|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
11-499 |
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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 11 YDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKV 90
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 91 EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGI 170
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 171 PGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQ 250
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 251 FVPIKVEQIEAgtpgrlRVVAQSTNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIY 330
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 331 AIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLE 410
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 411 WTIPSRDN-NKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVTKRSG 489
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 33519428 490 ASILQAGCUG 499
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
10-499 |
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 33519428 10 SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQ-DSRNYGW 88
Cdd:PTZ00052 3 TFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 89 KVEETvkHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNkGKEKIYSAERFLIATGERPRYL 168
Cdd:PTZ00052 83 KTSSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDN-SQEETITAKYILIATGGRPSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 169 -GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKF 247
Cdd:PTZ00052 160 eDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 248 IRQFVPIKVEQIEAgtpgRLRVVAQSTNSEeiiegEYNTVMLAIGRDACTRKIGLETVGVKINeKTGKIPVTDeEQTNVP 327
Cdd:PTZ00052 240 LEGVVPINIEKMDD----KIKVLFSDGTTE-----LFDTVLYATGRKPDIKGLNLNAIGVHVN-KSNKIIAPN-DCTNIP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 328 YIYAIGDILEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFW 407
Cdd:PTZ00052 309 NIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFN 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 408 PLEWTIPSRD--------------NNKCYAKIICNTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 473
Cdd:PTZ00052 389 TLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHP 468
|
490 500
....*....|....*....|....*.
gi 33519428 474 VCAEVFTTLSVTKRSGASILQAGCUG 499
Cdd:PTZ00052 469 TDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
31-482 |
2.14e-139 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 408.78 E-value: 2.14e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 31 AAQYGKKVMVLDfvtptplGTRwgLGGTCVNVGCIPKKLMHQAALLGQALQD-SRNYGWKVEETvKHDWDRMIEAVQNHI 109
Cdd:PRK06116 23 AAMYGAKVALIE-------AKR--LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRDAYI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 110 GSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKgkekiYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYC 189
Cdd:PRK06116 93 DRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIPDIPG-AEYGITSDGFFALEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 190 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlR 268
Cdd:PRK06116 167 PKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG-----S 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 269 VVAQSTNSEEIiegEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQ 348
Cdd:PRK06116 242 LTLTLEDGETL---TVDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 349 AGRLLAQRLYAG-STVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRDNnKCYAKIIC 427
Cdd:PRK06116 317 AGRRLSERLFNNkPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMKLVV 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 33519428 428 NTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 482
Cdd:PRK06116 396 VGKE-EKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
31-482 |
5.11e-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: 5.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 31 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDRMIEAVQNHIG 110
Cdd:COG1249 22 AAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGA-PSVDWAALMARKDKVVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 111 SLNWGYRVALREKKVVYENAYGQFIGPHRIKATNnkgkEKIYSAERFLIATGERPRYLGIPG-DKEYCISSDDLFSLPYC 189
Cdd:COG1249 92 RLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTG----GETLTADHIVIATGSRPRVPPIPGlDEVRVLTSDEALELEEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 190 PGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrLR 268
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG----VT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 269 VVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPVAIQ 348
Cdd:COG1249 244 VTLEDGGGEEAVEADK--VLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAHVASA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 349 AGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFgeENIEVYHSYFWPLEWTIpSRDNNKCYAKIICN 428
Cdd:COG1249 320 EGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAG--IDVKVGKFPFAANGRAL-ALGETEGFVKLIAD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 33519428 429 tKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 482
Cdd:COG1249 397 -AETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
11-482 |
1.68e-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: 1.68e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 11 YDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFVtptplgtrwglGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGW 88
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 89 KVEEtVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKekiYSAERFLIATGERPRYL 168
Cdd:TIGR01424 70 TVGK-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 169 GIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKF 247
Cdd:TIGR01424 146 ALPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 248 IRQFVPIKVEQIEAGtpgrlRVVAQSTNSEEIIEgeyNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVP 327
Cdd:TIGR01424 225 LPEDSITSISKDDDG-----RLKATLSKHEEIVA---DVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 328 YIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFW 407
Cdd:TIGR01424 296 SIYAVGDV-TDRINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33519428 408 PLEWTIPSRdNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 482
Cdd:TIGR01424 373 PMKATFSGR-QEKTLMKLVVDAKD-DKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
31-482 |
9.64e-108 |
|
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of animals, yeast, and a number of animal-resident bacteria. [Energy metabolism, Electron transport]
Pssm-ID: 273614 [Multi-domain] Cd Length: 450 Bit Score: 327.95 E-value: 9.64e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 31 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDRMIEAVQNHIG 110
Cdd:TIGR01421 21 AAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDAYVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 111 SLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKgkekiYSAERFLIATGERPRYL-GIPGdKEYCISSDDLFSLPYC 189
Cdd:TIGR01421 92 RLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIPG-AELGTDSDGFFALEEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 190 PGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlR 268
Cdd:TIGR01421 166 PKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG-----K 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 269 VVAQSTNSEEIIegEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPVAIQ 348
Cdd:TIGR01421 241 LVIHFEDGKSID--DVDELIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTPVAIA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 349 AGRLLAQRLYAGST-VKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIPSRdNNKCYAKIIC 427
Cdd:TIGR01421 317 AGRKLSERLFNGKTdDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSE-KQKCRMKLVC 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 33519428 428 NTKdNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 482
Cdd:TIGR01421 396 AGK-EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
2-491 |
9.24e-107 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 327.16 E-value: 9.24e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 2 NGPEDLPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFvtpTPLGTRW--GLGGTCVNVGCIPKKLMHQAALLG 77
Cdd:PLN02507 15 NADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGIceLPF---HPISSESigGVGGTCVIRGCVPKKILVYGATFG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 78 QALQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKV-VYENAyGQFIGPHRIKATNNKGKEKIYSAER 156
Cdd:PLN02507 92 GEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVkLYEGE-GKIVGPNEVEVTQLDGTKLRYTAKH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 157 FLIATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL-LRGFDQDMANK 235
Cdd:PLN02507 171 ILIATGSRAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMRAV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 236 IGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrLRVVaqSTNSEEIIEgeyNTVMLAIGRDACTRKIGLETVGVKInEKTGK 315
Cdd:PLN02507 250 VARNLEGRGINLHPRTNLTQLTKTEGG----IKVI--TDHGEEFVA---DVVLFATGRAPNTKRLNLEAVGVEL-DKAGA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 316 IPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKfG 395
Cdd:PLN02507 320 VKVDEYSRTNIPSIWAIGDV-TNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQ-A 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 396 EENIEVYHSYFWPLEWTIPSRdNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVC 475
Cdd:PLN02507 398 KGDILVFTSSFNPMKNTISGR-QEKTVMKLIVDAET-DKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSA 475
|
490
....*....|....*..
gi 33519428 476 AEVFTTL-SVTKRSGAS 491
Cdd:PLN02507 476 AEEFVTMrSVTRRVTAK 492
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
2-487 |
6.25e-102 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 316.43 E-value: 6.25e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 2 NGPEDlPKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMV--LDFVTPTPlGTRWGLGGTCVNVGCIPKKLMHQAALLGQA 79
Cdd:PLN02546 70 NGAES-ERHYDFDLFTIGAGSGGVRASRFASNFGASAAVceLPFATISS-DTLGGVGGTCVLRGCVPKKLLVYASKYSHE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 80 LQDSRNYGWKVEETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNnkgkeKIYSAERFLI 159
Cdd:PLN02546 148 FEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDG-----KLYTARNILI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 160 ATGERPRYLGIPGdKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGE 238
Cdd:PLN02546 223 AVGGRPFIPDIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 239 HMEEHGIKFIRQFVPIKVEQIEAGTpgrlrvVAQSTNsEEIIEGeYNTVMLAIGRDACTRKIGLETVGVKINeKTGKIPV 318
Cdd:PLN02546 302 QMSLRGIEFHTEESPQAIIKSADGS------LSLKTN-KGTVEG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEV 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 319 TDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEen 398
Cdd:PLN02546 373 DEYSRTSVPSIWAVGDV-TDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD-- 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 399 IEVYHSYFWPLEWTIpSRDNNKCYAKIICNTKDNeRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 478
Cdd:PLN02546 450 VDVFTANFRPLKATL-SGLPDRVFMKLIVCAKTN-KVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEE 527
|
....*....
gi 33519428 479 FTTLSVTKR 487
Cdd:PLN02546 528 FVTMRTPTR 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
55-483 |
2.37e-87 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 278.81 E-value: 2.37e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 55 LGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVkhDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQF 134
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 135 IGPHR--IKATNNKGKE----------------------KIYSAERFLIATGERPRYLGIPGdKEYCISSDDLFSLPYcP 190
Cdd:PTZ00058 160 LSENQvlIKKVSQVDGEadesdddevtivsagvsqlddgQVIEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 191 GKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEagTPGRLRV 269
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVK--EKNLTIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 270 VAQSTNSEeiiegEYNTVMLAIGRDACTRKIGLEtvGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEDK---------- 339
Cdd:PTZ00058 316 LSDGRKYE-----HFDYVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 340 -----------------------VELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGE 396
Cdd:PTZ00058 389 lklyneepylkkkentsgesyynVQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGK 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 397 ENIEVYHSYFWPLEWTI----PSrDNNKCYAKIICNTKDnERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIH 472
Cdd:PTZ00058 469 ENVKIYESRFTNLFFSVydmdPA-QKEKTYLKLVCVGKE-ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIH 546
|
490
....*....|.
gi 33519428 473 PVCAEVFTTLS 483
Cdd:PTZ00058 547 PTAAEEFVTMA 557
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
31-477 |
2.64e-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: 2.64e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 31 AAQYGKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVE-ETVKHDWDRMIEAVQNHI 109
Cdd:TIGR01423 23 ATLYKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDrSSVKANWKALIAAKNKAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 110 GSLNWGYRVALREKK-VVYENAYGQFIGPHRIKA-----TNNKGKEKIySAERFLIATGERPRYLGIPGDkEYCISSDDL 183
Cdd:TIGR01423 103 LDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVresadPKSAVKERL-QAEHILLATGSWPQMLGIPGI-EHCISSNEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 184 FSLPYCPGKTLVVGASYVALECAGFLAG---IGLDVTVMVR-SILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQi 259
Cdd:TIGR01423 181 FYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 260 eaGTPGRLRVVAQSTNseeiiEGEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDK 339
Cdd:TIGR01423 260 --NADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKK-GAIQVDEFSRTNVPNIYAIGDV-TDR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 340 VELTPVAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFgeENIEVYHSYFWPLEWTIPSRDNN 419
Cdd:TIGR01423 331 VMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYK 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 33519428 420 KCYAKIICNTKDNErVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAE 477
Cdd:TIGR01423 409 KFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
30-478 |
3.69e-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: 230.99 E-value: 3.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 30 EAAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKK-LMHQAALLGQALQdSRNYGWKVeETVKHDWDRMIEAVQNH 108
Cdd:TIGR01350 19 RAAQLGLKVALVE---------KEYLGGTCLNVGCIPTKaLLHSAEVYDEIKH-AKDLGIEV-ENVSVDWEKMQKRKNKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 109 IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKiYSAERFLIATGERPRYLGIP--GDKEYCISSDDLFSL 186
Cdd:TIGR01350 88 VKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLPGPfdFDGKVVITSTGALNL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 187 PYCPGKTLVVGASYVALECAGFLAGIGLDVTV--MVRSIlLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTp 264
Cdd:TIGR01350 167 EEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQV- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 265 grlrVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEdKVELTP 344
Cdd:TIGR01350 245 ----TYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIG-GPMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 345 VAIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAvekfGEENIEVYHSYFwplewtiPSRDNNK---- 420
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF-------PFAANGKalal 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33519428 421 ----CYAKIICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 478
Cdd:TIGR01350 386 getdGFVKIIAD-KKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
31-478 |
5.98e-62 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 209.23 E-value: 5.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 31 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDrmieAVQNH-- 108
Cdd:PRK06416 23 AAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAEN-VGIDFK----KVQEWkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 109 --IGSLNWGYRVALREKKVVYENAYGQFIGPHRIKATNNKGkEKIYSAERFLIATGERPRYL-GIPGDKEYCISSDDLFS 185
Cdd:PRK06416 89 gvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDG-EQTYTAKNIILATGSRPRELpGIEIDGRVIWTSDEALN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 186 LPYCPGKTLVVGASYVALECAGFLAGIGLDVTV---MVRsiLLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEAG 262
Cdd:PRK06416 168 LDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALKKRGIKIK---TGAKAKKVEQT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 263 TPGrLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEktGKIPVTDEEQTNVPYIYAIGDILEdKVEL 342
Cdd:PRK06416 243 DDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIVG-GPML 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 343 TPVAIQAGRLLAQRLyAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFwplewtipsRDNNKCY 422
Cdd:PRK06416 317 AHKASAEGIIAAEAI-AGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVVKFPF---------AGNGKAL 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33519428 423 A--------KIICNTKDNErVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEV 478
Cdd:PRK06416 385 AlgetdgfvKLIFDKKDGE-VLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
30-477 |
1.23e-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: 206.12 E-value: 1.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 30 EAAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVkhDWDRMIEAVQNHI 109
Cdd:TIGR02053 18 KAAELGASVAMVE---------RGPLGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATVAV--DFGELLEGKREVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 110 GSL-NWGYRVALREKKVVYENAYGQFIGPHRIKAtnNKGKEkIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSL 186
Cdd:TIGR02053 87 EELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGRE-VRGAKRFLIATGARPAIPPIPGLKEagY-LTSEEALAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 187 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQfVPIKVEQIEAgtpG 265
Cdd:TIGR02053 163 DRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTS-AQVKAVSVRG---G 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 266 RLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPV 345
Cdd:TIGR02053 239 GKIITVEKPGGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDER-GGILVDETLRTSNPGIYAAGDVT-GGLQLEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 346 AIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYHSYFWPLEWTIpsrDNNKCYAKI 425
Cdd:TIGR02053 315 AAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARIN---RDTRGFIKL 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 33519428 426 IC--NTKdneRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAE 477
Cdd:TIGR02053 392 VAepGTG---KVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
30-481 |
4.31e-60 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 204.26 E-value: 4.31e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 30 EAAQYGKKVMVLDfvtPTPLGtrwglgGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEEtVKHDWDRMIEAVQNHI 109
Cdd:PRK06292 21 RAAKLGKKVALIE---KGPLG------GTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADG-PKIDFKKVMARVRRER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 110 GSLNWGYRVALREK-KVVYENAYGQFIGPHRIKAtnnkgKEKIYSAERFLIATGER-PRYLGI-PGDKEYCISSDDLFSL 186
Cdd:PRK06292 91 DRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGSRvPPIPGVwLILGDRLLTSDDAFEL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 187 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIrqfVPIKVEQIEAGtPG 265
Cdd:PRK06292 166 DKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-FKIK---LGAKVTSVEKS-GD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 266 RLRVVAQSTNSEEIIEGEYntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILeDKVELTPV 345
Cdd:PRK06292 241 EKVEELEKGGKTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSVPGIYAAGDVN-GKPPLLHE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 346 AIQAGRLLAQRLYAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEWTIPSR--DNNKCYA 423
Cdd:PRK06292 317 AADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEV-----PFEAQGRARvmGKNDGFV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 33519428 424 KIICNtKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTT 481
Cdd:PRK06292 392 KVYAD-KKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRT 448
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
55-482 |
3.80e-53 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 185.79 E-value: 3.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 55 LGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDW----DRMIEAVQN-HIGSLNWgyrvaLREKK---VV 126
Cdd:PRK06370 39 LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFkavmARKRRIRARsRHGSEQW-----LRGLEgvdVF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 127 YENAygQFIGPHRIKATNnkgkeKIYSAERFLIATGERPRYLGIPG--DKEYcISSDDLFSLPYCPGKTLVVGASYVALE 204
Cdd:PRK06370 114 RGHA--RFESPNTVRVGG-----ETLRAKRIFINTGARAAIPPIPGldEVGY-LTNETIFSLDELPEHLVIIGGGYIGLE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 205 CAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQieagTPGRLRVVAQSTNSEEIIEGE 283
Cdd:PRK06370 186 FAQMFRRFGSEVTVIERGpRLLPREDEDVAAAVREILEREGIDVRLNAECIRVER----DGDGIAVGLDCNGGAPEITGS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 284 YntVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTV 363
Cdd:PRK06370 262 H--ILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRGAFTHTAYNDARIVAANLLDGGRR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 364 KCDYENVPTTVFTPLEYGACGLSEEKAVEKfGeENIEVYhsyfwplewTIPSRD--------NNKCYAKIICNtKDNERV 435
Cdd:PRK06370 338 KVSDRIVPYATYTDPPLARVGMTEAEARKS-G-RRVLVG---------TRPMTRvgravekgETQGFMKVVVD-ADTDRI 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 33519428 436 VGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 482
Cdd:PRK06370 406 LGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
29-350 |
2.36e-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: 2.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 29 KEAAQYGKKVMVLDfvtptplgtrwgLGGTCVNVGCIPKKLMHQAAllgqalqdsrnygwKVEETVKHDWDRMiEAVQNH 108
Cdd:pfam07992 17 LTLAQLGGKVTLIE------------DEGTCPYGGCVLSKALLGAA--------------EAPEIASLWADLY-KRKEEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 109 IGSLNWGYRVALREKKVVYENAYGQFIGPHrikatNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYC------ISSDD 182
Cdd:pfam07992 70 VKKLNNGIEVLLGTEVVSIDPGAKKVVLEE-----LVDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtLDSAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 183 LFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEa 261
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGVEVR---LGTSVKEII- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 262 GTPGRLRVVaqsTNSEEIIEGEynTVMLAIGRDACTRkiGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDILEDKVE 341
Cdd:pfam07992 221 GDGDGVEVI---LKDGTEIDAD--LVVVAIGRRPNTE--LLEAAGLELDE-RGGIVVDEYLRTSVPGIYAAGDCRVGGPE 292
|
....*....
gi 33519428 342 LTPVAIQAG 350
Cdd:pfam07992 293 LAQNAVAQG 301
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
56-478 |
7.19e-44 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 160.50 E-value: 7.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 56 GGTCVNVGCIPKKLMHQAALLGQALQDSRNYGwkVEETVKH-DWDRMIEAVQNHIGSLNWG---YRVALREKKVVYENAY 131
Cdd:PRK07846 34 GGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIAAGgeeYRGRDTPNIDVYRGHA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 132 gQFIGPHRIKAtnnkGKEKIYSAERFLIATGERPRYLGIPGDKE--YcISSDDLFSLPYCPGKTLVVGASYVALECAGFL 209
Cdd:PRK07846 112 -RFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSGvrY-HTSDTIMRLPELPESLVIVGGGFIAAEFAHVF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 210 AGIGLDVTVMVRS-ILLRGFDQDMANKIGEHMEEHgIKFIRQFVPIKVEQIEAGtpgrlrvVAQSTNSEEIIEGEynTVM 288
Cdd:PRK07846 186 SALGVRVTVVNRSgRLLRHLDDDISERFTELASKR-WDVRLGRNVVGVSQDGSG-------VTLRLDDGSTVEAD--VLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 289 LAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAG-STVKCDY 367
Cdd:PRK07846 256 VATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV-SSPYQLKHVANHEARVVQHNLLHPdDLIASDH 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 368 ENVPTTVFTPLEYGACGLSEEKAVEKfgEENIEVYH------SYFWPLEWTipsrdnnKCYAKIICNtKDNERVVGFHVL 441
Cdd:PRK07846 334 RFVPAAVFTHPQIASVGLTENEARAA--GLDITVKVqnygdvAYGWAMEDT-------TGFVKLIAD-RDTGRLLGAHII 403
|
410 420 430
....*....|....*....|....*....|....*...
gi 33519428 442 GPNAGEVTQGFAAALKCGLTKKQL-DSTIGIHPVCAEV 478
Cdd:PRK07846 404 GPQASTLIQPLIQAMSFGLDAREMaRGQYWIHPALPEV 441
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
10-488 |
2.55e-41 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 154.31 E-value: 2.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 10 SYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDFVTPTPLGTRwgLGGTCVNVGCIPKK-LMHQAALLGQALQDSRNYGW 88
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNPKGKPA--LGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 89 KVEEtVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIG----PHRIKATnNKGKEKIySAERFLIATGER 164
Cdd:PRK06327 80 HVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGktdaGYEIKVT-GEDETVI-TAKHVIIATGSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 165 PRYL-GIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEE 242
Cdd:PRK06327 157 PRHLpGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 243 HGIKFIrqfVPIKVEQIEAGTPGrLRVVAQSTNSEEIIEgEYNTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEE 322
Cdd:PRK06327 237 QGLDIH---LGVKIGEIKTGGKG-VSVAYTDADGEAQTL-EVDKLIVSIGRVPNTDGLGLEAVGLKLDER-GFIPVDDHC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 323 QTNVPYIYAIGDILEdKVELTPVAIQAGRLLAQRLyAGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVekfgEENIEVY 402
Cdd:PRK06327 311 RTNVPNVYAIGDVVR-GPMLAHKAEEEGVAVAERI-AGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLK----AEGVEYK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 403 HSYFwplewtiPSRDNNKC--------YAKIICNTKdNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPV 474
Cdd:PRK06327 385 AGKF-------PFMANGRAlamgepdgFVKIIADAK-TDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPT 456
|
490
....*....|....*.
gi 33519428 475 CAEVF--TTLSVTKRS 488
Cdd:PRK06327 457 LSEVWheAALAVDKRP 472
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
56-478 |
4.07e-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: 4.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 56 GGTCVNVGCIPKKLMHQAALLGQALQDSRNYGwkVEETVKH-DWDRMIEAVQNH----IGSLNWGYRVALREKKVVYENA 130
Cdd:TIGR03452 35 GGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRVFGDridpIAAGGEDYRRGDETPNIDVYDG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 131 YGQFIGPHRIKAtnnkGKEKIYSAERFLIATGERPR---YLGIPGDKEYciSSDDLFSLPYCPGKTLVVGASYVALECAG 207
Cdd:TIGR03452 113 HARFVGPRTLRT----GDGEEITGDQIVIAAGSRPYippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGYIAAEFAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 208 FLAGIGLDVTVMVRS-ILLRGFDQDMANKIGE----HMEEHGIKFIrqfvpIKVEQIEAGtpgrlrvVAQSTNSEEIIEG 282
Cdd:TIGR03452 187 VFSALGTRVTIVNRStKLLRHLDEDISDRFTEiakkKWDIRLGRNV-----TAVEQDGDG-------VTLTLDDGSTVTA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 283 EynTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDkVELTPVAIQAGRLLAQRL-YAGS 361
Cdd:TIGR03452 255 D--VLLVATGRVPNGDLLDAEAAGVEVDED-GRIKVDEYGRTSARGVWALGDVSSP-YQLKHVANAEARVVKHNLlHPND 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 362 TVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYH----SYFWPLEWTipsrdnnKCYAKIICNtKDNERVVG 437
Cdd:TIGR03452 331 LRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIQNygdvAYGWAMEDT-------TGFCKLIAD-RDTGKLLG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 33519428 438 FHVLGPNAGEVTQGFAAALKCGLTKKQL-DSTIGIHPVCAEV 478
Cdd:TIGR03452 403 AHIIGPQASSLIQPLITAMAFGLDAREMaRKQYWIHPALPEV 444
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
370-482 |
1.42e-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: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 370 VPTTVFTPLEYGACGLSEEKAVEKFGEenIEVYHSYFWPLEWTIPSRDNnKCYAKIICNtKDNERVVGFHVLGPNAGEVT 449
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDT-DGFVKLVAD-RETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 33519428 450 QGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 482
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
31-465 |
6.17e-36 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 140.29 E-value: 6.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 31 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQaLQDSRNYGWKVEETVKH-DWDRMIEAVQNhi 109
Cdd:PRK13748 117 AVEQGARVTLIE---------RGTIGGTCVNVGCVPSKIMIRAAHIAH-LRRESPFDGGIAATVPTiDRSRLLAQQQA-- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 110 gslnwgyRV-ALREKKvvYEN------------AYGQFIGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKE- 175
Cdd:PRK13748 185 -------RVdELRHAK--YEGildgnpaitvlhGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKEt 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 176 -YCISSDDLFSlPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLrgFDQDMAnkIGEHM----EEHGIKFIrq 250
Cdd:PRK13748 256 pYWTSTEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLF--FREDPA--IGEAVtaafRAEGIEVL-- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 251 fvpikvEQIEAGTpgrlrvVAQStNSEEIIEGEYNTV-----MLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTN 325
Cdd:PRK13748 329 ------EHTQASQ------VAHV-DGEFVLTTGHGELradklLVATGRAPNTRSLALDAAGVTVNAQ-GAIVIDQGMRTS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 326 VPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTvKCDYENVPTTVFTPLEYGACGLSEEKAvekfGEENIEVyHSY 405
Cdd:PRK13748 395 VPHIYAAGDC-TDQPQFVYVAAAAGTRAAINMTGGDA-ALDLTAMPAVVFTDPQVATVGYSEAEA----HHDGIET-DSR 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33519428 406 FWPLEwTIPSRDNN---KCYAKIICNTKDNeRVVGFHVLGPNAGEVTQGFAAALKCGLTKKQL 465
Cdd:PRK13748 468 TLTLD-NVPRALANfdtRGFIKLVIEEGSG-RLIGVQAVAPEAGELIQTAALAIRNRMTVQEL 528
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
8-447 |
3.00e-35 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 136.82 E-value: 3.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 8 PKSYDYDLIIIGGGSGGLAAAKEAAQYGKKVMVLDfvtptplgTRWGLGGTCVNVGCIPKKLMHQAAL-LGQALQDS--R 84
Cdd:PRK05249 1 MHMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlyS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 85 NYGWKVEETVKHDWDRMIEAVQNHIGSLnwgyRVALREKKVVYENAYGQFIGPHRIKATNNKGKEKIYSAERFLIATGER 164
Cdd:PRK05249 73 SYRVKLRITFADLLARADHVINKQVEVR----RGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 165 P-RYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEE 242
Cdd:PRK05249 149 PyRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 243 HGIKFI-RQfvpiKVEQIEAGTPGRLRVVAqstnSEEIIEGEynTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDE 321
Cdd:PRK05249 229 SGVTIRhNE----EVEKVEGGDDGVIVHLK----SGKKIKAD--CLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNEN 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 322 EQTNVPYIYAIGDiledkV----ELTPVAIQAGRLLAQRLYaGSTVKCDYENVPTTVFTPLEYGACGLSEEKAVekfgEE 397
Cdd:PRK05249 298 YQTAVPHIYAVGD-----VigfpSLASASMDQGRIAAQHAV-GEATAHLIEDIPTGIYTIPEISSVGKTEQELT----AA 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 33519428 398 NI--EVYHSYFWPLewtipSR-----DNNKCYaKIICNTKDnERVVGFHVLGPNAGE 447
Cdd:PRK05249 368 KVpyEVGRARFKEL-----ARaqiagDNVGML-KILFHRET-LEILGVHCFGERATE 417
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
56-477 |
2.88e-29 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 119.47 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 56 GGTCVNVGCIPKKLMHQAAllgqalqdsrNYGWKVEETVKHDwdrmiEAVQNHIGSLNWGyrvALREKKVVYENAYGQFI 135
Cdd:PRK07251 40 GGTCINIGCIPTKTLLVAA----------EKNLSFEQVMATK-----NTVTSRLRGKNYA---MLAGSGVDLYDAEAHFV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 136 GPHRIKATnnKGKEKI-YSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGI 212
Cdd:PRK07251 102 SNKVIEVQ--AGDEKIeLTAETIVINTGAVSNVLPIPGlaDSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 213 GLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpIKVEQIEAGTPGrlrvVAQSTNSEEIIegeYNTVMLAI 291
Cdd:PRK07251 180 GSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLN---AHTTEVKNDGDQ----VLVVTEDETYR---FDALLYAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 292 GRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYAGSTVKC-DYENV 370
Cdd:PRK07251 250 GRKPNTEPLGLENTDIELTER-GAIKVDDYCQTSVPGVFAVGDV-NGGPQFTYISLDDFRIVFGYLTGDGSYTLeDRGNV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 371 PTTVFTPLEYGACGLSEEKAVEKFGEenievYHSYFWPLEWTIPSRDNN--KCYAKIICNTKDNErVVGFHVLGPNAGEV 448
Cdd:PRK07251 328 PTTMFITPPLSQVGLTEKEAKEAGLP-----YAVKELLVAAMPRAHVNNdlRGAFKVVVNTETKE-ILGATLFGEGSQEI 401
|
410 420
....*....|....*....|....*....
gi 33519428 449 TQGFAAALKCGLTKKQLDSTIGIHPVCAE 477
Cdd:PRK07251 402 INLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
56-482 |
2.22e-28 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 117.19 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 56 GGTCVNVGCIP-KKLMHQAALlgqalqdsrnygwkveetvKHDWDRMIeAVQNHIGSLnwgyrvaLREK---------KV 125
Cdd:NF040477 40 GGTCINIGCIPtKTLVHDAEQ-------------------HQDFSTAM-QRKSSVVGF-------LRDKnyhnladldNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 126 VYENAYGQFIGPHRIKATNNKGKEKIYsAERFLIATGERPRYLGIPGDKEY--CISSDDLFSLPYCPGKTLVVGASYVAL 203
Cdd:NF040477 93 DVINGRAEFIDNHTLRVFQADGEQELR-GEKIFINTGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 204 ECAGFLAGIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIrqfVPIKVEQIEAgTPGRLRVVAQstnseeiiEG 282
Cdd:NF040477 172 EFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVELI---LNAQVQRVSS-HEGEVQLETA--------EG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 283 EY--NTVMLAIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLY-A 359
Cdd:NF040477 240 VLtvDALLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLgE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 360 GSTVKCDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEwTIPSrdnnkcyAKIICNTK--------- 430
Cdd:NF040477 318 GKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTL-----PVA-AIPR-------ARVMNDTRgvlkavvdn 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 33519428 431 DNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 482
Cdd:NF040477 385 KTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDL 436
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
31-481 |
3.96e-26 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 112.31 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 31 AAQYGKKVMVLDfvtptplGTRWGLGGTCVNVGCIPKKLMHQAA----------------LLGQALQDSRNYGWK----V 90
Cdd:PTZ00153 135 AMERGLKVIIFT-------GDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVErnqlV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 91 EETVKHDWDRMIEAVQNHIGSLNWGYRVALREKKVVYENAYGQFIGPH-RIKATNNKGKEK---IYSAERFLIATGERPR 166
Cdd:PTZ00153 208 ADTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKFCKNSEHVQVIYERgHIVDKNTIKSEKsgkEFKVKNIIIATGSTPN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 167 Y-LGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANkigeHMEEHG 244
Cdd:PTZ00153 288 IpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLLPLLDADVAK----YFERVF 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 245 IKF--IRQFVPIKVEQIEAGTPGRLRVVAQS-----------TNSEEIIEGEYNTVMLAIGRDACTRKIGLETVGVKINE 311
Cdd:PTZ00153 364 LKSkpVRVHLNTLIEYVRAGKGNQPVIIGHSerqtgesdgpkKNMNDIKETYVDSCLVATGRKPNTNNLGLDKLKIQMKR 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 312 ktGKIPVTD------EEQTNVPYIYAIGD-----ILEDKVELTPVAI------QAGRLLAQRLYAGSTVKCDYENVPTTV 374
Cdd:PTZ00153 444 --GFVSVDEhlrvlrEDQEVYDNIFCIGDangkqMLAHTASHQALKVvdwiegKGKENVNINVENWASKPIIYKNIPSVC 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 375 FTPLEYGACGLSEEKAVEKFGEENIEVYHSYF-------WPLEWTIPSRDNNKCYAKIICNT-------------KDNER 434
Cdd:PTZ00153 522 YTTPELAFIGLTEKEAKELYPPDNVGVEISFYkanskvlCENNISFPNNSKNNSYNKGKYNTvdntegmvkivylKDTKE 601
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 33519428 435 VVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTT 481
Cdd:PTZ00153 602 ILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
56-482 |
3.13e-23 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 102.01 E-value: 3.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 56 GGTCVNVGCIPKKLMhqaallgqaLQDSRNYGwkveetvkhDWDRMIE---AVQNHIGSLNWGYRVALREKKVVYENAyg 132
Cdd:PRK08010 40 GGTCINIGCIPTKTL---------VHDAQQHT---------DFVRAIQrknEVVNFLRNKNFHNLADMPNIDVIDGQA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 133 QFIGPHRIKaTNNKGKEKIYSAERFLIATGERPRYLGIPG--DKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLA 210
Cdd:PRK08010 100 EFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIPGitTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 211 GIGLDVTVM-VRSILLRGFDQDMANKIGEHMEEHGIKFIRQfvpikvEQIEAGTPGRLRVVAQSTNSEEIIEGeyntVML 289
Cdd:PRK08010 179 NFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILN------AHVERISHHENQVQVHSEHAQLAVDA----LLI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 290 AIGRDACTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDIlEDKVELTPVAIQAGRLLAQRLYA-GSTVKCDYE 368
Cdd:PRK08010 249 ASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNIWAMGDV-TGGLQFTYISLDDYRIVRDELLGeGKRSTDDRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 369 NVPTTVFTPLEYGACGLSEEKAVEKFGEENIEVYhsyfwPLEWTIPSR--DNNKCYAKIICNTKdNERVVGFHVLGPNAG 446
Cdd:PRK08010 327 NVPYSVFMTPPLSRVGMTEEQARESGADIQVVTL-----PVAAIPRARvmNDTRGVLKAIVDNK-TQRILGASLLCVDSH 400
|
410 420 430
....*....|....*....|....*....|....*.
gi 33519428 447 EVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 482
Cdd:PRK08010 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
31-473 |
3.93e-23 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 101.86 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 31 AAQYGKKVMVLDfvtptplgtRWGLGGTCVNVGCIPKKLMHQAALLGQALQDSRNYGWKVEETVKHDWDrmIEAVQNHIG 110
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEARVD--LPAVNARVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 111 SL----NWGYRVALREKKVVYENAYGQFI----GPHRIKATNNKGKEKIYSAERFLIATGERPRYLgiPG---DKEYCIS 179
Cdd:PRK07845 89 ALaaaqSADIRARLEREGVRVIAGRGRLIdpglGPHRVKVTTADGGEETLDADVVLIATGASPRIL--PTaepDGERILT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 180 SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVT-VMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQ 258
Cdd:PRK07845 167 WRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 259 IEAGtpgrlrVVAQSTNSEEiIEGEYntVMLAIGRDACTRKIGLETVGVKINEkTGKIPVTDEEQTNVPYIYAIGDIlED 338
Cdd:PRK07845 247 TGDG------VVVTLTDGRT-VEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIYAAGDC-TG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 339 KVELTPVAIQAGRL-LAQRLyaGSTVK-CDYENVPTTVFTPLEYGACGLSeEKAVEKfGEENIEVYhsyfwplewTIPSR 416
Cdd:PRK07845 316 VLPLASVAAMQGRIaMYHAL--GEAVSpLRLKTVASNVFTRPEIATVGVS-QAAIDS-GEVPARTV---------MLPLA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33519428 417 DNNKC--------YAKIICnTKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHP 473
Cdd:PRK07845 383 TNPRAkmsglrdgFVKLFC-RPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYP 446
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
136-352 |
4.44e-21 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 93.65 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 136 GPHRIKATNnkgkEKIYSAERFLIATGERPRYLGIPGDKE-------YCISSDdlfsLPYCPGKT-LVVGASYVALECAG 207
Cdd:COG0492 87 GPFRVTTDD----GTEYEAKAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEAL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 208 FLAGIGLDVTVMVRSILLRGfDQDMANKIGEHmeeHGIKFIRQFVPIKVEqieaGTPGRLRVVAQSTNSEEIIEGEYNTV 287
Cdd:COG0492 159 YLTKFASKVTLIHRRDELRA-SKILVERLRAN---PKIEVLWNTEVTEIE----GDGRVEGVTLKNVKTGEEKELEVDGV 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33519428 288 MLAIGRDACTRkiGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDKVELTPVAIQAGRL 352
Cdd:COG0492 231 FVAIGLKPNTE--LLKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAI 292
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
158-374 |
5.76e-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: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 158 LIATGERPRYLGIPGdkeycISSDDLFSL--------------PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS- 222
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddadalrealkEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 223 ILLRGFDQDMANKIGEHMEEHGIKFIRQFvpiKVEQIEAGTpgrlRVVAQSTNSEEIiegEYNTVMLAIG--------RD 294
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGE---TVVAIDGDD----KVAVTLTDGEEI---PADLVVVAPGvrpntelaKD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 295 ActrkigletvGVKINEkTGKIPVTDEEQTNVPYIYAIGDILE---------DKVELTPVAIQAGRLLAQRLyAGSTVKc 365
Cdd:COG0446 228 A----------GLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtgktVYIPLASAANKQGRVAAENI-LGGPAP- 294
|
....*....
gi 33519428 366 dYENVPTTV 374
Cdd:COG0446 295 -FPGLGTFI 302
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
192-268 |
4.60e-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: 4.60e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33519428 192 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPGRLR 268
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDrLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
158-357 |
9.40e-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: 9.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 158 LIATGERPRYLGIPG-DKEYCI---SSDDLFSL-PYCPGKT--LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGF 228
Cdd:COG1251 103 VLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 229 DQDMANKIGEHMEEHGIKFIRQfvpIKVEQIEaGTPGRLRVVaqsTNSEEIIEGEynTVMLAIG---RDACTRKIGLETV 305
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVRLG---TGVTEIE-GDDRVTGVR---LADGEELPAD--LVVVAIGvrpNTELARAAGLAVD 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33519428 306 -GVKINEKTgkipvtdeeQTNVPYIYAIGDILE--------DKVELTPVAIQAGRLLAQRL 357
Cdd:COG1251 254 rGIVVDDYL---------RTSDPDIYAAGDCAEhpgpvygrRVLELVAPAYEQARVAAANL 305
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
192-337 |
2.22e-13 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 72.12 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 192 KTLVVGASYVALECAGFLAGIGLDVTVMVRSI-LLRGFDQDMANKIGEHMEEHGIkfirqfvPIKVEQIEAGTPGRLrVV 270
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREI-------PYRLNEEIDAINGNE-VT 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33519428 271 AQSTNSEEiiegeYNTVMLAIGRDACTRKIglETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILE 337
Cdd:PRK13512 222 FKSGKVEH-----YDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIIT 280
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
159-391 |
7.06e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 64.00 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 159 IATGERPRYLGIPGDKEYCI---SSDDLFSL------------PYCPGKTLVVGASYVALECAGFLA----------GIG 213
Cdd:COG1252 103 IATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAellrkllrypGID 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 214 LD------VTVMVRsiLLRGFDQDMANKIGEHMEEHGIKFIRQFvpiKVEQIEAGTpgrlrvvAQSTNSEEIiegEYNTV 287
Cdd:COG1252 183 PDkvritlVEAGPR--ILPGLGEKLSEAAEKELEKRGVEVHTGT---RVTEVDADG-------VTLEDGEEI---PADTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 288 MLAIGRDA--CTRKIGLETvgvkinEKTGKIPVTDEEQT-NVPYIYAIGDI--LEDKVELT-----PVAIQAGRLLAQRL 357
Cdd:COG1252 248 IWAAGVKAppLLADLGLPT------DRRGRVLVDPTLQVpGHPNVFAIGDCaaVPDPDGKPvpktaQAAVQQAKVLAKNI 321
|
250 260 270
....*....|....*....|....*....|....*
gi 33519428 358 YAgstvkcDYENVPTTVFTPLEYGA-CGLSEEKAV 391
Cdd:COG1252 322 AA------LLRGKPLKPFRYRDKGClASLGRGAAV 350
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
194-465 |
3.84e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 61.98 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 194 LVVGASYVALECAGFLAGIGLDVTVMVRS--ILLRGFDQDMANKIGEHMEEHGIKFirqFVPIKVEQIEagtpGRLRVVA 271
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVEL---HLNEFVKSLI----GEDKVEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 272 QSTNseeiiEGEYNT--VMLAIGRDACTRKI---GLETVgvkineKTGKIPVTDEEQTNVPYIYAIGD------ILEDKV 340
Cdd:PRK09564 226 VVTD-----KGEYEAdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKN 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 341 ELTPVAIQA---GRLLAQRLyAGSTVKcdyenVPTT-------VFTpLEYGACGLSEEKAVEKfgeeNIEVY-------- 402
Cdd:PRK09564 295 VYVPLATTAnklGRMVGENL-AGRHVS-----FKGTlgsacikVLD-LEAARTGLTEEEAKKL----GIDYKtvfikdkn 363
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33519428 403 HSYFWPlewtipsrDNNKCYAKIICNtKDNERVVGFHVLGPNaGEV--TQGFAAALKCGLTKKQL 465
Cdd:PRK09564 364 HTNYYP--------GQEDLYVKLIYE-ADTKVILGGQIIGKK-GAVlrIDALAVAIYAKLTTQEL 418
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
158-335 |
2.71e-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: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 158 LIATG-ERPRYLGIPG-DKEYCIS----------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIG-LDVTVMVRsil 224
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 225 lRGFDqDMANKIGE--HMEEHGIKFIRQFVP-------------IKVEQIEAGTP---GRLRVVAqSTNSEEIIEGEynT 286
Cdd:COG0493 288 -RTRE-EMPASKEEveEALEEGVEFLFLVAPveiigdengrvtgLECVRMELGEPdesGRRRPVP-IEGSEFTLPAD--L 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 33519428 287 VMLAIGRDACTRKIgLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDI 335
Cdd:COG0493 363 VILAIGQTPDPSGL-EEELGLELDKR-GTI-VVDEEtyQTSLPGVFAGGDA 410
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
158-357 |
4.71e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 55.00 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 158 LIATGE-RPRYLGIPG-DKEYCISS-DDLFS-----LPYCP---------GKTLVVGASYVALECA--GFLAGiGLDVTV 218
Cdd:PRK12770 123 LIATGTwKSRKLGIPGeDLPGVYSAlEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAAleAVLLG-AEKVYL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 219 MVRsillRGFDQDMANKIG-EHMEEHGIKFIRQFVP--------------IKVEQIEAGTPGRLRVVAQsTNSEEIIegE 283
Cdd:PRK12770 202 AYR----RTINEAPAGKYEiERLIARGVEFLELVTPvriigegrvegvelAKMRLGEPDESGRPRPVPI-PGSEFVL--E 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 33519428 284 YNTVMLAIGRDAcTRKIGLETVGVKINEKtGKIPVTDEEQTNVPYIYAIGDILEDKVELTPvAIQAGRLLAQRL 357
Cdd:PRK12770 275 ADTVVFAIGEIP-TPPFAKECLGIELNRK-GEIVVDEKHMTSREGVFAAGDVVTGPSKIGK-AIKSGLRAAQSI 345
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
150-337 |
7.74e-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: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 150 KIYSAERFLIATGERPRYLGIPG-DKEYCI---SSDDLFSLPYCPGKTL---VVGASYVALECAGFLAGIGLDVTV--MV 220
Cdd:TIGR02374 93 RTLSYDKLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMDVSVihHA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 221 RSILLRGFDQDMANKIGEHMEEHGIKFIRQfvPIKVEQIEAGTPGRLRVvaqsTNSEEIiegEYNTVMLAIG---RDACT 297
Cdd:TIGR02374 173 PGLMAKQLDQTAGRLLQRELEQKGLTFLLE--KDTVEIVGATKADRIRF----KDGSSL---EADLIVMAAGirpNDELA 243
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 33519428 298 RKIGLetvgvKINektGKIPVTDEEQTNVPYIYAIGDILE 337
Cdd:TIGR02374 244 VSAGI-----KVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
144-359 |
7.86e-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: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 144 NNKGKEKIysaerFLIATGERPRYLGIPGDKEYCISSDDLF---------------SLPYCPGKTLVV-GASYVALECAG 207
Cdd:PRK12775 514 NDKGFDAV-----FLGVGAGAPTFLGIPGEFAGQVYSANEFltrvnlmggdkfpflDTPISLGKSVVViGAGNTAMDCLR 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 208 FLAGIGldvTVMVRSILLRGfDQDMANKIGE--HMEEHGIKFIRQFVPI-------------KVEQIEAGTP---GRLRV 269
Cdd:PRK12775 589 VAKRLG---APTVRCVYRRS-EAEAPARIEEirHAKEEGIDFFFLHSPVeiyvdaegsvrgmKVEEMELGEPdekGRRKP 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 270 VAqstnSEEIIEGEYNTVMLAIGRDAcTRKIGLETVGVKINeKTGKIPVTDE-----EQTNVPYIYAIGDILEDKVELTp 344
Cdd:PRK12775 665 MP----TGEFKDLECDTVIYALGTKA-NPIITQSTPGLALN-KWGNIAADDGklestQSTNLPGVFAGGDIVTGGATVI- 737
|
250
....*....|....*
gi 33519428 345 VAIQAGRLLAQRLYA 359
Cdd:PRK12775 738 LAMGAGRRAARSIAT 752
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
148-335 |
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 33519428 148 KEKIYSAerFLIATGE-RPRYLGIPGdkeycISSDDLFSL-----------PYCPG---------KTLVVGASYVALECA 206
Cdd:PRK12831 225 EEEGFDA--VFIGSGAgLPKFMGIPG-----ENLNGVFSAnefltrvnlmkAYKPEydtpikvgkKVAVVGGGNVAMDAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 207 GFLAGIGLDVTVMVRsillRGfDQDMANKIGE--HMEEHGIKFIRQFVPI-------------KVEQIEAGTP---GRLR 268
Cdd:PRK12831 298 RTALRLGAEVHIVYR----RS-EEELPARVEEvhHAKEEGVIFDLLTNPVeilgdengwvkgmKCIKMELGEPdasGRRR 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33519428 269 VVaQSTNSEEIIegEYNTVMLAIGRDAcTRKIGLETVGVKINEKtGKIpVTDEE--QTNVPYIYAIGDI 335
Cdd:PRK12831 373 PV-EIEGSEFVL--EVDTVIMSLGTSP-NPLISSTTKGLKINKR-GCI-VADEEtgLTSKEGVFAGGDA 435
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
154-335 |
1.59e-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: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 154 AERF---LIATGE-RPRYLGIPGDKEYCISS--------------DDLFSLPYCPGK-TLVVGASYVALECAGFLAGIGL 214
Cdd:PRK12778 515 EEGFkgiFIASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGKkVAVVGGGNTAMDSARTAKRLGA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 215 DvTVMvrsILLRGFDQDMANKIGE--HMEEHGIKF----------------IRQFVPIKVEQIEAGTPGRLRVVAqSTNS 276
Cdd:PRK12778 595 E-RVT---IVYRRSEEEMPARLEEvkHAKEEGIEFltlhnpieyladekgwVKQVVLQKMELGEPDASGRRRPVA-IPGS 669
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 277 EEIIEgeYNTVMLAIGRDActRKIGLETV-GVKINEKtGKIPVTDEEQTNVPYIYAIGDI 335
Cdd:PRK12778 670 TFTVD--VDLVIVSVGVSP--NPLVPSSIpGLELNRK-GTIVVDEEMQSSIPGIYAGGDI 724
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
158-355 |
1.96e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 53.26 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 158 LIATG-ERPRYLGIPGDK--------EYCISS---DDLFSLPycPGKTLVV-GASYVALECAGFLAGIGL-DVTVMVRsi 223
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDFLTRVnqaVADYDLP--VGKRVVViGGGNTAMDAARTAKRLGAeSVTIVYR-- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 224 llRGFDqDMANKIGE--HMEEHGIKFIRQFVPIKVEQIEAGTPG------RLRVVAQSTNSEEIIEGEY-----NTVMLA 290
Cdd:PRK11749 306 --RGRE-EMPASEEEveHAKEEGVEFEWLAAPVEILGDEGRVTGvefvrmELGEPDASGRRRVPIEGSEftlpaDLVIKA 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 33519428 291 IGRDAcTRKIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDIL--EDkveLTPVAIQAGRLLAQ 355
Cdd:PRK11749 383 IGQTP-NPLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIVtgAA---TVVWAVGDGKDAAE 445
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
152-333 |
1.01e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 50.30 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 152 YSAERFLIATGE--RPRYLGIPgdkEYCISSDDLFSL-PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGF 228
Cdd:pfam13738 117 YQARYVIIATGEfdFPNKLGVP---ELPKHYSYVKDFhPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDR 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 229 DQDMA--------NKIGEHMEEHGIKFIRQFVPIKVEQIEAGtpgrlrVVAQSTNSEEIIegEYNTVMLAIGRDaCTRKI 300
Cdd:pfam13738 194 DSDPSyslspdtlNRLEELVKNGKIKAHFNAEVKEITEVDVS------YKVHTEDGRKVT--SNDDPILATGYH-PDLSF 264
|
170 180 190
....*....|....*....|....*....|....
gi 33519428 301 gLETVGVKINEKtGKIPVTDE-EQTNVPYIYAIG 333
Cdd:pfam13738 265 -LKKGLFELDED-GRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
152-337 |
1.09e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 47.36 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 152 YSAERFLIATGERPRYLGIPGDKEY-------CISSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSIL 224
Cdd:PRK10262 104 YTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519428 225 LRGfDQDMANKIGEHMEEHGIKFIRQFVPIKVEQIEAGTPG-RLRVVAQSTNSEEIiegEYNTVMLAIGRDACTR----K 299
Cdd:PRK10262 181 FRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGvRLRDTQNSDNIESL---DVAGLFVAIGHSPNTAifegQ 256
|
170 180 190
....*....|....*....|....*....|....*...
gi 33519428 300 IGLETVGVKINEKTGKipvtDEEQTNVPYIYAIGDILE 337
Cdd:PRK10262 257 LELENGYIKVQSGIHG----NATQTSIPGVFAAGDVMD 290
|
|
| |
