|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
155-607 |
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: 722.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 155 YDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEY 234
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 235 NQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGI 314
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 315 QGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKVGSYMEQHGVKFLRK 394
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 395 FIPVMVQQLEKgspgklKVLAKSTEGTETIEGVYNTVLLAIGRDSCTRKIGLEKIGVKINEKSGKIPVNDVEQTNVPYVY 474
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 475 AVGDILEDKPELTPVAIQSGKLLAQRLFGASLEK------------------------------------IYHTLFWPLE 518
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVIcdyenvpttvftpleygacglseekavekfgeenveVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 519 WTVAGREN-NTCYAKIICNKFDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSG 597
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 291045268 598 LDITQKGCUG 607
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
152-607 |
2.30e-154 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 453.13 E-value: 2.30e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 152 DLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLGGTCVNVGCIPKKLMHQAALLGQAL-CDSRKF 230
Cdd:PTZ00052 1 HLTFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFhHDSQMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 231 GWEYNQQvrHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIkATNKKGQETYYTAAQFVIATGERPR 310
Cdd:PTZ00052 81 GWKTSSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 311 YL-GIQGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKVGSYMEQHGV 389
Cdd:PTZ00052 158 IPeDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 390 KFLRKFIPVMVQQLEKgspgKLKVL--AKSTEgtetiegVYNTVLLAIGRDSCTRKIGLEKIGVKINEKSGKIPVNDVeq 467
Cdd:PTZ00052 238 LFLEGVVPINIEKMDD----KIKVLfsDGTTE-------LFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 468 TNVPYVYAVGDILEDKPELTPVAIQSGKLLAQRLFGASLEKIYH-----TLFWPLEWTVAG------------------- 523
Cdd:PTZ00052 305 TNIPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYtfiptTIFTPIEYGACGysseaaiakygeddieeyl 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 524 -------------------RENN-------TCYAKIICNKFDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTI 577
Cdd:PTZ00052 385 qefntleiaavhrekheraRKDEydfdvssNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMI 464
|
490 500 510
....*....|....*....|....*....|
gi 291045268 578 GIHPTCGEVFTTLEITKSSGLDITQKGCUG 607
Cdd:PTZ00052 465 GIHPTDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
172-590 |
1.76e-105 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 325.57 E-value: 1.76e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 172 AKEAAILGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGQALCD-SRKFGWEYNQQvRHNWETMTKAIQ 250
Cdd:PRK06116 20 ANRAAMYGAKVALIE---------AKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 251 NHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKgqetyYTAAQFVIATGERPRYLGIQGdKEYCITSDDLFSL 330
Cdd:PRK06116 90 AYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIPDIPG-AEYGITSDGFFAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 331 PYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSIL-LRGFDQEMAEKVGSYMEQHGVKFLRKFIPvmvQQLEKGSPG 409
Cdd:PRK06116 164 EELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRLHTNAVP---KAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 410 KLKVlakSTEGTETIEgvYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKPELTPV 489
Cdd:PRK06116 241 SLTL---TLEDGETLT--VDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 490 AIQSGKLLAQRLF-------------------------------------GASLEKIYHTLFWPLEWTVAGREnNTCYAK 532
Cdd:PRK06116 314 AIAAGRRLSERLFnnkpdekldysniptvvfshppigtvglteeeareqyGEDNVKVYRSSFTPMYTALTGHR-QPCLMK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 291045268 533 IICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 590
Cdd:PRK06116 393 LVVVG-KEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
171-590 |
7.66e-94 |
|
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: 295.84 E-value: 7.66e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 171 CAKEAAILGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYnQQVRHNWETMTKAIQ 250
Cdd:COG1249 18 AAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISA-GAPSVDWAALMARKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 251 NHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATnkkGQETYyTAAQFVIATGERPRYLGIQG-DKEYCITSDDLFS 329
Cdd:COG1249 88 KVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT---GGETL-TADHIVIATGSRPRVPPIPGlDEVRVLTSDEALE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 330 LPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEKgSP 408
Cdd:COG1249 164 LEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDILTG---AKVTSVEK-TG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 409 GKLKVLAKSTEGTETIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILeDKPELTP 488
Cdd:COG1249 240 DGVTVTLEDGGGEEAVEA--DKVLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 489 VAIQSGKLLAQRLFGASLEKIYHTLF------WP-----------------------LEWTVAGR----ENNTCYAKIIC 535
Cdd:COG1249 316 VASAEGRVAAENILGKKPRPVDYRAIpsvvftDPeiasvglteeeareagidvkvgkFPFAANGRalalGETEGFVKLIA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 291045268 536 NKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 590
Cdd:COG1249 396 DA-ETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
155-590 |
3.55e-85 |
|
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: 272.84 E-value: 3.55e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 155 YDYDLIIIGGGSGGLSCAKEAAILGKKVMV--LDFVvpspqgtswglGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGW 232
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 233 EyNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQetyYTAAQFVIATGERPRYL 312
Cdd:TIGR01424 70 T-VGKARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 313 GIQGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVR-SILLRGFDQEMAEKVGSYMEQHGVKF 391
Cdd:TIGR01424 146 ALPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 392 LRKFIpvmVQQLEKGSPGKLKVlakSTEGTETIegVYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVP 471
Cdd:TIGR01424 225 LPEDS---ITSISKDDDGRLKA---TLSKHEEI--VADVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 472 YVYAVGDIlEDKPELTPVAIQSGKLLAQRLFGASLEK----------------------------------IYHTLFWPL 517
Cdd:TIGR01424 296 SIYAVGDV-TDRINLTPVAIHEATCFAETEFGNNPTSfdhdliatavfsqppigtvglteeearrkfgdieVYRAEFRPM 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291045268 518 EWTVAGRENNtCYAKIICNKFDhDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 590
Cdd:TIGR01424 375 KATFSGRQEK-TLMKLVVDAKD-DKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
172-590 |
8.59e-79 |
|
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: 256.31 E-value: 8.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 172 AKEAAILGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMTKAIQN 251
Cdd:TIGR01421 18 ARRAAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 252 HISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKgqetyYTAAQFVIATGERPRYL-GIQGdKEYCITSDDLFSL 330
Cdd:TIGR01421 89 YVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIPG-AELGTDSDGFFAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 331 PYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVR-SILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVmvqQLEKGSPG 409
Cdd:TIGR01421 163 EELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPV---KVEKTVEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 410 KLKVLAksTEGTETIEgvYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILeDKPELTPV 489
Cdd:TIGR01421 240 KLVIHF--EDGKSIDD--VDELIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 490 AIQSGKLLAQRLFG------------------------------ASLE-------KIYHTLFWPLEWTVaGRENNTCYAK 532
Cdd:TIGR01421 314 AIAAGRKLSERLFNgktddkldynnvptvvfshppigtigltekEAIEkygkeniKVYNSSFTPMYYAM-TSEKQKCRMK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 291045268 533 IIC-NKfdHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 590
Cdd:TIGR01421 393 LVCaGK--EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
151-590 |
2.20e-76 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 251.66 E-value: 2.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 151 EDLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDfvVP-SPQGTSW--GLGGTCVNVGCIPKKLMHQAALLGQALCDS 227
Cdd:PLN02507 20 NATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICE--LPfHPISSESigGVGGTCVIRGCVPKKILVYGATFGGEFEDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 228 RKFGWEYNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGE 307
Cdd:PLN02507 98 KNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 308 RPRYLGIQGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSIL-LRGFDQEMAEKVGSYMEQ 386
Cdd:PLN02507 178 RAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMRAVVARNLEG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 387 HGVKFLRKfipVMVQQLEKGSPGkLKVLAKSTEgtetiEGVYNTVLLAIGRDSCTRKIGLEKIGVKInEKSGKIPVNDVE 466
Cdd:PLN02507 257 RGINLHPR---TNLTQLTKTEGG-IKVITDHGE-----EFVADVVLFATGRAPNTKRLNLEAVGVEL-DKAGAVKVDEYS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 467 QTNVPYVYAVGDIlEDKPELTPVAIQSGKLLAQRLFGASLEK-----------------------------------IYH 511
Cdd:PLN02507 327 RTNIPSIWAIGDV-TNRINLTPVALMEGTCFAKTVFGGQPTKpdyenvacavfcipplsvvglseeeaveqakgdilVFT 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291045268 512 TLFWPLEWTVAGRENNTcYAKIICNKFDhDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 590
Cdd:PLN02507 406 SSFNPMKNTISGRQEKT-VMKLIVDAET-DKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTM 482
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
155-590 |
6.14e-76 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 252.10 E-value: 6.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 155 YDYDLIIIGGGSGGLSCAKEAAILGKKVMV--LDFVVPSPQGTSwGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGW 232
Cdd:PLN02546 78 YDFDLFTIGAGSGGVRASRFASNFGASAAVceLPFATISSDTLG-GVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGW 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 233 EYNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKkgqetYYTAAQFVIATGERPRYL 312
Cdd:PLN02546 157 KYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGK-----LYTARNILIAVGGRPFIP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 313 GIQGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKVGSYMEQHGVKF 391
Cdd:PLN02546 232 DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQkKVLRGFDEEVRDFVAEQMSLRGIEF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 392 LRKFIPvmvQQLEKGSPGKLKVlaKSTEGteTIEGvYNTVLLAIGRDSCTRKIGLEKIGVKINeKSGKIPVNDVEQTNVP 471
Cdd:PLN02546 311 HTEESP---QAIIKSADGSLSL--KTNKG--TVEG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 472 YVYAVGDIlEDKPELTPVAIQSGKLLAQRLFGASLEK----------------------------------IYHTLFWPL 517
Cdd:PLN02546 382 SIWAVGDV-TDRINLTPVALMEGGALAKTLFGNEPTKpdyravpsavfsqppigqvglteeqaieeygdvdVFTANFRPL 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291045268 518 EWTVAGRENNTCYAKIICNKfdHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 590
Cdd:PLN02546 461 KATLSGLPDRVFMKLIVCAK--TNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTM 531
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
171-586 |
3.58e-64 |
|
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: 217.90 E-value: 3.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 171 CAKEAAILGKKVMVldfvVPSPQgtswgLGGTCVNVGCIPKK-LMHQAALLGQALcDSRKFGWEYNqQVRHNWETMTKAI 249
Cdd:TIGR01350 16 AAIRAAQLGLKVAL----VEKEY-----LGGTCLNVGCIPTKaLLHSAEVYDEIK-HAKDLGIEVE-NVSVDWEKMQKRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 250 QNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETyYTAAQFVIATGERPRYL--GIQGDKEYCITSDDL 327
Cdd:TIGR01350 85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLpgPFDFDGKVVITSTGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 328 FSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTV--MVRSIlLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEK 405
Cdd:TIGR01350 164 LNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTN---TKVTAVEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 406 GspGKLKVLAKSTEGTETIEGVYntVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILEdKPE 485
Cdd:TIGR01350 240 N--DDQVTYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIG-GPM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 486 LTPVAIQSGKLLAQRLFGASLEKIYHTLFWPLEWT---VA--------------------------GR----ENNTCYAK 532
Cdd:TIGR01350 314 LAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTdpeVAsvglteeqakeagydvkigkfpfaanGKalalGETDGFVK 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 291045268 533 IICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 586
Cdd:TIGR01350 394 IIADK-KTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
175-585 |
6.14e-60 |
|
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: 207.52 E-value: 6.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 175 AAILGKKVMVLDfvVPSPQGTSW--GLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQ-VRHNWETMTKAIQN 251
Cdd:TIGR01423 23 ATLYKKRVAVVD--VQTHHGPPFyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDRSsVKANWKALIAAKNK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 252 HISSLNWGYRLSLRE-KAVAYVNSYGEFVEHHKI----KATNKKGQETYYTAAQFVIATGERPRYLGIQGDkEYCITSDD 326
Cdd:TIGR01423 101 AVLDINKSYEGMFADtEGLTFFLGWGALEDKNVVlvreSADPKSAVKERLQAEHILLATGSWPQMLGIPGI-EHCISSNE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 327 LFSLPYCPGKTLVVGASYVALECAGFLAGF---GLDVTVMVR-SILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVqq 402
Cdd:TIGR01423 180 AFYLDEPPRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRnNMILRGFDSTLRKELTKQLRANGINIMTNENPAKV-- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 403 lEKGSPGKLKVLAKSTEGTEtiegvYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlED 482
Cdd:TIGR01423 258 -TLNADGSKHVTFESGKTLD-----VDVVMMAIGRVPRTQTLQLDKVGVELTKK-GAIQVDEFSRTNVPNIYAIGDV-TD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 483 KPELTPVAIQSGKLLAQRLFGA--------------------------------SLEK--IYHTLFWPLEWTVAGRENNT 528
Cdd:TIGR01423 330 RVMLTPVAINEGAAFVDTVFGNkprktdhtrvasavfsippigtcglveedaakKFEKvaVYESSFTPLMHNISGSKYKK 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 291045268 529 CYAKIICNKFDHDrVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGE 585
Cdd:TIGR01423 410 FVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
199-590 |
7.90e-58 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 203.69 E-value: 7.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 199 LGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGweYNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEF 278
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYG--FDTQFSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 279 VEHHKIKATNKKGQETYY------------------------TAAQFVIATGERPRYLGIQGdKEYCITSDDLFSLPYcP 334
Cdd:PTZ00058 160 LSENQVLIKKVSQVDGEAdesdddevtivsagvsqlddgqviEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 335 GKTLVVGASYVALECAGFLAGFGLDVTVMVR-SILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEkgSPGKLKV 413
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVK--EKNLTIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 414 LAKSTEgtetiEGVYNTVLLAIGRDSCTRKIGLEkiGVKINEKSGKIPVNDVEQTNVPYVYAVGDILEDKP--------- 484
Cdd:PTZ00058 316 LSDGRK-----YEHFDYVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 485 ------------------------ELTPVAIQSGKLLAQRLFGASLE--------------------------------- 507
Cdd:PTZ00058 389 lklyneepylkkkentsgesyynvQLTPVAINAGRLLADRLFGPFSRttnyklipsvifshppigtiglseqeaidiygk 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 508 ---KIYHTLFWPLEWTVAGRE---NNTCYAKIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHP 581
Cdd:PTZ00058 469 envKIYESRFTNLFFSVYDMDpaqKEKTYLKLVCVG-KEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHP 547
|
....*....
gi 291045268 582 TCGEVFTTL 590
Cdd:PTZ00058 548 TAAEEFVTM 556
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
171-589 |
2.39e-54 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 191.54 E-value: 2.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 171 CAKEAAILGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYnQQVRHNWETMTKAIQ 250
Cdd:PRK06292 18 AARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHA-DGPKIDFKKVMARVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 251 NHISSLNWGYRLSLREK-AVAYVNSYGEFVEHHKIKATnkkgqETYYTAAQFVIATGER-PRYLGI-QGDKEYCITSDDL 327
Cdd:PRK06292 88 RERDRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEVN-----GERIEAKNIVIATGSRvPPIPGVwLILGDRLLTSDDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 328 FSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKVgsymeqhgVKFLRKFIPVM----VQQ 402
Cdd:PRK06292 163 FELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQA--------QKILSKEFKIKlgakVTS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 403 LEKGSpGKLKVLAKSTEGTETIEGVYntVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILeD 482
Cdd:PRK06292 235 VEKSG-DEKVEELEKGGKTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSVPGIYAAGDVN-G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 483 KPELTPVAIQSGKLLAQRLFGASLEKI-YHtlfwPLEWTV------AG--------RENNTCYA---------------- 531
Cdd:PRK06292 310 KPPLLHEAADEGRIAAENAAGDVAGGVrYH----PIPSVVftdpqiASvglteeelKAAGIDYVvgevpfeaqgrarvmg 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291045268 532 ------KIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLT-KQLLdDTIGIHPTCGEVFTT 589
Cdd:PRK06292 386 kndgfvKVYADK-KTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTvEDLL-RMPFYHPTLSEGLRT 448
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
171-586 |
1.50e-53 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 189.59 E-value: 1.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 171 CAKEAAILGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYnQQVRHNWetmtKAIQ 250
Cdd:PRK06416 19 AAIRAAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKA-ENVGIDF----KKVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 251 NH----ISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYyTAAQFVIATGERPRYL-GIQGDKEYCITSD 325
Cdd:PRK06416 85 EWkngvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTY-TAKNIILATGSRPRELpGIEIDGRVIWTSD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 326 DLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTV---MVRsiLLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQ 402
Cdd:PRK06416 164 EALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALKKRGIKIKTG---AKAKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 403 LEKGSPGkLKVLAKSTEGTETIEGVYntVLLAIGRDSCTRKIGLEKIGVKINEksGKIPVNDVEQTNVPYVYAVGDILEd 482
Cdd:PRK06416 239 VEQTDDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIVG- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 483 KPELTPVAIQSGKLLAQRLFGASLEKIYHTLfwP-----------------------LEWTVA-------GR---ENNTC 529
Cdd:PRK06416 313 GPMLAHKASAEGIIAAEAIAGNPHPIDYRGI--PavtythpevasvglteakakeegFDVKVVkfpfagnGKalaLGETD 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 291045268 530 -YAKIICNKFDHdRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 586
Cdd:PRK06416 391 gFVKLIFDKKDG-EVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
171-494 |
9.13e-51 |
|
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: 177.51 E-value: 9.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 171 CAKEAAILGKKVMVLdfvvpspqgtswGLGGTCVNVGCIPKKLMHQAALLGQALcdsrkfgweynqqvrHNWETMTKAIQ 250
Cdd:pfam07992 15 AALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAAEAPEIA---------------SLWADLYKRKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 251 NHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKikatnKKGQETYYTAAQFVIATGERPRYLGIQGDKEYC------ITS 324
Cdd:pfam07992 68 EVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEEL-----VDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtLDS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 325 DDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQL 403
Cdd:pfam07992 143 AEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGVEVRLG---TSVKEI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 404 EkGSPGKLKVLaksTEGTETIEgvYNTVLLAIGRDSCTRkiGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILEDK 483
Cdd:pfam07992 220 I-GDGDGVEVI---LKDGTEID--ADLVVVAIGRRPNTE--LLEAAGLELDER-GGIVVDEYLRTSVPGIYAAGDCRVGG 290
|
330
....*....|.
gi 291045268 484 PELTPVAIQSG 494
Cdd:pfam07992 291 PELAQNAVAQG 301
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
172-607 |
2.13e-46 |
|
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: 169.91 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 172 AKEAAILGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVrhNWETMTKAIQN 251
Cdd:TIGR02053 16 AIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATVAV--DFGELLEGKRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 252 HISSL-NWGYRLSLREKAVAYVNSYGEFVEHHKIKAtnKKGQETYYtAAQFVIATGERPRYLGIQGDKE--YcITSDDLF 328
Cdd:TIGR02053 85 VVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGREVRG-AKRFLIATGARPAIPPIPGLKEagY-LTSEEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 329 SLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEKGS 407
Cdd:TIGR02053 161 ALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTS---AQVKAVSVRG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 408 PGKLKVLAKSTEGTEtIEGVYntVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILeDKPELT 487
Cdd:TIGR02053 238 GGKIITVEKPGGQGE-VEADE--LLVATGRRPNTDGLGLEKAGVKLDER-GGILVDETLRTSNPGIYAAGDVT-GGLQLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 488 PVAIQSGKLLAQRLFGASLEKIYHTLF-------------------------------WPLEWTVAGREN--NTCYAKII 534
Cdd:TIGR02053 313 YVAAKEGVVAAENALGGANAKLDLLVIprvvftdpavasvglteaeaqkagiecdcrtLPLTNVPRARINrdTRGFIKLV 392
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291045268 535 CNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSglDITQKGCUG 607
Cdd:TIGR02053 393 AEP-GTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFYR--DVSKLSCCA 462
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
171-590 |
4.30e-41 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 154.98 E-value: 4.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 171 CAKEAAILGKKVMVLdfvvpspqGTSWgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMtKAIQ 250
Cdd:PRK06370 20 LAARAAGLGMKVALI--------ERGL-LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAV-MARK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 251 NHIS--SLNwGYRLSLREKA-VAYVNSYGEFVEHHKIKATNKKgqetyYTAAQFVIATGERPRYLGIQG--DKEYcITSD 325
Cdd:PRK06370 90 RRIRarSRH-GSEQWLRGLEgVDVFRGHARFESPNTVRVGGET-----LRAKRIFINTGARAAIPPIPGldEVGY-LTNE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 326 DLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKVGSYMEQHGVKFLrkfIPVMVQQLE 404
Cdd:PRK06370 163 TIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGpRLLPREDEDVAAAVREILEREGIDVR---LNAECIRVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 405 KGSPGKLkVLAKSTEGTETIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKP 484
Cdd:PRK06370 240 RDGDGIA-VGLDCNGGAPEITG--SHILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 485 ELTPVAIQSGKLLAQRLFG-----ASLEKIYHTLFW--PL--------EWTVAGRENNTC------------------YA 531
Cdd:PRK06370 315 AFTHTAYNDARIVAANLLDggrrkVSDRIVPYATYTdpPLarvgmteaEARKSGRRVLVGtrpmtrvgravekgetqgFM 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 291045268 532 KIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 590
Cdd:PRK06370 395 KVVVDA-DTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| GRX_GRXh_1_2_like |
cd03419 |
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ... |
67-148 |
9.71e-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: 131.51 E-value: 9.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 67 RVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQ 146
Cdd:cd03419 1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
|
..
gi 291045268 147 KL 148
Cdd:cd03419 81 KL 82
|
|
| GRX_euk |
TIGR02180 |
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ... |
68-149 |
3.24e-35 |
|
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: 127.36 E-value: 3.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 68 VVIFSKSYCPHSTRVKELFSSLGVE-CNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQ 146
Cdd:TIGR02180 1 VVVFSKSYCPYCKKAKEILAKLNVKpYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKLA 80
|
...
gi 291045268 147 KLL 149
Cdd:TIGR02180 81 ELL 83
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
175-586 |
3.21e-33 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 132.74 E-value: 3.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 175 AAILGKKVMVLDfVVPSPQGTSwGLGGTCVNVGCIPKK-LMHQAALLGQALCDSRKFGWEYNqQVRHNWETMTKAIQNHI 253
Cdd:PRK06327 23 AAQLGLKVACIE-AWKNPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGIHVD-GVKIDVAKMIARKDKVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 254 SSLNWGYRLSLREKAVAYVNSYGEFV----EHHKIKATNKKGQETyyTAAQFVIATGERPRYL-GIQGDKEYCITSDDLF 328
Cdd:PRK06327 100 KKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDETVI--TAKHVIIATGSEPRHLpGVPFDNKIILDNTGAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 329 SLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEKGS 407
Cdd:PRK06327 178 NFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTKQGLDIHLG---VKIGEIKTGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 408 PGKLKVLAKSTEGTETIEgvYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILEdKPELT 487
Cdd:PRK06327 255 KGVSVAYTDADGEAQTLE--VDKLIVSIGRVPNTDGLGLEAVGLKLDER-GFIPVDDHCRTNVPNVYAIGDVVR-GPMLA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 488 PVAIQSGKLLAQRLFGASLEKIYHTLFW-----P-LEW--------TVAGRE------------------NNTCYAKIIC 535
Cdd:PRK06327 331 HKAEEEGVAVAERIAGQKGHIDYNTIPWviytsPeIAWvgkteqqlKAEGVEykagkfpfmangralamgEPDGFVKIIA 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 291045268 536 NKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 586
Cdd:PRK06327 411 DA-KTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEV 460
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
179-586 |
1.44e-31 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 127.76 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 179 GKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGweYNQQVRH-NWETMTKAIQNHISSLN 257
Cdd:PRK07846 22 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 258 WG---YRLslREKA-VAYVNSYGEFVEHHKIKAtnkkGQETYYTAAQFVIATGERPRYLGIQGDKE--YcITSDDLFSLP 331
Cdd:PRK07846 91 AGgeeYRG--RDTPnIDVYRGHARFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSGvrY-HTSDTIMRLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 332 YCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKvgsYMEQHGVKF-LRkfIPVMVQQLEKGSPG 409
Cdd:PRK07846 164 ELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISER---FTELASKRWdVR--LGRNVVGVSQDGSG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 410 KLKVLAksteGTETIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKPELTPV 489
Cdd:PRK07846 239 VTLRLD----DGSTVEA--DVLLVATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV-SSPYQLKHV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 490 AIQSGKLLAQRLF-GASLEKIYHtLFWP-----------------------LEWTVA-----------GRENNTCYAKII 534
Cdd:PRK07846 311 ANHEARVVQHNLLhPDDLIASDH-RFVPaavfthpqiasvgltenearaagLDITVKvqnygdvaygwAMEDTTGFVKLI 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 291045268 535 CNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLT-KQLLDDTIGIHPTCGEV 586
Cdd:PRK07846 390 ADR-DTGRLLGAHIIGPQASTLIQPLIQAMSFGLDaREMARGQYWIHPALPEV 441
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
172-504 |
9.27e-30 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 122.57 E-value: 9.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 172 AKEAAILGKKVMVLDfvvpspqgTSWGLGGTCVNVGCIPKKLMHQAALlgqalcdsRKFGWEYNQQVRHN----WETMT- 246
Cdd:PRK05249 21 AMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVL--------RLIGFNQNPLYSSYrvklRITFAd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 247 ------KAIQNHISSLnwgyRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERP-RYLGIQGDKE 319
Cdd:PRK05249 85 llaradHVINKQVEVR----RGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPyRPPDVDFDHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 320 YCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFLRKFIpv 398
Cdd:PRK05249 161 RIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEE-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 399 mVQQLEKGSPGKLKVLaKSteGTeTIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGD 478
Cdd:PRK05249 239 -VEKVEGGDDGVIVHL-KS--GK-KIKA--DCLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNENYQTAVPHIYAVGD 310
|
330 340
....*....|....*....|....*.
gi 291045268 479 ILeDKPELTPVAIQSGKLLAQRLFGA 504
Cdd:PRK05249 311 VI-GFPSLASASMDQGRIAAQHAVGE 335
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
193-586 |
2.56e-29 |
|
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: 121.02 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 193 QGTswgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYN-QQVRhnWETMTKAIQNH----ISSLNWGYRLSLREK 267
Cdd:TIGR03452 31 KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLGIDAEiDSVR--WPDIVSRVFGDridpIAAGGEDYRRGDETP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 268 AVAYVNSYGEFVEHHKIKAtnkkGQETYYTAAQFVIATGERPR---YLGIQGDKEYciTSDDLFSLPYCPGKTLVVGASY 344
Cdd:TIGR03452 106 NIDVYDGHARFVGPRTLRT----GDGEEITGDQIVIAAGSRPYippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 345 VALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKvgsYMEQHGVKF---LRKFIpVMVQQLEKGspgklkvLAKSTEG 420
Cdd:TIGR03452 180 IAAEFAHVFSALGTRVTIVNRStKLLRHLDEDISDR---FTEIAKKKWdirLGRNV-TAVEQDGDG-------VTLTLDD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 421 TETIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEkSGKIPVNDVEQTNVPYVYAVGDILEDKpELTPVAIQSGKLLAQR 500
Cdd:TIGR03452 249 GSTVTA--DVLLVATGRVPNGDLLDAEAAGVEVDE-DGRIKVDEYGRTSARGVWALGDVSSPY-QLKHVANAEARVVKHN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 501 LFG-ASLEKIYHTlFWPL----------------EWTVAGR------------------ENNTCYAKIICNKfDHDRVIG 545
Cdd:TIGR03452 325 LLHpNDLRKMPHD-FVPSavfthpqiatvglteqEAREAGHditvkiqnygdvaygwamEDTTGFCKLIADR-DTGKLLG 402
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 291045268 546 FHILGPNAGEVTQGFAAAMKCGLT-KQLLDDTIGIHPTCGEV 586
Cdd:TIGR03452 403 AHIIGPQASSLIQPLITAMAFGLDaREMARKQYWIHPALPEV 444
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
171-606 |
2.90e-25 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 110.24 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 171 CAKEAAILGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYN-------------QQ 237
Cdd:PRK13748 113 AALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAAtvptidrsrllaqQQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 238 VRhnWETMTKAIQNHISSLNwgyrlslreKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGIQGD 317
Cdd:PRK13748 184 AR--VDELRHAKYEGILDGN---------PAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 318 KE--YCITSDDLFSlPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKVGSYMEQHGVKFLRKf 395
Cdd:PRK13748 253 KEtpYWTSTEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEH- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 396 ipvmVQQLEKGSPGKLKVLaksTEGTETIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINeKSGKIPVNDVEQTNVPYVYA 475
Cdd:PRK13748 331 ----TQASQVAHVDGEFVL---TTGHGELRA--DKLLVATGRAPNTRSLALDAAGVTVN-AQGAIVIDQGMRTSVPHIYA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 476 VGDIlEDKPELTPVAIQSGKLLAQRLFGAS----LEKIYHTLFW-PLEWTVAGRENNTCYAKI---------------IC 535
Cdd:PRK13748 401 AGDC-TDQPQFVYVAAAAGTRAAINMTGGDaaldLTAMPAVVFTdPQVATVGYSEAEAHHDGIetdsrtltldnvpraLA 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 536 NkFDHD------------RVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPT-------CGEVFTTleitkss 596
Cdd:PRK13748 480 N-FDTRgfiklvieegsgRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTmveglklAAQTFNK------- 551
|
490
....*....|
gi 291045268 597 glDITQKGCU 606
Cdd:PRK13748 552 --DVKQLSCC 559
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
172-505 |
7.02e-25 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 107.91 E-value: 7.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 172 AKEAAILGKKVMVLDfvvPSPQGtswgLGGTCVNVGCIPKKLMHQAAllgqalcdsrKFGWEYNQQVRHNwETMTkaiqn 251
Cdd:PRK07251 19 AAKLASAGKKVALVE---ESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQVMATK-NTVT----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 252 hiSSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATnkKGQETY-YTAAQFVIATGERPRYLGIQG--DKEYCITSDDLF 328
Cdd:PRK07251 76 --SRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQ--AGDEKIeLTAETIVINTGAVSNVLPIPGlaDSKHVYDSTGIQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 329 SLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEKGS 407
Cdd:PRK07251 152 SLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLN---AHTTEVKNDG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 408 PgklKVLAKSTEGTETiegvYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKPELT 487
Cdd:PRK07251 229 D---QVLVVTEDETYR----FDALLYATGRKPNTEPLGLENTDIELTER-GAIKVDDYCQTSVPGVFAVGDV-NGGPQFT 299
|
330
....*....|....*...
gi 291045268 488 PVAIQSGKLLAQRLFGAS 505
Cdd:PRK07251 300 YISLDDFRIVFGYLTGDG 317
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
508-590 |
8.37e-25 |
|
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: 99.17 E-value: 8.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 508 KIYHTLFWPLEWTVAGRENNtCYAKIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVF 587
Cdd:pfam02852 29 KVGKFPFAANGRALAYGDTD-GFVKLVADR-ETGKILGAHIVGPNAGELIQEAALAIKMGATVEDLANTIHIHPTLSEAL 106
|
...
gi 291045268 588 TTL 590
Cdd:pfam02852 107 VEA 109
|
|
| GRX_family |
cd02066 |
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
67-141 |
1.19e-22 |
|
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: 91.76 E-value: 1.19e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291045268 67 RVVIFSKSYCPHSTRVKELFSSLGVEcnVLELDQVDDGArVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQ 141
Cdd:cd02066 1 KVVVFSKSTCPYCKRAKRLLESLGIE--FEEIDILEDGE-LREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
200-590 |
1.64e-20 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 94.46 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 200 GGTCVNVGCIP-KKLMHQAallgqalcdsrkfgweynqQVRHNWETmtkAIQNHISSLNWgyrlsLREK---------AV 269
Cdd:NF040477 40 GGTCINIGCIPtKTLVHDA-------------------EQHQDFST---AMQRKSSVVGF-----LRDKnyhnladldNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 270 AYVNSYGEFVEHHKIKATNKKGQETYYTAAQFvIATGERPRYLGIQGDKEY--CITSDDLFSLPYCPGKTLVVGASYVAL 347
Cdd:NF040477 93 DVINGRAEFIDNHTLRVFQADGEQELRGEKIF-INTGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 348 ECAGFLAGFGLDVTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFLrkfIPVMVQQLEkgspgklkvlakSTEGT---ET 423
Cdd:NF040477 172 EFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVELI---LNAQVQRVS------------SHEGEvqlET 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 424 IEGVY--NTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKPELTPVAIQSGKLLAQRL 501
Cdd:NF040477 237 AEGVLtvDALLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 502 FGASL------EKIYHTLFW--PL--------EWTVAGRE-----------------NNT-CYAKIICNKfDHDRVIGFH 547
Cdd:NF040477 315 LGEGKrstddrQNVPYSVFMtpPLsrigmteeQARASGADiqvvtlpvaaiprarvmNDTrGVLKAVVDN-KTQRILGVS 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 291045268 548 ILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 590
Cdd:NF040477 394 LLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDL 436
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
296-494 |
9.21e-20 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 90.18 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 296 YTAAQFVIATGERPRYLGIQGDKE-------YCITSDdlfsLPYCPGKT-LVVGASYVALECAGFLAGFGLDVTVMVRSI 367
Cdd:COG0492 99 YEAKAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEALYLTKFASKVTLIHRRD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 368 LLRGfDQEMAEKVgsyMEQHGVKFLRKFIPVMVQ---QLEKgspgkLKVLAKSTEGTETIEgvYNTVLLAIGRDSCTRki 444
Cdd:COG0492 175 ELRA-SKILVERL---RANPKIEVLWNTEVTEIEgdgRVEG-----VTLKNVKTGEEKELE--VDGVFVAIGLKPNTE-- 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 291045268 445 GLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILEDKPELTPVAIQSG 494
Cdd:COG0492 242 LLKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEG 290
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
302-507 |
4.39e-19 |
|
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: 88.71 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 302 VIATGERPRYLGIQGdkeycITSDDLFSL------PYC--------PGKTLVVGASYVALECAGFLAGFGLDVTVMVRS- 366
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddaDALrealkefkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 367 ILLRGFDQEMAEKVGSYMEQHGVKFLRKFipvMVQQLEkgspGKLKVLAKSTEGtETIEgvYNTVLLAIGrdsctrkIG- 445
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGE---TVVAID----GDDKVAVTLTDG-EEIP--ADLVVVAPG-------VRp 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291045268 446 ----LEKIGVKINEkSGKIPVNDVEQTNVPYVYAVGDILE------DKPELTP---VAIQSGKLLAQRLFGASLE 507
Cdd:COG0446 221 ntelAKDAGLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasAANKQGRVAAENILGGPAP 294
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
175-478 |
9.27e-19 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 89.53 E-value: 9.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 175 AAILGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEY--NQQVRHNWETMTKAIQNH 252
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFidDGEARVDLPAVNARVKAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 253 ISSLNWGYRLSLREKAVAYVNSYGEFVE----HHKIKATNKKGQETYYTAAQFVIATGERPRYL-GIQGDKEYCITSDDL 327
Cdd:PRK07845 91 AAAQSADIRARLEREGVRVIAGRGRLIDpglgPHRVKVTTADGGEETLDADVVLIATGASPRILpTAEPDGERILTWRQL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 328 FSLPYCPGKTLVVGASYVALECAGFLAGFGLDVT-VMVRSILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEKG 406
Cdd:PRK07845 171 YDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVERTGDG 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291045268 407 spgklkVLAKSTEGTeTIEGVYntVLLAIGRDSCTRKIGLEKIGVKINEkSGKIPVNDVEQTNVPYVYAVGD 478
Cdd:PRK07845 251 ------VVVTLTDGR-TVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIYAAGD 312
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
336-412 |
2.64e-17 |
|
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: 76.86 E-value: 2.64e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291045268 336 KTLVVGASYVALECAGFLAGFGLDVTVMVRSI-LLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEKGSPGKLK 412
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDrLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
200-479 |
1.41e-16 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 82.37 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 200 GGTCVNVGCIPKK-LMHQAAllgqalcdsrkfgweynqqvRHNweTMTKAIQNHISSLNWgyrlsLREKA---------V 269
Cdd:PRK08010 40 GGTCINIGCIPTKtLVHDAQ--------------------QHT--DFVRAIQRKNEVVNF-----LRNKNfhnladmpnI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 270 AYVNSYGEFVEHHKIKaTNKKGQETYYTAAQFVIATGERPRYLGIQG--DKEYCITSDDLFSLPYCPGKTLVVGASYVAL 347
Cdd:PRK08010 93 DVIDGQAEFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIPGitTTPGVYDSTGLLNLKELPGHLGILGGGYIGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 348 ECAGFLAGFGLDVTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFlrkfipVMVQQLEKGSPGKLKVLAKSTEGTETIEG 426
Cdd:PRK08010 172 EFASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDI------ILNAHVERISHHENQVQVHSEHAQLAVDA 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 291045268 427 vyntVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDI 479
Cdd:PRK08010 246 ----LLIASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNIWAMGDV 293
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
302-504 |
2.79e-16 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 80.96 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 302 VIATGERPRYLGIQG-DKEYCI---TSDDLFSL-PYCPGKT--LVVGASYVALECAGFLAGFGLDVTVMVRS--ILLRGF 372
Cdd:COG1251 103 VLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 373 DQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEkgspGKLKVLAKSTEGTETIEGvyNTVLLAIG---RDSCTRKIGLEki 449
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVRLG---TGVTEIE----GDDRVTGVRLADGEELPA--DLVVVAIGvrpNTELARAAGLA-- 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291045268 450 gvkINeksGKIPVNDVEQTNVPYVYAVGDILE--------DKPELTPVAIQSGKLLAQRLFGA 504
Cdd:COG1251 252 ---VD---RGIVVDDYLRTSDPDIYAAGDCAEhpgpvygrRVLELVAPAYEQARVAAANLAGG 308
|
|
| GRX_bact |
TIGR02181 |
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
68-149 |
6.15e-16 |
|
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: 72.68 E-value: 6.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 68 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDqvDDGARVQEVLsEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQK 147
Cdd:TIGR02181 1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVD--GDPALRDEMM-QRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDP 77
|
..
gi 291045268 148 LL 149
Cdd:TIGR02181 78 LL 79
|
|
| Glutaredoxin |
pfam00462 |
Glutaredoxin; |
68-130 |
1.26e-15 |
|
Glutaredoxin;
Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 71.38 E-value: 1.26e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291045268 68 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDQvDDGARvqEVLSEITNQKTVPNIFVNKVHV 130
Cdd:pfam00462 1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDE-DPEIR--EELKELSGWPTVPQVFIDGEHI 60
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
172-478 |
2.14e-13 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 73.02 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 172 AKEAAILGKKVMVLdfvvpspQGTSWGLGGTCVNVGCIPKKLMHQAA----------------LLGQALCDSRKFGWEYN 235
Cdd:PTZ00153 132 AINAMERGLKVIIF-------TGDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVERN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 236 QQVRHNWETMTKAIQNH----ISSLNWGYRLSLREKAVAYVNSYGEFV-EHHKIKATN-----KKGQEtyYTAAQFVIAT 305
Cdd:PTZ00153 205 QLVADTVQIDITKLKEYtqsvIDKLRGGIENGLKSKKFCKNSEHVQVIyERGHIVDKNtikseKSGKE--FKVKNIIIAT 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 306 GERPRY-LGIQGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVT-VMVRSILLRGFDQEMAekvgSY 383
Cdd:PTZ00153 283 GSTPNIpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLLPLLDADVA----KY 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 384 MEQHGVKF--LRKFIPVMVQQLeKGSPGKLKVLAKSTEGTE-----------TIEGVY-NTVLLAIGRDSCTRKIGLEKI 449
Cdd:PTZ00153 359 FERVFLKSkpVRVHLNTLIEYV-RAGKGNQPVIIGHSERQTgesdgpkknmnDIKETYvDSCLVATGRKPNTNNLGLDKL 437
|
330 340 350
....*....|....*....|....*....|....*
gi 291045268 450 GVKINEksGKIPVND---VEQTN---VPYVYAVGD 478
Cdd:PTZ00153 438 KIQMKR--GFVSVDEhlrVLREDqevYDNIFCIGD 470
|
|
| GRX_GRXb_1_3_like |
cd03418 |
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ... |
68-143 |
2.49e-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: 65.30 E-value: 2.49e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291045268 68 VVIFSKSYCPHSTRVKELFSSLGVECNvlELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSG 143
Cdd:cd03418 2 VEIYTKPNCPYCVRAKALLDKKGVDYE--EIDVDGDPALREEMINRSGGRRTVPQIFIGDVHIGGCDDLYALERKG 75
|
|
| GrxC |
COG0695 |
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
67-150 |
7.17e-12 |
|
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 60.98 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 67 RVVIFSKSYCPHSTRVKELFSSLGV---ECNVLEldqvDDGARvqEVLSEITNQKTVPNIFVNKVHVGGCDqtfqayqSG 143
Cdd:COG0695 1 KVTLYTTPGCPYCARAKRLLDEKGIpyeEIDVDE----DPEAR--EELRERSGRRTVPVIFIGGEHLGGFD-------EG 67
|
....*..
gi 291045268 144 LLQKLLQ 150
Cdd:COG0695 68 ELDALLA 74
|
|
| GlrX-like_plant |
TIGR02189 |
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ... |
62-151 |
9.47e-12 |
|
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: 61.70 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 62 LIERSRVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQ 141
Cdd:TIGR02189 4 MVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALHI 83
|
90
....*....|
gi 291045268 142 SGLLQKLLQE 151
Cdd:TIGR02189 84 SGSLVPMLKQ 93
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
336-505 |
3.40e-11 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 65.57 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 336 KTLVVGASYVALECAGFLAGFGLDVTVMVRSI-LLRGFDQEMAEKVGSYMEQHGVKF-LRKFIPVMVQQLEKGSPGKlkv 413
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREIPYrLNEEIDAINGNEVTFKSGK--- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 414 lakstegTETiegvYNTVLLAIGRDSCTRKIglEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILE------DKPELT 487
Cdd:PRK13512 227 -------VEH----YDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIITshyrhvDLPASV 292
|
170 180
....*....|....*....|.
gi 291045268 488 PVAI---QSGKLLAQRLFGAS 505
Cdd:PRK13512 293 PLAWgahRAASIVAEQIAGND 313
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
300-507 |
6.86e-10 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 62.15 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 300 QFVIATGERPRYLGIQG-DKEYCI---TSDDLFSLPYCPGKTL---VVGASYVALECAGFLAGFGLDVTV--MVRSILLR 370
Cdd:TIGR02374 99 KLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMDVSVihHAPGLMAK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 371 GFDQEMAEKVGSYMEQHGVKFLrkfipVMVQQLEKGSPGKLKVLaKSTEGTETIEGVyntVLLAIG---RDSCTRKIGLe 447
Cdd:TIGR02374 179 QLDQTAGRLLQRELEQKGLTFL-----LEKDTVEIVGATKADRI-RFKDGSSLEADL---IVMAAGirpNDELAVSAGI- 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291045268 448 kigvKINeksGKIPVNDVEQTNVPYVYAVGDILEDKPE---LTPVAIQSGKLLAQRLFGASLE 507
Cdd:TIGR02374 249 ----KVN---RGIIVNDSMQTSDPDIYAVGECAEHNGRvygLVAPLYEQAKVLADHICGVECE 304
|
|
| PRK10638 |
PRK10638 |
glutaredoxin 3; Provisional |
68-150 |
1.38e-09 |
|
glutaredoxin 3; Provisional
Pssm-ID: 182607 [Multi-domain] Cd Length: 83 Bit Score: 54.83 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 68 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDqvDDGARVQEVLSEiTNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQK 147
Cdd:PRK10638 4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPID--GDAAKREEMIKR-SGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80
|
...
gi 291045268 148 LLQ 150
Cdd:PRK10638 81 LLK 83
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
302-501 |
5.61e-09 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 58.22 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 302 VIATGERPRYLGIQGDKEYCI---TSDDLFSL------------PYCPGKTLVVGASYVALECAGFLAGFgLDVTVMVRS 366
Cdd:COG1252 102 VIATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAEL-LRKLLRYPG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 367 I---------------LLRGFDQEMAEKVGSYMEQHGVKFLRKFipvMVQQLEKGspgklKVLaksTEGTETIEgvYNTV 431
Cdd:COG1252 181 IdpdkvritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGT---RVTEVDAD-----GVT---LEDGEEIP--ADTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 432 LLAIG-------RDSctrkiGLEKigvkinEKSGKIPVNDVEQT-NVPYVYAVGDI--LEDKPELT-----PVAIQSGKL 496
Cdd:COG1252 248 IWAAGvkappllADL-----GLPT------DRRGRVLVDPTLQVpGHPNVFAIGDCaaVPDPDGKPvpktaQAAVQQAKV 316
|
....*
gi 291045268 497 LAQRL 501
Cdd:COG1252 317 LAKNI 321
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
278-496 |
5.20e-08 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 55.43 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 278 FVEHH--KIKATNKK--------GQETYYTAAQFVIATGER---PRYLGIQGDKEYCITS-DDLFSLPYCPGKT-----L 338
Cdd:PRK09564 74 KTEHEvvKVDAKNKTitvknlktGSIFNDTYDKLMIATGARpiiPPIKNINLENVYTLKSmEDGLALKELLKDEeikniV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 339 VVGASYVALECAGFLAGFGLDVTVMVRS--ILLRGFDQEMAEKVGSYMEQHGVKfLRkfIPVMVQQLEkgspGKLKVlak 416
Cdd:PRK09564 154 IIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVE-LH--LNEFVKSLI----GEDKV--- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 417 stEGTETIEGVYNT--VLLAIGRDSCTRKI---GLEKIgvkineKSGKIPVNDVEQTNVPYVYAVGD------ILEDKPE 485
Cdd:PRK09564 224 --EGVVTDKGEYEAdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKNV 295
|
250
....*....|.
gi 291045268 486 LTPVAIQSGKL 496
Cdd:PRK09564 296 YVPLATTANKL 306
|
|
| grxA |
PRK11200 |
glutaredoxin 1; Provisional |
68-140 |
6.70e-08 |
|
glutaredoxin 1; Provisional
Pssm-ID: 183036 [Multi-domain] Cd Length: 85 Bit Score: 50.03 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 68 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDdgarvqeVLSE-ITNQK----------TVPNIFVNKVHVGGCDQt 136
Cdd:PRK11200 3 VVIFGRPGCPYCVRAKELAEKLSEERDDFDYRYVD-------IHAEgISKADlektvgkpveTVPQIFVDQKHIGGCTD- 74
|
....
gi 291045268 137 FQAY 140
Cdd:PRK11200 75 FEAY 78
|
|
| GRX_hybridPRX5 |
cd03029 |
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ... |
66-134 |
3.25e-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: 47.90 E-value: 3.25e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 291045268 66 SRVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGarvqEVLSEITNQKTVPNIFVNKVHVGGCD 134
Cdd:cd03029 1 ESVSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITG----RSLRAVTGAMTVPQVFIDGELIGGSD 65
|
|
| GRX_DEP |
cd03027 |
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ... |
67-132 |
4.40e-07 |
|
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: 47.41 E-value: 4.40e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291045268 67 RVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDgaRVQEvLSEITNQKTVPNIFVNKVHVGG 132
Cdd:cd03027 2 RVTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIFPE--RKAE-LEERTGSSVVPQIFFNEKLVGG 64
|
|
| GRX_PICOT_like |
cd03028 |
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ... |
59-146 |
2.03e-06 |
|
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: 45.95 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 59 LVGLIERSRVVIFSKSY-----CPHSTRVKELFSSLGVE---CNVLEldqvDDGARvqEVLSEITNQKTVPNIFVNKVHV 130
Cdd:cd03028 1 IKKLIKENPVVLFMKGTpeeprCGFSRKVVQILNQLGVDfgtFDILE----DEEVR--QGLKEYSNWPTFPQLYVNGELV 74
|
90
....*....|....*.
gi 291045268 131 GGCDQTFQAYQSGLLQ 146
Cdd:cd03028 75 GGCDIVKEMHESGELQ 90
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
302-499 |
7.28e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 48.64 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 302 VIATG-ERPRYLGIQGDK--------EYcITS----DDLFSLPycPGKTLVV-GASYVALECAGFLAGFG-LDVTVMVRs 366
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDF-LTRvnqaVADYDLP--VGKRVVViGGGNTAMDAARTAKRLGaESVTIVYR- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 367 illRGFDqEM---AEKVgSYMEQHGVKFLRKFIP------------VMVQQLEKGSPGKlkvlakSTEGTETIEGVY--- 428
Cdd:PRK11749 306 ---RGRE-EMpasEEEV-EHAKEEGVEFEWLAAPveilgdegrvtgVEFVRMELGEPDA------SGRRRVPIEGSEftl 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291045268 429 --NTVLLAIGRDSCTRKIGLEKiGVKINEKSGKIPVNDVEQTNVPYVYAVGDIL--EDkpeLTPVAIQSGKLLAQ 499
Cdd:PRK11749 375 paDLVIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVtgAA---TVVWAVGDGKDAAE 445
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
302-479 |
1.00e-04 |
|
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: 45.13 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 302 VIATG-ERPRYLGIQG-DKEYCIT----------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGFG-LDVTVMVRsil 368
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 369 lRGFDqEM---AEKVgSYMEQHGVKFL-----RKFIP--------VMVQQLEKGSP---GKLKVlaKSTEGTE-TIEGvy 428
Cdd:COG0493 288 -RTRE-EMpasKEEV-EEALEEGVEFLflvapVEIIGdengrvtgLECVRMELGEPdesGRRRP--VPIEGSEfTLPA-- 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 291045268 429 NTVLLAIGRDSCTRKIgLEKIGVKINEKsGKIPVNDVE-QTNVPYVYAVGDI 479
Cdd:COG0493 361 DLVILAIGQTPDPSGL-EEELGLELDKR-GTIVVDEETyQTSLPGVFAGGDA 410
|
|
| GRXA |
TIGR02183 |
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
68-140 |
1.18e-04 |
|
Glutaredoxin, GrxA 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 model includes the E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase.
Pssm-ID: 131238 [Multi-domain] Cd Length: 86 Bit Score: 40.97 E-value: 1.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 291045268 68 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGAR--VQEVLSEITNQ--KTVPNIFVNKVHVGGCDQtFQAY 140
Cdd:TIGR02183 2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEFRYIDIHAEgiSKADLEKTVGKpvETVPQIFVDEKHVGGCTD-FEQL 77
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
303-479 |
4.78e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 43.19 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 303 IATGE-RPRYLGIQGDKEYCITS--------------DDLFSLPYCPGK-TLVVGASYVALECAGFLAGFGLDvTVMvrs 366
Cdd:PRK12778 523 IASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGKkVAVVGGGNTAMDSARTAKRLGAE-RVT--- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 367 ILLRGFDQEM---AEKVgSYMEQHGVKFLRKFIP-------------VMVQQLEKGSP---GKLKVLAksTEG-TETIEg 426
Cdd:PRK12778 599 IVYRRSEEEMparLEEV-KHAKEEGIEFLTLHNPieyladekgwvkqVVLQKMELGEPdasGRRRPVA--IPGsTFTVD- 674
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 291045268 427 vYNTVLLAIGRDSctRKIGLEKI-GVKINEKsGKIPVNDVEQTNVPYVYAVGDI 479
Cdd:PRK12778 675 -VDLVIVSVGVSP--NPLVPSSIpGLELNRK-GTIVVDEEMQSSIPGIYAGGDI 724
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
302-501 |
6.11e-04 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 42.45 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 302 VIATGERPRYLGIQGDKEY-------------------CITSDDLFSLPYCPGKTL----VVGASYVALECAGFLAGFGL 358
Cdd:PTZ00318 118 VVAHGARPNTFNIPGVEERafflkevnhargirkrivqCIERASLPTTSVEERKRLlhfvVVGGGPTGVEFAAELADFFR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 359 D--------------VTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEkgspgklkVLAKSTEGTET 423
Cdd:PTZ00318 198 DdvrnlnpelveeckVTVLeAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKE--------VVLKDGEVIPT 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 424 IEGVYNTvllAIGRDSCTRKIGLEKigvkinEKSGKIPVND-VEQTNVPYVYAVGDI--LEDK--PELTPVAIQSGKLLA 498
Cdd:PTZ00318 270 GLVVWST---GVGPGPLTKQLKVDK------TSRGRISVDDhLRVKPIPNVFALGDCaaNEERplPTLAQVASQQGVYLA 340
|
...
gi 291045268 499 QRL 501
Cdd:PTZ00318 341 KEF 343
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
290-478 |
9.02e-04 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 42.41 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 290 KGQETYYTaaQFVIATGERPRYLGIQG-DKEYCI---TSDDLFSLPYCPGKT---LVVGASYVALECAGFLAGFGLDVTV 362
Cdd:PRK14989 96 AGRTVFYD--KLIMATGSYPWIPPIKGsETQDCFvyrTIEDLNAIEACARRSkrgAVVGGGLLGLEAAGALKNLGVETHV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 363 MVRSILLrgfdqeMAEKvgsyMEQHGVKFLRKFIPVMVQQLEKgSPGKLKVLAKSTEGTETIEGVYNTVL------LAIG 436
Cdd:PRK14989 174 IEFAPML------MAEQ----LDQMGGEQLRRKIESMGVRVHT-SKNTLEIVQEGVEARKTMRFADGSELevdfivFSTG 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 291045268 437 ---RDSCTRKIGLEkigvkINEKSGkIPVNDVEQTNVPYVYAVGD 478
Cdd:PRK14989 243 irpQDKLATQCGLA-----VAPRGG-IVINDSCQTSDPDIYAIGE 281
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
291-481 |
1.36e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 41.20 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 291 GQETYYTAAQFVIATGERPRYLGIQGDKEY-------CITSDDLFslpYCPGKTLVVGASYVALECAGFLAGFGLDVTVM 363
Cdd:PRK10262 99 GDSGEYTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 364 VRSILLRgfdqemAEK--VGSYMEQHGVKFLRKFIPVMVQQLEKGSPGKLKVLAKSTEGTETIEGV-YNTVLLAIGRDSC 440
Cdd:PRK10262 176 HRRDGFR------AEKilIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLdVAGLFVAIGHSPN 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 291045268 441 TR----KIGLEKIGVKIneKSGKipVNDVEQTNVPYVYAVGDILE 481
Cdd:PRK10262 250 TAifegQLELENGYIKV--QSGI--HGNATQTSIPGVFAAGDVMD 290
|
|
| NrdH |
cd02976 |
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
67-149 |
1.97e-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: 37.20 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291045268 67 RVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQvDDGARvqEVLSEITNQKTVPNIFVNkvhvggcDQTFQAYQSGLLQ 146
Cdd:cd02976 1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDE-DPEAL--EELKKLNGYRSVPVVVIG-------DEHLSGFRPDKLR 70
|
...
gi 291045268 147 KLL 149
Cdd:cd02976 71 ALL 73
|
|
| Uxx_star |
NF041212 |
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ... |
68-131 |
3.13e-03 |
|
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature.
Pssm-ID: 469116 [Multi-domain] Cd Length: 70 Bit Score: 36.67 E-value: 3.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291045268 68 VVIFSKSYCPHSTRVKELFSSLGVEcnVLELDQVDDGARVQEVLsEITN-QKTVPNIFVN-KVHVG 131
Cdd:NF041212 1 VVIYTKPGCPYCAAAKEDLARRGIP--FEEIDVSKDPEALEEML-RLTGgERIVPVIVEGgEVTVG 63
|
|
| |
