|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
31-519 |
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: 933.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 31 YDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKV 110
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 111 EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGI 190
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 191 PGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQ 270
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 271 FVPIKVEQIEAgtpgrlRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIY 350
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 351 AIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLE 430
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 431 WTIPSRDN-NKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSG 509
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 345100815 510 ASILQAGSCG 519
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
30-519 |
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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 30 SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQ-DSRNYGW 108
Cdd:PTZ00052 3 TFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 109 KVEETvkHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNkGKEKIYSAERFLIATGERPRYL 188
Cdd:PTZ00052 83 KTSSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDN-SQEETITAKYILIATGGRPSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 189 -GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKF 267
Cdd:PTZ00052 160 eDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 268 IRQFVPIKVEQIEAgtpgRLRVVAQSTNSEeiiegEYNTVMLAIGRDACTRKIGLETVGVKINeKTGKIPVTDeEQTNVP 347
Cdd:PTZ00052 240 LEGVVPINIEKMDD----KIKVLFSDGTTE-----LFDTVLYATGRKPDIKGLNLNAIGVHVN-KSNKIIAPN-DCTNIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 348 YIYAIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFW 427
Cdd:PTZ00052 309 NIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 428 PLEWTIPSRD--------------NNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 493
Cdd:PTZ00052 389 TLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHP 468
|
490 500
....*....|....*....|....*.
gi 345100815 494 VCAEVFTTLSVTKRSGASILQAGSCG 519
Cdd:PTZ00052 469 TDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
51-502 |
6.24e-139 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 408.39 E-value: 6.24e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 51 AAQYGKKVMVLDfvtptplGTRwgLGGTCVNVGCIPKKLMHQAALLGQALQD-SRNYGWKVEETvKHDWDRMIEAVQNHI 129
Cdd:PRK06116 23 AAMYGAKVALIE-------AKR--LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRDAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 130 GSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKgkekiYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYC 209
Cdd:PRK06116 93 DRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIPDIPG-AEYGITSDGFFALEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 210 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlR 288
Cdd:PRK06116 167 PKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG-----S 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 289 VVAQSTNSEEIiegEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQ 368
Cdd:PRK06116 242 LTLTLEDGETL---TVDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 369 AGRLLAQRLYAG-STVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNnKCYAKIIC 447
Cdd:PRK06116 317 AGRRLSERLFNNkPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMKLVV 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 345100815 448 NTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 502
Cdd:PRK06116 396 VGKE-EKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
51-502 |
1.88e-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: 1.88e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 51 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDRMIEAVQNHIG 130
Cdd:COG1249 22 AAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGA-PSVDWAALMARKDKVVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 131 SLNWGYRVALREKKVVYENAYGQFIGPHRIKATNnkgkEKIYSAERFLIATGERPRYLGIPG-DKEYCISSDDLFSLPYC 209
Cdd:COG1249 92 RLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTG----GETLTADHIVIATGSRPRVPPIPGlDEVRVLTSDEALELEEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 210 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrLR 288
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG----VT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 289 VVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPVAIQ 368
Cdd:COG1249 244 VTLEDGGGEEAVEADK--VLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAHVASA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 369 AGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFgeENIEVYHSYFWPLEWTIpSRDNNKCYAKIICN 448
Cdd:COG1249 320 EGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAG--IDVKVGKFPFAANGRAL-ALGETEGFVKLIAD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 345100815 449 tKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 502
Cdd:COG1249 397 -AETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
31-502 |
5.47e-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: 342.18 E-value: 5.47e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 31 YDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFVtptplgtrwglGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGW 108
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 109 KVEEtVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKekiYSAERFLIATGERPRYL 188
Cdd:TIGR01424 70 TVGK-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 189 GIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKF 267
Cdd:TIGR01424 146 ALPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 268 IRQFVPIKVEQIEAGtpgrlRVVAQSTNSEEIIEgeyNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVP 347
Cdd:TIGR01424 225 LPEDSITSISKDDDG-----RLKATLSKHEEIVA---DVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 348 YIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFW 427
Cdd:TIGR01424 296 SIYAVGDV-TDRINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345100815 428 PLEWTIPSRdNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 502
Cdd:TIGR01424 373 PMKATFSGR-QEKTLMKLVVDAKD-DKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
51-502 |
3.30e-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: 327.18 E-value: 3.30e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 51 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIG 130
Cdd:TIGR01421 21 AAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDAYVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 131 SLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKgkekiYSAERFLIATGERPRYL-GIPGdKEYCISSDDLFSLPYC 209
Cdd:TIGR01421 92 RLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIPG-AELGTDSDGFFALEEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 210 PGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlR 288
Cdd:TIGR01421 166 PKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG-----K 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 289 VVAQSTNSEEIIegEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPVAIQ 368
Cdd:TIGR01421 241 LVIHFEDGKSID--DVDELIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 369 AGRLLAQRLYAGST-VKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRdNNKCYAKIIC 447
Cdd:TIGR01421 317 AGRKLSERLFNGKTdDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSE-KQKCRMKLVC 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 345100815 448 NTKdNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 502
Cdd:TIGR01421 396 AGK-EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
22-511 |
3.37e-106 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 326.39 E-value: 3.37e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 22 NGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFvtpTPLGTRW--GLGGTCVNVGCIPKKLMHQAALLG 97
Cdd:PLN02507 15 NADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGIceLPF---HPISSESigGVGGTCVIRGCVPKKILVYGATFG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 98 QALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKV-VYENAyGQFIGPHRIKATNNKGKEKIYSAER 176
Cdd:PLN02507 92 GEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVkLYEGE-GKIVGPNEVEVTQLDGTKLRYTAKH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 177 FLIATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMANK 255
Cdd:PLN02507 171 ILIATGSRAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMRAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 256 IGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrLRVVaqSTNSEEIIEgeyNTVMLAIGRDACTRKIGLETVGVKInEKTGK 335
Cdd:PLN02507 250 VARNLEGRGINLHPRTNLTQLTKTEGG----IKVI--TDHGEEFVA---DVVLFATGRAPNTKRLNLEAVGVEL-DKAGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 336 IPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKfG 415
Cdd:PLN02507 320 VKVDEYSRTNIPSIWAIGDV-TNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQ-A 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 416 EENIEVYHSYFWPLEWTIPSRdNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVC 495
Cdd:PLN02507 398 KGDILVFTSSFNPMKNTISGR-QEKTVMKLIVDAET-DKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSA 475
|
490
....*....|....*..
gi 345100815 496 AEVFTTL-SVTKRSGAS 511
Cdd:PLN02507 476 AEEFVTMrSVTRRVTAK 492
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
14-507 |
5.65e-102 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 317.59 E-value: 5.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 14 LVPRGSHMNGPEDlPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFVTPTPlGTRWGLGGTCVNVGCIPKKLMH 91
Cdd:PLN02546 62 SVSRAAAPNGAES-ERHYDFDLFTIGAGSGGVRASRFASNFGASAAVceLPFATISS-DTLGGVGGTCVLRGCVPKKLLV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 92 QAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNnkgkeKI 171
Cdd:PLN02546 140 YASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDG-----KL 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 172 YSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQ 250
Cdd:PLN02546 215 YTARNILIAVGGRPFIPDIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 251 DMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTpgrlrvVAQSTNsEEIIEGeYNTVMLAIGRDACTRKIGLETVGVKIN 330
Cdd:PLN02546 294 EVRDFVAEQMSLRGIEFHTEESPQAIIKSADGS------LSLKTN-KGTVEG-FSHVMFATGRKPNTKNLGLEEVGVKMD 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 331 eKTGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKA 410
Cdd:PLN02546 366 -KNGAIEVDEYSRTSVPSIWAVGDV-TDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 411 VEKFGEenIEVYHSYFWPLEWTIpSRDNNKCYAKIICNTKDNeRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIG 490
Cdd:PLN02546 444 IEEYGD--VDVFTANFRPLKATL-SGLPDRVFMKLIVCAKTN-KVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVG 519
|
490
....*....|....*..
gi 345100815 491 IHPVCAEVFTTLSVTKR 507
Cdd:PLN02546 520 IHPTAAEEFVTMRTPTR 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
75-503 |
4.23e-87 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 278.81 E-value: 4.23e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 75 LGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVkhDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQF 154
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 155 IGPHR--IKATNNKGKE----------------------KIYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYcP 210
Cdd:PTZ00058 160 LSENQvlIKKVSQVDGEadesdddevtivsagvsqlddgQVIEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 211 GKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEagTPGRLRV 289
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVK--EKNLTIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 290 VAQSTNSEeiiegEYNTVMLAIGRDACTRKIGLEtvGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDK---------- 359
Cdd:PTZ00058 316 LSDGRKYE-----HFDYVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 360 -----------------------VELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGE 416
Cdd:PTZ00058 389 lklyneepylkkkentsgesyynVQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGK 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 417 ENIEVYHSYFWPLEWTI----PSrDNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIH 492
Cdd:PTZ00058 469 ENVKIYESRFTNLFFSVydmdPA-QKEKTYLKLVCVGKE-ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIH 546
|
490
....*....|.
gi 345100815 493 PVCAEVFTTLS 503
Cdd:PTZ00058 547 PTAAEEFVTMA 557
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
51-497 |
4.63e-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: 4.63e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 51 AAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVE-ETVKHDWDRMIEAVQNHI 129
Cdd:TIGR01423 23 ATLYKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDrSSVKANWKALIAAKNKAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 130 GSLNWGYRVALREKK-VVYENAYGQFIGPHRIKA-----TNNKGKEKIySAERFLIATGERPRYLGIPGDkEYCISSDDL 203
Cdd:TIGR01423 103 LDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVresadPKSAVKERL-QAEHILLATGSWPQMLGIPGI-EHCISSNEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 204 FSLPYCPGKTLVVGASYVALECAGFLAG---IGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQi 279
Cdd:TIGR01423 181 FYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 280 eaGTPGRLRVVAQSTNseeiiEGEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDK 359
Cdd:TIGR01423 260 --NADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKK-GAIQVDEFSRTNVPNIYAIGDV-TDR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 360 VELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFgeENIEVYHSYFWPLEWTIPSRDNN 439
Cdd:TIGR01423 331 VMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYK 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 345100815 440 KCYAKIICNTKDNErVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAE 497
Cdd:TIGR01423 409 KFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
50-498 |
8.48e-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: 8.48e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 50 EAAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKK-LMHQAALLGQALQdSRNYGWKVeETVKHDWDRMIEAVQNH 128
Cdd:TIGR01350 19 RAAQLGLKVALVE---------KEYLGGTCLNVGCIPTKaLLHSAEVYDEIKH-AKDLGIEV-ENVSVDWEKMQKRKNKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 129 IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKiYSAERFLIATGERPRYLGIP--GDKEYCISSDDLFSL 206
Cdd:TIGR01350 88 VKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLPGPfdFDGKVVITSTGALNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 207 PYCPGKTLVVGASYVALECAGFLAGIGLDVTV--MVRSIlLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTp 284
Cdd:TIGR01350 167 EEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQV- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 285 grlrVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEdKVELTP 364
Cdd:TIGR01350 245 ----TYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIG-GPMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 365 VAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAvekfGEENIEVYHSYFwplewtiPSRDNNK---- 440
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF-------PFAANGKalal 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 345100815 441 ----CYAKIICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 498
Cdd:TIGR01350 386 getdGFVKIIAD-KKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
51-498 |
1.63e-61 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 208.85 E-value: 1.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 51 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDrmieAVQNH-- 128
Cdd:PRK06416 23 AAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAEN-VGIDFK----KVQEWkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 129 --IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGkEKIYSAERFLIATGERPRYL-GIPGDKEYCISSDDLFS 205
Cdd:PRK06416 89 gvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDG-EQTYTAKNIILATGSRPRELpGIEIDGRVIWTSDEALN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 206 LPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRsiLLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEAG 282
Cdd:PRK06416 168 LDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALKKRGIKIK---TGAKAKKVEQT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 283 TPGrLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEktGKIPVTDEEQTNVPYIYAIGDILEdKVEL 362
Cdd:PRK06416 243 DDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIVG-GPML 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 363 TPVAIQAGRLLAQRLyAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFwplewtipsRDNNKCY 442
Cdd:PRK06416 317 AHKASAEGIIAAEAI-AGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVVKFPF---------AGNGKAL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345100815 443 A--------KIICNTKDNErVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 498
Cdd:PRK06416 385 AlgetdgfvKLIFDKKDGE-VLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
50-497 |
3.15e-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: 205.35 E-value: 3.15e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 50 EAAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVkhDWDRMIEAVQNHI 129
Cdd:TIGR02053 18 KAAELGASVAMVE---------RGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATVAV--DFGELLEGKREVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 130 GSL-NWGYRVALREKKVVYENAYGQFIGPHRIKAtnNKGKEkIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSL 206
Cdd:TIGR02053 87 EELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGRE-VRGAKRFLIATGARPAIPPIPGLKEagY-LTSEEALAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 207 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQfVPIKVEQIEAgtpG 285
Cdd:TIGR02053 163 DRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTS-AQVKAVSVRG---G 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 286 RLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPV 365
Cdd:TIGR02053 239 GKIITVEKPGGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDER-GGILVDETLRTSNPGIYAAGDVT-GGLQLEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 366 AIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIpsrDNNKCYAKI 445
Cdd:TIGR02053 315 AAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARIN---RDTRGFIKL 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 345100815 446 ICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAE 497
Cdd:TIGR02053 392 VAE-PGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
50-501 |
1.27e-59 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 203.49 E-value: 1.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 50 EAAQYGKKVMVLDfvtPTPLGtrwglgGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDRMIEAVQNHI 129
Cdd:PRK06292 21 RAAKLGKKVALIE---KGPLG------GTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADG-PKIDFKKVMARVRRER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 130 GSLNWGYRVALREK-KVVYENAYGQFIGPHRIKAtnnkgKEKIYSAERFLIATGER-PRYLGI-PGDKEYCISSDDLFSL 206
Cdd:PRK06292 91 DRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRvPPIPGVwLILGDRLLTSDDAFEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 207 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIrqfVPIKVEQIEAGtPG 285
Cdd:PRK06292 166 DKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-FKIK---LGAKVTSVEKS-GD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 286 RLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPV 365
Cdd:PRK06292 241 EKVEELEKGGKTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSVPGIYAAGDVN-GKPPLLHE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 366 AIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEWTIPSR--DNNKCYA 443
Cdd:PRK06292 317 AADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEV-----PFEAQGRARvmGKNDGFV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 345100815 444 KIICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTT 501
Cdd:PRK06292 392 KVYAD-KKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRT 448
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
75-502 |
9.63e-53 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 185.41 E-value: 9.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 75 LGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDW----DRMIEAVQN-HIGSLNWgyrvaLREKK---VV 146
Cdd:PRK06370 39 LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFkavmARKRRIRARsRHGSEQW-----LRGLEgvdVF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 147 YENAygQFIGPHRIKATNnkgkeKIYSAERFLIATGERPRYLGIPG--DKEYcISSDDLFSLPYCPGKTLVVGASYVALE 224
Cdd:PRK06370 114 RGHA--RFESPNTVRVGG-----ETLRAKRIFINTGARAAIPPIPGldEVGY-LTNETIFSLDELPEHLVIIGGGYIGLE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 225 CAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQieagTPGRLRVVAQSTNSEEIIEGE 303
Cdd:PRK06370 186 FAQMFRRFGSEVTVIERGpRLLPREDEDVAAAVREILEREGIDVRLNAECIRVER----DGDGIAVGLDCNGGAPEITGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 304 YntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTV 383
Cdd:PRK06370 262 H--ILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRGAFTHTAYNDARIVAANLLDGGRR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 384 KCDYENVPTTVFTPLEYGACGLSEEKAVEKfGeENIEVYhsyfwplewTIPSRD--------NNKCYAKIICNtKDNERV 455
Cdd:PRK06370 338 KVSDRIVPYATYTDPPLARVGMTEAEARKS-G-RRVLVG---------TRPMTRvgravekgETQGFMKVVVD-ADTDRI 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 345100815 456 VGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 502
Cdd:PRK06370 406 LGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
49-370 |
4.33e-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: 4.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 49 KEAAQYGKKVMVLDfvtptplgtrwgLGGTCVNVGCIPKKLMHQAAllgqalqdsrnygwKVEETVKHDWDRMiEAVQNH 128
Cdd:pfam07992 17 LTLAQLGGKVTLIE------------DEGTCPYGGCVLSKALLGAA--------------EAPEIASLWADLY-KRKEEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 129 IGSLNWGYRVALREKKVVYENAYGQFIGPHrikatNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYC------ISSDD 202
Cdd:pfam07992 70 VKKLNNGIEVLLGTEVVSIDPGAKKVVLEE-----LVDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtLDSAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 203 LFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEa 281
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGVEVR---LGTSVKEII- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 282 GTPGRLRVVaqsTNSEEIIEGEynTVMLAIGRDACTRkiGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDILEDKVE 361
Cdd:pfam07992 221 GDGDGVEVI---LKDGTEIDAD--LVVVAIGRRPNTE--LLEAAGLELDE-RGGIVVDEYLRTSVPGIYAAGDCRVGGPE 292
|
....*....
gi 345100815 362 LTPVAIQAG 370
Cdd:pfam07992 293 LAQNAVAQG 301
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
76-498 |
1.12e-43 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 160.50 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 76 GGTCVNVGCIPKKLMHQAALLGQALQDSRNYGwkVEETVKH-DWDRMIEAVQNHIGSLNWG---YRVALREKKVVYENAY 151
Cdd:PRK07846 34 GGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIAAGgeeYRGRDTPNIDVYRGHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 152 gQFIGPHRIKAtnnkGKEKIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSLPYCPGKTLVVGASYVALECAGFL 229
Cdd:PRK07846 112 -RFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSGvrY-HTSDTIMRLPELPESLVIVGGGFIAAEFAHVF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 230 AGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIRQFVPIKVEQIEAGtpgrlrvVAQSTNSEEIIEGEynTVM 308
Cdd:PRK07846 186 SALGVRVTVVNRSgRLLRHLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSG-------VTLRLDDGSTVEAD--VLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 309 LAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAG-STVKCDY 387
Cdd:PRK07846 256 VATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV-SSPYQLKHVANHEARVVQHNLLHPdDLIASDH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 388 ENVPTTVFTPLEYGACGLSEEKAVEKfgEENIEVYH------SYFWPLEWTipsrdnnKCYAKIICNtKDNERVVGFHVL 461
Cdd:PRK07846 334 RFVPAAVFTHPQIASVGLTENEARAA--GLDITVKVqnygdvAYGWAMEDT-------TGFVKLIAD-RDTGRLLGAHII 403
|
410 420 430
....*....|....*....|....*....|....*...
gi 345100815 462 GPNAGEVTQGFAAALKCGLTKKQL-DSTIGIHPVCAEV 498
Cdd:PRK07846 404 GPQASTLIQPLIQAMSFGLDAREMaRGQYWIHPALPEV 441
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
30-508 |
4.14e-41 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 153.93 E-value: 4.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 30 SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRwgLGGTCVNVGCIPKK-LMHQAALLGQALQDSRNYGW 108
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNPKGKPA--LGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 109 KVEEtVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIG----PHRIKATnNKGKEKIySAERFLIATGER 184
Cdd:PRK06327 80 HVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGktdaGYEIKVT-GEDETVI-TAKHVIIATGSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 185 PRYL-GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEE 262
Cdd:PRK06327 157 PRHLpGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 263 HGIKFIrqfVPIKVEQIEAGTPGrLRVVAQSTNSEEIIEgEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEE 342
Cdd:PRK06327 237 QGLDIH---LGVKIGEIKTGGKG-VSVAYTDADGEAQTL-EVDKLIVSIGRVPNTDGLGLEAVGLKLDER-GFIPVDDHC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 343 QTNVPYIYAIGDILEdKVELTPVAIQAGRLLAQRLyAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVekfgEENIEVY 422
Cdd:PRK06327 311 RTNVPNVYAIGDVVR-GPMLAHKAEEEGVAVAERI-AGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLK----AEGVEYK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 423 HSYFwplewtiPSRDNNKC--------YAKIICNTKdNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPV 494
Cdd:PRK06327 385 AGKF-------PFMANGRAlamgepdgFVKIIADAK-TDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPT 456
|
490
....*....|....*.
gi 345100815 495 CAEVF--TTLSVTKRS 508
Cdd:PRK06327 457 LSEVWheAALAVDKRP 472
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
76-498 |
7.36e-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: 147.21 E-value: 7.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 76 GGTCVNVGCIPKKLMHQAALLGQALQDSRNYGwkVEETVKH-DWDRMIEAVQNH----IGSLNWGYRVALREKKVVYENA 150
Cdd:TIGR03452 35 GGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRVFGDridpIAAGGEDYRRGDETPNIDVYDG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 151 YGQFIGPHRIKAtnnkGKEKIYSAERFLIATGERPR---YLGIPGDKEYciSSDDLFSLPYCPGKTLVVGASYVALECAG 227
Cdd:TIGR03452 113 HARFVGPRTLRT----GDGEEITGDQIVIAAGSRPYippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGYIAAEFAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 228 FLAGIGLDVTVMVRS-ILLRGFDQDMANKIGE----HMEEHGIKFIrqfvpIKVEQIEAGtpgrlrvVAQSTNSEEIIEG 302
Cdd:TIGR03452 187 VFSALGTRVTIVNRStKLLRHLDEDISDRFTEiakkKWDIRLGRNV-----TAVEQDGDG-------VTLTLDDGSTVTA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 303 EynTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDkVELTPVAIQAGRLLAQRL-YAGS 381
Cdd:TIGR03452 255 D--VLLVATGRVPNGDLLDAEAAGVEVDED-GRIKVDEYGRTSARGVWALGDVSSP-YQLKHVANAEARVVKHNLlHPND 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 382 TVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYH----SYFWPLEWTipsrdnnKCYAKIICNtKDNERVVG 457
Cdd:TIGR03452 331 LRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIQNygdvAYGWAMEDT-------TGFCKLIAD-RDTGKLLG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 345100815 458 FHVLGPNAGEVTQGFAAALKCGLTKKQL-DSTIGIHPVCAEV 498
Cdd:TIGR03452 403 AHIIGPQASSLIQPLITAMAFGLDAREMaRKQYWIHPALPEV 444
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
390-502 |
2.07e-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: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 390 VPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFWPLEWTIPSRDNnKCYAKIICNtKDNERVVGFHVLGPNAGEVT 469
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDT-DGFVKLVAD-RETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 345100815 470 QGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 502
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
51-485 |
8.25e-36 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 140.29 E-value: 8.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 51 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQaLQDSRNYGWKVEETVKH-DWDRMIEAVQNhi 129
Cdd:PRK13748 117 AVEQGARVTLIE---------RGTIGGTCVNVGCVPSKIMIRAAHIAH-LRRESPFDGGIAATVPTiDRSRLLAQQQA-- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 130 gslnwgyRV-ALREKKvvYEN------------AYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKE- 195
Cdd:PRK13748 185 -------RVdELRHAK--YEGildgnpaitvlhGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKEt 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 196 -YCISSDDLFSlPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLrgFDQDMAnkIGEHM----EEHGIKFIrq 270
Cdd:PRK13748 256 pYWTSTEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLF--FREDPA--IGEAVtaafRAEGIEVL-- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 271 fvpikvEQIEAGTpgrlrvVAQStNSEEIIEGEYNTV-----MLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTN 345
Cdd:PRK13748 329 ------EHTQASQ------VAHV-DGEFVLTTGHGELradklLVATGRAPNTRSLALDAAGVTVNAQ-GAIVIDQGMRTS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 346 VPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTvKCDYENVPTTVFTPLEYGACGLSEEKAvekfGEENIEVyHSY 425
Cdd:PRK13748 395 VPHIYAAGDC-TDQPQFVYVAAAAGTRAAINMTGGDA-ALDLTAMPAVVFTDPQVATVGYSEAEA----HHDGIET-DSR 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 345100815 426 FWPLEwTIPSRDNN---KCYAKIICNTKDNeRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQL 485
Cdd:PRK13748 468 TLTLD-NVPRALANfdtRGFIKLVIEEGSG-RLIGVQAVAPEAGELIQTAALAIRNRMTVQEL 528
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
28-467 |
5.98e-35 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 136.44 E-value: 5.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 28 PKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDfvtptplgTRWGLGGTCVNVGCIPKKLMHQAAL-LGQALQDS--R 104
Cdd:PRK05249 1 MHMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlyS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 105 NYGWKVEETVKHDWDRMIEAVQNHIGSLnwgyRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGER 184
Cdd:PRK05249 73 SYRVKLRITFADLLARADHVINKQVEVR----RGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 185 P-RYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEE 262
Cdd:PRK05249 149 PyRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 263 HGIKFI-RQfvpiKVEQIEAGTPGRLRVVAqstnSEEIIEGEynTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDE 341
Cdd:PRK05249 229 SGVTIRhNE----EVEKVEGGDDGVIVHLK----SGKKIKAD--CLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNEN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 342 EQTNVPYIYAIGDiledkV----ELTPVAIQAGRLLAQRLYaGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVekfgEE 417
Cdd:PRK05249 298 YQTAVPHIYAVGD-----VigfpSLASASMDQGRIAAQHAV-GEATAHLIEDIPTGIYTIPEISSVGKTEQELT----AA 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 345100815 418 NI--EVYHSYFWPLewtipSR-----DNNKCYaKIICNTKDnERVVGFHVLGPNAGE 467
Cdd:PRK05249 368 KVpyEVGRARFKEL-----ARaqiagDNVGML-KILFHRET-LEILGVHCFGERATE 417
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
76-497 |
3.54e-29 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 119.47 E-value: 3.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 76 GGTCVNVGCIPKKLMHQAAllgqalqdsrNYGWKVEETVKHDwdrmiEAVQNHIGSLNWGyrvALREKKVVYENAYGQFI 155
Cdd:PRK07251 40 GGTCINIGCIPTKTLLVAA----------EKNLSFEQVMATK-----NTVTSRLRGKNYA---MLAGSGVDLYDAEAHFV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 156 GPHRIKATnnKGKEKI-YSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGI 232
Cdd:PRK07251 102 SNKVIEVQ--AGDEKIeLTAETIVINTGAVSNVLPIPGlaDSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 233 GLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpIKVEQIEAGTPGrlrvVAQSTNSEEIIegeYNTVMLAI 311
Cdd:PRK07251 180 GSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLN---AHTTEVKNDGDQ----VLVVTEDETYR---FDALLYAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 312 GRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKC-DYENV 390
Cdd:PRK07251 250 GRKPNTEPLGLENTDIELTER-GAIKVDDYCQTSVPGVFAVGDV-NGGPQFTYISLDDFRIVFGYLTGDGSYTLeDRGNV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 391 PTTVFTPLEYGACGLSEEKAVEKFGEenievYHSYFWPLEWTIPSRDNN--KCYAKIICNTKDNErVVGFHVLGPNAGEV 468
Cdd:PRK07251 328 PTTMFITPPLSQVGLTEKEAKEAGLP-----YAVKELLVAAMPRAHVNNdlRGAFKVVVNTETKE-ILGATLFGEGSQEI 401
|
410 420
....*....|....*....|....*....
gi 345100815 469 TQGFAAALKCGLTKKQLDSTIGIHPVCAE 497
Cdd:PRK07251 402 INLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
76-502 |
2.71e-28 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 117.19 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 76 GGTCVNVGCIP-KKLMHQAALlgqalqdsrnygwkveetvKHDWDRMIeAVQNHIGSLnwgyrvaLREK---------KV 145
Cdd:NF040477 40 GGTCINIGCIPtKTLVHDAEQ-------------------HQDFSTAM-QRKSSVVGF-------LRDKnyhnladldNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 146 VYENAYGQFIGPHRIKATNNKGKEKIYsAERFLIATGERPRYLGIPGDKEY--CISSDDLFSLPYCPGKTLVVGASYVAL 223
Cdd:NF040477 93 DVINGRAEFIDNHTLRVFQADGEQELR-GEKIFINTGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 224 ECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEAgTPGRLRVVAQstnseeiiEG 302
Cdd:NF040477 172 EFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVELI---LNAQVQRVSS-HEGEVQLETA--------EG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 303 EY--NTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLY-A 379
Cdd:NF040477 240 VLtvDALLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLgE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 380 GSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEwTIPSrdnnkcyAKIICNTK--------- 450
Cdd:NF040477 318 GKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTL-----PVA-AIPR-------ARVMNDTRgvlkavvdn 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 345100815 451 DNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 502
Cdd:NF040477 385 KTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDL 436
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
51-501 |
5.78e-26 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 111.93 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 51 AAQYGKKVMVLDfvtptplGTRWGLGGTCVNVGCIPKKLMHQAA----------------LLGQALQDSRNYGWK----V 110
Cdd:PTZ00153 135 AMERGLKVIIFT-------GDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVErnqlV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 111 EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPH-RIKATNNKGKEK---IYSAERFLIATGERPR 186
Cdd:PTZ00153 208 ADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYERgHIVDKNTIKSEKsgkEFKVKNIIIATGSTPN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 187 Y-LGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANkigeHMEEHG 264
Cdd:PTZ00153 288 IpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLLPLLDADVAK----YFERVF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 265 IKF--IRQFVPIKVEQIEAGTPGRLRVVAQS-----------TNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINE 331
Cdd:PTZ00153 364 LKSkpVRVHLNTLIEYVRAGKGNQPVIIGHSerqtgesdgpkKNMNDIKETYVDSCLVATGRKPNTNNLGLDKLKIQMKR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 332 ktGKIPVTD------EEQTNVPYIYAIGD-----ILEDKVELTPVAI------QAGRLLAQRLYAGSTVKCDYENVPTTV 394
Cdd:PTZ00153 444 --GFVSVDEhlrvlrEDQEVYDNIFCIGDangkqMLAHTASHQALKVvdwiegKGKENVNINVENWASKPIIYKNIPSVC 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 395 FTPLEYGACGLSEEKAVEKFGEENIEVYHSYF-------WPLEWTIPSRDNNKCYAKIICNT-------------KDNER 454
Cdd:PTZ00153 522 YTTPELAFIGLTEKEAKELYPPDNVGVEISFYkanskvlCENNISFPNNSKNNSYNKGKYNTvdntegmvkivylKDTKE 601
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 345100815 455 VVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTT 501
Cdd:PTZ00153 602 ILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
76-502 |
3.60e-23 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 102.01 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 76 GGTCVNVGCIPKKLMhqaallgqaLQDSRNYGwkveetvkhDWDRMIE---AVQNHIGSLNWGYRVALREKKVVYENAyg 152
Cdd:PRK08010 40 GGTCINIGCIPTKTL---------VHDAQQHT---------DFVRAIQrknEVVNFLRNKNFHNLADMPNIDVIDGQA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 153 QFIGPHRIKaTNNKGKEKIYSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLA 230
Cdd:PRK08010 100 EFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIPGitTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 231 GIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpikvEQIEAGTPGRLRVVAQSTNSEEIIEGeyntVML 309
Cdd:PRK08010 179 NFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILN------AHVERISHHENQVQVHSEHAQLAVDA----LLI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 310 AIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYA-GSTVKCDYE 388
Cdd:PRK08010 249 ASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNIWAMGDV-TGGLQFTYISLDDYRIVRDELLGeGKRSTDDRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 389 NVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEWTIPSR--DNNKCYAKIICNTKdNERVVGFHVLGPNAG 466
Cdd:PRK08010 327 NVPYSVFMTPPLSRVGMTEEQARESGADIQVVTL-----PVAAIPRARvmNDTRGVLKAIVDNK-TQRILGASLLCVDSH 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 345100815 467 EVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 502
Cdd:PRK08010 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
51-493 |
8.51e-23 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 101.09 E-value: 8.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 51 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDrmIEAVQNHIG 130
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEARVD--LPAVNARVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 131 SL----NWGYRVALREKKVVYENAYGQFI----GPHRIKATNNKGKEKIYSAERFLIATGERPRYLgiPG---DKEYCIS 199
Cdd:PRK07845 89 ALaaaqSADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGASPRIL--PTaepDGERILT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 200 SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQ 278
Cdd:PRK07845 167 WRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 279 IEAGtpgrlrVVAQSTNSEEiIEGEYntVMLAIGRDACTRKIGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDIlED 358
Cdd:PRK07845 247 TGDG------VVVTLTDGRT-VEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIYAAGDC-TG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 359 KVELTPVAIQAGRL-LAQRLyaGSTVK-CDYENVPTTVFTPLEYGACGLSeEKAVEKfGEENIEVYhsyfwplewTIPSR 436
Cdd:PRK07845 316 VLPLASVAAMQGRIaMYHAL--GEAVSpLRLKTVASNVFTRPEIATVGVS-QAAIDS-GEVPARTV---------MLPLA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345100815 437 DNNKC--------YAKIICnTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 493
Cdd:PRK07845 383 TNPRAkmsglrdgFVKLFC-RPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYP 446
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
156-372 |
5.61e-21 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 93.26 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 156 GPHRIKATNnkgkEKIYSAERFLIATGERPRYLGIPGDKE-------YCISSDdlfsLPYCPGKT-LVVGASYVALECAG 227
Cdd:COG0492 87 GPFRVTTDD----GTEYEAKAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEAL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 228 FLAGIGLDVTVMVRSILLRGfDQDMANKIGEHmeeHGIKFIRQFVPIKVEqieaGTPGRLRVVAQSTNSEEIIEGEYNTV 307
Cdd:COG0492 159 YLTKFASKVTLIHRRDELRA-SKILVERLRAN---PKIEVLWNTEVTEIE----GDGRVEGVTLKNVKTGEEKELEVDGV 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345100815 308 MLAIGRDACTRkiGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRL 372
Cdd:COG0492 231 FVAIGLKPNTE--LLKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAI 292
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
178-377 |
7.29e-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: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 178 LIATGERPRYLGIPGdkeycISSDDLFSL--------------PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS- 242
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddadalrealkEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 243 ILLRGFDQDMANKIGEHMEEHGIKFIRQFvpiKVEQIEAGTpgrlRVVAQSTNSEEIiegEYNTVMLAIG--------RD 314
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGE---TVVAIDGDD----KVAVTLTDGEEI---PADLVVVAPGvrpntelaKD 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 345100815 315 ActrkigletvGVKINEkTGKIPVTDEEQTNVPYIYAIGDILE---------DKVELTPVAIQAGRLLAQRL 377
Cdd:COG0446 228 A----------GLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtgktVYIPLASAANKQGRVAAENI 288
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
212-288 |
5.80e-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: 5.80e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 345100815 212 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLR 288
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDrLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
178-377 |
1.40e-17 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 84.81 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 178 LIATGERPRYLGIPG-DKEYCI---SSDDLFSL-PYCPGKT--LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGF 248
Cdd:COG1251 103 VLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 249 DQDMANKIGEHMEEHGIKFIRQfvpIKVEQIEaGTPGRLRVVaqsTNSEEIIEGEynTVMLAIG---RDACTRKIGLETV 325
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVRLG---TGVTEIE-GDDRVTGVR---LADGEELPAD--LVVVAIGvrpNTELARAAGLAVD 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 345100815 326 -GVKINEKTgkipvtdeeQTNVPYIYAIGDILE--------DKVELTPVAIQAGRLLAQRL 377
Cdd:COG1251 254 rGIVVDDYL---------RTSDPDIYAAGDCAEhpgpvygrRVLELVAPAYEQARVAAANL 305
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
212-357 |
2.41e-13 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 72.12 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 212 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIkfirqfvPIKVEQIEAGTPGRLrVV 290
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREI-------PYRLNEEIDAINGNE-VT 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 345100815 291 AQSTNSEEiiegeYNTVMLAIGRDACTRKIglETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILE 357
Cdd:PRK13512 222 FKSGKVEH-----YDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIIT 280
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
179-411 |
9.47e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 63.61 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 179 IATGERPRYLGIPGDKEYCI---SSDDLFSL------------PYCPGKTLVVGASYVALECAGFLA----------GIG 233
Cdd:COG1252 103 IATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAellrkllrypGID 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 234 LD------VTVMVRsiLLRGFDQDMANKIGEHMEEHGIKFIRQFvpiKVEQIEAGTpgrlrvvAQSTNSEEIiegEYNTV 307
Cdd:COG1252 183 PDkvritlVEAGPR--ILPGLGEKLSEAAEKELEKRGVEVHTGT---RVTEVDADG-------VTLEDGEEI---PADTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 308 MLAIGRDA--CTRKIGLETvgvkinEKTGKIPVTDEEQT-NVPYIYAIGDI--LEDKVELT-----PVAIQAGRLLAQRL 377
Cdd:COG1252 248 IWAAGVKAppLLADLGLPT------DRRGRVLVDPTLQVpGHPNVFAIGDCaaVPDPDGKPvpktaQAAVQQAKVLAKNI 321
|
250 260 270
....*....|....*....|....*....|....*
gi 345100815 378 YAgstvkcDYENVPTTVFTPLEYGA-CGLSEEKAV 411
Cdd:COG1252 322 AA------LLRGKPLKPFRYRDKGClASLGRGAAV 350
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
214-485 |
3.68e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 61.98 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 214 LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGFDQDMANKIGEHMEEHGIKFirqFVPIKVEQIEagtpGRLRVVA 291
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVEL---HLNEFVKSLI----GEDKVEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 292 QSTNseeiiEGEYNT--VMLAIGRDACTRKI---GLETVgvkineKTGKIPVTDEEQTNVPYIYAIGD------ILEDKV 360
Cdd:PRK09564 226 VVTD-----KGEYEAdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKN 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 361 ELTPVAIQA---GRLLAQRLyAGSTVKcdyenVPTT-------VFTpLEYGACGLSEEKAVEKfgeeNIEVY-------- 422
Cdd:PRK09564 295 VYVPLATTAnklGRMVGENL-AGRHVS-----FKGTlgsacikVLD-LEAARTGLTEEEAKKL----GIDYKtvfikdkn 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 345100815 423 HSYFWPlewtipsrDNNKCYAKIICNtKDNERVVGFHVLGPNaGEV--TQGFAAALKCGLTKKQL 485
Cdd:PRK09564 364 HTNYYP--------GQEDLYVKLIYE-ADTKVILGGQIIGKK-GAVlrIDALAVAIYAKLTTQEL 418
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
178-355 |
2.75e-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: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 178 LIATG-ERPRYLGIPG-DKEYCIS----------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIG-LDVTVMVRsil 244
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 245 lRGFDqDMANKIGE--HMEEHGIKFIRQFVP-------------IKVEQIEAGTP---GRLRVVAqSTNSEEIIEGEynT 306
Cdd:COG0493 288 -RTRE-EMPASKEEveEALEEGVEFLFLVAPveiigdengrvtgLECVRMELGEPdesGRRRPVP-IEGSEFTLPAD--L 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 345100815 307 VMLAIGRDACTRKIgLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDI 355
Cdd:COG0493 363 VILAIGQTPDPSGL-EEELGLELDKR-GTI-VVDEEtyQTSLPGVFAGGDA 410
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
178-377 |
6.72e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 54.61 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 178 LIATGE-RPRYLGIPG-DKEYCISS-DDLFS-----LPYCP---------GKTLVVGASYVALECA--GFLAGiGLDVTV 238
Cdd:PRK12770 123 LIATGTwKSRKLGIPGeDLPGVYSAlEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAAleAVLLG-AEKVYL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 239 MVRsillRGFDQDMANKIG-EHMEEHGIKFIRQFVP--------------IKVEQIEAGTPGRLRVVAQsTNSEEIIegE 303
Cdd:PRK12770 202 AYR----RTINEAPAGKYEiERLIARGVEFLELVTPvriigegrvegvelAKMRLGEPDESGRPRPVPI-PGSEFVL--E 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 345100815 304 YNTVMLAIGRDAcTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDKVELTPvAIQAGRLLAQRL 377
Cdd:PRK12770 275 ADTVVFAIGEIP-TPPFAKECLGIELNRK-GEIVVDEKHMTSREGVFAAGDVVTGPSKIGK-AIKSGLRAAQSI 345
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
170-357 |
8.36e-08 |
|
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: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 170 KIYSAERFLIATGERPRYLGIPG-DKEYCI---SSDDLFSLPYCPGKTL---VVGASYVALECAGFLAGIGLDVTV--MV 240
Cdd:TIGR02374 93 RTLSYDKLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMDVSVihHA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 241 RSILLRGFDQDMANKIGEHMEEHGIKFIRQfvPIKVEQIEAGTPGRLRVvaqsTNSEEIiegEYNTVMLAIG---RDACT 317
Cdd:TIGR02374 173 PGLMAKQLDQTAGRLLQRELEQKGLTFLLE--KDTVEIVGATKADRIRF----KDGSSL---EADLIVMAAGirpNDELA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 345100815 318 RKIGLetvgvKINektGKIPVTDEEQTNVPYIYAIGDILE 357
Cdd:TIGR02374 244 VSAGI-----KVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
164-379 |
8.42e-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: 8.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 164 NNKGKEKIysaerFLIATGERPRYLGIPGDKEYCISSDDLF---------------SLPYCPGKTLVV-GASYVALECAG 227
Cdd:PRK12775 514 NDKGFDAV-----FLGVGAGAPTFLGIPGEFAGQVYSANEFltrvnlmggdkfpflDTPISLGKSVVViGAGNTAMDCLR 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 228 FLAGIGldvTVMVRSILLRGfDQDMANKIGE--HMEEHGIKFIRQFVPI-------------KVEQIEAGTP---GRLRV 289
Cdd:PRK12775 589 VAKRLG---APTVRCVYRRS-EAEAPARIEEirHAKEEGIDFFFLHSPVeiyvdaegsvrgmKVEEMELGEPdekGRRKP 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 290 VAqstnSEEIIEGEYNTVMLAIGRDAcTRKIGLETVGVKINeKTGKIPVTDE-----EQTNVPYIYAIGDILEDKVELTp 364
Cdd:PRK12775 665 MP----TGEFKDLECDTVIYALGTKA-NPIITQSTPGLALN-KWGNIAADDGklestQSTNLPGVFAGGDIVTGGATVI- 737
|
250
....*....|....*
gi 345100815 365 VAIQAGRLLAQRLYA 379
Cdd:PRK12775 738 LAMGAGRRAARSIAT 752
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
168-355 |
1.10e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 54.25 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 168 KEKIYSAerFLIATGE-RPRYLGIPGdkeycISSDDLFSL-----------PYCPG---------KTLVVGASYVALECA 226
Cdd:PRK12831 225 EEEGFDA--VFIGSGAgLPKFMGIPG-----ENLNGVFSAnefltrvnlmkAYKPEydtpikvgkKVAVVGGGNVAMDAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 227 GFLAGIGLDVTVMVRsillRGfDQDMANKIGE--HMEEHGIKFIRQFVPI-------------KVEQIEAGTP---GRLR 288
Cdd:PRK12831 298 RTALRLGAEVHIVYR----RS-EEELPARVEEvhHAKEEGVIFDLLTNPVeilgdengwvkgmKCIKMELGEPdasGRRR 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 345100815 289 VVaQSTNSEEIIegEYNTVMLAIGRDAcTRKIGLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDI 355
Cdd:PRK12831 373 PV-EIEGSEFVL--EVDTVIMSLGTSP-NPLISSTTKGLKINKR-GCI-VADEEtgLTSKEGVFAGGDA 435
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
174-355 |
1.68e-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: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 174 AERF---LIATGE-RPRYLGIPGDKEYCISS--------------DDLFSLPYCPGK-TLVVGASYVALECAGFLAGIGL 234
Cdd:PRK12778 515 EEGFkgiFIASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGKkVAVVGGGNTAMDSARTAKRLGA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 235 DvTVMvrsILLRGFDQDMANKIGE--HMEEHGIKF----------------IRQFVPIKVEQIEAGTPGRLRVVAqSTNS 296
Cdd:PRK12778 595 E-RVT---IVYRRSEEEMPARLEEvkHAKEEGIEFltlhnpieyladekgwVKQVVLQKMELGEPDASGRRRPVA-IPGS 669
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 297 EEIIEgeYNTVMLAIGRDActRKIGLETV-GVKINEKtGKIPVTDEEQTNVPYIYAIGDI 355
Cdd:PRK12778 670 TFTVD--VDLVIVSVGVSP--NPLVPSSIpGLELNRK-GTIVVDEEMQSSIPGIYAGGDI 724
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
178-375 |
1.97e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 53.26 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 178 LIATG-ERPRYLGIPGDK--------EYCISS---DDLFSLPycPGKTLVV-GASYVALECAGFLAGIGL-DVTVMVRsi 243
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDFLTRVnqaVADYDLP--VGKRVVViGGGNTAMDAARTAKRLGAeSVTIVYR-- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 244 llRGFDqDMANKIGE--HMEEHGIKFIRQFVPIKVEQIEAGTPG------RLRVVAQSTNSEEIIEGEY-----NTVMLA 310
Cdd:PRK11749 306 --RGRE-EMPASEEEveHAKEEGVEFEWLAAPVEILGDEGRVTGvefvrmELGEPDASGRRRVPIEGSEftlpaDLVIKA 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 345100815 311 IGRDAcTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDIL--EDkveLTPVAIQAGRLLAQ 375
Cdd:PRK11749 383 IGQTP-NPLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVtgAA---TVVWAVGDGKDAAE 445
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
172-353 |
1.01e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 50.69 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 172 YSAERFLIATGE--RPRYLGIPgdkEYCISSDDLFSL-PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGF 248
Cdd:pfam13738 117 YQARYVIIATGEfdFPNKLGVP---ELPKHYSYVKDFhPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 249 DQDMA--------NKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlrVVAQSTNSEEIIegEYNTVMLAIGRDaCTRKI 320
Cdd:pfam13738 194 DSDPSyslspdtlNRLEELVKNGKIKAHFNAEVKEITEVDVS------YKVHTEDGRKVT--SNDDPILATGYH-PDLSF 264
|
170 180 190
....*....|....*....|....*....|....
gi 345100815 321 gLETVGVKINEKtGKIPVTDE-EQTNVPYIYAIG 353
Cdd:pfam13738 265 -LKKGLFELDED-GRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
172-357 |
1.28e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 47.36 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 172 YSAERFLIATGERPRYLGIPGDKEY-------CISSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL 244
Cdd:PRK10262 104 YTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 345100815 245 LRGfDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPG-RLRVVAQSTNSEEIiegEYNTVMLAIGRDACTR----K 319
Cdd:PRK10262 181 FRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGvRLRDTQNSDNIESL---DVAGLFVAIGHSPNTAifegQ 256
|
170 180 190
....*....|....*....|....*....|....*...
gi 345100815 320 IGLETVGVKINEKTGKipvtDEEQTNVPYIYAIGDILE 357
Cdd:PRK10262 257 LELENGYIKVQSGIHG----NATQTSIPGVFAAGDVMD 290
|
|
| |
