|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
91-579 |
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: 800.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 91 YDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEY 170
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 171 NQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGI 250
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 251 QGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKVGSYMEQHGVKFLRK 330
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 331 FIPVMVQQLEKgspgklKVLAKSTEGTETIEGVYNTVLLAIGRDSCTRKIGLEKIGVKINEKSGKIPVNDVEQTNVPYVY 410
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 411 AVGDILEDKPELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLEIYHTLFWPLE 490
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 491 WTVAGREN-NTCYAKIICNKFDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSG 569
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 5764543 570 LDITQKGCUG 579
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
88-579 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 520.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 88 DLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDFVVPSPQGTSWGLGGTCVNVGCIPKKLMHQAALLGQAL-CDSRKF 166
Cdd:PTZ00052 1 HLTFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFhHDSQMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 167 GWEYNQQvrHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIkATNKKGQETYYTAAQFVIATGERPR 246
Cdd:PTZ00052 81 GWKTSSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 247 YL-GIQGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKVGSYMEQHGV 325
Cdd:PTZ00052 158 IPeDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 326 KFLRKFIPVMVQQLEKgspgKLKVL--AKSTEgtetiegVYNTVLLAIGRDSCTRKIGLEKIGVKINEKSGKIPVNDVeq 403
Cdd:PTZ00052 238 LFLEGVVPINIEKMDD----KIKVLfsDGTTE-------LFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 404 TNVPYVYAVGDILEDKPELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLEIYH 483
Cdd:PTZ00052 305 TNIPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 484 TLFWPLEWTVAGRE--------------NNTCYAKIICNKFDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTI 549
Cdd:PTZ00052 385 QEFNTLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMI 464
|
490 500 510
....*....|....*....|....*....|
gi 5764543 550 GIHPTCGEVFTTLEITKSSGLDITQKGCUG 579
Cdd:PTZ00052 465 GIHPTDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
108-562 |
6.55e-126 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 377.19 E-value: 6.55e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 108 AKEAAILGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGQALCD-SRKFGWEYNQQvRHNWETMTKAIQ 186
Cdd:PRK06116 20 ANRAAMYGAKVALIE---------AKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 187 NHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKgqetyYTAAQFVIATGERPRYLGIQGdKEYCITSDDLFSL 266
Cdd:PRK06116 90 AYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIPDIPG-AEYGITSDGFFAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 267 PYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSIL-LRGFDQEMAEKVGSYMEQHGVKFLRKFIPvmvQQLEKGSPG 345
Cdd:PRK06116 164 EELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRLHTNAVP---KAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 346 KLKVlakSTEGTETIEgvYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKPELTPV 425
Cdd:PRK06116 241 SLTL---TLEDGETLT--VDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 426 AIQSGKLLAQRLFGA-SLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLEIYHTLFWPLEWTVAGRENnTCYAK 504
Cdd:PRK06116 314 AIAAGRRLSERLFNNkPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 5764543 505 IICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 562
Cdd:PRK06116 393 LVVVG-KEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
107-562 |
1.45e-109 |
|
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: 335.52 E-value: 1.45e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 107 CAKEAAILGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYnQQVRHNWETMTKAIQ 186
Cdd:COG1249 18 AAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISA-GAPSVDWAALMARKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 187 NHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATnkkGQETYyTAAQFVIATGERPRYLGIQG-DKEYCITSDDLFS 265
Cdd:COG1249 88 KVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT---GGETL-TADHIVIATGSRPRVPPIPGlDEVRVLTSDEALE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 266 LPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEKgSP 344
Cdd:COG1249 164 LEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDILTG---AKVTSVEK-TG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 345 GKLKVLAKSTEGTETIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILeDKPELTP 424
Cdd:COG1249 240 DGVTVTLEDGGGEEAVEA--DKVLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 425 VAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEvyKKENLEIYHTLFWPLEWTVAGRENnTCYAK 504
Cdd:COG1249 316 VASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEARE--AGIDVKVGKFPFAANGRALALGET-EGFVK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 5764543 505 IICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 562
Cdd:COG1249 393 LIADA-ETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
91-562 |
1.09e-99 |
|
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: 309.82 E-value: 1.09e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 91 YDYDLIIIGGGSGGLSCAKEAAILGKKVMV--LDFVvpspqgtswglGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGW 168
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 169 EyNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQetyYTAAQFVIATGERPRYL 248
Cdd:TIGR01424 70 T-VGKARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 249 GIQGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVR-SILLRGFDQEMAEKVGSYMEQHGVKF 327
Cdd:TIGR01424 146 ALPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 328 LRKFIpvmVQQLEKGSPGKLKVlakSTEGTETIegVYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVP 407
Cdd:TIGR01424 225 LPEDS---ITSISKDDDGRLKA---TLSKHEEI--VADVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 408 YVYAVGDIlEDKPELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEvyKKENLEIYHTLFW 487
Cdd:TIGR01424 296 SIYAVGDV-TDRINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARR--KFGDIEVYRAEFR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5764543 488 PLEWTVAGRENNtCYAKIICNKFDhDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 562
Cdd:TIGR01424 373 PMKATFSGRQEK-TLMKLVVDAKD-DKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
108-562 |
3.21e-98 |
|
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: 306.00 E-value: 3.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 108 AKEAAILGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMTKAIQN 187
Cdd:TIGR01421 18 ARRAAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 188 HISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKgqetyYTAAQFVIATGERPRYL-GIQGdKEYCITSDDLFSL 266
Cdd:TIGR01421 89 YVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIPG-AELGTDSDGFFAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 267 PYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVR-SILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVmvqQLEKGSPG 345
Cdd:TIGR01421 163 EELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPV---KVEKTVEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 346 KLKVLAksTEGTETIEgvYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILeDKPELTPV 425
Cdd:TIGR01421 240 KLVIHF--EDGKSIDD--VDELIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 426 AIQSGKLLAQRLF-GASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLEIYHTLFWPLEWTVaGRENNTCYAK 504
Cdd:TIGR01421 314 AIAAGRKLSERLFnGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAM-TSEKQKCRMK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 5764543 505 IIC-NKfdHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 562
Cdd:TIGR01421 393 LVCaGK--EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
91-562 |
1.49e-91 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 292.16 E-value: 1.49e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 91 YDYDLIIIGGGSGGLSCAKEAAILGKKVMV--LDFVVPSPQGTSwGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGW 168
Cdd:PLN02546 78 YDFDLFTIGAGSGGVRASRFASNFGASAAVceLPFATISSDTLG-GVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGW 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 169 EYNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKkgqetYYTAAQFVIATGERPRYL 248
Cdd:PLN02546 157 KYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGK-----LYTARNILIAVGGRPFIP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 249 GIQGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSI-LLRGFDQEMAEKVGSYMEQHGVKF 327
Cdd:PLN02546 232 DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAEQMSLRGIEF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 328 LRKFIPvmvQQLEKGSPGKLKVlaKSTEGTetIEGvYNTVLLAIGRDSCTRKIGLEKIGVKINeKSGKIPVNDVEQTNVP 407
Cdd:PLN02546 311 HTEESP---QAIIKSADGSLSL--KTNKGT--VEG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 408 YVYAVGDIlEDKPELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKkeNLEIYHTLFW 487
Cdd:PLN02546 382 SIWAVGDV-TDRINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYG--DVDVFTANFR 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5764543 488 PLEWTVAGRENNTCYAKIICNKfdHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 562
Cdd:PLN02546 459 PLKATLSGLPDRVFMKLIVCAK--TNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTM 531
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
87-562 |
2.34e-91 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 289.79 E-value: 2.34e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 87 EDLAYDYDLIIIGGGSGGLSCAKEAAILGKKVMVLDfvVP-SPQGTSW--GLGGTCVNVGCIPKKLMHQAALLGQALCDS 163
Cdd:PLN02507 20 NATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICE--LPfHPISSESigGVGGTCVIRGCVPKKILVYGATFGGEFEDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 164 RKFGWEYNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGE 243
Cdd:PLN02507 98 KNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 244 RPRYLGIQGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSIL-LRGFDQEMAEKVGSYMEQ 322
Cdd:PLN02507 178 RAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMRAVVARNLEG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 323 HGVKFLRKfipVMVQQLEKGSPGkLKVLAKSTEgtetiEGVYNTVLLAIGRDSCTRKIGLEKIGVKInEKSGKIPVNDVE 402
Cdd:PLN02507 257 RGINLHPR---TNLTQLTKTEGG-IKVITDHGE-----EFVADVVLFATGRAPNTKRLNLEAVGVEL-DKAGAVKVDEYS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 403 QTNVPYVYAVGDIlEDKPELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLeIY 482
Cdd:PLN02507 327 RTNIPSIWAIGDV-TNRINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGDIL-VF 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 483 HTLFWPLEWTVAGRENNTcYAKIICNKFDhDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 562
Cdd:PLN02507 405 TSSFNPMKNTISGRQEKT-VMKLIVDAET-DKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTM 482
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
135-562 |
2.34e-77 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 255.31 E-value: 2.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 135 LGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGweYNQQVRHNWETMTKAIQNHISSLNWGYRLSLREKAVAYVNSYGEF 214
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYG--FDTQFSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 215 VEHHKIKATNKKGQETYY------------------------TAAQFVIATGERPRYLGIQGdKEYCITSDDLFSLPYcP 270
Cdd:PTZ00058 160 LSENQVLIKKVSQVDGEAdesdddevtivsagvsqlddgqviEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 271 GKTLVVGASYVALECAGFLAGFGLDVTVMVR-SILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEkgSPGKLKV 349
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVK--EKNLTIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 350 LAKSTEgtetiEGVYNTVLLAIGRDSCTRKIGLEkiGVKINEKSGKIPVNDVEQTNVPYVYAVGDILEDKP--------- 420
Cdd:PTZ00058 316 LSDGRK-----YEHFDYVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 421 ------------------------ELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKK 476
Cdd:PTZ00058 389 lklyneepylkkkentsgesyynvQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGK 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 477 ENLEIYHTLFWPLEWTVAGRE---NNTCYAKIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHP 553
Cdd:PTZ00058 469 ENVKIYESRFTNLFFSVYDMDpaqKEKTYLKLVCVG-KEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHP 547
|
....*....
gi 5764543 554 TCGEVFTTL 562
Cdd:PTZ00058 548 TAAEEFVTM 556
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
107-558 |
1.52e-74 |
|
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: 244.86 E-value: 1.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 107 CAKEAAILGKKVMVldfvVPSPQgtswgLGGTCVNVGCIPKK-LMHQAALLGQALcDSRKFGWEYNqQVRHNWETMTKAI 185
Cdd:TIGR01350 16 AAIRAAQLGLKVAL----VEKEY-----LGGTCLNVGCIPTKaLLHSAEVYDEIK-HAKDLGIEVE-NVSVDWEKMQKRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 186 QNHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETyYTAAQFVIATGERPRYL--GIQGDKEYCITSDDL 263
Cdd:TIGR01350 85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLpgPFDFDGKVVITSTGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 264 FSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTV--MVRSIlLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEK 341
Cdd:TIGR01350 164 LNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTN---TKVTAVEK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 342 GspGKLKVLAKSTEGTETIEGVYntVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILEdKPE 421
Cdd:TIGR01350 240 N--DDQVTYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIG-GPM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 422 LTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAievyKKENLEIYHTLFwPLewTVAGR----E 497
Cdd:TIGR01350 314 LAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF-PF--AANGKalalG 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5764543 498 NNTCYAKIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 558
Cdd:TIGR01350 387 ETDGFVKIIADK-KTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
111-557 |
1.97e-73 |
|
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: 242.57 E-value: 1.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 111 AAILGKKVMVLDfvVPSPQGTSW--GLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQ-VRHNWETMTKAIQN 187
Cdd:TIGR01423 23 ATLYKKRVAVVD--VQTHHGPPFyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDRSsVKANWKALIAAKNK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 188 HISSLNWGYRLSLRE-KAVAYVNSYGEFVEHHKI----KATNKKGQETYYTAAQFVIATGERPRYLGIQGDkEYCITSDD 262
Cdd:TIGR01423 101 AVLDINKSYEGMFADtEGLTFFLGWGALEDKNVVlvreSADPKSAVKERLQAEHILLATGSWPQMLGIPGI-EHCISSNE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 263 LFSLPYCPGKTLVVGASYVALECAGFLAGF---GLDVTVMVR-SILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVqq 338
Cdd:TIGR01423 180 AFYLDEPPRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRnNMILRGFDSTLRKELTKQLRANGINIMTNENPAKV-- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 339 lEKGSPGKLKVLAKSTEGTEtiegvYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlED 418
Cdd:TIGR01423 258 -TLNADGSKHVTFESGKTLD-----VDVVMMAIGRVPRTQTLQLDKVGVELTKK-GAIQVDEFSRTNVPNIYAIGDV-TD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 419 KPELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKenLEIYHTLFWPLEWTVAGREN 498
Cdd:TIGR01423 330 RVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEK--VAVYESSFTPLMHNISGSKY 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 5764543 499 NTCYAKIICNKFDHDrVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGE 557
Cdd:TIGR01423 408 KKFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
107-558 |
2.34e-62 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 212.70 E-value: 2.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 107 CAKEAAILGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYnQQVRHNWetmtKAIQ 186
Cdd:PRK06416 19 AAIRAAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKA-ENVGIDF----KKVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 187 NH----ISSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYyTAAQFVIATGERPRYL-GIQGDKEYCITSD 261
Cdd:PRK06416 85 EWkngvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQTY-TAKNIILATGSRPRELpGIEIDGRVIWTSD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 262 DLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTV---MVRsiLLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQ 338
Cdd:PRK06416 164 EALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALKKRGIKIKTG---AKAKK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 339 LEKGSPGkLKVLAKSTEGTETIEGVYntVLLAIGRDSCTRKIGLEKIGVKINEksGKIPVNDVEQTNVPYVYAVGDILEd 418
Cdd:PRK06416 239 VEQTDDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIVG- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 419 KPELTPVAIQSGKLLAQRLFGASLEkCDYINVPTTVFTPLEYGCCGLSEEKAIEvyKKENLEIYHTLFwplewtvAGR-- 496
Cdd:PRK06416 313 GPMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKE--EGFDVKVVKFPF-------AGNgk 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5764543 497 ---ENNTC-YAKIICNKFDHdRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 558
Cdd:PRK06416 383 alaLGETDgFVKLIFDKKDG-EVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
107-561 |
1.05e-61 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 210.80 E-value: 1.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 107 CAKEAAILGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYnQQVRHNWETMTKAIQ 186
Cdd:PRK06292 18 AARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHA-DGPKIDFKKVMARVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 187 NHISSLNWGYRLSLREK-AVAYVNSYGEFVEHHKIKATnkkgqETYYTAAQFVIATGER-PRYLGI-QGDKEYCITSDDL 263
Cdd:PRK06292 88 RERDRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEVN-----GERIEAKNIVIATGSRvPPIPGVwLILGDRLLTSDDA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 264 FSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKVgsymeqhgVKFLRKFIPVM----VQQ 338
Cdd:PRK06292 163 FELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQA--------QKILSKEFKIKlgakVTS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 339 LEKGSpGKLKVLAKSTEGTETIEGVYntVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILeD 418
Cdd:PRK06292 235 VEKSG-DEKVEELEKGGKTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSVPGIYAAGDVN-G 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 419 KPELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAievyKKENLEIYHTLFwPLEWTVAGR-E 497
Cdd:PRK06292 310 KPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEEL----KAAGIDYVVGEV-PFEAQGRARvM 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5764543 498 NNTCYA-KIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLT-KQLLdDTIGIHPTCGEVFTT 561
Cdd:PRK06292 385 GKNDGFvKVYADK-KTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTvEDLL-RMPFYHPTLSEGLRT 448
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
108-579 |
3.63e-58 |
|
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: 201.50 E-value: 3.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 108 AKEAAILGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVrhNWETMTKAIQN 187
Cdd:TIGR02053 16 AIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATVAV--DFGELLEGKRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 188 HISSL-NWGYRLSLREKAVAYVNSYGEFVEHHKIKAtnKKGQETYYtAAQFVIATGERPRYLGIQGDKE--YcITSDDLF 264
Cdd:TIGR02053 85 VVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGREVRG-AKRFLIATGARPAIPPIPGLKEagY-LTSEEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 265 SLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEKGS 343
Cdd:TIGR02053 161 ALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTS---AQVKAVSVRG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 344 PGKLKVLAKSTEGTEtIEGVYntVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILeDKPELT 423
Cdd:TIGR02053 238 GGKIITVEKPGGQGE-VEADE--LLVATGRRPNTDGLGLEKAGVKLDER-GGILVDETLRTSNPGIYAAGDVT-GGLQLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 424 PVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIevykkENLEIYHTLFWPLEWTVAGREN--NTC 501
Cdd:TIGR02053 313 YVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQ-----KAGIECDCRTLPLTNVPRARINrdTRG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5764543 502 YAKIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSglDITQKGCUG 579
Cdd:TIGR02053 388 FIKLVAEP-GTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFYR--DVSKLSCCA 462
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
107-430 |
7.93e-51 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 177.12 E-value: 7.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 107 CAKEAAILGKKVMVLdfvvpspqgtswGLGGTCVNVGCIPKKLMHQAALLGQALcdsrkfgweynqqvrHNWETMTKAIQ 186
Cdd:pfam07992 15 AALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAAEAPEIA---------------SLWADLYKRKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 187 NHISSLNWGYRLSLREKAVAYVNSYGEFVEHHKikatnKKGQETYYTAAQFVIATGERPRYLGIQGDKEYC------ITS 260
Cdd:pfam07992 68 EVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEEL-----VDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtLDS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 261 DDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQL 339
Cdd:pfam07992 143 AEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGVEVRLG---TSVKEI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 340 EkGSPGKLKVLaksTEGTETIEgvYNTVLLAIGRDSCTRkiGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILEDK 419
Cdd:pfam07992 220 I-GDGDGVEVI---LKDGTEID--ADLVVVAIGRRPNTE--LLEAAGLELDER-GGIVVDEYLRTSVPGIYAAGDCRVGG 290
|
330
....*....|.
gi 5764543 420 PELTPVAIQSG 430
Cdd:pfam07992 291 PELAQNAVAQG 301
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
107-562 |
9.27e-50 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 178.47 E-value: 9.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 107 CAKEAAILGKKVMVLdfvvpspqGTSWgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYNQQVRHNWETMtKAIQ 186
Cdd:PRK06370 20 LAARAAGLGMKVALI--------ERGL-LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAV-MARK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 187 NHIS--SLNwGYRLSLREKA-VAYVNSYGEFVEHHKIKATNKKgqetyYTAAQFVIATGERPRYLGIQG--DKEYcITSD 261
Cdd:PRK06370 90 RRIRarSRH-GSEQWLRGLEgVDVFRGHARFESPNTVRVGGET-----LRAKRIFINTGARAAIPPIPGldEVGY-LTNE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 262 DLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSI-LLRGFDQEMAEKVGSYMEQHGVKFLrkfIPVMVQQLE 340
Cdd:PRK06370 163 TIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPrLLPREDEDVAAAVREILEREGIDVR---LNAECIRVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 341 KGSPGKLkVLAKSTEGTETIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKP 420
Cdd:PRK06370 240 RDGDGIA-VGLDCNGGAPEITG--SHILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 421 ELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEvyKKENLEIYHTLFwplewTVAGRENNT 500
Cdd:PRK06370 315 AFTHTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARK--SGRRVLVGTRPM-----TRVGRAVEK 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5764543 501 C----YAKIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 562
Cdd:PRK06370 388 GetqgFMKVVVDA-DTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
115-558 |
7.68e-41 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 153.96 E-value: 7.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 115 GKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGweYNQQVRH-NWETMTKAIQNHISSLN 193
Cdd:PRK07846 22 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 194 WG---YRLslREKA-VAYVNSYGEFVEHHKIKAtnkkGQETYYTAAQFVIATGERPRYLGIQGDKE--YcITSDDLFSLP 267
Cdd:PRK07846 91 AGgeeYRG--RDTPnIDVYRGHARFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSGvrY-HTSDTIMRLP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 268 YCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKvgsYMEQHGVKF-LRkfIPVMVQQLEKGSPG 345
Cdd:PRK07846 164 ELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISER---FTELASKRWdVR--LGRNVVGVSQDGSG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 346 KLKVLAksteGTETIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKPELTPV 425
Cdd:PRK07846 239 VTLRLD----DGSTVEA--DVLLVATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV-SSPYQLKHV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 426 AIQSGKLLAQRLF-GASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIE------VYKKENLEIYHTlfWPLEWTvagren 498
Cdd:PRK07846 311 ANHEARVVQHNLLhPDDLIASDHRFVPAAVFTHPQIASVGLTENEARAaglditVKVQNYGDVAYG--WAMEDT------ 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5764543 499 nTCYAKIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLT-KQLLDDTIGIHPTCGEV 558
Cdd:PRK07846 383 -TGFVKLIADR-DTGRLLGAHIIGPQASTLIQPLIQAMSFGLDaREMARGQYWIHPALPEV 441
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
111-558 |
2.04e-40 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 153.16 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 111 AAILGKKVMVLDfVVPSPQGTSwGLGGTCVNVGCIPKK-LMHQAALLGQALCDSRKFGWEYNqQVRHNWETMTKAIQNHI 189
Cdd:PRK06327 23 AAQLGLKVACIE-AWKNPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGIHVD-GVKIDVAKMIARKDKVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 190 SSLNWGYRLSLREKAVAYVNSYGEFV----EHHKIKATNKKGQETyyTAAQFVIATGERPRYL-GIQGDKEYCITSDDLF 264
Cdd:PRK06327 100 KKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDETVI--TAKHVIIATGSEPRHLpGVPFDNKIILDNTGAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 265 SLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEKGS 343
Cdd:PRK06327 178 NFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTKQGLDIHLG---VKIGEIKTGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 344 PGKLKVLAKSTEGTETIEgvYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILEdKPELT 423
Cdd:PRK06327 255 KGVSVAYTDADGEAQTLE--VDKLIVSIGRVPNTDGLGLEAVGLKLDER-GFIPVDDHCRTNVPNVYAIGDVVR-GPMLA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 424 PVAIQSGKLLAQRLFGASlEKCDYINVPTTVFTPLEYGCCGLSEEKAievyKKENLEIYHTLFwPleWTVAGRE----NN 499
Cdd:PRK06327 331 HKAEEEGVAVAERIAGQK-GHIDYNTIPWVIYTSPEIAWVGKTEQQL----KAEGVEYKAGKF-P--FMANGRAlamgEP 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 5764543 500 TCYAKIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 558
Cdd:PRK06327 403 DGFVKIIADA-KTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEV 460
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
129-558 |
1.67e-38 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 147.21 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 129 QGTswgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYN-QQVRhnWETMTKAIQNH----ISSLNWGYRLSLREK 203
Cdd:TIGR03452 31 KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLGIDAEiDSVR--WPDIVSRVFGDridpIAAGGEDYRRGDETP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 204 AVAYVNSYGEFVEHHKIKAtnkkGQETYYTAAQFVIATGERPR---YLGIQGDKEYciTSDDLFSLPYCPGKTLVVGASY 280
Cdd:TIGR03452 106 NIDVYDGHARFVGPRTLRT----GDGEEITGDQIVIAAGSRPYippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 281 VALECAGFLAGFGLDVTVMVRS-ILLRGFDQEMAEKvgsYMEQHGVKF---LRKFIpVMVQQLEKGspgklkvLAKSTEG 356
Cdd:TIGR03452 180 IAAEFAHVFSALGTRVTIVNRStKLLRHLDEDISDR---FTEIAKKKWdirLGRNV-TAVEQDGDG-------VTLTLDD 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 357 TETIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEkSGKIPVNDVEQTNVPYVYAVGDILEDKpELTPVAIQSGKLLAQR 436
Cdd:TIGR03452 249 GSTVTA--DVLLVATGRVPNGDLLDAEAAGVEVDE-DGRIKVDEYGRTSARGVWALGDVSSPY-QLKHVANAEARVVKHN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 437 LFG-ASLEKCDYINVPTTVFTPLEYGCCGLSEEKAIEVYKKENLEIYHTLFWPLEWTVagrENNTCYAKIICNKfDHDRV 515
Cdd:TIGR03452 325 LLHpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIQNYGDVAYGWAM---EDTTGFCKLIADR-DTGKL 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 5764543 516 IGFHILGPNAGEVTQGFAAAMKCGLT-KQLLDDTIGIHPTCGEV 558
Cdd:TIGR03452 401 LGAHIIGPQASSLIQPLITAMAFGLDaREMARKQYWIHPALPEV 444
|
|
| GRX_GRXh_1_2_like |
cd03419 |
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ... |
3-84 |
2.61e-36 |
|
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: 129.97 E-value: 2.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 3 RVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQ 82
Cdd:cd03419 1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
|
..
gi 5764543 83 KL 84
Cdd:cd03419 81 KL 82
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
450-562 |
6.80e-36 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 129.98 E-value: 6.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 450 VPTTVFTPLEYGCCGLSEEKAIEvyKKENLEIYHTLFWPLEWTVAGRENNtCYAKIICNKfDHDRVIGFHILGPNAGEVT 529
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKE--KGGEVKVGKFPFAANGRALAYGDTD-GFVKLVADR-ETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 5764543 530 QGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 562
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| GRX_euk |
TIGR02180 |
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ... |
4-85 |
2.24e-34 |
|
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: 124.66 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 4 VVIFSKSYCPHSTRVKELFSSLGVE-CNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQ 82
Cdd:TIGR02180 1 VVVFSKSYCPYCKKAKEILAKLNVKpYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKLA 80
|
...
gi 5764543 83 KLL 85
Cdd:TIGR02180 81 ELL 83
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
108-557 |
6.93e-33 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 131.43 E-value: 6.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 108 AKEAAILGKKVMVLDfvvpspqgTSWGLGGTCVNVGCIPKKLMHQAALlgqalcdsRKFGWEYNQQVRHN----WETMT- 182
Cdd:PRK05249 21 AMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVL--------RLIGFNQNPLYSSYrvklRITFAd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 183 ------KAIQNHISSLnwgyRLSLREKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERP-RYLGIQGDKE 255
Cdd:PRK05249 85 llaradHVINKQVEVR----RGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPyRPPDVDFDHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 256 YCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFLRKFIpv 334
Cdd:PRK05249 161 RIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEE-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 335 mVQQLEKGSPGKLKVLaKSteGTeTIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGD 414
Cdd:PRK05249 239 -VEKVEGGDDGVIVHL-KS--GK-KIKA--DCLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNENYQTAVPHIYAVGD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 415 ILeDKPELTPVAIQSGKLLAQRLFG-ASLEKCDYInvPTTVFTPLEYGCCGLSEEKAievyKKENLeiyhtlfwPLEWTV 493
Cdd:PRK05249 311 VI-GFPSLASASMDQGRIAAQHAVGeATAHLIEDI--PTGIYTIPEISSVGKTEQEL----TAAKV--------PYEVGR 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5764543 494 AG-REN--------NTCYAKIICNKFDHdRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGE 557
Cdd:PRK05249 376 ARfKELaraqiagdNVGMLKILFHRETL-EILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPTMAE 447
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
107-578 |
3.57e-30 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 124.88 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 107 CAKEAAILGKKVMVLDfvvpspQGTswgLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEYN-------------QQ 173
Cdd:PRK13748 113 AALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAAtvptidrsrllaqQQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 174 VRhnWETMTKAIQNHISSLNwgyrlslreKAVAYVNSYGEFVEHHKIKATNKKGQETYYTAAQFVIATGERPRYLGIQGD 253
Cdd:PRK13748 184 AR--VDELRHAKYEGILDGN---------PAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 254 KE--YCITSDDLFSlPYCPGKTLVVGASYVALECAGFLAGFGLDVTVMVRSILLRGFDQEMAEKVGSYMEQHGVKFLRKf 331
Cdd:PRK13748 253 KEtpYWTSTEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEH- 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 332 ipvmVQQLEKGSPGKLKVLaksTEGTETIEGvyNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYA 411
Cdd:PRK13748 331 ----TQASQVAHVDGEFVL---TTGHGELRA--DKLLVATGRAPNTRSLALDAAGVTVNAQ-GAIVIDQGMRTSVPHIYA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 412 VGDIlEDKPELTPVAIQSGKLLAQRLFGASlEKCDYINVPTTVFTPLEYGCCGLSEEKAievyKKENLEIyhtlfwplEW 491
Cdd:PRK13748 401 AGDC-TDQPQFVYVAAAAGTRAAINMTGGD-AALDLTAMPAVVFTDPQVATVGYSEAEA----HHDGIET--------DS 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 492 TVAGRENntcYAKIICNkFDHD------------RVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPT----- 554
Cdd:PRK13748 467 RTLTLDN---VPRALAN-FDTRgfiklvieegsgRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTmvegl 542
|
490 500
....*....|....*....|....*.
gi 5764543 555 --CGEVFTTleitkssglDITQKGCU 578
Cdd:PRK13748 543 klAAQTFNK---------DVKQLSCC 559
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
108-557 |
6.61e-30 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 122.55 E-value: 6.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 108 AKEAAILGKKVMVLDfvvPSPQGtswgLGGTCVNVGCIPKKLMHQAAllgqalcdsrKFGWEYNQQVRHNwETMTkaiqn 187
Cdd:PRK07251 19 AAKLASAGKKVALVE---ESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQVMATK-NTVT----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 188 hiSSLNWGYRLSLREKAVAYVNSYGEFVEHHKIKATnkKGQETY-YTAAQFVIATGERPRYLGIQG--DKEYCITSDDLF 264
Cdd:PRK07251 76 --SRLRGKNYAMLAGSGVDLYDAEAHFVSNKVIEVQ--AGDEKIeLTAETIVINTGAVSNVLPIPGlaDSKHVYDSTGIQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 265 SLPYCPGKTLVVGASYVALECAGFLAGFGLDVTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEKGS 343
Cdd:PRK07251 152 SLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLN---AHTTEVKNDG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 344 PgklKVLAKSTEGTETiegvYNTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKPELT 423
Cdd:PRK07251 229 D---QVLVVTEDETYR----FDALLYATGRKPNTEPLGLENTDIELTER-GAIKVDDYCQTSVPGVFAVGDV-NGGPQFT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 424 PVAIQSGKLLAQRLFGAS---LEkcDYINVPTTVFTPLEYGCCGLSEEKAIEV---YKKENLeiyhtlfwPLEWTVAGRE 497
Cdd:PRK07251 300 YISLDDFRIVFGYLTGDGsytLE--DRGNVPTTMFITPPLSQVGLTEKEAKEAglpYAVKEL--------LVAAMPRAHV 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5764543 498 NNTCYA--KIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGE 557
Cdd:PRK07251 370 NNDLRGafKVVVNT-ETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
136-562 |
2.04e-26 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 112.18 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 136 GGTCVNVGCIP-KKLMHQAallgqalcdsrkfgweynqQVRHNWETmtkAIQNHISSLNWgyrlsLREK---------AV 205
Cdd:NF040477 40 GGTCINIGCIPtKTLVHDA-------------------EQHQDFST---AMQRKSSVVGF-----LRDKnyhnladldNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 206 AYVNSYGEFVEHHKIKATNKKGQETYYTAAQFvIATGERPRYLGIQGDKEY--CITSDDLFSLPYCPGKTLVVGASYVAL 283
Cdd:NF040477 93 DVINGRAEFIDNHTLRVFQADGEQELRGEKIF-INTGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 284 ECAGFLAGFGLDVTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFLrkfIPVMVQQLEkgspgklkvlakSTEGT---ET 359
Cdd:NF040477 172 EFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVELI---LNAQVQRVS------------SHEGEvqlET 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 360 IEGVY--NTVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKPELTPVAIQSGKLLAQRL 437
Cdd:NF040477 237 AEGVLtvDALLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 438 FGASLEKC-DYINVPTTVFTPLEYGCCGLSEEKAievyKKENLEIyHTLFWPLEWTVAGRENNTCYA--KIICNKfDHDR 514
Cdd:NF040477 315 LGEGKRSTdDRQNVPYSVFMTPPLSRIGMTEEQA----RASGADI-QVVTLPVAAIPRARVMNDTRGvlKAVVDN-KTQR 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 5764543 515 VIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 562
Cdd:NF040477 389 ILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDL 436
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
136-562 |
3.28e-22 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 99.70 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 136 GGTCVNVGCIPKK-LMHQAAllgqalcdsrkfgweynqqvRHNweTMTKAIQNHISSLNWgyrlsLREKA---------V 205
Cdd:PRK08010 40 GGTCINIGCIPTKtLVHDAQ--------------------QHT--DFVRAIQRKNEVVNF-----LRNKNfhnladmpnI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 206 AYVNSYGEFVEHHKIKaTNKKGQETYYTAAQFVIATGERPRYLGIQG--DKEYCITSDDLFSLPYCPGKTLVVGASYVAL 283
Cdd:PRK08010 93 DVIDGQAEFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIPGitTTPGVYDSTGLLNLKELPGHLGILGGGYIGV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 284 ECAGFLAGFGLDVTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFlrkfipVMVQQLEKGSPGKLKVLAKSTEGTETIEG 362
Cdd:PRK08010 172 EFASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDI------ILNAHVERISHHENQVQVHSEHAQLAVDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 363 vyntVLLAIGRDSCTRKIGLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDIlEDKPELTPVAIQSGKLLAQRLFGASL 442
Cdd:PRK08010 246 ----LLIASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNIWAMGDV-TGGLQFTYISLDDYRIVRDELLGEGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 443 EKC-DYINVPTTVFTPLEYGCCGLSEEKAievykKENLEIYHTLFWPLEWTVAGRENNTCYA---KIICNKfdHDRVIGF 518
Cdd:PRK08010 320 RSTdDRKNVPYSVFMTPPLSRVGMTEEQA-----RESGADIQVVTLPVAAIPRARVMNDTRGvlkAIVDNK--TQRILGA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 5764543 519 HILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 562
Cdd:PRK08010 393 SLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| GRX_family |
cd02066 |
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
3-77 |
3.84e-22 |
|
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.
Pssm-ID: 239017 [Multi-domain] Cd Length: 72 Bit Score: 90.22 E-value: 3.84e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5764543 3 RVVIFSKSYCPHSTRVKELFSSLGVEcnVLELDQVDDGArVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQ 77
Cdd:cd02066 1 KVVVFSKSTCPYCKRAKRLLESLGIE--FEEIDILEDGE-LREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
108-561 |
1.59e-20 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 95.75 E-value: 1.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 108 AKEAAILGKKVMVLdfvvpspQGTSWGLGGTCVNVGCIPKKLMHQAA----------------LLGQALCDSRKFGWEYN 171
Cdd:PTZ00153 132 AINAMERGLKVIIF-------TGDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVERN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 172 QQVRHNWETMTKAIQNH----ISSLNWGYRLSLREKAVAYVNSYGEFV-EHHKIKATN-----KKGQEtyYTAAQFVIAT 241
Cdd:PTZ00153 205 QLVADTVQIDITKLKEYtqsvIDKLRGGIENGLKSKKFCKNSEHVQVIyERGHIVDKNtikseKSGKE--FKVKNIIIAT 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 242 GERPRY-LGIQGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGFGLDVT-VMVRSILLRGFDQEMAekvgSY 319
Cdd:PTZ00153 283 GSTPNIpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLLPLLDADVA----KY 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 320 MEQHGVKF--LRKFIPVMVQQLeKGSPGKLKVLAKSTEGTE-----------TIEGVY-NTVLLAIGRDSCTRKIGLEKI 385
Cdd:PTZ00153 359 FERVFLKSkpVRVHLNTLIEYV-RAGKGNQPVIIGHSERQTgesdgpkknmnDIKETYvDSCLVATGRKPNTNNLGLDKL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 386 GVKINEksGKIPVND---VEQTN---VPYVYAVGD-----ILEDKPELTPVAI------QSGKLLAQRLFGASLEKCDYI 448
Cdd:PTZ00153 438 KIQMKR--GFVSVDEhlrVLREDqevYDNIFCIGDangkqMLAHTASHQALKVvdwiegKGKENVNINVENWASKPIIYK 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 449 NVPTTVFTPLEYGCCGLSEEKAIEVYKKENL--EIYH-----TLFWPLEWTVAGRENNTCYAKIICNKFDH--------- 512
Cdd:PTZ00153 516 NIPSVCYTTPELAFIGLTEKEAKELYPPDNVgvEISFykansKVLCENNISFPNNSKNNSYNKGKYNTVDNtegmvkivy 595
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 5764543 513 ----DRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTT 561
Cdd:PTZ00153 596 lkdtKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
232-430 |
1.13e-19 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 89.79 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 232 YTAAQFVIATGERPRYLGIQGDKE-------YCITSDdlfsLPYCPGKT-LVVGASYVALECAGFLAGFGLDVTVMVRSI 303
Cdd:COG0492 99 YEAKAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEALYLTKFASKVTLIHRRD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 304 LLRGfDQEMAEKVgsyMEQHGVKFLRKFIPVMVQ---QLEKgspgkLKVLAKSTEGTETIEgvYNTVLLAIGRDSCTRki 380
Cdd:COG0492 175 ELRA-SKILVERL---RANPKIEVLWNTEVTEIEgdgRVEG-----VTLKNVKTGEEKELE--VDGVFVAIGLKPNTE-- 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5764543 381 GLEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILEDKPELTPVAIQSG 430
Cdd:COG0492 242 LLKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEG 290
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
238-463 |
1.49e-19 |
|
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];
Pssm-ID: 440215 [Multi-domain] Cd Length: 322 Bit Score: 89.87 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 238 VIATGERPRYLGIQGdkeycITSDDLFSL------PYC--------PGKTLVVGASYVALECAGFLAGFGLDVTVMVRS- 302
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddaDALrealkefkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 303 ILLRGFDQEMAEKVGSYMEQHGVKFLRKFipvMVQQLEkgspGKLKVLAKSTEGtETIEgvYNTVLLAIGrdsctrkIG- 381
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGE---TVVAID----GDDKVAVTLTDG-EEIP--ADLVVVAPG-------VRp 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 382 ----LEKIGVKINEkSGKIPVNDVEQTNVPYVYAVGDILE------DKPELTP---VAIQSGKLLAQRLFGASLEkcdYI 448
Cdd:COG0446 221 ntelAKDAGLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasAANKQGRVAAENILGGPAP---FP 296
|
250
....*....|....*
gi 5764543 449 NVPTTVFTPleYGCC 463
Cdd:COG0446 297 GLGTFISKV--FDLC 309
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
111-553 |
2.74e-19 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 90.69 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 111 AAILGKKVMVLDfvvpspqgtSWGLGGTCVNVGCIPKKLMHQAALLGQALCDSRKFGWEY--NQQVRHNWETMTKAIQNH 188
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFidDGEARVDLPAVNARVKAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 189 ISSLNWGYRLSLREKAVAYVNSYGEFVE----HHKIKATNKKGQETYYTAAQFVIATGERPRYL-GIQGDKEYCITSDDL 263
Cdd:PRK07845 91 AAAQSADIRARLEREGVRVIAGRGRLIDpglgPHRVKVTTADGGEETLDADVVLIATGASPRILpTAEPDGERILTWRQL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 264 FSLPYCPGKTLVVGASYVALECAGFLAGFGLDVT-VMVRSILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEKG 342
Cdd:PRK07845 171 YDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESVERTGDG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 343 spgklkVLAKSTEGTeTIEGVYntVLLAIGRDSCTRKIGLEKIGVKINEkSGKIPVNDVEQTNVPYVYAVGDILEDKPeL 422
Cdd:PRK07845 251 ------VVVTLTDGR-TVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIYAAGDCTGVLP-L 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 423 TPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSeEKAIEVYKKEnleiYHTLFWPLewtvagREN---- 498
Cdd:PRK07845 320 ASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVS-QAAIDSGEVP----ARTVMLPL------ATNprak 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 5764543 499 ----NTCYAKIICNKfDHDRVIGFHILGPNAGEVTQGFAAAMKCGLTKQLLDDTIGIHP 553
Cdd:PRK07845 389 msglRDGFVKLFCRP-GTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYP 446
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
272-348 |
3.92e-17 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 76.09 E-value: 3.92e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5764543 272 KTLVVGASYVALECAGFLAGFGLDVTVMVRSI-LLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEKGSPGKLK 348
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDrLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
238-522 |
9.82e-17 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 82.50 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 238 VIATGERPRYLGIQG-DKEYCI---TSDDLFSL-PYCPGKT--LVVGASYVALECAGFLAGFGLDVTVMVRS--ILLRGF 308
Cdd:COG1251 103 VLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 309 DQEMAEKVGSYMEQHGVKFLRKfipVMVQQLEkgspGKLKVLAKSTEGTETIEGvyNTVLLAIG---RDSCTRKIGLEki 385
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVRLG---TGVTEIE----GDDRVTGVRLADGEELPA--DLVVVAIGvrpNTELARAAGLA-- 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 386 gvkINeksGKIPVNDVEQTNVPYVYAVGDILE--------DKPELTPVAIQSGKLLAQRLFGASLEKCDYINVPTTVFTP 457
Cdd:COG1251 252 ---VD---RGIVVDDYLRTSDPDIYAAGDCAEhpgpvygrRVLELVAPAYEQARVAAANLAGGPAAYEGSVPSTKLKVFG 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5764543 458 LEYGCCGLSEEKAIEVykkenleiyhtlfwplewtVAGRENNTCYAKIIcnkFDHDRVIGFHILG 522
Cdd:COG1251 326 VDVASAGDAEGDEEVV-------------------VRGDPARGVYKKLV---LRDGRLVGAVLVG 368
|
|
| GRX_bact |
TIGR02181 |
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
4-85 |
6.45e-16 |
|
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]
Pssm-ID: 274017 [Multi-domain] Cd Length: 79 Bit Score: 72.68 E-value: 6.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 4 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDqvDDGARVQEVLsEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQK 83
Cdd:TIGR02181 1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVD--GDPALRDEMM-QRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDP 77
|
..
gi 5764543 84 LL 85
Cdd:TIGR02181 78 LL 79
|
|
| Glutaredoxin |
pfam00462 |
Glutaredoxin; |
4-66 |
3.32e-15 |
|
Glutaredoxin;
Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 70.23 E-value: 3.32e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5764543 4 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDQvDDGARvqEVLSEITNQKTVPNIFVNKVHV 66
Cdd:pfam00462 1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDE-DPEIR--EELKELSGWPTVPQVFIDGEHI 60
|
|
| GRX_GRXb_1_3_like |
cd03418 |
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ... |
4-79 |
3.65e-13 |
|
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.
Pssm-ID: 239510 [Multi-domain] Cd Length: 75 Bit Score: 64.92 E-value: 3.65e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5764543 4 VVIFSKSYCPHSTRVKELFSSLGVECNvlELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSG 79
Cdd:cd03418 2 VEIYTKPNCPYCVRAKALLDKKGVDYE--EIDVDGDPALREEMINRSGGRRTVPQIFIGDVHIGGCDDLYALERKG 75
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
214-545 |
5.11e-12 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 68.14 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 214 FVEHH--KIKATNKK--------GQETYYTAAQFVIATGER---PRYLGIQGDKEYCITS-DDLFSLPYCPGKT-----L 274
Cdd:PRK09564 74 KTEHEvvKVDAKNKTitvknlktGSIFNDTYDKLMIATGARpiiPPIKNINLENVYTLKSmEDGLALKELLKDEeikniV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 275 VVGASYVALECAGFLAGFGLDVTVMVRS--ILLRGFDQEMAEKVGSYMEQHGVKfLRkfIPVMVQQLEkgspGKLKVlak 352
Cdd:PRK09564 154 IIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVE-LH--LNEFVKSLI----GEDKV--- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 353 stEGTETIEGVYNT--VLLAIGRDSCTRKI---GLEKIgvkineKSGKIPVNDVEQTNVPYVYAVGD------ILEDKPE 421
Cdd:PRK09564 224 --EGVVTDKGEYEAdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKNV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 422 LTPVAIQS---GKLLAQRLFGASLEKCDYINVPTTVFTPLEYGCCGLSEEKAievyKKENLE--------IYHTLFWPle 490
Cdd:PRK09564 296 YVPLATTAnklGRMVGENLAGRHVSFKGTLGSACIKVLDLEAARTGLTEEEA----KKLGIDyktvfikdKNHTNYYP-- 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 5764543 491 wtvaGRENntCYAKIICNKFDHdRVIGFHILGPNaGEV--TQGFAAAMKCGLTKQLL 545
Cdd:PRK09564 370 ----GQED--LYVKLIYEADTK-VILGGQIIGKK-GAVlrIDALAVAIYAKLTTQEL 418
|
|
| GrxC |
COG0695 |
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
3-86 |
1.58e-11 |
|
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 60.21 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 3 RVVIFSKSYCPHSTRVKELFSSLGV---ECNVLEldqvDDGARvqEVLSEITNQKTVPNIFVNKVHVGGCDqtfqayqSG 79
Cdd:COG0695 1 KVTLYTTPGCPYCARAKRLLDEKGIpyeEIDVDE----DPEAR--EELRERSGRRTVPVIFIGGEHLGGFD-------EG 67
|
....*..
gi 5764543 80 LLQKLLQ 86
Cdd:COG0695 68 ELDALLA 74
|
|
| GlrX-like_plant |
TIGR02189 |
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ... |
4-87 |
1.66e-11 |
|
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: 60.93 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 4 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGARVQEVLSEITNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQK 83
Cdd:TIGR02189 10 VVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALHISGSLVP 89
|
....
gi 5764543 84 LLQE 87
Cdd:TIGR02189 90 MLKQ 93
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
272-441 |
3.14e-11 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 65.57 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 272 KTLVVGASYVALECAGFLAGFGLDVTVMVRSI-LLRGFDQEMAEKVGSYMEQHGVKF-LRKFIPVMVQQLEKGSPGKlkv 349
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREIPYrLNEEIDAINGNEVTFKSGK--- 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 350 lakstegTETiegvYNTVLLAIGRDSCTRKIglEKIGVKINEKsGKIPVNDVEQTNVPYVYAVGDILE------DKPELT 423
Cdd:PRK13512 227 -------VEH----YDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIITshyrhvDLPASV 292
|
170 180
....*....|....*....|.
gi 5764543 424 PVAI---QSGKLLAQRLFGAS 441
Cdd:PRK13512 293 PLAWgahRAASIVAEQIAGND 313
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
238-471 |
2.63e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 62.46 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 238 VIATGERPRYLGIQGDKEYCI---TSDDLFSL------------PYCPGKTLVVGASYVALECAGFLAGFgLDVTVMVRS 302
Cdd:COG1252 102 VIATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAEL-LRKLLRYPG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 303 I---------------LLRGFDQEMAEKVGSYMEQHGVKFLRKFipvMVQQLEKGspgklKVLaksTEGTETIEgvYNTV 367
Cdd:COG1252 181 IdpdkvritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGT---RVTEVDAD-----GVT---LEDGEEIP--ADTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 368 LLAIG-------RDSctrkiGLEKigvkinEKSGKIPVNDVEQT-NVPYVYAVGDI--LEDKPELT-----PVAIQSGKL 432
Cdd:COG1252 248 IWAAGvkappllADL-----GLPT------DRRGRVLVDPTLQVpGHPNVFAIGDCaaVPDPDGKPvpktaQAAVQQAKV 316
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 5764543 433 LAQRLFgASLEkcdyiNVPTTVFTPLEYGC-CGLSEEKAI 471
Cdd:COG1252 317 LAKNIA-ALLR-----GKPLKPFRYRDKGClASLGRGAAV 350
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
236-443 |
6.38e-10 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 62.15 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 236 QFVIATGERPRYLGIQG-DKEYCI---TSDDLFSLPYCPGKTL---VVGASYVALECAGFLAGFGLDVTV--MVRSILLR 306
Cdd:TIGR02374 99 KLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMDVSVihHAPGLMAK 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 307 GFDQEMAEKVGSYMEQHGVKFLrkfipVMVQQLEKGSPGKLKVLaKSTEGTETIEGVyntVLLAIG---RDSCTRKIGLe 383
Cdd:TIGR02374 179 QLDQTAGRLLQRELEQKGLTFL-----LEKDTVEIVGATKADRI-RFKDGSSLEADL---IVMAAGirpNDELAVSAGI- 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5764543 384 kigvKINeksGKIPVNDVEQTNVPYVYAVGDILEDKPE---LTPVAIQSGKLLAQRLFGASLE 443
Cdd:TIGR02374 249 ----KVN---RGIIVNDSMQTSDPDIYAVGECAEHNGRvygLVAPLYEQAKVLADHICGVECE 304
|
|
| PRK10638 |
PRK10638 |
glutaredoxin 3; Provisional |
4-86 |
1.31e-09 |
|
glutaredoxin 3; Provisional
Pssm-ID: 182607 [Multi-domain] Cd Length: 83 Bit Score: 54.83 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 4 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDqvDDGARVQEVLSEiTNQKTVPNIFVNKVHVGGCDQTFQAYQSGLLQK 83
Cdd:PRK10638 4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPID--GDAAKREEMIKR-SGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80
|
...
gi 5764543 84 LLQ 86
Cdd:PRK10638 81 LLK 83
|
|
| grxA |
PRK11200 |
glutaredoxin 1; Provisional |
4-76 |
1.33e-07 |
|
glutaredoxin 1; Provisional
Pssm-ID: 183036 [Multi-domain] Cd Length: 85 Bit Score: 49.26 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 4 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDdgarvqeVLSE-ITNQK----------TVPNIFVNKVHVGGCDQt 72
Cdd:PRK11200 3 VVIFGRPGCPYCVRAKELAEKLSEERDDFDYRYVD-------IHAEgISKADlektvgkpveTVPQIFVDQKHIGGCTD- 74
|
....
gi 5764543 73 FQAY 76
Cdd:PRK11200 75 FEAY 78
|
|
| GRX_hybridPRX5 |
cd03029 |
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ... |
2-70 |
1.90e-07 |
|
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing peroxiredoxin (PRX) and GRX domains, which is found in some pathogenic bacteria and cyanobacteria. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins. PRX-GRX hybrid proteins from Haemophilus influenza and Neisseria meningitis exhibit GSH-dependent peroxidase activity. The flow of reducing equivalents in the catalytic cycle of the hybrid protein goes from NADPH -> GSH reductase -> GSH -> GRX domain of hybrid -> PRX domain of hybrid -> peroxide substrate.
Pssm-ID: 239327 [Multi-domain] Cd Length: 72 Bit Score: 48.67 E-value: 1.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5764543 2 ERVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGarvqEVLSEITNQKTVPNIFVNKVHVGGCD 70
Cdd:cd03029 1 ESVSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITG----RSLRAVTGAMTVPQVFIDGELIGGSD 65
|
|
| GRX_DEP |
cd03027 |
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ... |
3-68 |
4.19e-07 |
|
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of uncharacterized proteins containing a GRX domain and additional domains DEP and DUF547, both of which have unknown functions. GRX is a glutathione (GSH) dependent reductase containing a redox active CXXC motif in a TRX fold. It has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. By altering the redox state of target proteins, GRX is involved in many cellular functions.
Pssm-ID: 239325 [Multi-domain] Cd Length: 73 Bit Score: 47.41 E-value: 4.19e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5764543 3 RVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDgaRVQEvLSEITNQKTVPNIFVNKVHVGG 68
Cdd:cd03027 2 RVTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIFPE--RKAE-LEERTGSSVVPQIFFNEKLVGG 64
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
238-435 |
5.28e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 49.02 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 238 VIATG-ERPRYLGIQGDK--------EYcITS----DDLFSLPycPGKTLVV-GASYVALECAGFLAGFGL-DVTVMVRs 302
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDF-LTRvnqaVADYDLP--VGKRVVViGGGNTAMDAARTAKRLGAeSVTIVYR- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 303 illRGFDqEM---AEKVgSYMEQHGVKFLRKFIP------------VMVQQLEKGSPGKlkvlakSTEGTETIEGVY--- 364
Cdd:PRK11749 306 ---RGRE-EMpasEEEV-EHAKEEGVEFEWLAAPveilgdegrvtgVEFVRMELGEPDA------SGRRRVPIEGSEftl 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5764543 365 --NTVLLAIGRDSCTRKIGLEKiGVKINEKSGKIPVNDVEQTNVPYVYAVGDIL--EDkpeLTPVAIQSGKLLAQ 435
Cdd:PRK11749 375 paDLVIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVtgAA---TVVWAVGDGKDAAE 445
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
238-415 |
7.74e-05 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 45.51 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 238 VIATG-ERPRYLGIQG-DKEYCIT----------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGFG-LDVTVMVRsil 304
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYR--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 305 lRGFDqEM---AEKVgSYMEQHGVKFL-----RKFIP--------VMVQQLEKGSP---GKLKVlaKSTEGTE-TIEGvy 364
Cdd:COG0493 288 -RTRE-EMpasKEEV-EEALEEGVEFLflvapVEIIGdengrvtgLECVRMELGEPdesGRRRP--VPIEGSEfTLPA-- 360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5764543 365 NTVLLAIGRDSCTRKIgLEKIGVKINEKsGKIPVNDVE-QTNVPYVYAVGDI 415
Cdd:COG0493 361 DLVILAIGQTPDPSGL-EEELGLELDKR-GTIVVDEETyQTSLPGVFAGGDA 410
|
|
| GRX_PICOT_like |
cd03028 |
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ... |
1-82 |
1.28e-04 |
|
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: 40.94 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 1 AERVVIFSKSY-----CPHSTRVKELFSSLGVE---CNVLEldqvDDGARvqEVLSEITNQKTVPNIFVNKVHVGGCDQT 72
Cdd:cd03028 7 ENPVVLFMKGTpeeprCGFSRKVVQILNQLGVDfgtFDILE----DEEVR--QGLKEYSNWPTFPQLYVNGELVGGCDIV 80
|
90
....*....|
gi 5764543 73 FQAYQSGLLQ 82
Cdd:cd03028 81 KEMHESGELQ 90
|
|
| GRXA |
TIGR02183 |
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
4-76 |
2.26e-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: 40.20 E-value: 2.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5764543 4 VVIFSKSYCPHSTRVKELFSSLGVECNVLELDQVDDGAR--VQEVLSEITNQ--KTVPNIFVNKVHVGGCDQtFQAY 76
Cdd:TIGR02183 2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEFRYIDIHAEgiSKADLEKTVGKpvETVPQIFVDEKHVGGCTD-FEQL 77
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
239-415 |
5.46e-04 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 42.81 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 239 IATGE-RPRYLGIQGDKEYCITS--------------DDLFSLPYCPGK-TLVVGASYVALECAGFLAGFGLDvTVMvrs 302
Cdd:PRK12778 523 IASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGKkVAVVGGGNTAMDSARTAKRLGAE-RVT--- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 303 ILLRGFDQEM---AEKVgSYMEQHGVKFLRKFIP-------------VMVQQLEKGSP---GKLKVLAksTEG-TETIEg 362
Cdd:PRK12778 599 IVYRRSEEEMparLEEV-KHAKEEGIEFLTLHNPieyladekgwvkqVVLQKMELGEPdasGRRRPVA--IPGsTFTVD- 674
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5764543 363 vYNTVLLAIGRDSctRKIGLEKI-GVKINEKsGKIPVNDVEQTNVPYVYAVGDI 415
Cdd:PRK12778 675 -VDLVIVSVGVSP--NPLVPSSIpGLELNRK-GTIVVDEEMQSSIPGIYAGGDI 724
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
238-437 |
5.73e-04 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 42.45 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 238 VIATGERPRYLGIQGDKEY-------------------CITSDDLFSLPYCPGKTL----VVGASYVALECAGFLAGFGL 294
Cdd:PTZ00318 118 VVAHGARPNTFNIPGVEERafflkevnhargirkrivqCIERASLPTTSVEERKRLlhfvVVGGGPTGVEFAAELADFFR 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 295 D--------------VTVM-VRSILLRGFDQEMAEKVGSYMEQHGVKFLRKFIPVMVQQLEkgspgklkVLAKSTEGTET 359
Cdd:PTZ00318 198 DdvrnlnpelveeckVTVLeAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKE--------VVLKDGEVIPT 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 360 IEGVYNTvllAIGRDSCTRKIGLEKigvkinEKSGKIPVND-VEQTNVPYVYAVGDI--LEDK--PELTPVAIQSGKLLA 434
Cdd:PTZ00318 270 GLVVWST---GVGPGPLTKQLKVDK------TSRGRISVDDhLRVKPIPNVFALGDCaaNEERplPTLAQVASQQGVYLA 340
|
...
gi 5764543 435 QRL 437
Cdd:PTZ00318 341 KEF 343
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
227-417 |
7.57e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 41.97 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 227 GQETYYTAAQFVIATGERPRYLGIQGDKEY-------CITSDDLFslpYCPGKTLVVGASYVALECAGFLAGFGLDVTVM 299
Cdd:PRK10262 99 GDSGEYTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 300 VRSILLRgfdqemAEK--VGSYMEQHGVKFLRKFIPVMVQQLEKGSPGKLKVLAKSTEGTETIEGV-YNTVLLAIGRDSC 376
Cdd:PRK10262 176 HRRDGFR------AEKilIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESLdVAGLFVAIGHSPN 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 5764543 377 TR----KIGLEKIGVKIneKSGKipVNDVEQTNVPYVYAVGDILE 417
Cdd:PRK10262 250 TAifegQLELENGYIKV--QSGI--HGNATQTSIPGVFAAGDVMD 290
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
226-414 |
9.79e-04 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 42.03 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 226 KGQETYYTaaQFVIATGERPRYLGIQG-DKEYCI---TSDDLFSLPYCPGKT---LVVGASYVALECAGFLAGFGLDVTV 298
Cdd:PRK14989 96 AGRTVFYD--KLIMATGSYPWIPPIKGsETQDCFvyrTIEDLNAIEACARRSkrgAVVGGGLLGLEAAGALKNLGVETHV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5764543 299 MVRSILLrgfdqeMAEKvgsyMEQHGVKFLRKFIPVMVQQLEKgSPGKLKVLAKSTEGTETIEGVYNTVL------LAIG 372
Cdd:PRK14989 174 IEFAPML------MAEQ----LDQMGGEQLRRKIESMGVRVHT-SKNTLEIVQEGVEARKTMRFADGSELevdfivFSTG 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 5764543 373 ---RDSCTRKIGLEkigvkINEKSGkIPVNDVEQTNVPYVYAVGD 414
Cdd:PRK14989 243 irpQDKLATQCGLA-----VAPRGG-IVINDSCQTSDPDIYAIGE 281
|
|
| NrdH |
cd02976 |
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
3-68 |
3.26e-03 |
|
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active CXXC motif within a TRX fold, characterized by a glutaredoxin (GRX)-like sequence and TRX-like activity profile. In vitro, it displays protein disulfide reductase activity that is dependent on TRX reductase, not glutathione (GSH). It is part of the NrdHIEF operon, where NrdEF codes for class Ib ribonucleotide reductase (RNR-Ib), an efficient enzyme at low oxygen levels. Under these conditions when GSH is mostly conjugated to spermidine, NrdH can still function and act as a hydrogen donor for RNR-Ib. It has been suggested that the NrdHEF system may be the oldest RNR reducing system, capable of functioning in a microaerophilic environment, where GSH was not yet available. NrdH from Corynebacterium ammoniagenes can form domain-swapped dimers, although it is unknown if this happens in vivo. Domain-swapped dimerization, which results in the blocking of the TRX reductase binding site, could be a mechanism for regulating the oxidation state of the protein.
Pssm-ID: 239274 [Multi-domain] Cd Length: 73 Bit Score: 36.43 E-value: 3.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5764543 3 RVVIFSKSYCPHSTRVKELFSSLGVECNVLELDQvDDGARvqEVLSEITNQKTVPNIFVNKVHVGG 68
Cdd:cd02976 1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDE-DPEAL--EELKKLNGYRSVPVVVIGDEHLSG 63
|
|
| Uxx_star |
NF041212 |
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like ... |
4-67 |
4.09e-03 |
|
Uxx-star family glutaredoxin-like (seleno)protein; A number of proteins with glutaredoxin-like folds, a length of about 75 amino acids, and a CxxC, C/UxxT, or CxxS motif near the N-terminus end with a UXX-COOH motif. That final motif typically is missed during coding region feature prediction by genome annotation pipelines. This HMM covers proteins from several distinctive families with this feature. The seed alignment illustrates the final selenocysteine or aligned Cys or Ser residues, but the HMM also hits proteins that lack an equivalent motif at the C-terminus. This C-terminal selenocysteine-containing motif has not yet been described in the literature.
Pssm-ID: 469116 [Multi-domain] Cd Length: 70 Bit Score: 36.28 E-value: 4.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5764543 4 VVIFSKSYCPHSTRVKELFSSLGVEcnVLELDQVDDGARVQEVLsEITN-QKTVPNIFVN-KVHVG 67
Cdd:NF041212 1 VVIYTKPGCPYCAAAKEDLARRGIP--FEEIDVSKDPEALEEML-RLTGgERIVPVIVEGgEVTVG 63
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