIRQFVPIKVEqieaGTPGRLRVVAQSTNSEEIIEGEYNTV 301
Cdd:COG0492 159 YLTKFASKVTLIHRRDELRA-SKILVERLRAN---PKIEVLWNTEVTEIE----GDGRVEGVTLKNVKTGEEKELEVDGV 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
2ZZ0_A 302 MLAIGRDACTRkiGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRL 366
Cdd:COG0492 231 FVAIGLKPNTE--LLKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAI 292
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
172-371 |
6.26e-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: 93.72 E-value: 6.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 172 LIATGERPRYLGIPGdkeycISSDDLFSL--------------PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS- 236
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddadalrealkEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 237 ILLRGFDQDMANKIGEHMEEHGIKFIRQFvpiKVEQIEAGTpgrlRVVAQSTNSEEIiegEYNTVMLAIG--------RD 308
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGE---TVVAIDGDD----KVAVTLTDGEEI---PADLVVVAPGvrpntelaKD 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2ZZ0_A 309 ActrkigletvGVKINEkTGKIPVTDEEQTNVPYIYAIGDILE---------DKVELTPVAIQAGRLLAQRL 371
Cdd:COG0446 228 A----------GLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtgktVYIPLASAANKQGRVAAENI 288
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
206-282 |
4.88e-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: 81.48 E-value: 4.88e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2ZZ0_A 206 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLR 282
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDrLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
172-371 |
9.35e-18 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 85.19 E-value: 9.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 172 LIATGERPRYLGIPG-DKEYCI---SSDDLFSL-PYCPGKT--LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGF 242
Cdd:COG1251 103 VLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 243 DQDMANKIGEHMEEHGIKFIRQfvpIKVEQIEaGTPGRLRVVaqsTNSEEIIEGEynTVMLAIG---RDACTRKIGLETV 319
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVRLG---TGVTEIE-GDDRVTGVR---LADGEELPAD--LVVVAIGvrpNTELARAAGLAVD 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
2ZZ0_A 320 -GVKINEKTgkipvtdeeQTNVPYIYAIGDILE--------DKVELTPVAIQAGRLLAQRL 371
Cdd:COG1251 254 rGIVVDDYL---------RTSDPDIYAAGDCAEhpgpvygrRVLELVAPAYEQARVAAANL 305
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
206-351 |
2.35e-13 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 72.12 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 206 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIkfirqfvPIKVEQIEAGTPGRLrVV 284
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREI-------PYRLNEEIDAINGNE-VT 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2ZZ0_A 285 AQSTNSEEiiegeYNTVMLAIGRDACTRKIglETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILE 351
Cdd:PRK13512 222 FKSGKVEH-----YDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIIT 280
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
173-405 |
7.42e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 64.00 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 173 IATGERPRYLGIPGDKEYCI---SSDDLFSL------------PYCPGKTLVVGASYVALECAGFLA----------GIG 227
Cdd:COG1252 103 IATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAellrkllrypGID 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 228 LD------VTVMVRsiLLRGFDQDMANKIGEHMEEHGIKFIRQFvpiKVEQIEAGTpgrlrvvAQSTNSEEIiegEYNTV 301
Cdd:COG1252 183 PDkvritlVEAGPR--ILPGLGEKLSEAAEKELEKRGVEVHTGT---RVTEVDADG-------VTLEDGEEI---PADTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 302 MLAIGRDA--CTRKIGLETvgvkinEKTGKIPVTDEEQT-NVPYIYAIGDI--LEDKVELT-----PVAIQAGRLLAQRL 371
Cdd:COG1252 248 IWAAGVKAppLLADLGLPT------DRRGRVLVDPTLQVpGHPNVFAIGDCaaVPDPDGKPvpktaQAAVQQAKVLAKNI 321
|
250 260 270
....*....|....*....|....*....|....*
2ZZ0_A 372 YAgstvkcDYENVPTTVFTPLEYGA-CGLSEEKAV 405
Cdd:COG1252 322 AA------LLRGKPLKPFRYRDKGClASLGRGAAV 350
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
208-479 |
4.49e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 61.59 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 208 LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGFDQDMANKIGEHMEEHGIKFirqFVPIKVEQIEagtpGRLRVVA 285
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVEL---HLNEFVKSLI----GEDKVEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 286 QSTNseeiiEGEYNT--VMLAIGRDACTRKI---GLETVgvkineKTGKIPVTDEEQTNVPYIYAIGD------ILEDKV 354
Cdd:PRK09564 226 VVTD-----KGEYEAdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKN 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 355 ELTPVAIQA---GRLLAQRLyAGSTVKcdyenVPTT-------VFTpLEYGACGLSEEKAVEKfgeeNIEVY-------- 416
Cdd:PRK09564 295 VYVPLATTAnklGRMVGENL-AGRHVS-----FKGTlgsacikVLD-LEAARTGLTEEEAKKL----GIDYKtvfikdkn 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
2ZZ0_A 417 HSYFWPlewtipsrDNNKCYAKIICNtKDNERVVGFHVLGPNaGEV--TQGFAAALKCGLTKKQL 479
Cdd:PRK09564 364 HTNYYP--------GQEDLYVKLIYE-ADTKVILGGQIIGKK-GAVlrIDALAVAIYAKLTTQEL 418
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
172-349 |
2.79e-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: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 172 LIATG-ERPRYLGIPG-DKEYCIS----------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIG-LDVTVMVRsil 238
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 239 lRGFDqDMANKIGE--HMEEHGIKFIRQFVP-------------IKVEQIEAGTP---GRLRVVAqSTNSEEIIEGEynT 300
Cdd:COG0493 288 -RTRE-EMPASKEEveEALEEGVEFLFLVAPveiigdengrvtgLECVRMELGEPdesGRRRPVP-IEGSEFTLPAD--L 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
2ZZ0_A 301 VMLAIGRDACTRKIgLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDI 349
Cdd:COG0493 363 VILAIGQTPDPSGL-EEELGLELDKR-GTI-VVDEEtyQTSLPGVFAGGDA 410
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
172-371 |
5.24e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 55.00 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 172 LIATGE-RPRYLGIPG-DKEYCISS-DDLFS-----LPYCP---------GKTLVVGASYVALECA--GFLAGiGLDVTV 232
Cdd:PRK12770 123 LIATGTwKSRKLGIPGeDLPGVYSAlEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAAleAVLLG-AEKVYL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 233 MVRsillRGFDQDMANKIG-EHMEEHGIKFIRQFVP--------------IKVEQIEAGTPGRLRVVAQsTNSEEIIegE 297
Cdd:PRK12770 202 AYR----RTINEAPAGKYEiERLIARGVEFLELVTPvriigegrvegvelAKMRLGEPDESGRPRPVPI-PGSEFVL--E 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2ZZ0_A 298 YNTVMLAIGRDAcTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDKVELTPvAIQAGRLLAQRL 371
Cdd:PRK12770 275 ADTVVFAIGEIP-TPPFAKECLGIELNRK-GEIVVDEKHMTSREGVFAAGDVVTGPSKIGK-AIKSGLRAAQSI 345
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
164-351 |
8.13e-08 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 55.22 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 164 KIYSAERFLIATGERPRYLGIPG-DKEYCI---SSDDLFSLPYCPGKTL---VVGASYVALECAGFLAGIGLDVTV--MV 234
Cdd:TIGR02374 93 RTLSYDKLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMDVSVihHA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 235 RSILLRGFDQDMANKIGEHMEEHGIKFIRQfvPIKVEQIEAGTPGRLRVvaqsTNSEEIiegEYNTVMLAIG---RDACT 311
Cdd:TIGR02374 173 PGLMAKQLDQTAGRLLQRELEQKGLTFLLE--KDTVEIVGATKADRIRF----KDGSSL---EADLIVMAAGirpNDELA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
2ZZ0_A 312 RKIGLetvgvKINektGKIPVTDEEQTNVPYIYAIGDILE 351
Cdd:TIGR02374 244 VSAGI-----KVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
158-373 |
8.32e-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: 54.95 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 158 NNKGKEKIysaerFLIATGERPRYLGIPGDKEYCISSDDLF---------------SLPYCPGKTLVV-GASYVALECAG 221
Cdd:PRK12775 514 NDKGFDAV-----FLGVGAGAPTFLGIPGEFAGQVYSANEFltrvnlmggdkfpflDTPISLGKSVVViGAGNTAMDCLR 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 222 FLAGIGldvTVMVRSILLRGfDQDMANKIGE--HMEEHGIKFIRQFVPI-------------KVEQIEAGTP---GRLRV 283
Cdd:PRK12775 589 VAKRLG---APTVRCVYRRS-EAEAPARIEEirHAKEEGIDFFFLHSPVeiyvdaegsvrgmKVEEMELGEPdekGRRKP 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 284 VAqstnSEEIIEGEYNTVMLAIGRDAcTRKIGLETVGVKINeKTGKIPVTDE-----EQTNVPYIYAIGDILEDKVELTp 358
Cdd:PRK12775 665 MP----TGEFKDLECDTVIYALGTKA-NPIITQSTPGLALN-KWGNIAADDGklestQSTNLPGVFAGGDIVTGGATVI- 737
|
250
....*....|....*
2ZZ0_A 359 VAIQAGRLLAQRLYA 373
Cdd:PRK12775 738 LAMGAGRRAARSIAT 752
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
162-349 |
1.16e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 54.25 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 162 KEKIYSAerFLIATGE-RPRYLGIPGdkeycISSDDLFSL-----------PYCPG---------KTLVVGASYVALECA 220
Cdd:PRK12831 225 EEEGFDA--VFIGSGAgLPKFMGIPG-----ENLNGVFSAnefltrvnlmkAYKPEydtpikvgkKVAVVGGGNVAMDAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 221 GFLAGIGLDVTVMVRsillRGfDQDMANKIGE--HMEEHGIKFIRQFVPI-------------KVEQIEAGTP---GRLR 282
Cdd:PRK12831 298 RTALRLGAEVHIVYR----RS-EEELPARVEEvhHAKEEGVIFDLLTNPVeilgdengwvkgmKCIKMELGEPdasGRRR 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2ZZ0_A 283 VVaQSTNSEEIIegEYNTVMLAIGRDAcTRKIGLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDI 349
Cdd:PRK12831 373 PV-EIEGSEFVL--EVDTVIMSLGTSP-NPLISSTTKGLKINKR-GCI-VADEEtgLTSKEGVFAGGDA 435
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
168-349 |
1.71e-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: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 168 AERF---LIATGE-RPRYLGIPGDKEYCISS--------------DDLFSLPYCPGK-TLVVGASYVALECAGFLAGIGL 228
Cdd:PRK12778 515 EEGFkgiFIASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGKkVAVVGGGNTAMDSARTAKRLGA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 229 DvTVMvrsILLRGFDQDMANKIGE--HMEEHGIKF----------------IRQFVPIKVEQIEAGTPGRLRVVAqSTNS 290
Cdd:PRK12778 595 E-RVT---IVYRRSEEEMPARLEEvkHAKEEGIEFltlhnpieyladekgwVKQVVLQKMELGEPDASGRRRPVA-IPGS 669
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 291 EEIIEgeYNTVMLAIGRDActRKIGLETV-GVKINEKtGKIPVTDEEQTNVPYIYAIGDI 349
Cdd:PRK12778 670 TFTVD--VDLVIVSVGVSP--NPLVPSSIpGLELNRK-GTIVVDEEMQSSIPGIYAGGDI 724
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
172-369 |
2.11e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 53.26 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 172 LIATG-ERPRYLGIPGDK--------EYCISS---DDLFSLPycPGKTLVV-GASYVALECAGFLAGIGL-DVTVMVRsi 237
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDFLTRVnqaVADYDLP--VGKRVVViGGGNTAMDAARTAKRLGAeSVTIVYR-- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 238 llRGFDqDMANKIGE--HMEEHGIKFIRQFVPIKVEQIEAGTPG------RLRVVAQSTNSEEIIEGEY-----NTVMLA 304
Cdd:PRK11749 306 --RGRE-EMPASEEEveHAKEEGVEFEWLAAPVEILGDEGRVTGvefvrmELGEPDASGRRRVPIEGSEftlpaDLVIKA 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
2ZZ0_A 305 IGRDAcTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDIL--EDkveLTPVAIQAGRLLAQ 369
Cdd:PRK11749 383 IGQTP-NPLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVtgAA---TVVWAVGDGKDAAE 445
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
166-347 |
9.51e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 50.69 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 166 YSAERFLIATGE--RPRYLGIPgdkEYCISSDDLFSL-PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGF 242
Cdd:pfam13738 117 YQARYVIIATGEfdFPNKLGVP---ELPKHYSYVKDFhPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 243 DQDMA--------NKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlrVVAQSTNSEEIIegEYNTVMLAIGRDaCTRKI 314
Cdd:pfam13738 194 DSDPSyslspdtlNRLEELVKNGKIKAHFNAEVKEITEVDVS------YKVHTEDGRKVT--SNDDPILATGYH-PDLSF 264
|
170 180 190
....*....|....*....|....*....|....
2ZZ0_A 315 gLETVGVKINEKtGKIPVTDE-EQTNVPYIYAIG 347
Cdd:pfam13738 265 -LKKGLFELDED-GRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
166-351 |
1.15e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 47.36 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 166 YSAERFLIATGERPRYLGIPGDKEY-------CISSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL 238
Cdd:PRK10262 104 YTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2ZZ0_A 239 LRGfDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPG-RLRVVAQSTNSEEIiegEYNTVMLAIGRDACTR----K 313
Cdd:PRK10262 181 FRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGvRLRDTQNSDNIESL---DVAGLFVAIGHSPNTAifegQ 256
|
170 180 190
....*....|....*....|....*....|....*...
2ZZ0_A 314 IGLETVGVKINEKTGKipvtDEEQTNVPYIYAIGDILE 351
Cdd:PRK10262 257 LELENGYIKVQSGIHG----NATQTSIPGVFAAGDVMD 290
|
|
| |
