|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
118-606 |
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: 854.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 118 YDYDLIVIGGGSGGLACSKEAATLGKKVMVLDYVVPTPLGTSWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQY 197
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 198 DEQVKHNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKGQVTYHTAETFVLATGERPRYLGI 277
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 278 PGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRSILLRGFDQEMAEKIGAHMETHGVTFIRK 357
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 358 FVPTQVERLEDgtpgrlKVTAKSTEGPEFFEGEYNTVLIAIGRDACTRNIGLQTIGVKINEKNGKVPVNDEERTNVPYVY 437
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 438 AIGDILDGKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGKQNLEVYHSLFWPLE 517
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 518 WTVPGRDN-NTCYAKIICNKLDGNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTTMDITKSSG 596
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 170671712 597 QDITQRGCUG 606
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
117-606 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 547.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 117 TYDYDLIVIGGGSGGLACSKEAATLGKKVMVLDYVVPTPLGTSWGLGGTCVNVGCIPKKLMHQAALLGQALK-DSRAYGW 195
Cdd:PTZ00052 3 TFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 196 QYDEqvKHNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIkATNRKGQVTYHTAETFVLATGERPRYL 275
Cdd:PTZ00052 83 KTSS--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 276 -GIPGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRSILLRGFDQEMAEKIGAHMETHGVTF 354
Cdd:PTZ00052 160 eDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 355 IRKFVPTQVERLEDgtpgRLKV--TAKSTEgpeffegEYNTVLIAIGRDACTRNIGLQTIGVKINEKNGKVPVNDEerTN 432
Cdd:PTZ00052 240 LEGVVPINIEKMDD----KIKVlfSDGTTE-------LFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC--TN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 433 VPYVYAIGDILDGKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGKQNLEVYHSL 512
Cdd:PTZ00052 307 IPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 513 FWPLEWTVPGRD--------------NNTCYAKIICNKLDGNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGI 578
Cdd:PTZ00052 387 FNTLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGI 466
|
490 500
....*....|....*....|....*...
gi 170671712 579 HPTCAEVFTTMDITKSSGQDITQRGCUG 606
Cdd:PTZ00052 467 HPTDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
117-589 |
5.93e-150 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 439.98 E-value: 5.93e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 117 TYDYDLIVIGGGSGGLACSKEAATLGKKVMVLDYVVptplgtswgLGGTCVNVGCIPKKLMHQAALLGQALKD-SRAYGW 195
Cdd:PRK06116 2 TKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKR---------LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 196 QYDEQvKHNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKgqvtyHTAETFVLATGERPRYL 275
Cdd:PRK06116 73 DVTEN-KFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 276 GIPGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRSIL-LRGFDQEMAEKIGAHMETHGVTF 354
Cdd:PRK06116 147 DIPG-AEYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 355 IRKFVPTQVERLEDGtpgRLKVTAKSTEgpeffEGEYNTVLIAIGRDACTRNIGLQTIGVKINEKnGKVPVNDEERTNVP 434
Cdd:PRK06116 226 HTNAVPKAVEKNADG---SLTLTLEDGE-----TLTVDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 435 YVYAIGDIlDGKLELTPVAIQAGKLLARRLYGG-SSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGKQNLEVYHSLF 513
Cdd:PRK06116 297 GIYAVGDV-TGRVELTPVAIAAGRRLSERLFNNkPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSF 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170671712 514 WPLEWTVPGRDNnTCYAKIICNKLDgNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTTM 589
Cdd:PRK06116 376 TPMYTALTGHRQ-PCLMKLVVVGKE-EKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
117-589 |
4.61e-127 |
|
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: 381.36 E-value: 4.61e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 117 TYDYDLIVIGGGSGGLACSKEAATLGKKVMVLDyvvptplgtSWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQ 196
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 197 YDEqVKHNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKgqvTYhTAETFVLATGERPRYLG 276
Cdd:COG1249 72 AGA-PSVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGGE---TL-TADHIVIATGSRPRVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 277 IPG-DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRS-ILLRGFDQEMAEKIGAHMETHGVTF 354
Cdd:COG1249 147 IPGlDEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 355 IRKFVPTQVERLEDGtpgrLKVTAKSTEGPEFFEGEYntVLIAIGRDACTRNIGLQTIGVKINEKnGKVPVNDEERTNVP 434
Cdd:COG1249 227 LTGAKVTSVEKTGDG----VTVTLEDGGGEEAVEADK--VLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 435 YVYAIGDILdGKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGkqNLEVYHSLFW 514
Cdd:COG1249 300 GIYAIGDVT-GGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGI--DVKVGKFPFA 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170671712 515 PLewtvpGR----DNNTCYAKIICNKLDGnRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTTM 589
Cdd:COG1249 377 AN-----GRalalGETEGFVKLIADAETG-RILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
118-589 |
1.15e-112 |
|
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: 344.10 E-value: 1.15e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 118 YDYDLIVIGGGSGGLACSKEAATLGKKVMV--LDYVvptplgtswglGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGW 195
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 196 QyDEQVKHNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKGQVtyhTAETFVLATGERPRYL 275
Cdd:TIGR01424 70 T-VGKARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKTY---TAEKILIAVGGRPPKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 276 GIPGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVR-SILLRGFDQEMAEKIGAHMETHGVTF 354
Cdd:TIGR01424 146 ALPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 355 IRKFVPTQVERLEDgtpGRLKVTakSTEGPEFfegEYNTVLIAIGRDACTRNIGLQTIGVKINEKnGKVPVNDEERTNVP 434
Cdd:TIGR01424 225 LPEDSITSISKDDD---GRLKAT--LSKHEEI---VADVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 435 YVYAIGDILDgKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGKqnLEVYHSLFW 514
Cdd:TIGR01424 296 SIYAVGDVTD-RINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170671712 515 PLEWTVPGRDNNtCYAKIICNKLDgNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTTM 589
Cdd:TIGR01424 373 PMKATFSGRQEK-TLMKLVVDAKD-DKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
120-589 |
1.67e-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: 341.43 E-value: 1.67e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATLGKKVMVLDyvvptplgtSWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQYDE 199
Cdd:TIGR01421 3 YDYLVIGGGSGGIASARRAAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 200 QVKHNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKgqvtyHTAETFVLATGERPRYL-GIP 278
Cdd:TIGR01421 74 ENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 279 GdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVR-SILLRGFDQEMAEKIGAHMETHGVTFIRK 357
Cdd:TIGR01421 149 G-AELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 358 FVPTQVERLEDGtpgrlKVTAKSTEGPEFFegEYNTVLIAIGRDACTRNIGLQTIGVKINEKnGKVPVNDEERTNVPYVY 437
Cdd:TIGR01421 228 SKPVKVEKTVEG-----KLVIHFEDGKSID--DVDELIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 438 AIGDILdGKLELTPVAIQAGKLLARRLYGGSST-KCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGKQNLEVYHSLFWPL 516
Cdd:TIGR01421 300 ALGDVV-GKVELTPVAIAAGRKLSERLFNGKTDdKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPM 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170671712 517 EWTVpGRDNNTCYAKIICNKLDgNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTTM 589
Cdd:TIGR01421 379 YYAM-TSEKQKCRMKLVCAGKE-EKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
118-589 |
4.08e-111 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 344.17 E-value: 4.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 118 YDYDLIVIGGGSGGLACSKEAATLGKKVMVLDYVVPT-PLGTSWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQ 196
Cdd:PLN02546 78 YDFDLFTIGAGSGGVRASRFASNFGASAAVCELPFATiSSDTLGGVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWK 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 197 YDEQVKHNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRkgqvtYHTAETFVLATGERPRYLG 276
Cdd:PLN02546 158 YETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGK-----LYTARNILIAVGGRPFIPD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 277 IPGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRSI-LLRGFDQEMAEKIGAHMETHGVTFI 355
Cdd:PLN02546 233 IPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAEQMSLRGIEFH 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 356 RKFVPTQVERLEDGTPGrLKVTAKSTEGpeffegeYNTVLIAIGRDACTRNIGLQTIGVKINeKNGKVPVNDEERTNVPY 435
Cdd:PLN02546 312 TEESPQAIIKSADGSLS-LKTNKGTVEG-------FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVPS 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 436 VYAIGDILDgKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGkqNLEVYHSLFWP 515
Cdd:PLN02546 383 IWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYG--DVDVFTANFRP 459
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170671712 516 LEWTVPGRDNNTCYAKIICNKLdgNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTTM 589
Cdd:PLN02546 460 LKATLSGLPDRVFMKLIVCAKT--NKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTM 531
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
98-589 |
6.32e-107 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 331.01 E-value: 6.32e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 98 KAYENGTLQRILGDVKDAETYDYDLIVIGGGSGGLACSKEAATLGKKVMVLDyvVP-TPLGTSW--GLGGTCVNVGCIPK 174
Cdd:PLN02507 4 KMLIDGEVAKVNADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICE--LPfHPISSESigGVGGTCVIRGCVPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 175 KLMHQAALLGQALKDSRAYGWQYDEQVKHNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKG 254
Cdd:PLN02507 82 KILVYGATFGGEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 255 QVTYHTAETFVLATGERPRYLGIPGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRSIL-LR 333
Cdd:PLN02507 162 TKLRYTAKHILIATGSRAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 334 GFDQEMAEKIGAHMETHGVTFIRKFVPTQVERLEDGtpgrLKVTakSTEGPEFfegEYNTVLIAIGRDACTRNIGLQTIG 413
Cdd:PLN02507 241 GFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG----IKVI--TDHGEEF---VADVVLFATGRAPNTKRLNLEAVG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 414 VKInEKNGKVPVNDEERTNVPYVYAIGDILDgKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLA 493
Cdd:PLN02507 312 VEL-DKAGAVKVDEYSRTNIPSIWAIGDVTN-RINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 494 EEKAIEEyGKQNLEVYHSLFWPLEWTVPGRDNNTCYAKIICNKLDgnRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLD 573
Cdd:PLN02507 390 EEEAVEQ-AKGDILVFTSSFNPMKNTISGRQEKTVMKLIVDAETD--KVLGASMCGPDAPEIMQGIAVALKCGATKAQFD 466
|
490
....*....|....*.
gi 170671712 574 ETIGIHPTCAEVFTTM 589
Cdd:PLN02507 467 STVGIHPSAAEEFVTM 482
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
119-589 |
1.95e-92 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 295.37 E-value: 1.95e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 119 DYDLIVIGGGSGGLACSKEAATLGKKVMVLDYVVptplgtswgLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQYD 198
Cdd:PTZ00058 48 VYDLIVIGGGSGGMAAARRAARNKAKVALVEKDY---------LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 199 EQVkhNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKGQ-----------VTYH-------- 259
Cdd:PTZ00058 119 FSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKVSQVdgeadesdddeVTIVsagvsqld 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 260 -----TAETFVLATGERPRYLGIPGdKEYCITSDDLFSLPYcPGKTLVVGASYVALECAGFLAGLGLDVTVMVR-SILLR 333
Cdd:PTZ00058 197 dgqviEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 334 GFDQEMAEKIGAHMETHGVTFIRKFVPTQVERLEDGTpgrlkVTAKSTEGPEFFEGEYntVLIAIGRDACTRNIGLQtiG 413
Cdd:PTZ00058 275 KFDETIINELENDMKKNNINIITHANVEEIEKVKEKN-----LTIYLSDGRKYEHFDY--VIYCVGRSPNTEDLNLK--A 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 414 VKINEKNGKVPVNDEERTNVPYVYAIGDILDGK---------------------------------LELTPVAIQAGKLL 460
Cdd:PTZ00058 346 LNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnllklyneepylkkkentsgesyynVQLTPVAINAGRLL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 461 ARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGKQNLEVYHSLFWPLEWTV----PGRDNNTcYAKIICNK 536
Cdd:PTZ00058 426 ADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVydmdPAQKEKT-YLKLVCVG 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 170671712 537 LDgNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTTM 589
Cdd:PTZ00058 505 KE-ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
120-589 |
5.02e-91 |
|
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: 289.57 E-value: 5.02e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATL-GKKVMVLDyvVPTPLGTSW--GLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQ 196
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATLyKKRVAVVD--VQTHHGPPFyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 197 YD-EQVKHNWEIMVEAVQNYIGSLNWGYRLSLRE-KSVTYQNSYGEFVEPHKI---KATNRKGQVTYH-TAETFVLATGE 270
Cdd:TIGR01423 82 FDrSSVKANWKALIAAKNKAVLDINKSYEGMFADtEGLTFFLGWGALEDKNVVlvrESADPKSAVKERlQAEHILLATGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 271 RPRYLGIPGDkEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAG---LGLDVTVMVR-SILLRGFDQEMAEKIGAH 346
Cdd:TIGR01423 162 WPQMLGIPGI-EHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTKQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 347 METHGVTFIRKFVPTQVERLEDGTPgrlKVTAKSTEgpeffEGEYNTVLIAIGRDACTRNIGLQTIGVKINeKNGKVPVN 426
Cdd:TIGR01423 241 LRANGINIMTNENPAKVTLNADGSK---HVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELT-KKGAIQVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 427 DEERTNVPYVYAIGDILDgKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGKqnL 506
Cdd:TIGR01423 312 EFSRTNVPNIYAIGDVTD-RVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEK--V 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 507 EVYHSLFWPLEWTVPGRDNNTCYAKIICNKLDGNrVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVF 586
Cdd:TIGR01423 389 AVYESSFTPLMHNISGSKYKKFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEEL 467
|
...
gi 170671712 587 TTM 589
Cdd:TIGR01423 468 CSM 470
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
120-585 |
3.78e-85 |
|
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: 273.36 E-value: 3.78e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATLGKKVMVL--DYvvptplgtswgLGGTCVNVGCIPKK-LMHQAALLGQAlKDSRAYGWQ 196
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVekEY-----------LGGTCLNVGCIPTKaLLHSAEVYDEI-KHAKDLGIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 197 YDEqVKHNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKGQVTYhTAETFVLATGERPRYLG 276
Cdd:TIGR01350 70 VEN-VSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEETL-EAKNIIIATGSRPRSLP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 277 IP--GDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTV--MVRSILlRGFDQEMAEKIGAHMETHGV 352
Cdd:TIGR01350 148 GPfdFDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRIL-PGEDAEVSKVLQKALKKKGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 353 TFIRKfvpTQVERLEDGtPGRLKVTAKSTEgPEFFEGEYntVLIAIGRDACTRNIGLQTIGVKINEkNGKVPVNDEERTN 432
Cdd:TIGR01350 227 KILTN---TKVTAVEKN-DDQVTYENKGGE-TETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDE-RGRIVVDEYMRTN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 433 VPYVYAIGDILdGKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEeygkQNLEVYHSL 512
Cdd:TIGR01350 299 VPGIYAIGDVI-GGPMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKE----AGYDVKIGK 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170671712 513 FwPLewTVPGR----DNNTCYAKIICNKLDGnRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEV 585
Cdd:TIGR01350 374 F-PF--AANGKalalGETDGFVKIIADKKTG-EILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
119-585 |
1.28e-76 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 250.83 E-value: 1.28e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 119 DYDLIVIGGGSGGLACSKEAATLGKKVMVL--DYvvptplgtswgLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQ 196
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVekEK-----------LGGTCLNRGCIPSKALLHAAERADEARHSEDFGIK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 197 YDEQvkhnwEIMVEAVQNY----IGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKGQVTYhTAETFVLATGERP 272
Cdd:PRK06416 73 AENV-----GIDFKKVQEWkngvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTY-TAKNIILATGSRP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 273 RYL-GIPGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTV---MVRsiLLRGFDQEMAEKIGAHME 348
Cdd:PRK06416 147 RELpGIEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 349 THGVTFIRKFVPTQVERLEDGtpgrLKVTAKSTEGPEFFEGEYntVLIAIGRDACTRNIGLQTIGVKINEknGKVPVNDE 428
Cdd:PRK06416 225 KRGIKIKTGAKAKKVEQTDDG----VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 429 ERTNVPYVYAIGDILdGKLELTPVAIQAGKLLARRLYGGSSTkCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGkqNLEV 508
Cdd:PRK06416 297 LRTNVPNIYAIGDIV-GGPMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKEEGF--DVKV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 509 YHSLFwplewTVPGR----DNNTCYAKIICNKLDGNrVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAE 584
Cdd:PRK06416 373 VKFPF-----AGNGKalalGETDGFVKLIFDKKDGE-VLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
|
.
gi 170671712 585 V 585
Cdd:PRK06416 447 A 447
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
119-588 |
7.34e-72 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 238.54 E-value: 7.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 119 DYDLIVIGGGSGGLACSKEAATLGKKVMVLDyvvPTPLGtswglgGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQYD 198
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIE---KGPLG------GTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 199 EqVKHNWEIMVEAVQNYIGSLNWGYRLSLREKS-VTYQNSYGEFVEPHKIKATNRkgqvTYHtAETFVLATGER-PRYLG 276
Cdd:PRK06292 74 G-PKIDFKKVMARVRRERDRFVGGVVEGLEKKPkIDKIKGTARFVDPNTVEVNGE----RIE-AKNIVIATGSRvPPIPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 277 I-PGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRS-ILLRGFDQEMAEKIGAHMETHgVTF 354
Cdd:PRK06292 148 VwLILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-FKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 355 IRKFVPTQVERLEDGtpgrLKVTAKSTEGPEFFEGEYntVLIAIGRDACTRNIGLQTIGVKINEKnGKVPVNDEERTNVP 434
Cdd:PRK06292 227 KLGAKVTSVEKSGDE----KVEELEKGGKTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSVP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 435 YVYAIGDIlDGKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGKqnlevYHSLFW 514
Cdd:PRK06292 300 GIYAAGDV-NGKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGID-----YVVGEV 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170671712 515 PLEWTVPGR-DNNTCYA-KIICNKLDGnRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTT 588
Cdd:PRK06292 374 PFEAQGRARvMGKNDGFvKVYADKKTG-RLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRT 448
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
120-606 |
1.49e-66 |
|
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: 224.61 E-value: 1.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATLGKKVMVLDYvvptplGTswgLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQYDE 199
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVER------GP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 200 QVkhNWEIMVEAVQNYIGSL-NWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKGQVTYhtaETFVLATGERPRYLGIP 278
Cdd:TIGR02053 72 AV--DFGELLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKVDLGREVRGA---KRFLIATGARPAIPPIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 279 GDKE--YcITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRS-ILLRGFDQEMAEKIGAHMETHGVTFI 355
Cdd:TIGR02053 147 GLKEagY-LTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 356 RKFVPTQVERLEDGtpgrLKVTAKSTEGPEFFEGEYntVLIAIGRDACTRNIGLQTIGVKINEkNGKVPVNDEERTNVPY 435
Cdd:TIGR02053 226 TSAQVKAVSVRGGG----KIITVEKPGGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDE-RGGILVDETLRTSNPG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 436 VYAIGDILDGkLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGkqnleVYHSLFWP 515
Cdd:TIGR02053 299 IYAAGDVTGG-LQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGI-----ECDCRTLP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 516 LEWTVPGRDN--NTCYAKIICNKLDGnRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTTMDITK 593
Cdd:TIGR02053 373 LTNVPRARINrdTRGFIKLVAEPGTG-KVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTF 451
|
490
....*....|...
gi 170671712 594 SSgqDITQRGCUG 606
Cdd:TIGR02053 452 YR--DVSKLSCCA 462
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
120-584 |
2.14e-61 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 210.83 E-value: 2.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATLGKKVMVLdyvvptplGTSWgLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQYDE 199
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALI--------ERGL-LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 200 QVKHNWEIMVEAVQNYIGSLNWGYRLSLRE-KSVTYQNSYGEFVEPHKIKATNRKgqvtyHTAETFVLATGERPRYLGIP 278
Cdd:PRK06370 77 PVSVDFKAVMARKRRIRARSRHGSEQWLRGlEGVDVFRGHARFESPNTVRVGGET-----LRAKRIFINTGARAAIPPIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 279 G--DKEYcITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRS-ILLRGFDQEMAEKIGAHMETHGVTFI 355
Cdd:PRK06370 152 GldEVGY-LTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGpRLLPREDEDVAAAVREILEREGIDVR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 356 rkfVPTQVERLEDgTPGRLKVTAKSTEGPEFFEGEYntVLIAIGRDACTRNIGLQTIGVKINEKnGKVPVNDEERTNVPY 435
Cdd:PRK06370 231 ---LNAECIRVER-DGDGIAVGLDCNGGAPEITGSH--ILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 436 VYAIGDIlDGKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAiEEYGKqNLEVYhslfwp 515
Cdd:PRK06370 304 IYAAGDC-NGRGAFTHTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEA-RKSGR-RVLVG------ 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170671712 516 lewTVP----GR----DNNTCYAKIICNKlDGNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAE 584
Cdd:PRK06370 375 ---TRPmtrvGRavekGETQGFMKVVVDA-DTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
120-457 |
1.60e-59 |
|
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: 200.62 E-value: 1.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATLGKKVMVLdyvvptplgtswGLGGTCVNVGCIPKKLMHQAALLGQALKDsraygwqyde 199
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAAEAPEIASL---------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 200 qvkhnWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKgqvtyHTAETFVLATGERPRYLGIPG 279
Cdd:pfam07992 59 -----WADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDGDGET-----ITYDRLVIATGARPRLPPIPG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 280 DKEYC------ITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRS-ILLRGFDQEMAEKIGAHMETHGV 352
Cdd:pfam07992 129 VELNVgflvrtLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 353 TFIRKFVPTQVERLEDGtpgrlkVTAKSTEGPEFfegEYNTVLIAIGRDACTRniGLQTIGVKINEkNGKVPVNDEERTN 432
Cdd:pfam07992 209 EVRLGTSVKEIIGDGDG------VEVILKDGTEI---DADLVVVAIGRRPNTE--LLEAAGLELDE-RGGIVVDEYLRTS 276
|
330 340
....*....|....*....|....*
gi 170671712 433 VPYVYAIGDILDGKLELTPVAIQAG 457
Cdd:pfam07992 277 VPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
119-585 |
1.23e-47 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 173.22 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 119 DYDLIVIGGGSGGLACSKEAAtlGKKVMVLDYvvptplGTswgLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGwqYD 198
Cdd:PRK07846 1 HYDLIIIGTGSGNSILDERFA--DKRIAIVEK------GT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 199 EQVKH-NWEIMVEAVQNYIGSLNWG---YRlSLREKSVTYQNSYGEFVEPHKIkatnRKGQVTYHTAETFVLATGERPRY 274
Cdd:PRK07846 68 AELDGvRWPDIVSRVFGRIDPIAAGgeeYR-GRDTPNIDVYRGHARFIGPKTL----RTGDGEEITADQVVIAAGSRPVI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 275 LGIPGDKE--YcITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRS-ILLRGFDQEMAEKI----GAHM 347
Cdd:PRK07846 143 PPVIADSGvrY-HTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISERFtelaSKRW 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 348 ETHGVTFIrkfvpTQVERLEDGTPGRLkvtakstEGPEFFEGEynTVLIAIGRDACTRNIGLQTIGVKINEkNGKVPVND 427
Cdd:PRK07846 222 DVRLGRNV-----VGVSQDGSGVTLRL-------DDGSTVEAD--VLLVATGRVPNGDLLDAAAAGVDVDE-DGRVVVDE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 428 EERTNVPYVYAIGDILDgKLELTPVAIQAGKLLARRLYGGSS-TKCDYINVPTTVFTPLEYGSCGLAEEKAIEE------ 500
Cdd:PRK07846 287 YQRTSAEGVFALGDVSS-PYQLKHVANHEARVVQHNLLHPDDlIASDHRFVPAAVFTHPQIASVGLTENEARAAglditv 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 501 ---------YGkqnlevyhslfWPLEWTvpgrdnnTCYAKIICNKLDGnRVVGFHVLGPNAGEVTQGFAAAIKCGLT-KE 570
Cdd:PRK07846 366 kvqnygdvaYG-----------WAMEDT-------TGFVKLIADRDTG-RLLGAHIIGPQASTLIQPLIQAMSFGLDaRE 426
|
490
....*....|....*
gi 170671712 571 LLDETIGIHPTCAEV 585
Cdd:PRK07846 427 MARGQYWIHPALPEV 441
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
119-585 |
1.66e-47 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 173.19 E-value: 1.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 119 DYDLIVIGGGSGGLACSKEAATLGKKVMVLDYVVPTPLGTSwgLGGTCVNVGCIPKK-LMHQAALLGQALKDSRAYGWQY 197
Cdd:PRK06327 4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNPKGKPA--LGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGIHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 198 DEqVKHNWEIMVEAVQNYIGSLNWGYRLSLREKSVTYQNSYGEFV----EPHKIKATNRKGQVTyhTAETFVLATGERPR 273
Cdd:PRK06327 82 DG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDETVI--TAKHVIIATGSEPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 274 YL-GIPGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVM-VRSILLRGFDQEMAEKIGAHMETHG 351
Cdd:PRK06327 159 HLpGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTKQG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 352 VTFIRKFVPTQVERLEDGTpgRLKVTAKSTEGPEFfegEYNTVLIAIGRDACTRNIGLQTIGVKINEkNGKVPVNDEERT 431
Cdd:PRK06327 239 LDIHLGVKIGEIKTGGKGV--SVAYTDADGEAQTL---EVDKLIVSIGRVPNTDGLGLEAVGLKLDE-RGFIPVDDHCRT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 432 NVPYVYAIGDILDGKLeLTPVAIQAGKLLARRLYGGSStKCDYINVPTTVFTPLEYGSCGLAEEKAIEEygkqNLEVYHS 511
Cdd:PRK06327 313 NVPNVYAIGDVVRGPM-LAHKAEEEGVAVAERIAGQKG-HIDYNTIPWVIYTSPEIAWVGKTEQQLKAE----GVEYKAG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 512 LFwplewtvPGRDNN--------TCYAKIICNKlDGNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCA 583
Cdd:PRK06327 387 KF-------PFMANGralamgepDGFVKIIADA-KTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLS 458
|
..
gi 170671712 584 EV 585
Cdd:PRK06327 459 EV 460
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
116-584 |
4.23e-45 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 166.10 E-value: 4.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 116 ETYDYDLIVIGGGSGGLACSKEAATLGKKVMVLDyvvptplgTSWGLGGTCVNVGCIPKKLMHQAAL-LGQALKDS--RA 192
Cdd:PRK05249 2 HMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlySS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 193 YGWQYD---EQVKHNWEIM----VEAVQNYigslnwgyrlsLREKSVTYQNSYGEFVEPHKIKATNRKGQVTYHTAETFV 265
Cdd:PRK05249 74 YRVKLRitfADLLARADHVinkqVEVRRGQ-----------YERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 266 LATGERP-RYLGIPGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVM-VRSILLRGFDQEMAEKI 343
Cdd:PRK05249 143 IATGSRPyRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDAL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 344 GAHMETHGVTFIRKFVPTQVERLEDGTPGRL----KVTAkstegpeffegeyNTVLIAIGRDACTRNIGLQTIGVKINEK 419
Cdd:PRK05249 223 SYHLRDSGVTIRHNEEVEKVEGGDDGVIVHLksgkKIKA-------------DCLLYANGRTGNTDGLNLENAGLEADSR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 420 nGKVPVNDEERTNVPYVYAIGDILdGKLELTPVAIQAGKLLARRLYGGSSTKcdYIN-VPTTVFTPLEYGSCGLAEEKAI 498
Cdd:PRK05249 290 -GQLKVNENYQTAVPHIYAVGDVI-GFPSLASASMDQGRIAAQHAVGEATAH--LIEdIPTGIYTIPEISSVGKTEQELT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 499 EE---YgkqnlEVYHSLFwplewtvpgRDN--------NTCYAKIICNkLDGNRVVGFHVLGPNAGEVTQGFAAAIKCGL 567
Cdd:PRK05249 366 AAkvpY-----EVGRARF---------KELaraqiagdNVGMLKILFH-RETLEILGVHCFGERATEIIHIGQAIMEQKG 430
|
490
....*....|....*..
gi 170671712 568 TKELLDETIGIHPTCAE 584
Cdd:PRK05249 431 TIEYFVNTTFNYPTMAE 447
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
119-585 |
4.71e-41 |
|
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: 154.92 E-value: 4.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 119 DYDLIVIGGGSGGLACSKEAAtlGKKVMVLDYvvptplGTswgLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGwqYD 198
Cdd:TIGR03452 2 HYDLIIIGTGSGNSIPDPRFA--DKRIAIVEK------GT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--ID 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 199 EQVKH-NWEIMVEAV-QNYIGSLNWG---YRLSLREKSVTYQNSYGEFVEPHKIkatnRKGQVTYHTAETFVLATGERPR 273
Cdd:TIGR03452 69 AEIDSvRWPDIVSRVfGDRIDPIAAGgedYRRGDETPNIDVYDGHARFVGPRTL----RTGDGEEITGDQIVIAAGSRPY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 274 ---YLGIPGDKEYciTSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRS-ILLRGFDQEMAEK------- 342
Cdd:TIGR03452 145 ippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRStKLLRHLDEDISDRfteiakk 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 343 ----------IGAHMETHGVTFirkfvptqveRLEDGTpgrlKVTAkstegpeffegeyNTVLIAIGRDACTRNIGLQTI 412
Cdd:TIGR03452 223 kwdirlgrnvTAVEQDGDGVTL----------TLDDGS----TVTA-------------DVLLVATGRVPNGDLLDAEAA 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 413 GVKINEkNGKVPVNDEERTNVPYVYAIGDIlDGKLELTPVAIQAGKLLARRLYGGSS-TKCDYINVPTTVFTPLEYGSCG 491
Cdd:TIGR03452 276 GVEVDE-DGRIKVDEYGRTSARGVWALGDV-SSPYQLKHVANAEARVVKHNLLHPNDlRKMPHDFVPSAVFTHPQIATVG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 492 LAEEKA----------IEEYGkqnlEVYHSlfWPLEWTvpgrdnnTCYAKIICNKlDGNRVVGFHVLGPNAGEVTQGFAA 561
Cdd:TIGR03452 354 LTEQEAreaghditvkIQNYG----DVAYG--WAMEDT-------TGFCKLIADR-DTGKLLGAHIIGPQASSLIQPLIT 419
|
490 500
....*....|....*....|....*
gi 170671712 562 AIKCGLT-KELLDETIGIHPTCAEV 585
Cdd:TIGR03452 420 AMAFGLDaREMARKQYWIHPALPEV 444
|
|
| GRX_GRXh_1_2_like |
cd03419 |
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ... |
27-108 |
6.49e-41 |
|
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: 143.06 E-value: 6.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 27 RVMIFSKSYCPYCHRVKELFSSLGVQYYALELDVTDDGPSIQQVLAELTNQRTVPNVFINGKHIGGCDATYKAYENGTLQ 106
Cdd:cd03419 1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
|
..
gi 170671712 107 RI 108
Cdd:cd03419 81 KL 82
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
120-584 |
1.30e-37 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 144.89 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATLGKKVMVLDYvvptplgTSWGLGGTCVNVGCIPKKLMHQAAllgqalkdsrAYGWQYDE 199
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVALVEE-------SKAMYGGTCINIGCIPTKTLLVAA----------EKNLSFEQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 200 QVKHNweimvEAVQNYIGSLNWGyrlSLREKSVTYQNSYGEFVEPHKIKATNRKGQVTYhTAETFVLATGERPRYLGIPG 279
Cdd:PRK07251 67 VMATK-----NTVTSRLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIEL-TAETIVINTGAVSNVLPIPG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 280 --DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVM-VRSILLRGFDQEMAEKIGAHMETHGVTFIR 356
Cdd:PRK07251 138 laDSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 357 KFVPTQVERLEDgtpgRLKVTaksTEGPEFfegEYNTVLIAIGRDACTRNIGLQTIGVKINEkNGKVPVNDEERTNVPYV 436
Cdd:PRK07251 218 NAHTTEVKNDGD----QVLVV---TEDETY---RFDALLYATGRKPNTEPLGLENTDIELTE-RGAIKVDDYCQTSVPGV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 437 YAIGDIlDGKLELTPVAIQAGKLLARRLYGGSS-TKCDYINVPTTVFTPLEYGSCGLAEEKAIEE---YGKQNLEVYhsl 512
Cdd:PRK07251 287 FAVGDV-NGGPQFTYISLDDFRIVFGYLTGDGSyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAglpYAVKELLVA--- 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170671712 513 fwplewTVP-GRDNNTCYA--KIICNKlDGNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAE 584
Cdd:PRK07251 363 ------AMPrAHVNNDLRGafKVVVNT-ETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
477-589 |
1.63e-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: 134.60 E-value: 1.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 477 VPTTVFTPLEYGSCGLAEEKAIEEYGKqnLEVYHSLFWPLEWTVPGRDNNtCYAKIICNKLDGnRVVGFHVLGPNAGEVT 556
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADRETG-KILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 170671712 557 QGFAAAIKCGLTKELLDETIGIHPTCAEVFTTM 589
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
94-605 |
5.70e-37 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 145.29 E-value: 5.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 94 DATYKAYENGTLQRILGDVKDAETYDYD-----LIVIGGGSGGLACSKEAATLGKKVMVLDYvvptplGTswgLGGTCVN 168
Cdd:PRK13748 68 DAPPTDNRGGLLDKMRGWLGGADKHSGNerplhVAVIGSGGAAMAAALKAVEQGARVTLIER------GT---IGGTCVN 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 169 VGCIPKKLMHQAALLGQ----------------ALKDSRAYGWQYD--EQVKHnweimveavQNYIGSLNWGYRLSLREK 230
Cdd:PRK13748 139 VGCVPSKIMIRAAHIAHlrrespfdggiaatvpTIDRSRLLAQQQArvDELRH---------AKYEGILDGNPAITVLHG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 231 SVTYQNSygefvepHKIKATNRKGQVTYHTAETFVLATGERPRYLGIPGDKE--YCITSDDLFSlPYCPGKTLVVGASYV 308
Cdd:PRK13748 210 EARFKDD-------QTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKEtpYWTSTEALVS-DTIPERLAVIGSSVV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 309 ALECAGFLAGLGLDVTVMVRSILLRGFDQEMAEKIGAHMETHGVTFIRKFVPTQVeRLEDGtpgrlKVTAKSTEGpeffE 388
Cdd:PRK13748 282 ALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQV-AHVDG-----EFVLTTGHG----E 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 389 GEYNTVLIAIGRDACTRNIGLQTIGVKINeKNGKVPVNDEERTNVPYVYAIGDILDgKLELTPVAIQAGKLLARRLYGGS 468
Cdd:PRK13748 352 LRADKLLVATGRAPNTRSLALDAAGVTVN-AQGAIVIDQGMRTSVPHIYAAGDCTD-QPQFVYVAAAAGTRAAINMTGGD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 469 STkCDYINVPTTVFTPLEYGSCGLAEEKAieeyGKQNLEVyHSLFWPLEwTVPGRDNN---TCYAKIICNKLDGnRVVGF 545
Cdd:PRK13748 430 AA-LDLTAMPAVVFTDPQVATVGYSEAEA----HHDGIET-DSRTLTLD-NVPRALANfdtRGFIKLVIEEGSG-RLIGV 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 546 HVLGPNAGEVTQGFAAAIKCGLT-KELLDETI-------GIHpTCAEVFTtmditkssgQDITQRGCU 605
Cdd:PRK13748 502 QAVAPEAGELIQTAALAIRNRMTvQELADQLFpyltmveGLK-LAAQTFN---------KDVKQLSCC 559
|
|
| GRX_euk |
TIGR02180 |
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ... |
28-109 |
1.63e-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: 128.13 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGV-QYYALELDVTDDGPSIQQVLAELTNQRTVPNVFINGKHIGGCDATYKAYENGTLQ 106
Cdd:TIGR02180 1 VVVFSKSYCPYCKKAKEILAKLNVkPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKLA 80
|
...
gi 170671712 107 RIL 109
Cdd:TIGR02180 81 ELL 83
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
120-457 |
9.30e-30 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 119.45 E-value: 9.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATLGKKVMVLDYVVPtplgtswglGGTCVNVGCI------PKKLMhqaallGQALKDsRAY 193
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEP---------GGQLATTKEIenypgfPEGIS------GPELAE-RLR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 194 gwqydEQVKH-NWEIMVEAVQNyigslnwgyrLSLREksvtyqnsygefvEPHKIKATNRkgqvTYHTAETFVLATGERP 272
Cdd:COG0492 65 -----EQAERfGAEILLEEVTS----------VDKDD-------------GPFRVTTDDG----TEYEAKAVIIATGAGP 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 273 RYLGIPGDKE-------YCITSDdlfsLPYCPGKT-LVVGASYVALECAGFLAGLGLDVTVMVRSILLRGfDQEMAEKIg 344
Cdd:COG0492 113 RKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEALYLTKFASKVTLIHRRDELRA-SKILVERL- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 345 ahMETHGVTFIrkfVPTQVERLEdGTPGRLKVTAKSTEGPEFFEGEYNTVLIAIGRDACTRniGLQTIGVKINEkNGKVP 424
Cdd:COG0492 187 --RANPKIEVL---WNTEVTEIE-GDGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTE--LLKGLGLELDE-DGYIV 257
|
330 340 350
....*....|....*....|....*....|...
gi 170671712 425 VNDEERTNVPYVYAIGDILDGKLELTPVAIQAG 457
Cdd:COG0492 258 VDEDMETSVPGVFAAGDVRDYKYRQAATAAGEG 290
|
|
| GRX_family |
cd02066 |
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
27-101 |
3.47e-29 |
|
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: 110.25 E-value: 3.47e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170671712 27 RVMIFSKSYCPYCHRVKELFSSLGVQYYalELDVTDDGpSIQQVLAELTNQRTVPNVFINGKHIGGCDATYKAYE 101
Cdd:cd02066 1 KVVVFSKSTCPYCKRAKRLLESLGIEFE--EIDILEDG-ELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
118-586 |
9.12e-29 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 119.50 E-value: 9.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 118 YDYDLIVIGGGSGGLACSKEAATLGKKVMVLDYvvptplgTSWGLGGTCVNVGCIPKKLmhqaallgqalkdsraygWQY 197
Cdd:NF040477 2 NHYQAIIIGFGKAGKTLAATLAKAGWRVAIIEQ-------SAQMYGGTCINIGCIPTKT------------------LVH 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 198 DEQVKHNWEIMVEAVQNYIGSL-NWGYRLSLREKSVTYQNSYGEFVEPHKIKATNRKGQVTYHtAETFVLATGERPRYLG 276
Cdd:NF040477 57 DAEQHQDFSTAMQRKSSVVGFLrDKNYHNLADLDNVDVINGRAEFIDNHTLRVFQADGEQELR-GEKIFINTGAQSVLPP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 277 IPGDKEY--CITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVM-VRSILLRGFDQEMAEKIGAHMETHGVT 353
Cdd:NF040477 136 IPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 354 FIrkfVPTQVERLEDgTPGRLKVtakstegpEFFEGEY--NTVLIAIGRDACTRNIGLQTIGVKINEKnGKVPVNDEERT 431
Cdd:NF040477 216 LI---LNAQVQRVSS-HEGEVQL--------ETAEGVLtvDALLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 432 NVPYVYAIGDIlDGKLELTPVAIQAGKLLARRLYG-GSSTKCDYINVPTTVFTPLEYGSCGLAEEKAiEEYGKQNLEVyh 510
Cdd:NF040477 283 TADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLGeGKRSTDDRQNVPYSVFMTPPLSRIGMTEEQA-RASGADIQVV-- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 511 SLfwPLEwTVPG----RDNNTCYAKIICNKldGNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVF 586
Cdd:NF040477 359 TL--PVA-AIPRarvmNDTRGVLKAVVDNK--TQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESL 433
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
122-580 |
2.01e-27 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 115.73 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 122 LIVIGGGSGGLACSKEAATLGKKVMVLDyvvptplgtSWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRAYGWQYDEQV 201
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 202 KHNweIMVEAVQNYIGSL----NWGYRLSLREKSVTYQNSYGEFVE----PHKIKATNRKGQVTYHTAETFVLATGERPR 273
Cdd:PRK07845 75 EAR--VDLPAVNARVKALaaaqSADIRARLEREGVRVIAGRGRLIDpglgPHRVKVTTADGGEETLDADVVLIATGASPR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 274 YLgiPG---DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVT-VMVRSILLRGFDQEMAEKIGAHMET 349
Cdd:PRK07845 153 IL--PTaepDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFAR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 350 HGVTFIRKFVPTQVERLEDGtpgrlkVTAKSTEGPEfFEGEYntVLIAIGRDACTRNIGLQTIGVKINEkNGKVPVNDEE 429
Cdd:PRK07845 231 RGMTVLKRSRAESVERTGDG------VVVTLTDGRT-VEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 430 RTNVPYVYAIGDIlDGKLELTPVAIQAGKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAeEKAIEEyGKQNLEVY 509
Cdd:PRK07845 301 RTSVPGIYAAGDC-TGVLPLASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVS-QAAIDS-GEVPARTV 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170671712 510 hslfwplewTVPGRDN--------NTCYAKIICNKLDGnRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHP 580
Cdd:PRK07845 378 ---------MLPLATNprakmsglRDGFVKLFCRPGTG-VVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYP 446
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
120-588 |
5.17e-26 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 113.09 E-value: 5.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATLGKKVMVLDyvvptplGTSWGLGGTCVNVGCIPKKLMHQAALLGQALKDSR---AYGWQ 196
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFT-------GDDDSIGGTCVNVGCIPSKALLYATGKYRELKNLAklyTYGIY 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 197 YD-------------EQVKHNWEIMVEAVQNY----IGSLNWGYRLSLREKSVTYQNSYGEFV-EPHKIKATN----RKG 254
Cdd:PTZ00153 190 TNafkngkndpvernQLVADTVQIDITKLKEYtqsvIDKLRGGIENGLKSKKFCKNSEHVQVIyERGHIVDKNtiksEKS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 255 QVTYHTaETFVLATGERPRY-LGIPGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVT-VMVRSILL 332
Cdd:PTZ00153 270 GKEFKV-KNIIIATGSTPNIpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLL 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 333 RGFDQEMA---EKI---GAHMETHGVTFIRkfvptQVERLEDGTP---GRLKVTAKSTEGP-----EFFEGEYNTVLIAI 398
Cdd:PTZ00153 349 PLLDADVAkyfERVflkSKPVRVHLNTLIE-----YVRAGKGNQPviiGHSERQTGESDGPkknmnDIKETYVDSCLVAT 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 399 GRDACTRNIGLQTIGVKINEknGKVPVND------EERTNVPYVYAIGDIlDGKLELTPVA-IQA-----------GKLL 460
Cdd:PTZ00153 424 GRKPNTNNLGLDKLKIQMKR--GFVSVDEhlrvlrEDQEVYDNIFCIGDA-NGKQMLAHTAsHQAlkvvdwiegkgKENV 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 461 ARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEYGKQNLEVYHSLF-------WPLEWTVPGRDNNTCYAKII 533
Cdd:PTZ00153 501 NINVENWASKPIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEISFYkanskvlCENNISFPNNSKNNSYNKGK 580
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 534 CN-------------KLDGNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTT 588
Cdd:PTZ00153 581 YNtvdntegmvkivyLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
120-584 |
3.48e-25 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 108.56 E-value: 3.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATLGKKVMVLDYvvptplgTSWGLGGTCVNVGCIPKK-LMHQAAllgQALKDSRAYgwqyd 198
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQ-------SNAMYGGTCINIGCIPTKtLVHDAQ---QHTDFVRAI----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 199 eQVKHnweimveAVQNYIGSLNWGYRLSLREKSVTyqNSYGEFVEPHKIKATNRKGQVTYHTAETFVlATGERPRYLGIP 278
Cdd:PRK08010 69 -QRKN-------EVVNFLRNKNFHNLADMPNIDVI--DGQAEFINNHSLRVHRPEGNLEIHGEKIFI-NTGAQTVVPPIP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 279 G--DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGLGLDVTVM-VRSILLRGFDQEMAEKIGAHMETHGVTFI 355
Cdd:PRK08010 138 GitTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDII 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 356 rkfVPTQVERLedgTPGRLKVTAKSTEGPEFFEGeyntVLIAIGRDACTRNIGLQTIGVKINEKnGKVPVNDEERTNVPY 435
Cdd:PRK08010 218 ---LNAHVERI---SHHENQVQVHSEHAQLAVDA----LLIASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADN 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 436 VYAIGDILDGkLELTPVAIQAGKLLARRLYG-GSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIEEygKQNLEVyhsLFW 514
Cdd:PRK08010 287 IWAMGDVTGG-LQFTYISLDDYRIVRDELLGeGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARES--GADIQV---VTL 360
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170671712 515 PLEWTVPGR---DNNTCYAKIICNKLdgNRVVGFHVLGPNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAE 584
Cdd:PRK08010 361 PVAAIPRARvmnDTRGVLKAIVDNKT--QRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSE 431
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
253-490 |
5.05e-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: 102.97 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 253 KGQVTYHTAETF-----VLATGERPRYLGIPGdkeycITSDDLFSL--------------PYCPGKTLVVGASYVALECA 313
Cdd:COG0446 66 AKTVTLRDGETLsydklVLATGARPRPPPIPG-----LDLPGVFTLrtlddadalrealkEFKGKRAVVIGGGPIGLELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 314 GFLAGLGLDVTVMVRS-ILLRGFDQEMAEKIGAHMETHGVTFIRKFvptQVERLEDGTpgrlKVTAKSTEGPEFfegEYN 392
Cdd:COG0446 141 EALRKRGLKVTLVERApRLLGVLDPEMAALLEEELREHGVELRLGE---TVVAIDGDD----KVAVTLTDGEEI---PAD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 393 TVLIAIGrdacTR-NIGL-QTIGVKINEKNGkVPVNDEERTNVPYVYAIGD------ILDGK---LELTPVAIQAGKLLA 461
Cdd:COG0446 211 LVVVAPG----VRpNTELaKDAGLALGERGW-IKVDETLQTSDPDVYAAGDcaevphPVTGKtvyIPLASAANKQGRVAA 285
|
250 260
....*....|....*....|....*....
gi 170671712 462 RRLYGGSSTkcdYINVPTTVFTPleYGSC 490
Cdd:COG0446 286 ENILGGPAP---FPGLGTFISKV--FDLC 309
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
255-549 |
1.61e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 100.22 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 255 QVTYHTAETF-----VLATGERPRYLGIPG-DKEYCI---TSDDLFSL-PYCPGKT--LVVGASYVALECAGFLAGLGLD 322
Cdd:COG1251 88 TVTLADGETLpydklVLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 323 VTVMVRS--ILLRGFDQEMAEKIGAHMETHGVTFIRKfvpTQVERLEdGTPGRLKVTAKSteGpEFFEGEynTVLIAIGr 400
Cdd:COG1251 168 VTVVERAprLLPRQLDEEAGALLQRLLEALGVEVRLG---TGVTEIE-GDDRVTGVRLAD--G-EELPAD--LVVVAIG- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 401 dacTR-NIGL-QTIGVKINekNGkVPVNDEERTNVPYVYAIGDI------LDGK--LELTPVAIQAGKLLARRLYGGSST 470
Cdd:COG1251 238 ---VRpNTELaRAAGLAVD--RG-IVVDDYLRTSDPDIYAAGDCaehpgpVYGRrvLELVAPAYEQARVAAANLAGGPAA 311
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 170671712 471 KCDYINVPTTVFTPLEYGSCGLAEEKAIEeygkqnlevyhslfwpLEWTVPGRDNntcYAKIIcnkLDGNRVVGFHVLG 549
Cdd:COG1251 312 YEGSVPSTKLKVFGVDVASAGDAEGDEEV----------------VVRGDPARGV---YKKLV---LRDGRLVGAVLVG 368
|
|
| Glutaredoxin |
pfam00462 |
Glutaredoxin; |
28-90 |
1.98e-22 |
|
Glutaredoxin;
Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 90.64 E-value: 1.98e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGVQYYalELDVTDDgPSIQQVLAELTNQRTVPNVFINGKHI 90
Cdd:pfam00462 1 VVLYTKPTCPFCKRAKRLLKSLGVDFE--EIDVDED-PEIREELKELSGWPTVPQVFIDGEHI 60
|
|
| GRX_bact |
TIGR02181 |
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
28-109 |
9.24e-19 |
|
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: 80.77 E-value: 9.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGVQYYalELDVTDDgPSIQQVLAELTNQRTVPNVFINGKHIGGCDATYKAYENGTLQR 107
Cdd:TIGR02181 1 VTIYTKPYCPYCTRAKALLSSKGVTFT--EIRVDGD-PALRDEMMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDP 77
|
..
gi 170671712 108 IL 109
Cdd:TIGR02181 78 LL 79
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
299-375 |
1.11e-18 |
|
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: 80.71 E-value: 1.11e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 299 KTLVVGASYVALECAGFLAGLGLDVTVMVRSI-LLRGFDQEMAEKIGAHMETHGVTFIRKFVPTQVERLEDGTPGRLK 375
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDrLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| GrxC |
COG0695 |
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
27-94 |
1.23e-18 |
|
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 80.24 E-value: 1.23e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 27 RVMIFSKSYCPYCHRVKELFSSLGVQYyaLELDVTDDgPSIQQVLAELTNQRTVPNVFINGKHIGGCD 94
Cdd:COG0695 1 KVTLYTTPGCPYCARAKRLLDEKGIPY--EEIDVDED-PEAREELRERSGRRTVPVIFIGGEHLGGFD 65
|
|
| GRX_GRXb_1_3_like |
cd03418 |
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ... |
28-103 |
1.82e-18 |
|
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: 79.94 E-value: 1.82e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGVQYyaLELDVTDDgPSIQQVLAELTNQR-TVPNVFINGKHIGGCDATYKAYENG 103
Cdd:cd03418 2 VEIYTKPNCPYCVRAKALLDKKGVDY--EEIDVDGD-PALREEMINRSGGRrTVPQIFIGDVHIGGCDDLYALERKG 75
|
|
| GlrX-like_plant |
TIGR02189 |
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ... |
19-109 |
1.58e-16 |
|
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: 75.18 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 19 VRTLIATHRVMIFSKSYCPYCHRVKELFSSLGVQYYALELDVTDDGPSIQQVLAELTNQRTVPNVFINGKHIGGCDATYK 98
Cdd:TIGR02189 1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMA 80
|
90
....*....|.
gi 170671712 99 AYENGTLQRIL 109
Cdd:TIGR02189 81 LHISGSLVPML 91
|
|
| PRK10638 |
PRK10638 |
glutaredoxin 3; Provisional |
28-109 |
3.73e-15 |
|
glutaredoxin 3; Provisional
Pssm-ID: 182607 [Multi-domain] Cd Length: 83 Bit Score: 70.62 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGVQYYALELDvtdDGPSIQQVLAELTNQRTVPNVFINGKHIGGCDATYKAYENGTLQR 107
Cdd:PRK10638 4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPID---GDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80
|
..
gi 170671712 108 IL 109
Cdd:PRK10638 81 LL 82
|
|
| GRX_PICOT_like |
cd03028 |
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ... |
19-106 |
1.86e-12 |
|
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: 63.28 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 19 VRTLIATHRVMIFSKSY-----CPYCHRVKELFSSLGVQYYALelDVTDDgPSIQQVLAELTNQRTVPNVFINGKHIGGC 93
Cdd:cd03028 1 IKKLIKENPVVLFMKGTpeeprCGFSRKVVQILNQLGVDFGTF--DILED-EEVRQGLKEYSNWPTFPQLYVNGELVGGC 77
|
90
....*....|...
gi 170671712 94 DATYKAYENGTLQ 106
Cdd:cd03028 78 DIVKEMHESGELQ 90
|
|
| GlrX-dom |
TIGR02190 |
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to ... |
28-95 |
7.26e-12 |
|
Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain.
Pssm-ID: 131245 [Multi-domain] Cd Length: 79 Bit Score: 61.39 E-value: 7.26e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGVQYYALELDVTDDGPSIQQVlaelTNQRTVPNVFINGKHIGGCDA 95
Cdd:TIGR02190 10 VVVFTKPGCPFCAKAKATLKEKGYDFEEIPLGNDARGRSLRAV----TGATTVPQVFIGGKLIGGSDE 73
|
|
| GRX_hybridPRX5 |
cd03029 |
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ... |
28-95 |
1.75e-11 |
|
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: 59.84 E-value: 1.75e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGVQYYALELDVTDDGPSIQQVlaelTNQRTVPNVFINGKHIGGCDA 95
Cdd:cd03029 3 VSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRAV----TGAMTVPQVFIDGELIGGSDD 66
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
250-606 |
3.07e-11 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 66.39 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 250 TNRKGQVTYhtaETFVLATGERPRYLGIPG-DKEYCI---TSDDLFSLPYCPGKTL---VVGASYVALECAGFLAGLGLD 322
Cdd:TIGR02374 89 TDAGRTLSY---DKLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 323 VTV--MVRSILLRGFDQEMAEKIGAHMETHGVTFIrkfVPTQVERLedgtpgrlkVTAKSTEGPEFFEG---EYNTVLIA 397
Cdd:TIGR02374 166 VSVihHAPGLMAKQLDQTAGRLLQRELEQKGLTFL---LEKDTVEI---------VGATKADRIRFKDGsslEADLIVMA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 398 IG---RDACTRNIGLQTigvkinekNGKVPVNDEERTNVPYVYAIGDI--LDGKL-ELTPVAIQAGKLLARRLYGGS--- 468
Cdd:TIGR02374 234 AGirpNDELAVSAGIKV--------NRGIIVNDSMQTSDPDIYAVGECaeHNGRVyGLVAPLYEQAKVLADHICGVEcee 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 469 ------STKCDYINVpttvftplEYGSCGLAEE----KAIEEYGKQNlEVYHSLFWplewtvpgRDNNTCYAKIICNKLD 538
Cdd:TIGR02374 306 yegsdlSAKLKLLGV--------DVWSAGDAQEtertTSIKIYDEQK-GIYKKLVL--------SDDKLLGAVLFGDTSD 368
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 539 GNRVvgFHVLGpNAGEVTQGFAAAIKCGLTKELLDETIGIHPTCAEVFTTMDITKSSGQDITQRGCUG 606
Cdd:TIGR02374 369 YGRL--LDMVL-KQADISEDPAIIKPQISGPEAGGPGVEAMPDSEQICSCNTVTKGAIIDAIHTGSCT 433
|
|
| GlrX_YruB |
TIGR02196 |
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the ... |
27-94 |
7.22e-11 |
|
Glutaredoxin-like protein, YruB-family; This glutaredoxin-like protein family contains the conserved CxxC motif and includes the Clostridium pasteurianum protein YruB which has been cloned from a rubredoxin operon. Somewhat related to NrdH, it is unknown whether this protein actually interacts with glutathione/glutathione reducatase, or, like NrdH, some other reductant system.
Pssm-ID: 274027 [Multi-domain] Cd Length: 74 Bit Score: 58.16 E-value: 7.22e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 27 RVMIFSKSYCPYCHRVKELFSSLGVQYyaLELDVTDDGPSIQQVLaELTNQRTVPNVFINGKHIGGCD 94
Cdd:TIGR02196 1 KVKVYTTPWCPPCVKAKEYLTSKGVAF--EEIDVEKDAAAREELL-KVYGQRGVPVIVIGHKIVVGFD 65
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
301-572 |
8.71e-11 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 64.29 E-value: 8.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 301 LVVGASYVALECAGFLAGLGLDVTVMVRS--ILLRGFDQEMAEKIGAHMETHGVTFirkFVPTQVERLEdgtpGRLKVTA 378
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVEL---HLNEFVKSLI----GEDKVEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 379 KSTEgpeffEGEYNT--VLIAIGRDACT---RNIGLQTIgvkineKNGKVPVNDEERTNVPYVYAIGD------ILDGKL 447
Cdd:PRK09564 226 VVTD-----KGEYEAdvVIVATGVKPNTeflEDTGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKN 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 448 ELTPVAIQA---GKLLARRLYGGSSTKCDYINVPTTVFTPLEYGSCGLAEEKAIeeygKQNLEVYHSLFWPLEWT--VPG 522
Cdd:PRK09564 295 VYVPLATTAnklGRMVGENLAGRHVSFKGTLGSACIKVLDLEAARTGLTEEEAK----KLGIDYKTVFIKDKNHTnyYPG 370
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 170671712 523 RDNntCYAKIICNKlDGNRVVGFHVLGPNaGEV--TQGFAAAIKCGLTKELL 572
Cdd:PRK09564 371 QED--LYVKLIYEA-DTKVILGGQIIGKK-GAVlrIDALAVAIYAKLTTQEL 418
|
|
| GRX_DEP |
cd03027 |
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ... |
27-92 |
9.04e-11 |
|
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: 57.81 E-value: 9.04e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170671712 27 RVMIFSKSYCPYCHRVKELFSSLGVQYYALELDVTddgPSIQQVLAELTNQRTVPNVFINGKHIGG 92
Cdd:cd03027 2 RVTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIF---PERKAELEERTGSSVVPQIFFNEKLVGG 64
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
299-443 |
9.58e-11 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 64.03 E-value: 9.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 299 KTLVVGASYVALECAGFLAGLGLDVTVMVRSI-LLRGFDQEMAEKIGAHMETHGVTFirKFvPTQVERLEDGTpgrlkVT 377
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREIPY--RL-NEEIDAINGNE-----VT 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 378 AKS--TEgpeffegEYNTVLIAIGRDACTRNIglQTIGVKINEKnGKVPVNDEERTNVPYVYAIGDIL 443
Cdd:PRK13512 222 FKSgkVE-------HYDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDII 279
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
265-515 |
1.20e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 63.61 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 265 VLATGERPRYLGIPGDKEYCI---TSDDLFSL------------PYCPGKTLVVGASYVALECAGFLAGLgLDVTVMVRS 329
Cdd:COG1252 102 VIATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAEL-LRKLLRYPG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 330 I---------------LLRGFDQEMAEKIGAHMETHGVTFIRKfvpTQVERLEDGtpgrlKVTAKSteGPEFfegEYNTV 394
Cdd:COG1252 181 IdpdkvritlveagprILPGLGEKLSEAAEKELEKRGVEVHTG---TRVTEVDAD-----GVTLED--GEEI---PADTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 395 LIAIGRDA--CTRNIGLQTigvkinEKNGKVPVNDEERT-NVPYVYAIGD---ILDGKLELTP----VAIQAGKLLA--- 461
Cdd:COG1252 248 IWAAGVKAppLLADLGLPT------DRRGRVLVDPTLQVpGHPNVFAIGDcaaVPDPDGKPVPktaqAAVQQAKVLAkni 321
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 170671712 462 -RRLYGGsstkcdyinvPTTVFTPLEYGS-CGLAEEKAIEEYGKQNLE---------VYHSLFWP 515
Cdd:COG1252 322 aALLRGK----------PLKPFRYRDKGClASLGRGAAVADVGGLKLSgflawllkrAIHLYFLP 376
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
265-461 |
4.64e-10 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 62.12 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 265 VLATG-ERPRYLGIPGDK--------EYcITS----DDLFSLPycPGKTLVV-GASYVALECAGFLAGLG-LDVTVMVRs 329
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDF-LTRvnqaVADYDLP--VGKRVVViGGGNTAMDAARTAKRLGaESVTIVYR- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 330 illRGFDqEM---AEKIgAHMETHGVTFIRKFVPTQV------------ERLEDGTP---GRLKVTaksTEGPEFFEgEY 391
Cdd:PRK11749 306 ---RGRE-EMpasEEEV-EHAKEEGVEFEWLAAPVEIlgdegrvtgvefVRMELGEPdasGRRRVP---IEGSEFTL-PA 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170671712 392 NTVLIAIGRDActRNIGLQTI-GVKINEKNGKVPVNDEERTNVPYVYAIGDILDGKlELTPVAIQAGKLLA 461
Cdd:PRK11749 377 DLVIKAIGQTP--NPLILSTTpGLELNRWGTIIADDETGRTSLPGVFAGGDIVTGA-ATVVWAVGDGKDAA 444
|
|
| NrdH |
cd02976 |
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
27-92 |
1.49e-08 |
|
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: 51.84 E-value: 1.49e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170671712 27 RVMIFSKSYCPYCHRVKELFSSLGVQYYalELDVTDDgPSIQQVLAELTNQRTVPNVFINGKHIGG 92
Cdd:cd02976 1 EVTVYTKPDCPYCKATKRFLDERGIPFE--EVDVDED-PEALEELKKLNGYRSVPVVVIGDEHLSG 63
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
265-442 |
9.20e-08 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 54.76 E-value: 9.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 265 VLATG-ERPRYLGIPG-DKEYCIT----------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGLG-LDVTVMVRsil 331
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 332 lRGFDqEMA----EKIGAHMEthGVTFI-----RKFVPTQ--------VERLEDGTP---GRLKVTAKstEGPEFFEgEY 391
Cdd:COG0493 288 -RTRE-EMPaskeEVEEALEE--GVEFLflvapVEIIGDEngrvtgleCVRMELGEPdesGRRRPVPI--EGSEFTL-PA 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 170671712 392 NTVLIAIGRDACTRNIgLQTIGVKINeKNGKVPVNDEE-RTNVPYVYAIGDI 442
Cdd:COG0493 361 DLVILAIGQTPDPSGL-EEELGLELD-KRGTIVVDEETyQTSLPGVFAGGDA 410
|
|
| grxA |
PRK11200 |
glutaredoxin 1; Provisional |
28-94 |
2.02e-07 |
|
glutaredoxin 1; Provisional
Pssm-ID: 183036 [Multi-domain] Cd Length: 85 Bit Score: 48.88 E-value: 2.02e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGVQYYALE---LDVTDDGPSiQQVLAELTNQ--RTVPNVFINGKHIGGCD 94
Cdd:PRK11200 3 VVIFGRPGCPYCVRAKELAEKLSEERDDFDyryVDIHAEGIS-KADLEKTVGKpvETVPQIFVDQKHIGGCT 73
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
272-462 |
1.08e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 51.56 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 272 PRYLGIPGD--------KEYcITSDDL-------FSLPYCPGK-TLVVGASYVALECAGFLAGLGLDVTVMVRsillRGf 335
Cdd:PRK12831 241 PKFMGIPGEnlngvfsaNEF-LTRVNLmkaykpeYDTPIKVGKkVAVVGGGNVAMDAARTALRLGAEVHIVYR----RS- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 336 DQEM---AEKIGaHMETHGVTFIRKFVPTQV-------------ERLEDGTP---GRLKVTAKstEGPEfFEGEYNTVLI 396
Cdd:PRK12831 315 EEELparVEEVH-HAKEEGVIFDLLTNPVEIlgdengwvkgmkcIKMELGEPdasGRRRPVEI--EGSE-FVLEVDTVIM 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 397 AIGRDAcTRNIGLQTIGVKINeKNGKVPVNDEE-RTNVPYVYAIGDILDGklELTPV-AIQAGKLLAR 462
Cdd:PRK12831 391 SLGTSP-NPLISSTTKGLKIN-KRGCIVADEETgLTSKEGVFAGGDAVTG--AATVIlAMGAGKKAAK 454
|
|
| PTZ00062 |
PTZ00062 |
glutaredoxin; Provisional |
18-111 |
1.68e-06 |
|
glutaredoxin; Provisional
Pssm-ID: 240250 [Multi-domain] Cd Length: 204 Bit Score: 49.02 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 18 RVRTLIATHRVMIFSKS-----YCPYCHRVKELFSSLGVQYYALelDVTDDgPSIQQVLAELTNQRTVPNVFINGKHIGG 92
Cdd:PTZ00062 105 KIERLIRNHKILLFMKGsktfpFCRFSNAVVNMLNSSGVKYETY--NIFED-PDLREELKVYSNWPTYPQLYVNGELIGG 181
|
90
....*....|....*....
gi 170671712 93 CDATYKAYENGTLQRILGD 111
Cdd:PTZ00062 182 HDIIKELYESNSLRKVIPD 200
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
121-212 |
2.54e-06 |
|
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: 49.98 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 121 DLIVIGGGSGGLACSKEAATLGKKVMVLDYVVPTPLGTSWGLGGTCVnvgcipkklmhqAALLGQALKDSRAYGWQY--- 197
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGGIDA------------LGNPPQGGIDSPELHPTDtlk 68
|
90
....*....|....*...
gi 170671712 198 --DEQVKHNW-EIMVEAV 212
Cdd:pfam00890 69 glDELADHPYvEAFVEAA 86
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
264-464 |
3.42e-06 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 50.32 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 264 FVLATGERPRYLGIPGDKEYCITSDDLF---------------SLPYCPGKTLVV-GASYVALECAGFLAGLGldvTVMV 327
Cdd:PRK12775 522 FLGVGAGAPTFLGIPGEFAGQVYSANEFltrvnlmggdkfpflDTPISLGKSVVViGAGNTAMDCLRVAKRLG---APTV 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 328 RSILLRGfDQEMAEKIGA--HMETHGVTFIRKFVPTQVERLEDGTPGRLKVTAKSTEGP------------EFFEGEYNT 393
Cdd:PRK12775 599 RCVYRRS-EAEAPARIEEirHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKVEEMELGEPdekgrrkpmptgEFKDLECDT 677
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 170671712 394 VLIAIGRDAcTRNIGLQTIGVKINeKNGKVPVNDE-----ERTNVPYVYAIGDILDGKLELTpVAIQAGKLLARRL 464
Cdd:PRK12775 678 VIYALGTKA-NPIITQSTPGLALN-KWGNIAADDGklestQSTNLPGVFAGGDIVTGGATVI-LAMGAGRRAARSI 750
|
|
| GRX_GRX_like |
cd03031 |
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ... |
39-113 |
4.17e-06 |
|
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: 46.85 E-value: 4.17e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 170671712 39 CHRVKELFSSLGVQYYalELDVTDDG---PSIQQVLAELTNQRTVPNVFINGKHIGGCDATYKAYENGTLQRILGDVK 113
Cdd:cd03031 19 CNNVRAILESFRVKFD--ERDVSMDSgfrEELRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLLKGIR 94
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
265-464 |
9.51e-06 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 48.06 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 265 VLATGE-RPRYLGIPGDKEYCITS--DDLFS-----LPYCP---------GKTLVVGASYVALECAGFLAGLGLDVTVMV 327
Cdd:PRK12770 123 LIATGTwKSRKLGIPGEDLPGVYSalEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAALEAVLLGAEKVYLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 328 --RSIllrgfDQEMAekiGAHM----ETHGVTFIRKFVPTQVE-----------RLEDGTP---GRLKVTAksTEGPEfF 387
Cdd:PRK12770 203 yrRTI-----NEAPA---GKYEierlIARGVEFLELVTPVRIIgegrvegvelaKMRLGEPdesGRPRPVP--IPGSE-F 271
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170671712 388 EGEYNTVLIAIGRDAcTRNIGLQTIGVKINeKNGKVPVNDEERTNVPYVYAIGDILDGKLELTPvAIQAGKLLARRL 464
Cdd:PRK12770 272 VLEADTVVFAIGEIP-TPPFAKECLGIELN-RKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGK-AIKSGLRAAQSI 345
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
245-444 |
3.12e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 46.21 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 245 HKIKATNRKGQVT----YHTAETFVLATGERPRYLGIPGDKEY-------CITSDDLFslpYCPGKTLVVGASYVALECA 313
Cdd:PRK10262 86 NKVDLQNRPFRLTgdsgEYTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 314 GFLAGLGLDVTVMVRSILLRgfdqemAEKIGAHMETHGVTFIRKFVPTQvERLEDGTPGRLKVTA---KSTEGPEFFEG- 389
Cdd:PRK10262 163 LYLSNIASEVHLIHRRDGFR------AEKILIKRLMDKVENGNIILHTN-RTLEEVTGDQMGVTGvrlRDTQNSDNIESl 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 390 EYNTVLIAIGRDACTRNIGLQtigvkINEKNGKVPVN-----DEERTNVPYVYAIGDILD 444
Cdd:PRK10262 236 DVAGLFVAIGHSPNTAIFEGQ-----LELENGYIKVQsgihgNATQTSIPGVFAAGDVMD 290
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
257-440 |
1.16e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 44.52 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 257 TYHtAETFVLATGE--RPRYLGIPgdkEYCITSDDLFSL-PYCPGKTLVVGASYVALECAGFLAGLGLDVTVMVRSILLR 333
Cdd:pfam13738 116 TYQ-ARYVIIATGEfdFPNKLGVP---ELPKHYSYVKDFhPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 334 GFD------------QEMAE-----KIGAHMETHgVTFIRKFVPTQVERLEDGTpgrlKVTAkstegpeffegeYNTVLI 396
Cdd:pfam13738 192 DRDsdpsyslspdtlNRLEElvkngKIKAHFNAE-VKEITEVDVSYKVHTEDGR----KVTS------------NDDPIL 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 170671712 397 AIGRDActrNIGLQTIGVKINEKNGKVPVNDE-ERTNVPYVYAIG 440
Cdd:pfam13738 255 ATGYHP---DLSFLKKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| GRXA |
TIGR02183 |
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
28-93 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGVQYYALE---LDVTDDGPSiQQVLAELTNQ--RTVPNVFINGKHIGGC 93
Cdd:TIGR02183 2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEfryIDIHAEGIS-KADLEKTVGKpvETVPQIFVDEKHVGGC 71
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
116-164 |
1.60e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 1.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 170671712 116 ETYDYDLIVIGGGSGGLACSKEAATLGKKVMVLDYVVPTPLGTS--WGLGG 164
Cdd:PRK12834 1 MAMDADVIVVGAGLAGLVAAAELADAGKRVLLLDQENEANLGGQafWSLGG 51
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
116-164 |
4.01e-04 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 43.24 E-value: 4.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 170671712 116 ETYDYDLIVIGGGSGGLACSKEAATLGKKVMVLDYVVPTPLG--TSWGLGG 164
Cdd:COG3573 2 AAMDADVIVVGAGLAGLVAAAELADAGRRVLLLDQEPEANLGgqAFWSFGG 52
|
|
| PHA03050 |
PHA03050 |
glutaredoxin; Provisional |
19-92 |
4.29e-04 |
|
glutaredoxin; Provisional
Pssm-ID: 165343 [Multi-domain] Cd Length: 108 Bit Score: 40.00 E-value: 4.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 170671712 19 VRTLIATHRVMIFSKSYCPYCHRVKELFSSLGVQYYALEL-DVTDDGPS--IQQVLAELTNQRTVPNVFINGKHIGG 92
Cdd:PHA03050 6 VQQRLANNKVTIFVKFTCPFCRNALDILNKFSFKRGAYEIvDIKEFKPEneLRDYFEQITGGRTVPRIFFGKTSIGG 82
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
120-149 |
5.84e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 42.57 E-value: 5.84e-04
10 20 30
....*....|....*....|....*....|
gi 170671712 120 YDLIVIGGGSGGLACSKEAATLGKKVMVLD 149
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIE 30
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
117-163 |
6.27e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 42.89 E-value: 6.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 170671712 117 TYDYDLIVIGGGSGGLACSKEAATLGKKVMVLDYVVPTPLGTSWGLG 163
Cdd:PRK12839 6 THTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGATAWSGG 52
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
272-445 |
1.06e-03 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 42.04 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 272 PRYLGIPGDKEYCITS--------------DDLFSLPYCPGK-TLVVGASYVALECAGFLAGLGLDvTVMvrsILLRGFD 336
Cdd:PRK12778 530 PNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGKkVAVVGGGNTAMDSARTAKRLGAE-RVT---IVYRRSE 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 337 QEM---AEKIgAHMETHGVTFIRKFVPTQV-------------ERLEDGTP---GRLKVTAksTEGPEFfEGEYNTVLIA 397
Cdd:PRK12778 606 EEMparLEEV-KHAKEEGIEFLTLHNPIEYladekgwvkqvvlQKMELGEPdasGRRRPVA--IPGSTF-TVDVDLVIVS 681
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 170671712 398 IGrdaCTRN-IGLQTI-GVKINEKnGKVPVNDEERTNVPYVYAIGDILDG 445
Cdd:PRK12778 682 VG---VSPNpLVPSSIpGLELNRK-GTIVVDEEMQSSIPGIYAGGDIVRG 727
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
119-200 |
2.45e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 40.86 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 119 DYDLIVIGGGSGGLACSKEAATLGKKVMVLDyvvptplgTSWGLGGTCVNVG---CIPKKLMHQAALLGQALKDSRAY-- 193
Cdd:PRK06134 12 ECDVLVIGSGAAGLSAAVTAAWHGLKVIVVE--------KDPVFGGTTAWSGgwmWIPRNPLARRAGIVEDIEQPRTYlr 83
|
90
....*....|
gi 170671712 194 ---GWQYDEQ 200
Cdd:PRK06134 84 helGARYDAA 93
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
117-148 |
2.53e-03 |
|
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: 40.59 E-value: 2.53e-03
10 20 30
....*....|....*....|....*....|..
gi 170671712 117 TYDYDLIVIGGGSGGLACSKEAATLGKKVMVL 148
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVL 32
|
|
| PTZ00367 |
PTZ00367 |
squalene epoxidase; Provisional |
105-149 |
3.30e-03 |
|
squalene epoxidase; Provisional
Pssm-ID: 240384 [Multi-domain] Cd Length: 567 Bit Score: 40.22 E-value: 3.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 170671712 105 LQRILGDVKDAET---YDYDLIVIGGGSGGLACSKEAATLGKKVMVLD 149
Cdd:PTZ00367 16 LNRILSRLRFKPArtnYDYDVIIVGGSIAGPVLAKALSKQGRKVLMLE 63
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
237-469 |
3.46e-03 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 39.90 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 237 SYGEFVE-------PH-KIKATNRKGQV------TYHTAEtFVLATGERPRYLGIPGD---------KEYCITSDDLFSl 293
Cdd:PRK04965 63 SAGEFAEqfnlrlfPHtWVTDIDAEAQVvksqgnQWQYDK-LVLATGASAFVPPIPGRelmltlnsqQEYRAAETQLRD- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 294 pycPGKTLVVGASYVALECAGFLAGLGLDVTVMVR--SILLRGFDQEMAEKIGAHMETHGVTFIRKfvpTQVERLEDgTP 371
Cdd:PRK04965 141 ---AQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNaaSLLASLMPPEVSSRLQHRLTEMGVHLLLK---SQLQGLEK-TD 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 372 GRLKVTAksTEGPEFfegEYNTVLIAIGRDActrNIGL-QTIGVKINEknGKVpVNDEERTNVPYVYAIGDI--LDGKLE 448
Cdd:PRK04965 214 SGIRATL--DSGRSI---EVDAVIAAAGLRP---NTALaRRAGLAVNR--GIV-VDSYLQTSAPDIYALGDCaeINGQVL 282
|
250 260
....*....|....*....|...
gi 170671712 449 --LTPVAIQAgKLLARRLYGGSS 469
Cdd:PRK04965 283 pfLQPIQLSA-MALAKNLLGQNT 304
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
119-164 |
5.37e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.50 E-value: 5.37e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 170671712 119 DYDLIVIGGGSGGLACSKEAATLGKKVMVLD--YVvptPLGTSWGLGG 164
Cdd:COG0665 2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLErgRP---GSGASGRNAG 46
|
|
| GlrX_actino |
TIGR02200 |
Glutaredoxin-like protein; This family of glutaredoxin-like proteins is limited to the ... |
28-89 |
7.41e-03 |
|
Glutaredoxin-like protein; This family of glutaredoxin-like proteins is limited to the Actinobacteria and contains the conserved CxxC motif.
Pssm-ID: 131255 [Multi-domain] Cd Length: 77 Bit Score: 35.59 E-value: 7.41e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGVQYYAleLDVTDDGPSIQQVLAELTNQRTVPNVFINGKH 89
Cdd:TIGR02200 2 ITVYGTTWCGYCAQLMRTLDKLGAAYEW--VDIEEDEGAADRVVSVNNGNMTVPTVKFADGS 61
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| TrbB |
TIGR02738 |
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ... |
4-85 |
7.59e-03 |
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type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system. This protein has been predicted to contain a thioredoxin fold, contains a conserved pair of cysteines and has been shown to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. The protein is closely related to TraF (TIGR02739) which is somewhat longer, lacks the cysteine motif and is apparently not functional as a disulfide bond isomerase.
Pssm-ID: 131785 Cd Length: 153 Bit Score: 37.48 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 170671712 4 PGQTQLPDWDGLKLRVRTLIATHRVMIFSKSYCPYCHR----VKELFSSLGVQYYALELD-VTDDG--------PSIQQV 70
Cdd:TIGR02738 30 PPQGLTAATDNAPQGRHANQDDYALVFFYQSTCPYCHQfapvLKRFSQQFGLPVYAFSLDgQGLTGfpdplpatPEVMQT 109
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90
....*....|....*
gi 170671712 71 LAELTNQRTVPNVFI 85
Cdd:TIGR02738 110 FFPNPRPVVTPATFL 124
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| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
119-149 |
8.29e-03 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 39.06 E-value: 8.29e-03
10 20 30
....*....|....*....|....*....|....
gi 170671712 119 DYDLIVIGGGSGGLACskeAATL---GKKVMVLD 149
Cdd:COG1233 3 MYDVVVIGAGIGGLAA---AALLaraGYRVTVLE 33
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|
| PRK12759 |
PRK12759 |
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional |
28-94 |
8.77e-03 |
|
bifunctional gluaredoxin/ribonucleoside-diphosphate reductase subunit beta; Provisional
Pssm-ID: 139206 [Multi-domain] Cd Length: 410 Bit Score: 38.85 E-value: 8.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 170671712 28 VMIFSKSYCPYCHRVKELFSSLGVQYYALELDvtDDGPSI-------QQVLAELTNQRTVPNVFINGKHIGGCD 94
Cdd:PRK12759 4 VRIYTKTNCPFCDLAKSWFGANDIPFTQISLD--DDVKRAefyaevnKNILLVEEHIRTVPQIFVGDVHIGGYD 75
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