|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
164-652 |
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: 826.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 164 HDYDLIVIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTSWGLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGWDY 243
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 244 NQQVKHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKIKATNKKGQETFYTASKFVIATGERPRYLGI 323
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 324 QGDKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGFDQEMAEKVGSYLEQQGVKFQRK 403
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 404 FTPILVQQLEKglpgrlKVVAKSTEGPETVEGTYNTVLLAIGRDSCTRKIGLEKIGVKINEKNGKIPVNDVEQTNVPHVY 483
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 484 AIGDVLEGKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYTKENLEVYHTFFWPLE 563
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 564 WTVAGRDN-NTCYAKIICNKFDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTMEITKSSG 642
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 296040479 643 LDITQKGCUG 652
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
161-652 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 549.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 161 DSTHDYDLIVIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTSWGLGGTCVNVGCIPKKLMHQAALLGHALQ-DARKY 239
Cdd:PTZ00052 1 HLTFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 240 GWDYNQqvKHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKIkATNKKGQETFYTASKFVIATGERPR 319
Cdd:PTZ00052 81 GWKTSS--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 320 YL-GIQGDKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGFDQEMAEKVGSYLEQQGV 398
Cdd:PTZ00052 158 IPeDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 399 KFQRKFTPILVQQLEKglpgRLKVV--AKSTEgpetvegTYNTVLLAIGRDSCTRKIGLEKIGVKINEKNGKIPVNDVeq 476
Cdd:PTZ00052 238 LFLEGVVPINIEKMDD----KIKVLfsDGTTE-------LFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 477 TNVPHVYAIGDVLEGKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYTKENLEVYH 556
Cdd:PTZ00052 305 TNIPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 557 TFFWPLEWTVAGRD--------------NNTCYAKIICNKFDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTI 622
Cdd:PTZ00052 385 QEFNTLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMI 464
|
490 500 510
....*....|....*....|....*....|
gi 296040479 623 GIHPTCGEVFTTMEITKSSGLDITQKGCUG 652
Cdd:PTZ00052 465 GIHPTDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
163-635 |
3.54e-143 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 424.18 E-value: 3.54e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 163 THDYDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGHALQD-ARKYGW 241
Cdd:PRK06116 2 TKDYDLIVIGGGSGGIASANRAAMYGAKVALIE---------AKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 242 DYNQQvKHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKIKATNKKgqetfYTASKFVIATGERPRYL 321
Cdd:PRK06116 73 DVTEN-KFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 322 GIQGdKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRSVL-LRGFDQEMAEKVGSYLEQQGVKF 400
Cdd:PRK06116 147 DIPG-AEYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 401 QRKFTPilvQQLEKGLPGRLKVvakSTEGPETVegTYNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVP 480
Cdd:PRK06116 226 HTNAVP---KAVEKNADGSLTL---TLEDGETL--TVDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 481 HVYAIGDVlEGKPELTPVAIQAGKLLARRLF-GISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYTKENLEVYHTFF 559
Cdd:PRK06116 297 GIYAVGDV-TGRVELTPVAIAAGRRLSERLFnNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSF 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296040479 560 WPLEWTVAGRDNnTCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTM 635
Cdd:PRK06116 376 TPMYTALTGHRQ-PCLMKLVVVG-KEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
163-635 |
2.32e-131 |
|
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: 394.07 E-value: 2.32e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 163 THDYDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGWD 242
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 243 YnQQVKHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKIKATnkkGQETfYTASKFVIATGERPRYLG 322
Cdd:COG1249 72 A-GAPSVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT---GGET-LTADHIVIATGSRPRVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 323 IQG-DKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKF 400
Cdd:COG1249 147 IPGlDEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 401 QRKFTpilVQQLEKGlPGRLKVVAKSTEGPETVEGTYntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVP 480
Cdd:COG1249 227 LTGAK---VTSVEKT-GDGVTVTLEDGGGEEAVEADK--VLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 481 HVYAIGDVLeGKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMytKENLEVYHTFFW 560
Cdd:COG1249 300 GIYAIGDVT-GGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREA--GIDVKVGKFPFA 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296040479 561 PLEWTVAGRDNnTCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTM 635
Cdd:COG1249 377 ANGRALALGET-EGFVKLIADA-ETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
166-635 |
3.18e-111 |
|
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: 342.20 E-value: 3.18e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 166 YDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGWDYNQ 245
Cdd:TIGR01421 3 YDYLVIGGGSGGIASARRAAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 246 QVKHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKIKATNKKgqetfYTASKFVIATGERPRYL-GIQ 324
Cdd:TIGR01421 74 ENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 325 GdKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFDQEMAEKVGSYLEQQGVKFQRK 403
Cdd:TIGR01421 149 G-AELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 404 FTPIlvqQLEKGLPGRLKV-VAKSTEGPETVEgtyntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHV 482
Cdd:TIGR01421 228 SKPV---KVEKTVEGKLVIhFEDGKSIDDVDE-----LIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGI 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 483 YAIGDVLeGKPELTPVAIQAGKLLARRLF-GISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYTKENLEVYHTFFWP 561
Cdd:TIGR01421 299 YALGDVV-GKVELTPVAIAAGRKLSERLFnGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTP 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296040479 562 LEWTVaGRDNNTCYAKIIC-NKfdNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTM 635
Cdd:TIGR01421 378 MYYAM-TSEKQKCRMKLVCaGK--EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
165-635 |
2.44e-106 |
|
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: 329.46 E-value: 2.44e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 165 DYDLIVIGGGSGGLSCAKEAANLGKKVMV--LDFVvpspqgtswglGGTCVNVGCIPKKLMHQAALLGHALQDARKYGWD 242
Cdd:TIGR01424 2 DYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 243 yNQQVKHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKIKATNKKGQetfYTASKFVIATGERPRYLG 322
Cdd:TIGR01424 71 -VGKARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKPA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 323 IQGdKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFDQEMAEKVGSYLEQQGVKFQ 401
Cdd:TIGR01424 147 LPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRIL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 402 RKftpILVQQLEKGLPGRLKVVAKSTEGPETvegtyNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPH 481
Cdd:TIGR01424 226 PE---DSITSISKDDDGRLKATLSKHEEIVA-----DVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTPS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 482 VYAIGDVLEgKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYTKenLEVYHTFFWP 561
Cdd:TIGR01424 297 IYAVGDVTD-RINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRP 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296040479 562 LEWTVAGRDNNtCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTM 635
Cdd:TIGR01424 374 MKATFSGRQEK-TLMKLVVDA-KDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
164-635 |
4.40e-104 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 327.22 E-value: 4.40e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 164 HDYDLIVIGGGSGGLSCAKEAANLGKKVMV--LDFVVPSPQGTSwGLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGW 241
Cdd:PLN02546 78 YDFDLFTIGAGSGGVRASRFASNFGASAAVceLPFATISSDTLG-GVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGW 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 242 DYNQQVKHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKIKATNKkgqetFYTASKFVIATGERPRYL 321
Cdd:PLN02546 157 KYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGK-----LYTARNILIAVGGRPFIP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 322 GIQGdKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRSV-LLRGFDQEMAEKVGSYLEQQGVKF 400
Cdd:PLN02546 232 DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAEQMSLRGIEF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 401 QRKFTPilvQQLEKGLPGRLKVvaKSTEGpeTVEGtYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVP 480
Cdd:PLN02546 311 HTEESP---QAIIKSADGSLSL--KTNKG--TVEG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 481 HVYAIGDVLEgKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYTkeNLEVYHTFFW 560
Cdd:PLN02546 382 SIWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYG--DVDVFTANFR 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296040479 561 PLEWTVAGRDNNTCYAKIICNKfdNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTM 635
Cdd:PLN02546 459 PLKATLSGLPDRVFMKLIVCAK--TNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTM 531
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
160-635 |
1.04e-103 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 324.46 E-value: 1.04e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 160 DDSTHDYDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvVP-SPQGTSW--GLGGTCVNVGCIPKKLMHQAALLGHALQDA 236
Cdd:PLN02507 20 NATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICE--LPfHPISSESigGVGGTCVIRGCVPKKILVYGATFGGEFEDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 237 RKYGWDYNQQVKHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKIKATNKKGQETFYTASKFVIATGE 316
Cdd:PLN02507 98 KNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 317 RPRYLGIQGdKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRSVL-LRGFDQEMAEKVGSYLEQ 395
Cdd:PLN02507 178 RAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMRAVVARNLEG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 396 QGVKFQRKFTpilVQQLEKgLPGRLKVVAKSTEgpetvEGTYNTVLLAIGRDSCTRKIGLEKIGVKInEKNGKIPVNDVE 475
Cdd:PLN02507 257 RGINLHPRTN---LTQLTK-TEGGIKVITDHGE-----EFVADVVLFATGRAPNTKRLNLEAVGVEL-DKAGAVKVDEYS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 476 QTNVPHVYAIGDVlEGKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYTKENLeVY 555
Cdd:PLN02507 327 RTNIPSIWAIGDV-TNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGDIL-VF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 556 HTFFWPLEWTVAGRDNNTcYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTM 635
Cdd:PLN02507 405 TSSFNPMKNTISGRQEKT-VMKLIVDA-ETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTM 482
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
166-631 |
2.38e-89 |
|
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: 285.69 E-value: 2.38e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 166 YDLIVIGGGSGGLSCAKEAANLGKKVMVldfvVPSPQgtswgLGGTCVNVGCIPKK-LMHQAALLgHALQDARKYGWDYN 244
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVAL----VEKEY-----LGGTCLNVGCIPTKaLLHSAEVY-DEIKHAKDLGIEVE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 245 QqVKHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKIKATNKKGQETfYTASKFVIATGERPRYL--G 322
Cdd:TIGR01350 72 N-VSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLpgP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 323 IQGDKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTV---MVRsvLLRGFDQEMAEKVGSYLEQQGVK 399
Cdd:TIGR01350 150 FDFDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTViemLDR--ILPGEDAEVSKVLQKALKKKGVK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 400 FqrkFTPILVQQLEKGlpGRLKVVAKSTEGPETVEGTYntVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNV 479
Cdd:TIGR01350 228 I---LTNTKVTAVEKN--DDQVTYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDE-RGRIVVDEYMRTNV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 480 PHVYAIGDVLeGKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEmytkENLEVYHTFF 559
Cdd:TIGR01350 300 PGIYAIGDVI-GGPMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKE----AGYDVKIGKF 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296040479 560 wPLewTVAGR----DNNTCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 631
Cdd:TIGR01350 375 -PF--AANGKalalGETDGFVKIIADK-KTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
165-635 |
2.52e-86 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 280.73 E-value: 2.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 165 DYDLIVIGGGSGGLSCAKEAANLGKKVMVLDFVVpspqgtswgLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGWDyn 244
Cdd:PTZ00058 48 VYDLIVIGGGSGGMAAARRAARNKAKVALVEKDY---------LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFD-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 245 QQVKHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKIKATNKKGQETFY------------------- 305
Cdd:PTZ00058 117 TQFSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKVSQVDGEAdesdddevtivsagvsqld 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 306 -----TASKFVIATGERPRYLGIQGdKEYCITSDDLFSLPYcPGNTLIVGASYVGLECAGFLAGLGLDVTVMVR-SVLLR 379
Cdd:PTZ00058 197 dgqviEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 380 GFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKglPGRLKVVAKSTEgpetvEGTYNTVLLAIGRDSCTRKIGLEkiG 459
Cdd:PTZ00058 275 KFDETIINELENDMKKNNINIITHANVEEIEKVKE--KNLTIYLSDGRK-----YEHFDYVIYCVGRSPNTEDLNLK--A 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 460 VKINEKNGKIPVNDVEQTNVPHVYAIGDVLEGKP---------------------------------ELTPVAIQAGKLL 506
Cdd:PTZ00058 346 LNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvQLTPVAINAGRLL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 507 ARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYTKENLEVYHTFFWPLEWTV---AGRDNNTCYAKIICNKf 583
Cdd:PTZ00058 426 ADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVydmDPAQKEKTYLKLVCVG- 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 296040479 584 DNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTM 635
Cdd:PTZ00058 505 KEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
166-635 |
1.62e-81 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 266.07 E-value: 1.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 166 YDLIVIGGGSGGLSCAKEAANL-GKKVMVLDfvVPSPQGTSW--GLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGWD 242
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATLyKKRVAVVD--VQTHHGPPFyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 243 YNQQ-VKHNWETMREAIQNHIGSLNWGYRVTLRE-KGVTYVNSFGEFVELHKIKA-----TNKKGQETFyTASKFVIATG 315
Cdd:TIGR01423 82 FDRSsVKANWKALIAAKNKAVLDINKSYEGMFADtEGLTFFLGWGALEDKNVVLVresadPKSAVKERL-QAEHILLATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 316 ERPRYLGIQGDkEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAG---LGLDVTVMVR-SVLLRGFDQEMAEKVGS 391
Cdd:TIGR01423 161 SWPQMLGIPGI-EHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 392 YLEQQGVKFQRKFTPilvQQLEKGLPGRLKVVAKSTEgpetvEGTYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPV 471
Cdd:TIGR01423 240 QLRANGINIMTNENP---AKVTLNADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELT-KKGAIQV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 472 NDVEQTNVPHVYAIGDVlEGKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYtkEN 551
Cdd:TIGR01423 311 DEFSRTNVPNIYAIGDV-TDRVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EK 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 552 LEVYHTFFWPLEWTVAGRDNNTCYAKIICNKFDNDrVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 631
Cdd:TIGR01423 388 VAVYESSFTPLMHNISGSKYKKFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEE 466
|
....
gi 296040479 632 FTTM 635
Cdd:TIGR01423 467 LCSM 470
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
163-634 |
1.33e-80 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 262.42 E-value: 1.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 163 THDYDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGWD 242
Cdd:PRK06292 1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 243 YnQQVKHNWETMREAIQNHIGSLNWGYRVTLREK-GVTYVNSFGEFVELHKIKATnkkgqETFYTASKFVIATGER-PRY 320
Cdd:PRK06292 72 A-DGPKIDFKKVMARVRRERDRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEVN-----GERIEAKNIVIATGSRvPPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 321 LGI-QGDKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQgV 398
Cdd:PRK06292 146 PGVwLILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-F 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 399 KFqrkFTPILVQQLEKGlPGRLKVVAKSTEGPETVEGTYntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTN 478
Cdd:PRK06292 225 KI---KLGAKVTSVEKS-GDEKVEELEKGGKTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 479 VPHVYAIGDVLeGKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYtkenlEVYHTF 558
Cdd:PRK06292 298 VPGIYAAGDVN-GKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAG-----IDYVVG 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296040479 559 FWPLEWTVAGR-DNNTCYA-KIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLT-KQLLdDTIGIHPTCGEVFTT 634
Cdd:PRK06292 372 EVPFEAQGRARvMGKNDGFvKVYADK-KTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTvEDLL-RMPFYHPTLSEGLRT 448
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
165-636 |
4.55e-77 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 253.53 E-value: 4.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 165 DYDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGwdyn 244
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFG---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 245 qqVKHNWETM-REAIQNH----IGSLNWGYRVTLREKGVTYVNSFGEFVELHKIKATNKKGQETfYTASKFVIATGERPR 319
Cdd:PRK06416 71 --IKAENVGIdFKKVQEWkngvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQT-YTAKNIILATGSRPR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 320 YL-GIQGDKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTV---MVRsvLLRGFDQEMAEKVGSYLEQ 395
Cdd:PRK06416 148 ELpGIEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALKK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 396 QGVKFqrkFTPILVQQLEKGLPGrLKVVAKSTEGPETVEGTYntVLLAIGRDSCTRKIGLEKIGVKINEknGKIPVNDVE 475
Cdd:PRK06416 226 RGIKI---KTGAKAKKVEQTDDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 476 QTNVPHVYAIGDVLeGKPELTPVAIQAGKLLARRLFGISLEkCDYINVPTTVFTPLEYGCCGLSEEKAIEMYtkENLEVY 555
Cdd:PRK06416 298 RTNVPNIYAIGDIV-GGPMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKEEG--FDVKVV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 556 HTFFwplewtvAGR------DNNTCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCG 629
Cdd:PRK06416 374 KFPF-------AGNgkalalGETDGFVKLIFDK-KDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLS 445
|
....*..
gi 296040479 630 EVftTME 636
Cdd:PRK06416 446 EA--LGE 450
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
166-652 |
2.35e-70 |
|
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: 235.78 E-value: 2.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 166 YDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGwdYNQ 245
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGG--LAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 246 QVKHNWETMREAIQNHIGSL-NWGYRVTLREKGVTYVNSFGEFVELHKIKAtnKKGQETFYtASKFVIATGERPRYLGIQ 324
Cdd:TIGR02053 70 TVAVDFGELLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGREVRG-AKRFLIATGARPAIPPIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 325 GDKE--YcITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKFQ 401
Cdd:TIGR02053 147 GLKEagY-LTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 402 rkfTPILVQQLEKGLPGRLKVVAKStEGPETVEGTYntVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPH 481
Cdd:TIGR02053 226 ---TSAQVKAVSVRGGGKIITVEKP-GGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDE-RGGILVDETLRTSNPG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 482 VYAIGDVLeGKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIemytkENLEVYHTFFWP 561
Cdd:TIGR02053 299 IYAAGDVT-GGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQ-----KAGIECDCRTLP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 562 LEWTVAGRDN--NTCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTMEITK 639
Cdd:TIGR02053 373 LTNVPRARINrdTRGFIKLVAEP-GTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTF 451
|
490
....*....|...
gi 296040479 640 SSglDITQKGCUG 652
Cdd:TIGR02053 452 YR--DVSKLSCCA 462
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
166-630 |
1.71e-65 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 222.77 E-value: 1.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 166 YDLIVIGGGSGGLSCAKEAANLGKKVMVLdfvvpspqGTSWgLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGWDYNQ 245
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALI--------ERGL-LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 246 QVKHNWET----MREAIQN-HIGSLNWgyrvtLRE-KGVTYVNSFGEFVELHKIKATNKKgqetfYTASKFVIATGERPR 319
Cdd:PRK06370 77 PVSVDFKAvmarKRRIRARsRHGSEQW-----LRGlEGVDVFRGHARFESPNTVRVGGET-----LRAKRIFINTGARAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 320 YLGIQG--DKEYcITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRSV-LLRGFDQEMAEKVGSYLEQQ 396
Cdd:PRK06370 147 IPPIPGldEVGY-LTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPrLLPREDEDVAAAVREILERE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 397 GVKFQRKFTPILVQQLEKGLpgRLKVVakSTEGPETVEGTYntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQ 476
Cdd:PRK06370 226 GIDVRLNAECIRVERDGDGI--AVGLD--CNGGAPEITGSH--ILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 477 TNVPHVYAIGDVlEGKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEmyTKENLEVYH 556
Cdd:PRK06370 299 TTNPGIYAAGDC-NGRGAFTHTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARK--SGRRVLVGT 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296040479 557 TffwPLewTVAGR----DNNTCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGE 630
Cdd:PRK06370 376 R---PM--TRVGRavekGETQGFMKVVVDA-DTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
166-503 |
9.63e-63 |
|
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: 210.25 E-value: 9.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 166 YDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspqgtswgLGGTCVNVGCIPKKLMHQAALLGHALqdarkygwdynq 245
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE------------DEGTCPYGGCVLSKALLGAAEAPEIA------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 246 qvkHNWETMREAIQNHIGSLNWGYRVTLREKGVTYVNSFGEFVELHKikatnKKGQETFYTASKFVIATGERPRYLGIQG 325
Cdd:pfam07992 57 ---SLWADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEEL-----VDGDGETITYDRLVIATGARPRLPPIPG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 326 DKEYC------ITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGV 398
Cdd:pfam07992 129 VELNVgflvrtLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 399 KFQrkfTPILVQQLEkGLPGRLKVVaksTEGPETVEgtYNTVLLAIGRDSCTRkiGLEKIGVKINEkNGKIPVNDVEQTN 478
Cdd:pfam07992 209 EVR---LGTSVKEII-GDGDGVEVI---LKDGTEID--ADLVVVAIGRRPNTE--LLEAAGLELDE-RGGIVVDEYLRTS 276
|
330 340
....*....|....*....|....*
gi 296040479 479 VPHVYAIGDVLEGKPELTPVAIQAG 503
Cdd:pfam07992 277 VPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
163-631 |
3.74e-50 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 181.28 E-value: 3.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 163 THDYDLIVIGGGSGGLSCAKEAANLGKKVMVLDfVVPSPQGTSwGLGGTCVNVGCIPKK-LMHQAALL---GHALQD--- 235
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIE-AWKNPKGKP-ALGGTCLNVGCIPSKaLLASSEEFenaGHHFADhgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 236 -ARKYGWDYNQQVKHnwetmREAIqnhIGSLNWGYRVTLREKGVTYVNSFGEFV----ELHKIKATNKKGQETfyTASKF 310
Cdd:PRK06327 80 hVDGVKIDVAKMIAR-----KDKV---VKKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDETVI--TAKHV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 311 VIATGERPRYL-GIQGDKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEK 388
Cdd:PRK06327 150 IIATGSEPRHLpGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 389 VGSYLEQQGVKFQRKFTPILVQQLEKGLpgrlkVVAKSTEGPETVEGTYNTVLLAIGRDSCTRKIGLEKIGVKINEkNGK 468
Cdd:PRK06327 230 AAKAFTKQGLDIHLGVKIGEIKTGGKGV-----SVAYTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDE-RGF 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 469 IPVNDVEQTNVPHVYAIGDVLeGKPELTPVAIQAGKLLARRLFGISlEKCDYINVPTTVFTPLEYGCCGLSEEKAiemyT 548
Cdd:PRK06327 304 IPVDDHCRTNVPNVYAIGDVV-RGPMLAHKAEEEGVAVAERIAGQK-GHIDYNTIPWVIYTSPEIAWVGKTEQQL----K 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 549 KENLEVYHTFFwPleWTVAGR----DNNTCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGI 624
Cdd:PRK06327 378 AEGVEYKAGKF-P--FMANGRalamGEPDGFVKIIADA-KTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHA 453
|
....*..
gi 296040479 625 HPTCGEV 631
Cdd:PRK06327 454 HPTLSEV 460
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
165-631 |
4.74e-49 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 177.84 E-value: 4.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 165 DYDLIVIGGGSGGLSCAKEAAnlGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGWDyn 244
Cdd:PRK07846 1 HYDLIIIGTGSGNSILDERFA--DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLGVD-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 245 QQVKH-NWETMREAIQNHIGSLNWG---YRVtLREKGVTYVNSFGEFVELHKIKAtnkkGQETFYTASKFVIATGERPRY 320
Cdd:PRK07846 68 AELDGvRWPDIVSRVFGRIDPIAAGgeeYRG-RDTPNIDVYRGHARFIGPKTLRT----GDGEEITADQVVIAAGSRPVI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 321 LGIQGDKE--YcITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKvgsYLEQQG 397
Cdd:PRK07846 143 PPVIADSGvrY-HTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISER---FTELAS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 398 VKFQRKF--TPILVQQLEKGlpgrlkvVAKSTEGPETVEGtyNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVE 475
Cdd:PRK07846 219 KRWDVRLgrNVVGVSQDGSG-------VTLRLDDGSTVEA--DVLLVATGRVPNGDLLDAAAAGVDVDE-DGRVVVDEYQ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 476 QTNVPHVYAIGDVlEGKPELTPVAIQAGKLLARRLF-GISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEmyTKENLEV 554
Cdd:PRK07846 289 RTSAEGVFALGDV-SSPYQLKHVANHEARVVQHNLLhPDDLIASDHRFVPAAVFTHPQIASVGLTENEARA--AGLDITV 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 555 YHTFF------WPLEWTvagrdnnTCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLT-KQLLDDTIGIHPT 627
Cdd:PRK07846 366 KVQNYgdvaygWAMEDT-------TGFVKLIADR-DTGRLLGAHIIGPQASTLIQPLIQAMSFGLDaREMARGQYWIHPA 437
|
....
gi 296040479 628 CGEV 631
Cdd:PRK07846 438 LPEV 441
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
162-630 |
5.78e-47 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 172.26 E-value: 5.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 162 STHDYDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspqgTSWGLGGTCVNVGCIPKKLMHQAALlghALQDARKYGW 241
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVL---RLIGFNQNPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 242 DYNQQVKHN--WETMREAIQNHIGSlnwgyRVTLREK-----GVTYVNSFGEFVELHKIKATNKKGQETFYTASKFVIAT 314
Cdd:PRK05249 71 YSSYRVKLRitFADLLARADHVINK-----QVEVRRGqyernRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 315 GERP-RYLGIQGDKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSY 392
Cdd:PRK05249 146 GSRPyRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 393 LEQQGVKFqrkftpilvqqlekglpgRLKVVAKSTEGpeTVEGTY-----------NTVLLAIGRDSCTRKIGLEKIGVK 461
Cdd:PRK05249 226 LRDSGVTI------------------RHNEEVEKVEG--GDDGVIvhlksgkkikaDCLLYANGRTGNTDGLNLENAGLE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 462 INEKnGKIPVNDVEQTNVPHVYAIGDVLeGKPELTPVAIQAGKLLARRLFGISLEKcdYIN-VPTTVFTPLEYGCCGLSE 540
Cdd:PRK05249 286 ADSR-GQLKVNENYQTAVPHIYAVGDVI-GFPSLASASMDQGRIAAQHAVGEATAH--LIEdIPTGIYTIPEISSVGKTE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 541 EKAIEM---YtkenlEVYHTFFwplewtvagRDN--------NTCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAM 609
Cdd:PRK05249 362 QELTAAkvpY-----EVGRARF---------KELaraqiagdNVGMLKILFHR-ETLEILGVHCFGERATEIIHIGQAIM 426
|
490 500
....*....|....*....|.
gi 296040479 610 KCGLTKQLLDDTIGIHPTCGE 630
Cdd:PRK05249 427 EQKGTIEYFVNTTFNYPTMAE 447
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
165-631 |
4.60e-43 |
|
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: 161.08 E-value: 4.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 165 DYDLIVIGGGSGGlSCAKEAaNLGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGHALQDARKYGWDYN 244
Cdd:TIGR03452 2 HYDLIIIGTGSGN-SIPDPR-FADKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLGIDAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 245 QQvKHNWETMREAIQNH----IGSLNWGYRVTLREKGVTYVNSFGEFVElhkiKATNKKGQETFYTASKFVIATGERPR- 319
Cdd:TIGR03452 71 ID-SVRWPDIVSRVFGDridpIAAGGEDYRRGDETPNIDVYDGHARFVG----PRTLRTGDGEEITGDQIVIAAGSRPYi 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 320 --YLGIQGDKEYciTSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKvgsYLEQQ 396
Cdd:TIGR03452 146 ppAIADSGVRYH--TNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRStKLLRHLDEDISDR---FTEIA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 397 GVKF--QRKFTPILVQQLEKGlpgrlkvVAKSTEGPETVEGtyNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDV 474
Cdd:TIGR03452 221 KKKWdiRLGRNVTAVEQDGDG-------VTLTLDDGSTVTA--DVLLVATGRVPNGDLLDAEAAGVEVDE-DGRIKVDEY 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 475 EQTNVPHVYAIGDVleGKP-ELTPVAIQAGKLLARRLFG-ISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIE----MYT 548
Cdd:TIGR03452 291 GRTSARGVWALGDV--SSPyQLKHVANAEARVVKHNLLHpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREaghdITV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 549 KenLEVYH--TFFWPLEWTvagrdnnTCYAKIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLT-KQLLDDTIGIH 625
Cdd:TIGR03452 369 K--IQNYGdvAYGWAMEDT-------TGFCKLIADR-DTGKLLGAHIIGPQASSLIQPLITAMAFGLDaREMARKQYWIH 438
|
....*.
gi 296040479 626 PTCGEV 631
Cdd:TIGR03452 439 PALPEV 444
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
166-630 |
3.78e-40 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 152.60 E-value: 3.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 166 YDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvPSPQGtswgLGGTCVNVGCIPKKLMHQAAllghalqdarKYGWDYNQ 245
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVALVE---ESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 246 QVKHnwetmREAIQNHIGSLNWGyrvTLREKGVTYVNSFGEFVELHKIKATNKKGQETFyTASKFVIATGERPRYLGIQG 325
Cdd:PRK07251 67 VMAT-----KNTVTSRLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIEL-TAETIVINTGAVSNVLPIPG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 326 --DKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFQR 402
Cdd:PRK07251 138 laDSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 403 KFTPILVQQLEKglpgrlKVVAKSTEGPEtvegTYNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHV 482
Cdd:PRK07251 218 NAHTTEVKNDGD------QVLVVTEDETY----RFDALLYATGRKPNTEPLGLENTDIELTE-RGAIKVDDYCQTSVPGV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 483 YAIGDVlEGKPELTPVAIQAGKLLARRLFGIS---LEkcDYINVPTTVFTPLEYGCCGLSEEKAIEmytkENLEVYHTff 559
Cdd:PRK07251 287 FAVGDV-NGGPQFTYISLDDFRIVFGYLTGDGsytLE--DRGNVPTTMFITPPLSQVGLTEKEAKE----AGLPYAVK-- 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296040479 560 wplEWTVA----GRDNNTCYA--KIICNKfDNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGE 630
Cdd:PRK07251 358 ---ELLVAamprAHVNNDLRGafKVVVNT-ETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
523-635 |
1.35e-37 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 135.37 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 523 VPTTVFTPLEYGCCGLSEEKAIEMYTKenLEVYHTFFWPLEWTVAGRDNNtCYAKIICNKfDNDRVIGFHLLGPNAGEVT 602
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADR-ETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 296040479 603 QGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTM 635
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| GRX_GRXh_1_2_like |
cd03419 |
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ... |
76-157 |
4.88e-37 |
|
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.
Pssm-ID: 239511 [Multi-domain] Cd Length: 82 Bit Score: 132.66 E-value: 4.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 76 RVMIFSKSYCPHSSRVKELFSSLGVNYYILELDQVDDGANVQEVLTEISNQKTVPNIFVNKVHVGGCDRIFQAHQNGLLQ 155
Cdd:cd03419 1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
|
..
gi 296040479 156 KL 157
Cdd:cd03419 81 KL 82
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
170-651 |
2.89e-35 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 140.67 E-value: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 170 VIGGGSGGLSCAKEAANLGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGH----------------AL 233
Cdd:PRK13748 103 VIGSGGAAMAAALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHlrrespfdggiaatvpTI 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 234 QDARKYGwdyNQQVKhnWETMREAIQNHIGSLNwgyrvtlreKGVTYVNSFGEFVELHKIKATNKKGQETFYTASKFVIA 313
Cdd:PRK13748 174 DRSRLLA---QQQAR--VDELRHAKYEGILDGN---------PAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 314 TGERPRYLGIQGDKE--YCITSDDLFSlPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGFDQEMAEKVGS 391
Cdd:PRK13748 240 TGASPAVPPIPGLKEtpYWTSTEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 392 YLEQQGVKFQRKFTPILVQQLEKglpgrlKVVAKSTEGpetvEGTYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPV 471
Cdd:PRK13748 319 AFRAEGIEVLEHTQASQVAHVDG------EFVLTTGHG----ELRADKLLVATGRAPNTRSLALDAAGVTVN-AQGAIVI 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 472 NDVEQTNVPHVYAIGDVLEgKPELTPVAIQAGKLLARRLFGISlEKCDYINVPTTVFTPLEYGCCGLSEEKAiemyTKEN 551
Cdd:PRK13748 388 DQGMRTSVPHIYAAGDCTD-QPQFVYVAAAAGTRAAINMTGGD-AALDLTAMPAVVFTDPQVATVGYSEAEA----HHDG 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 552 LEVyhtffwplEWTVAGRDNntcYAKIICNkFDND------------RVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLD 619
Cdd:PRK13748 462 IET--------DSRTLTLDN---VPRALAN-FDTRgfiklvieegsgRLIGVQAVAPEAGELIQTAALAIRNRMTVQELA 529
|
490 500 510
....*....|....*....|....*....|....*....
gi 296040479 620 DTIGIHPT-------CGEVFTTmeitkssglDITQKGCU 651
Cdd:PRK13748 530 DQLFPYLTmveglklAAQTFNK---------DVKQLSCC 559
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
165-632 |
4.07e-34 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 135.29 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 165 DYDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspQGTSWgLGGTCVNVGCIP-KKLMHQAALLG-HALQDARKygwd 242
Cdd:NF040477 3 HYQAIIIGFGKAGKTLAATLAKAGWRVAIIE------QSAQM-YGGTCINIGCIPtKTLVHDAEQHQdFSTAMQRK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 243 ynQQVKHnweTMREAIQNHIGSLNwgyrvtlrekGVTYVNSFGEFVELHKIKATNKKGQETFYtASKFVIATGERPRYLG 322
Cdd:NF040477 72 --SSVVG---FLRDKNYHNLADLD----------NVDVINGRAEFIDNHTLRVFQADGEQELR-GEKIFINTGAQSVLPP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 323 IQGDKEY--CITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVK 399
Cdd:NF040477 136 IPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 400 FqrkftpILVQQLEKGLPGRLKVVAKSTEGPETVEGtyntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNV 479
Cdd:NF040477 216 L------ILNAQVQRVSSHEGEVQLETAEGVLTVDA----LLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 480 PHVYAIGDVlEGKPELTPVAIQAGKLLARRLFGISLEKC-DYINVPTTVFTPLEYGCCGLSEEKAiemytKENLEVYHTF 558
Cdd:NF040477 285 DNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLGEGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQA-----RASGADIQVV 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296040479 559 FWPLEWTVAGR---DNNTCYAKIICNKfdNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVF 632
Cdd:NF040477 359 TLPVAAIPRARvmnDTRGVLKAVVDNK--TQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESL 433
|
|
| GRX_euk |
TIGR02180 |
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ... |
77-158 |
3.18e-33 |
|
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.
Pssm-ID: 274016 [Multi-domain] Cd Length: 83 Bit Score: 121.97 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 77 VMIFSKSYCPHSSRVKELFSSLGVN-YYILELDQVDDGANVQEVLTEISNQKTVPNIFVNKVHVGGCDRIFQAHQNGLLQ 155
Cdd:TIGR02180 1 VVVFSKSYCPYCKKAKEILAKLNVKpYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKLA 80
|
...
gi 296040479 156 KLL 158
Cdd:TIGR02180 81 ELL 83
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
162-634 |
6.76e-29 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 122.33 E-value: 6.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 162 STHDYDLIVIGGGSGGLSCAKEAANLGKKVMVLdfvvpspQGTSWGLGGTCVNVGCIPKKLMHQAA-------------- 227
Cdd:PTZ00153 113 SDEEYDVGIIGCGVGGHAAAINAMERGLKVIIF-------TGDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklyt 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 228 --LLGHALQDARKYGWDYNQ----QVKHNWETMREAIQNHIGSLNWGYRVTLREKG-------VTYVNSFGEFVELHKIK 294
Cdd:PTZ00153 186 ygIYTNAFKNGKNDPVERNQlvadTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKfcknsehVQVIYERGHIVDKNTIK 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 295 AtNKKGQEtfYTASKFVIATGERPRY-LGIQGDKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVT-VM 372
Cdd:PTZ00153 266 S-EKSGKE--FKVKNIIIATGSTPNIpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 373 VRSVLLRGFDQEMAekvgSYLEQQGVKFQ--RKFTPILVQQLEKGLPGRLKVVAKS--TEGPETVEGTYNT--------- 439
Cdd:PTZ00153 343 YSPQLLPLLDADVA----KYFERVFLKSKpvRVHLNTLIEYVRAGKGNQPVIIGHSerQTGESDGPKKNMNdiketyvds 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 440 VLLAIGRDSCTRKIGLEKIGVKINEknGKIPVND---VEQTN---VPHVYAIGDVlEGKPELTPVA-IQA---------- 502
Cdd:PTZ00153 419 CLVATGRKPNTNNLGLDKLKIQMKR--GFVSVDEhlrVLREDqevYDNIFCIGDA-NGKQMLAHTAsHQAlkvvdwiegk 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 503 -GKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEMYTKENLEVYHTFF-------WPLEWTVAGRDNNTC 574
Cdd:PTZ00153 496 gKENVNINVENWASKPIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEISFYkanskvlCENNISFPNNSKNNS 575
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296040479 575 YAKIICNKFDN-------------DRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTT 634
Cdd:PTZ00153 576 YNKGKYNTVDNtegmvkivylkdtKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
166-630 |
3.42e-28 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 117.81 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 166 YDLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspQGTSWgLGGTCVNVGCIPKKLMhqaallghaLQDARKYGwDYNQ 245
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIE------QSNAM-YGGTCINIGCIPTKTL---------VHDAQQHT-DFVR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 246 QVKHnwetmREAIQNHIGSLNWGYRVTLreKGVTYVNSFGEFVELHKIKaTNKKGQETFYTASKFVIATGERPRYLGIQG 325
Cdd:PRK08010 67 AIQR-----KNEVVNFLRNKNFHNLADM--PNIDVIDGQAEFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIPG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 326 --DKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFqr 402
Cdd:PRK08010 139 itTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDI-- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 403 kftpILVQQLEKGLPGRLKVVAKSTEGPETVEGtyntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHV 482
Cdd:PRK08010 217 ----ILNAHVERISHHENQVQVHSEHAQLAVDA----LLIASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 483 YAIGDVlEGKPELTPVAIQAGKLLARRLFGISLEKC-DYINVPTTVFTPLEYGCCGLSEEKAIEmyTKENLEVYHTFFWP 561
Cdd:PRK08010 288 WAMGDV-TGGLQFTYISLDDYRIVRDELLGEGKRSTdDRKNVPYSVFMTPPLSRVGMTEEQARE--SGADIQVVTLPVAA 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296040479 562 LEWTVAGRDNNTCYAKIICNKfdNDRVIGFHLLGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGE 630
Cdd:PRK08010 365 IPRARVMNDTRGVLKAIVDNK--TQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSE 431
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
168-545 |
4.02e-27 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 114.96 E-value: 4.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 168 LIVIGGGSGGLSCAKEAANLGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKK----------LMHQAALLGHALQDAR 237
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIE---------RDGLGGAAVLTDCVPSKtliataevrtELRRAAELGIRFIDDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 238 KYGWDY---NQQVKHNWETMREAIqnhigslnwgyRVTLREKGVTYVNSFGEFVEL----HKIKATNKKGQETFYTASKF 310
Cdd:PRK07845 75 EARVDLpavNARVKALAAAQSADI-----------RARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 311 VIATGERPRYL-GIQGDKEYCITSDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLGLDVT-VMVRSVLLRGFDQEMAEK 388
Cdd:PRK07845 144 LIATGASPRILpTAEPDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 389 VGSYLEQQGVKFQRKFTPILVQQLEKGlpgrlkVVAKSTEGpETVEGTYntVLLAIGRDSCTRKIGLEKIGVKINEkNGK 468
Cdd:PRK07845 224 LEEVFARRGMTVLKRSRAESVERTGDG------VVVTLTDG-RTVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGH 293
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296040479 469 IPVNDVEQTNVPHVYAIGDVlEGKPELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSeEKAIE 545
Cdd:PRK07845 294 ITVDRVSRTSVPGIYAAGDC-TGVLPLASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVS-QAAID 368
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
166-503 |
1.15e-24 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 104.82 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 166 YDLIVIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTSWglggTCV-NVGCIPKKLMhQAALLGHALQDARKYGwdyn 244
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATT----KEIeNYPGFPEGIS-GPELAERLREQAERFG---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 245 qqvkhnwetmreaiqnhigslnwgyrVTLREKGVTYVNSFGEFVELHkikaTNKkgqETFYTASKFVIATGERPRYLGIQ 324
Cdd:COG0492 72 --------------------------AEILLEEVTSVDKDDGPFRVT----TDD---GTEYEAKAVIIATGAGPRKLGLP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 325 GDKE-------YCITSDdlfsLPYCPG-NTLIVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGfDQEMAEKVgsyLEQQ 396
Cdd:COG0492 119 GEEEfegrgvsYCATCD----GFFFRGkDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRA-SKILVERL---RANP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 397 GVKFQRKFTPILVQqLEKGLPGrlkVVAKSTEGPETVEGTYNTVLLAIGRDSCTRkiGLEKIGVKINEkNGKIPVNDVEQ 476
Cdd:COG0492 191 KIEVLWNTEVTEIE-GDGRVEG---VTLKNVKTGEEKELEVDGVFVAIGLKPNTE--LLKGLGLELDE-DGYIVVDEDME 263
|
330 340
....*....|....*....|....*..
gi 296040479 477 TNVPHVYAIGDVLEGKPELTPVAIQAG 503
Cdd:COG0492 264 TSVPGVFAAGDVRDYKYRQAATAAGEG 290
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
311-536 |
3.13e-24 |
|
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: 103.74 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 311 VIATGERPRYLGIQGdkeycITSDDLFSL------PYC--------PGNTLIVGASYVGLECAGFLAGLGLDVTVMVRS- 375
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddaDALrealkefkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 376 VLLRGFDQEMAEKVGSYLEQQGVKFQRKFTpilVQQLEkglpGRLKVVAKSTEGpETVEgtYNTVLLAIGrdsctrkIG- 454
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGET---VVAID----GDDKVAVTLTDG-EEIP--ADLVVVAPG-------VRp 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 455 ----LEKIGVKINEKNGkIPVNDVEQTNVPHVYAIGDVLE------GKPELTP---VAIQAGKLLARRLFGISLEkcdYI 521
Cdd:COG0446 221 ntelAKDAGLALGERGW-IKVDETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasAANKQGRVAAENILGGPAP---FP 296
|
250
....*....|....*
gi 296040479 522 NVPTTVFTPleYGCC 536
Cdd:COG0446 297 GLGTFISKV--FDLC 309
|
|
| GRX_family |
cd02066 |
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
76-150 |
8.02e-23 |
|
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.
Pssm-ID: 239017 [Multi-domain] Cd Length: 72 Bit Score: 92.14 E-value: 8.02e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296040479 76 RVMIFSKSYCPHSSRVKELFSSLGVNYYilELDQVDDGAnVQEVLTEISNQKTVPNIFVNKVHVGGCDRIFQAHQ 150
Cdd:cd02066 1 KVVVFSKSTCPYCKRAKRLLESLGIEFE--EIDILEDGE-LREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
274-595 |
5.45e-20 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 92.51 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 274 REKGVTYVnsFGEFVElhKIKATNKK-----GQETFYtaSKFVIATGERPRYLGIQG-DKEYCI---TSDDLFSL-PYCP 343
Cdd:COG1251 67 EENGIDLR--LGTRVT--AIDRAARTvtladGETLPY--DKLVLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 344 G--NTLIVGASYVGLECAGFLAGLGLDVTVMVRS--VLLRGFDQEMAEKVGSYLEQQGVKFqrkftpilvqqlekglpgR 419
Cdd:COG1251 141 PgkRVVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQLDEEAGALLQRLLEALGVEV------------------R 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 420 LKVVAKSTEGPETVEG-------TYNT--VLLAIG---RDSCTRKIGLEkigvkINekNGkIPVNDVEQTNVPHVYAIGD 487
Cdd:COG1251 203 LGTGVTEIEGDDRVTGvrladgeELPAdlVVVAIGvrpNTELARAAGLA-----VD--RG-IVVDDYLRTSDPDIYAAGD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 488 VLE------GKP--ELTPVAIQAGKLLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEkaiemytkENLEVyhtff 559
Cdd:COG1251 275 CAEhpgpvyGRRvlELVAPAYEQARVAAANLAGGPAAYEGSVPSTKLKVFGVDVASAGDAEG--------DEEVV----- 341
|
330 340 350
....*....|....*....|....*....|....*.
gi 296040479 560 wplewtVAGRDNNTCYAKIIcnkFDNDRVIGFHLLG 595
Cdd:COG1251 342 ------VRGDPARGVYKKLV---LRDGRLVGAVLVG 368
|
|
| Glutaredoxin |
pfam00462 |
Glutaredoxin; |
77-139 |
5.99e-17 |
|
Glutaredoxin;
Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 75.23 E-value: 5.99e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296040479 77 VMIFSKSYCPHSSRVKELFSSLGVNYYILELDQVDDganVQEVLTEISNQKTVPNIFVNKVHV 139
Cdd:pfam00462 1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPE---IREELKELSGWPTVPQVFIDGEHI 60
|
|
| GRX_bact |
TIGR02181 |
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
77-158 |
8.48e-17 |
|
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]
Pssm-ID: 274017 [Multi-domain] Cd Length: 79 Bit Score: 75.37 E-value: 8.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 77 VMIFSKSYCPHSSRVKELFSSLGVNYYILELDqvDDGANVQEVLtEISNQKTVPNIFVNKVHVGGCDRIFQAHQNGLLQK 156
Cdd:TIGR02181 1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVD--GDPALRDEMM-QRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDP 77
|
..
gi 296040479 157 LL 158
Cdd:TIGR02181 78 LL 79
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
345-421 |
1.52e-16 |
|
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: 74.55 E-value: 1.52e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296040479 345 NTLIVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKGLPGRLK 421
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRdRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| GlrX-like_plant |
TIGR02189 |
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ... |
70-158 |
2.38e-14 |
|
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.
Pssm-ID: 274023 [Multi-domain] Cd Length: 99 Bit Score: 69.02 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 70 DLIEGNRVMIFSKSYCPHSSRVKELFSSLGVNYYILELDQVDDGANVQEVLTEISNQKTVPNIFVNKVHVGGCDRIFQAH 149
Cdd:TIGR02189 3 RMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALH 82
|
....*....
gi 296040479 150 QNGLLQKLL 158
Cdd:TIGR02189 83 ISGSLVPML 91
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
292-618 |
8.68e-14 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 73.92 E-value: 8.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 292 KIKATNKKGQETF-YTASKFVIATGER---PRYLGIQGDKEYCITS-DD------LFSLPYCPgNTLIVGASYVGLECAG 360
Cdd:PRK09564 88 TITVKNLKTGSIFnDTYDKLMIATGARpiiPPIKNINLENVYTLKSmEDglalkeLLKDEEIK-NIVIIGAGFIGLEAVE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 361 FLAGLGLDVTVMVRS--VLLRGFDQEMAEKVGSYLEQQGVKFQrkftpilVQQLEKGLPGRLKVvakstEGPETVEGTYN 438
Cdd:PRK09564 167 AAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELH-------LNEFVKSLIGEDKV-----EGVVTDKGEYE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 439 T--VLLAIGRDSCTRKI---GLEKIgvkineKNGKIPVNDVEQTNVPHVYAIGD------VLEGKPELTPVAIQA---GK 504
Cdd:PRK09564 235 AdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKNVYVPLATTAnklGR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 505 LLARRLFGISLEKCDYINVPTTVFTPLEYGCCGLSEEKA----IEMYTKENLEVYHTFFWPlewtvagrDNNTCYAKIIC 580
Cdd:PRK09564 309 MVGENLAGRHVSFKGTLGSACIKVLDLEAARTGLTEEEAkklgIDYKTVFIKDKNHTNYYP--------GQEDLYVKLIY 380
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 296040479 581 NKfDNDRVIGFHLLGPNaGEV--TQGFAAAMKCGLTKQLL 618
Cdd:PRK09564 381 EA-DTKVILGGQIIGKK-GAVlrIDALAVAIYAKLTTQEL 418
|
|
| GRX_GRXb_1_3_like |
cd03418 |
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ... |
77-152 |
5.64e-13 |
|
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.
Pssm-ID: 239510 [Multi-domain] Cd Length: 75 Bit Score: 64.53 E-value: 5.64e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296040479 77 VMIFSKSYCPHSSRVKELFSSLGVNYYilELDQVDDGANVQEvLTEISNQ-KTVPNIFVNKVHVGGCDRIFQAHQNG 152
Cdd:cd03418 2 VEIYTKPNCPYCVRAKALLDKKGVDYE--EIDVDGDPALREE-MINRSGGrRTVPQIFIGDVHIGGCDDLYALERKG 75
|
|
| PRK10638 |
PRK10638 |
glutaredoxin 3; Provisional |
77-159 |
2.42e-11 |
|
glutaredoxin 3; Provisional
Pssm-ID: 182607 [Multi-domain] Cd Length: 83 Bit Score: 60.22 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 77 VMIFSKSYCPHSSRVKELFSSLGVNYYILEldqVDDGANVQEVLTEISNQKTVPNIFVNKVHVGGCDRIFQAHQNGLLQK 156
Cdd:PRK10638 4 VEIYTKATCPFCHRAKALLNSKGVSFQEIP---IDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80
|
...
gi 296040479 157 LLQ 159
Cdd:PRK10638 81 LLK 83
|
|
| GrxC |
COG0695 |
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
76-143 |
3.15e-11 |
|
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 59.44 E-value: 3.15e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296040479 76 RVMIFSKSYCPHSSRVKELFSSLGVNYyiLELDqVDDGANVQEVLTEISNQKTVPNIFVNKVHVGGCD 143
Cdd:COG0695 1 KVTLYTTPGCPYCARAKRLLDEKGIPY--EEID-VDEDPEAREELRERSGRRTVPVIFIGGEHLGGFD 65
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
311-544 |
4.44e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 65.15 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 311 VIATGERPRYLGIQGDKEYCI---TSDDLFSL------------PYCPGNTLIVGASYVGLECAGFLAGL--------GL 367
Cdd:COG1252 102 VIATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAELlrkllrypGI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 368 D--------VTVMVRsvLLRGFDQEMAEKVGSYLEQQGVKFQRKFTpilVQQLEKGlpgrlKVVaksTEGPETVEgtYNT 439
Cdd:COG1252 182 DpdkvritlVEAGPR--ILPGLGEKLSEAAEKELEKRGVEVHTGTR---VTEVDAD-----GVT---LEDGEEIP--ADT 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 440 VLLAIG-------RDSctrkiGLEKigvkinEKNGKIPVNDVEQT-NVPHVYAIGD---VLEGKPELTP----VAIQAGK 504
Cdd:COG1252 247 VIWAAGvkappllADL-----GLPT------DRRGRVLVDPTLQVpGHPNVFAIGDcaaVPDPDGKPVPktaqAAVQQAK 315
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 296040479 505 LLARRLFGISLEKcdyinvPTTVFTPLEYGC-CGLSEEKAI 544
Cdd:COG1252 316 VLAKNIAALLRGK------PLKPFRYRDKGClASLGRGAAV 350
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
276-512 |
7.99e-11 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 64.42 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 276 KGVTyVNSFGEFVELH----KIKATNKKGQETFYTA-SKFVIATGERPRYLGIQGDKEYCI-----TSD-DLFSLPYCPG 344
Cdd:PRK13512 71 KQIT-VKTYHEVIAINderqTVTVLNRKTNEQFEESyDKLILSPGASANSLGFESDITFTLrnledTDAiDQFIKANQVD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 345 NTLIVGASYVGLECAGFLAGLGLDVTVMVRSV-LLRGFDQEMAEkvgsyleqqgvkfqrkftPILvQQLEK-GLPGRLKV 422
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQ------------------PIL-DELDKrEIPYRLNE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 423 VAKSTEGPET------VEgTYNTVLLAIGRDSCTRKIglEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDVLEG----- 491
Cdd:PRK13512 211 EIDAINGNEVtfksgkVE-HYDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIITShyrhv 286
|
250 260
....*....|....*....|....*
gi 296040479 492 -KPELTPVAI---QAGKLLARRLFG 512
Cdd:PRK13512 287 dLPASVPLAWgahRAASIVAEQIAG 311
|
|
| GRX_PICOT_like |
cd03028 |
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ... |
70-155 |
4.12e-10 |
|
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of PICOT and GRX-PICOT-like proteins. The non-PICOT members of this family contain only the GRX-like domain, whereas PICOT contains an N-terminal TRX-like domain followed by one to three GRX-like domains. It is interesting to note that PICOT from plants contain three repeats of the GRX-like domain, metazoan proteins (except for insect) have two repeats, while fungal sequences contain only one copy of the domain. PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli. Both GRX and TRX domains of PICOT are required for its activity. Characterized non-PICOT members of this family include CXIP1, a CAX-interacting protein in Arabidopsis thaliana, and PfGLP-1, a GRX-like protein from Plasmodium falciparum.
Pssm-ID: 239326 Cd Length: 90 Bit Score: 56.73 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 70 DLIEGNRVMIFSKSY-----CPHSSRVKELFSSLGVNYY---ILEldqvDDgaNVQEVLTEISNQKTVPNIFVNKVHVGG 141
Cdd:cd03028 3 KLIKENPVVLFMKGTpeeprCGFSRKVVQILNQLGVDFGtfdILE----DE--EVRQGLKEYSNWPTFPQLYVNGELVGG 76
|
90
....*....|....
gi 296040479 142 CDRIFQAHQNGLLQ 155
Cdd:cd03028 77 CDIVKEMHESGELQ 90
|
|
| GRX_hybridPRX5 |
cd03029 |
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ... |
77-143 |
6.75e-07 |
|
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.
Pssm-ID: 239327 [Multi-domain] Cd Length: 72 Bit Score: 47.13 E-value: 6.75e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296040479 77 VMIFSKSYCPHSSRVKELFSSLGVNYYILELDQVDDGanvqEVLTEISNQKTVPNIFVNKVHVGGCD 143
Cdd:cd03029 3 VSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITG----RSLRAVTGAMTVPQVFIDGELIGGSD 65
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
311-508 |
6.86e-07 |
|
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: 52.06 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 311 VIATG-ERPRYLGIQG-DKEYCIT----------SDDLFSLPYCPGNTLIVGASYVGLECAGFLAGLG-LDVTVMVRsvl 377
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 378 lRGFDqEM---AEKVgSYLEQQGVKFQ-----RKF--------TPILVQQLEKGLP---GRLKvvakstegPETVEGTY- 437
Cdd:COG0493 288 -RTRE-EMpasKEEV-EEALEEGVEFLflvapVEIigdengrvTGLECVRMELGEPdesGRRR--------PVPIEGSEf 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296040479 438 ----NTVLLAIGRDSCTRKIgLEKIGVKINeKNGKIPVNDVE-QTNVPHVYAIGDVLEGkPELTPVAIQAGKLLAR 508
Cdd:COG0493 357 tlpaDLVILAIGQTPDPSGL-EEELGLELD-KRGTIVVDEETyQTSLPGVFAGGDAVRG-PSLVVWAIAEGRKAAR 429
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
311-510 |
2.52e-06 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 49.99 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 311 VIATGE-RPRYLGIQGDKEYCITS--DDLFS-----LPYCP---------GNTLIVGASYVGLECAGFLAGLGLDVTVMV 373
Cdd:PRK12770 123 LIATGTwKSRKLGIPGEDLPGVYSalEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAALEAVLLGAEKVYLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 374 -RsvllRGFDQEMAekvGSY----LEQQGVKFQRKFTPILVQQlEKGLPG----RLKVVAKSTEG---PETVEGT----- 436
Cdd:PRK12770 203 yR----RTINEAPA---GKYeierLIARGVEFLELVTPVRIIG-EGRVEGvelaKMRLGEPDESGrprPVPIPGSefvle 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296040479 437 YNTVLLAIGrDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDVLEGkPELTPVAIQAGKLLARRL 510
Cdd:PRK12770 275 ADTVVFAIG-EIPTPPFAKECLGIELN-RKGEIVVDEKHMTSREGVFAAGDVVTG-PSKIGKAIKSGLRAAQSI 345
|
|
| GRX_DEP |
cd03027 |
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ... |
76-141 |
3.68e-06 |
|
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions.
Pssm-ID: 239325 [Multi-domain] Cd Length: 73 Bit Score: 45.09 E-value: 3.68e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296040479 76 RVMIFSKSYCPHSSRVKELFSSLGVNYyiLELDqVDDGANVQEVLTEISNQKTVPNIFVNKVHVGG 141
Cdd:cd03027 2 RVTIYSRLGCEDCTAVRLFLREKGLPY--VEIN-IDIFPERKAELEERTGSSVVPQIFFNEKLVGG 64
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
163-209 |
6.13e-06 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 49.44 E-value: 6.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 296040479 163 THDYDLIVIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTSWGLG 209
Cdd:PRK12839 6 THTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGATAWSGG 52
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
311-507 |
7.44e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 49.02 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 311 VIATG-ERPRYLGIQGDK--------EYcITS----DDLFSLPycPGNTLIV-GASYVGLECAGFLAGLG-LDVTVMVRs 375
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDF-LTRvnqaVADYDLP--VGKRVVViGGGNTAMDAARTAKRLGaESVTIVYR- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 376 vllRGFDqEM---AEKVgSYLEQQGVKFQRKFTPILVQQLEKGLPG------RLKVVAKSTEGPETVEGTY-----NTVL 441
Cdd:PRK11749 306 ---RGRE-EMpasEEEV-EHAKEEGVEFEWLAAPVEILGDEGRVTGvefvrmELGEPDASGRRRVPIEGSEftlpaDLVI 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296040479 442 LAIGRDSCTRKIGLEKiGVKINEKNGKIPVNDVEQTNVPHVYAIGDVLEGkPELTPVAIQAGKLLA 507
Cdd:PRK11749 381 KAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTG-AATVVWAVGDGKDAA 444
|
|
| grxA |
PRK11200 |
glutaredoxin 1; Provisional |
77-149 |
9.04e-06 |
|
glutaredoxin 1; Provisional
Pssm-ID: 183036 [Multi-domain] Cd Length: 85 Bit Score: 44.25 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 77 VMIFSKSYCPHSSRVKELFSSL-----GVNY-YIlelDQVDDGANVQEVLTEISNQ-KTVPNIFVNKVHVGGCDRiFQAH 149
Cdd:PRK11200 3 VVIFGRPGCPYCVRAKELAEKLseerdDFDYrYV---DIHAEGISKADLEKTVGKPvETVPQIFVDQKHIGGCTD-FEAY 78
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
164-210 |
2.77e-05 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 46.82 E-value: 2.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 296040479 164 HDYDLIVIGGGSGGLSCAKEAANLGKKVMVLDFVVPsPQGTSWGLGG 210
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRP-GSGASGRNAG 46
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
167-287 |
3.13e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 46.90 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 167 DLIVIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTSWGLGGTCVnVGCiPKKLMHQAALLghALQDARK-YGWDYNQ 245
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGGIDA-LGN-PPQGGIDSPEL--HPTDTLKgLDELADH 76
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 296040479 246 Q-VKHNWETMREAIQNHIgslNWGYRVTLREKGVTYVNSFGEF 287
Cdd:pfam00890 77 PyVEAFVEAAPEAVDWLE---ALGVPFSRTEDGHLDLRPLGGL 116
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
299-487 |
3.25e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 47.04 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 299 KGQETFYtaSKFVIATGERPRYLGIQG-DKEYCI---TSDDLFSLPYCPGNT---LIVGASYVGLECAGFLAGLGLDVTV 371
Cdd:PRK14989 96 AGRTVFY--DKLIMATGSYPWIPPIKGsETQDCFvyrTIEDLNAIEACARRSkrgAVVGGGLLGLEAAGALKNLGVETHV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 372 MVRSVLLrgfdqeMAEKvgsyLEQQG-VKFQRKFTPILVQ-QLEKGlpgRLKVVAKSTEGPETV---EGT---YNTVLLA 443
Cdd:PRK14989 174 IEFAPML------MAEQ----LDQMGgEQLRRKIESMGVRvHTSKN---TLEIVQEGVEARKTMrfaDGSeleVDFIVFS 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 296040479 444 IG---RDSCTRKIGLEkIGvkineKNGKIPVNDVEQTNVPHVYAIGD 487
Cdd:PRK14989 241 TGirpQDKLATQCGLA-VA-----PRGGIVINDSCQTSDPDIYAIGE 281
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
163-194 |
4.70e-05 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 46.36 E-value: 4.70e-05
10 20 30
....*....|....*....|....*....|..
gi 296040479 163 THDYDLIVIGGGSGGLSCAKEAANLGKKVMVL 194
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVL 32
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
269-512 |
8.26e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 45.29 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 269 YRVTLREKgvTYVNSFGefVELHKIKAtnkKGQEtfYTASKFVIATGERPRYLGIQGD---------KEYCITSDDLFSl 339
Cdd:PRK04965 71 FNLRLFPH--TWVTDID--AEAQVVKS---QGNQ--WQYDKLVLATGASAFVPPIPGRelmltlnsqQEYRAAETQLRD- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 340 pycPGNTLIVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFdqeMAEKVGSYLE----QQGVKFQRKFTpilVQQLEK 414
Cdd:PRK04965 141 ---AQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNaASLLASL---MPPEVSSRLQhrltEMGVHLLLKSQ---LQGLEK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 415 GLPGrlkVVAKSTEGpETVEgtYNTVLLAIGRDSCT---RKIGLEKigvkinekNGKIPVNDVEQTNVPHVYAIGDV--L 489
Cdd:PRK04965 212 TDSG---IRATLDSG-RSIE--VDAVIAAAGLRPNTalaRRAGLAV--------NRGIVVDSYLQTSAPDIYALGDCaeI 277
|
250 260
....*....|....*....|....*
gi 296040479 490 EGK--PELTPVAIQAgKLLARRLFG 512
Cdd:PRK04965 278 NGQvlPFLQPIQLSA-MALAKNLLG 301
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
166-195 |
1.33e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 44.88 E-value: 1.33e-04
10 20 30
....*....|....*....|....*....|
gi 296040479 166 YDLIVIGGGSGGLSCAKEAANLGKKVMVLD 195
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIE 30
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
162-195 |
1.52e-04 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 44.78 E-value: 1.52e-04
10 20 30
....*....|....*....|....*....|....
gi 296040479 162 STHDYDLIVIGGGSGGLSCAKEAANLGKKVMVLD 195
Cdd:COG3573 2 AAMDADVIVVGAGLAGLVAAAELADAGRRVLLLD 35
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
305-486 |
1.66e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 44.14 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 305 YTASKFVIATGE--RPRYLGIqgdKEYCITSDDLFSL-PYCPGNTLIVGASYVGLECAGFLAGLGLDVTVmvrsvLLRGF 381
Cdd:pfam13738 117 YQARYVIIATGEfdFPNKLGV---PELPKHYSYVKDFhPYAGQKVVVIGGYNSAVDAALELVRKGARVTV-----LYRGS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 382 DQEMAEKVGSYleqqGVKfqrkftPILVQQLEKGL-PGRLKV-----VAKSTEGPETV-----EGT----YNTVLLAIGR 446
Cdd:pfam13738 189 EWEDRDSDPSY----SLS------PDTLNRLEELVkNGKIKAhfnaeVKEITEVDVSYkvhteDGRkvtsNDDPILATGY 258
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 296040479 447 DSCTRKigLEKIGVKINEkNGKIPVND-VEQTNVPHVYAIG 486
Cdd:pfam13738 259 HPDLSF--LKKGLFELDE-DGRPVLTEeTESTNVPGLFLAG 296
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
309-510 |
2.04e-04 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 44.37 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 309 KFVIATGERPRYLGIQGDKEY-------------------CITSDDLFSLPYCPGNTL----IVGASYVGLECAGFLAGL 365
Cdd:PTZ00318 116 KLVVAHGARPNTFNIPGVEERafflkevnhargirkrivqCIERASLPTTSVEERKRLlhfvVVGGGPTGVEFAAELADF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 366 GLD--------------VTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEkglpgrlkVVAKSTEGP 430
Cdd:PTZ00318 196 FRDdvrnlnpelveeckVTVLeAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKE--------VVLKDGEVI 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 431 ETVEGTYNTvllAIGRDSCTRKIGLEKigvkinEKNGKIPVND-VEQTNVPHVYAIGDV--LEGK--PELTPVAIQAGKL 505
Cdd:PTZ00318 268 PTGLVVWST---GVGPGPLTKQLKVDK------TSRGRISVDDhLRVKPIPNVFALGDCaaNEERplPTLAQVASQQGVY 338
|
....*
gi 296040479 506 LARRL 510
Cdd:PTZ00318 339 LAKEF 343
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
165-239 |
2.19e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 44.33 E-value: 2.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296040479 165 DYDLIVIGGGSGGLSCAKEAANLGKKVMVldfVVPSPQgtswgLGGTCVNVG---CIPKKLMHQAALLGHALQDARKY 239
Cdd:PRK06134 12 ECDVLVIGSGAAGLSAAVTAAWHGLKVIV---VEKDPV-----FGGTTAWSGgwmWIPRNPLARRAGIVEDIEQPRTY 81
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
163-195 |
4.64e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 43.35 E-value: 4.64e-04
10 20 30
....*....|....*....|....*....|...
gi 296040479 163 THDYDLIVIGGGSGGLSCAKEAANLGKKVMVLD 195
Cdd:PRK12834 2 AMDADVIVVGAGLAGLVAAAELADAGKRVLLLD 34
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
167-210 |
5.19e-04 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 42.77 E-value: 5.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 296040479 167 DLIVIGGGSGGLSCAKEAANLGKKVMVLD-FVVPSpQGTSWGLGG 210
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLErGDDPG-SGASGRNAG 44
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
287-490 |
9.22e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 41.97 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 287 FVELHKIKATNK----KGQETFYTASKFVIATGERPRYLGIQGDKEY-------CITSDDLFslpYCPGNTLIVGASYVG 355
Cdd:PRK10262 82 FDHINKVDLQNRpfrlTGDSGEYTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 356 LECAGFLAGLGLDVTVMVRSVLLRGfDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKGLPGrLKVvaKSTEGPETVEG 435
Cdd:PRK10262 159 VEEALYLSNIASEVHLIHRRDGFRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTG-VRL--RDTQNSDNIES 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296040479 436 -TYNTVLLAIGRDSCTrkiglEKIGVKINEKNGKIPVN-----DVEQTNVPHVYAIGDVLE 490
Cdd:PRK10262 235 lDVAGLFVAIGHSPNT-----AIFEGQLELENGYIKVQsgihgNATQTSIPGVFAAGDVMD 290
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
165-194 |
1.01e-03 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 42.14 E-value: 1.01e-03
10 20 30
....*....|....*....|....*....|
gi 296040479 165 DYDLIVIGGGSGGLSCAKEAANLGKKVMVL 194
Cdd:PRK05329 2 KFDVLVIGGGLAGLTAALAAAEAGKRVALV 31
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
170-212 |
1.17e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 37.90 E-value: 1.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 296040479 170 VIGGGSGGLSCAKEAANLGKKVMVLDfvvpspqgTSWGLGGTC 212
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLE--------KRDRLGGNA 35
|
|
| NrdH |
cd02976 |
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
76-141 |
1.39e-03 |
|
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.
Pssm-ID: 239274 [Multi-domain] Cd Length: 73 Bit Score: 37.59 E-value: 1.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296040479 76 RVMIFSKSYCPHSSRVKELFSSLGVNYyilELDQVDDGANVQEVLTEISNQKTVPNIFVNKVHVGG 141
Cdd:cd02976 1 EVTVYTKPDCPYCKATKRFLDERGIPF---EEVDVDEDPEALEELKKLNGYRSVPVVVIGDEHLSG 63
|
|
| PTZ00062 |
PTZ00062 |
glutaredoxin; Provisional |
71-161 |
1.74e-03 |
|
glutaredoxin; Provisional
Pssm-ID: 240250 [Multi-domain] Cd Length: 204 Bit Score: 40.16 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 71 LIEGNRVMIFSKS-----YCPHSSRVKELFSSLGV---NYYILElDQvddgaNVQEVLTEISNQKTVPNIFVNKVHVGGC 142
Cdd:PTZ00062 109 LIRNHKILLFMKGsktfpFCRFSNAVVNMLNSSGVkyeTYNIFE-DP-----DLREELKVYSNWPTYPQLYVNGELIGGH 182
|
90
....*....|....*....
gi 296040479 143 DRIFQAHQNGLLQKLLQDD 161
Cdd:PTZ00062 183 DIIKELYESNSLRKVIPDD 201
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
312-491 |
2.35e-03 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 41.27 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 312 IATGE-RPRYLGIQGDKEYCITS--------------DDLFSLPYCPG-NTLIVGASYVGLECAGFLAGLGLDvTVMVrs 375
Cdd:PRK12778 523 IASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGkKVAVVGGGNTAMDSARTAKRLGAE-RVTI-- 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 376 vLLRGFDQEM---AEKVgSYLEQQGVKFQRKFTPI-------------LVQQLEKGLP---GRLKVVAksTEGpETVEGT 436
Cdd:PRK12778 600 -VYRRSEEEMparLEEV-KHAKEEGIEFLTLHNPIeyladekgwvkqvVLQKMELGEPdasGRRRPVA--IPG-STFTVD 674
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 296040479 437 YNTVLLAIGRDSctRKIGLEKI-GVKINEKnGKIPVNDVEQTNVPHVYAIGDVLEG 491
Cdd:PRK12778 675 VDLVIVSVGVSP--NPLVPSSIpGLELNRK-GTIVVDEEMQSSIPGIYAGGDIVRG 727
|
|
| PLN02661 |
PLN02661 |
Putative thiazole synthesis |
158-210 |
2.83e-03 |
|
Putative thiazole synthesis
Pssm-ID: 178267 Cd Length: 357 Bit Score: 40.58 E-value: 2.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 296040479 158 LQDDSTH-DYDLIVIGGGSGGLSCAKEaanLGK----KVMVLDFVVpSPQGTSWgLGG 210
Cdd:PLN02661 84 MTDMITYaDTDVVIVGAGSAGLSCAYE---LSKnpnvKVAIIEQSV-SPGGGAW-LGG 136
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
163-195 |
3.21e-03 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 40.60 E-value: 3.21e-03
10 20 30
....*....|....*....|....*....|...
gi 296040479 163 THDYDLIVIGGGSGGLSCAKEAANLGKKVMVLD 195
Cdd:COG1233 1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLE 33
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
165-191 |
3.23e-03 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 40.16 E-value: 3.23e-03
10 20
....*....|....*....|....*..
gi 296040479 165 DYDLIVIGGGSGGLSCAKEAANLGKKV 191
Cdd:COG3075 2 KFDVVVIGGGLAGLTAAIRAAEAGLRV 28
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
167-209 |
3.57e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 39.38 E-value: 3.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 296040479 167 DLIVIGGGSGGLSCAKE-AANLGKKVMVLDFVVpSPQGTSWGLG 209
Cdd:pfam01946 19 DVVIVGAGSSGLTAAYYlAKNRGLKVAIIERSV-SPGGGAWLGG 61
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
348-508 |
4.75e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 40.00 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 348 IVGASYVGLECAGFLAGLGLDVTVMVRsvllRGfDQEM---AEKVGsYLEQQGVKFQRKFTPILVQQLEKGlpgRLKVV- 423
Cdd:PRK12831 286 VVGGGNVAMDAARTALRLGAEVHIVYR----RS-EEELparVEEVH-HAKEEGVIFDLLTNPVEILGDENG---WVKGMk 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 424 ----------AKSTEGPETVEGTY-----NTVLLAIGRdSCTRKIGLEKIGVKINeKNGKIPVN-DVEQTNVPHVYAIGD 487
Cdd:PRK12831 357 cikmelgepdASGRRRPVEIEGSEfvlevDTVIMSLGT-SPNPLISSTTKGLKIN-KRGCIVADeETGLTSKEGVFAGGD 434
|
170 180
....*....|....*....|..
gi 296040479 488 VLEGkpELTPV-AIQAGKLLAR 508
Cdd:PRK12831 435 AVTG--AATVIlAMGAGKKAAK 454
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
167-316 |
6.46e-03 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 39.51 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 167 DLIVIGGGSGGLSCAKEAANLGKKVMVLDfvvPSP----QGTSwGLGGTCVN--------VGCIPKKLMHQ-AALLGHAL 233
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVE---RRGflggMLTS-GLVGPDMGfylnkeqvVGGIAREFRQRlRARGGLPG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 234 QDARKYGWdynqqVKHNWETMREAIQNhigslnwgyrvTLREKGVTYVnsFGEFV--------ELHKIKATNKKGQETFy 305
Cdd:pfam12831 77 PYGLRGGW-----VPFDPEVAKAVLDE-----------MLAEAGVTVL--LHTRVvgvvkeggRITGVTVETKGGRITI- 137
|
170
....*....|.
gi 296040479 306 TASKFVIATGE 316
Cdd:pfam12831 138 RAKVFIDATGD 148
|
|
| GRX_GRX_like |
cd03031 |
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ... |
90-160 |
7.75e-03 |
|
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.
Pssm-ID: 239329 [Multi-domain] Cd Length: 147 Bit Score: 37.22 E-value: 7.75e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296040479 90 RVKELFSSLGVNYYI--LELDqVDDGANVQEVLTEISNQKTVPNIFVNKVHVGGCDRIFQAHQNGLLQKLLQD 160
Cdd:cd03031 21 NVRAILESFRVKFDErdVSMD-SGFREELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKG 92
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
423-508 |
7.84e-03 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 39.38 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296040479 423 VAKSTEGPETVEGTYNT-----VLLAIGRDSCTRKIgLEKIGVKINEkNGKIPVNDVE-QTNVPHVYAIGDVLEGkPELT 496
Cdd:PRK12810 370 TELGEGDFEPVEGSEFVlpadlVLLAMGFTGPEAGL-LAQFGVELDE-RGRVAAPDNAyQTSNPKVFAAGDMRRG-QSLV 446
|
90
....*....|..
gi 296040479 497 PVAIQAGKLLAR 508
Cdd:PRK12810 447 VWAIAEGRQAAR 458
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
163-195 |
8.43e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 39.15 E-value: 8.43e-03
10 20 30
....*....|....*....|....*....|...
gi 296040479 163 THDYDLIVIGGGSGGLSCAKEAANLGKKVMVLD 195
Cdd:PRK09126 1 MMHSDIVVVGAGPAGLSFARSLAGSGLKVTLIE 33
|
|
| |
