|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
164-652 |
0e+00 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 793.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 164 HDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEY 243
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 244 NQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETFYTASKFVIATGERPRYLGI 323
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 324 QGDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGFDQEMAEKVGSYLEQQGVKFQRK 403
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 404 FTPILVQQLEKglpgklKVVAKSTEGPETVEGIYNTVLLAIGRDSCTRKIGLEKIGVKINEKNGKIPVNDVEQTNVPHVY 483
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 484 AIGDILDGKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLE 563
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 564 WTVAGRDN-NTCYAKIICNKFDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSG 642
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 510120858 643 LDITQKGCUG 652
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
161-652 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 526.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 161 DSAHDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQ-DAKKY 239
Cdd:PTZ00052 1 HLTFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 240 GWEYNQqvKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIkATNKKGQETFYTASKFVIATGERPR 319
Cdd:PTZ00052 81 GWKTSS--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 320 YL-GIQGDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGFDQEMAEKVGSYLEQQGV 398
Cdd:PTZ00052 158 IPeDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 399 KFQRKFTPILVQQLEKglpgKLKVV--AKSTEgpetvegIYNTVLLAIGRDSCTRKIGLEKIGVKINEKNGKIPVNDVeq 476
Cdd:PTZ00052 238 LFLEGVVPINIEKMDD----KIKVLfsDGTTE-------LFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 477 TNVPHVYAIGDILDGKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYH 556
Cdd:PTZ00052 305 TNIPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 557 TLFWPLEWTVAGRD--------------NNTCYAKIICNKFDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTI 622
Cdd:PTZ00052 385 QEFNTLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMI 464
|
490 500 510
....*....|....*....|....*....|
gi 510120858 623 GIHPTCGEVFTTLEITKSSGLDITQKGCUG 652
Cdd:PTZ00052 465 GIHPTDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
181-635 |
7.74e-129 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 387.20 E-value: 7.74e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 181 AKEAANLGKKVMVLDfvvpspqgtTWGLGGTCVNVGCIPKKLMHQAALLGHALQD-AKKYGWEYNQQvKHNWEAMTEAIQ 259
Cdd:PRK06116 20 ANRAAMYGAKVALIE---------AKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 260 SHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKgqetfYTASKFVIATGERPRYLGIQGdKEYCITSDDLFSL 339
Cdd:PRK06116 90 AYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIPDIPG-AEYGITSDGFFAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 340 PYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVL-LRGFDQEMAEKVGSYLEQQGVKFQRKFTPilvQQLEKGLPG 418
Cdd:PRK06116 164 EELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRLHTNAVP---KAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 419 KLKVvakSTEGPETVEgiYNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDIlDGKPELTPV 498
Cdd:PRK06116 241 SLTL---TLEDGETLT--VDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 499 AIQAGKLLARRLF-GVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLEWTVAGRDNnTCYAK 577
Cdd:PRK06116 314 AIAAGRRLSERLFnNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 510120858 578 IICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 635
Cdd:PRK06116 393 LVVVG-KEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
180-635 |
4.21e-118 |
|
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: 359.79 E-value: 4.21e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 180 CAKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYnQQVKHNWEAMTEAIQ 259
Cdd:COG1249 18 AAIRAAQLGLKVALVE------KGR---LGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISA-GAPSVDWAALMARKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 260 SHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATnkkGQETfYTASKFVIATGERPRYLGIQG-DKEYCITSDDLFS 338
Cdd:COG1249 88 KVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT---GGET-LTADHIVIATGSRPRVPPIPGlDEVRVLTSDEALE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 339 LPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKFQRKFTpilVQQLEKGlP 417
Cdd:COG1249 164 LEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDILTGAK---VTSVEKT-G 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 418 GKLKVVAKSTEGPETVEGiyNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILdGKPELTP 497
Cdd:COG1249 240 DGVTVTLEDGGGEEAVEA--DKVLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 498 VAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFWPLEWTVAGRDNnTCYAK 577
Cdd:COG1249 316 VASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEARE--AGIDVKVGKFPFAANGRALALGET-EGFVK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 510120858 578 IICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 635
Cdd:COG1249 393 LIADA-ETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
181-635 |
2.64e-100 |
|
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: 313.70 E-value: 2.64e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 181 AKEAANLGKKVMVLDfvvpspqgtTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQS 260
Cdd:TIGR01421 18 ARRAAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 261 HIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKgqetfYTASKFVIATGERPRYL-GIQGdKEYCITSDDLFSL 339
Cdd:TIGR01421 89 YVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIPG-AELGTDSDGFFAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 340 PYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPIlvqQLEKGLPG 418
Cdd:TIGR01421 163 EELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPV---KVEKTVEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 419 KLKV-VAKSTEGPETVEgiyntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILdGKPELTP 497
Cdd:TIGR01421 240 KLVIhFEDGKSIDDVDE-----LIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 498 VAIQAGKLLARRLF-GVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLEWTVaGRDNNTCYA 576
Cdd:TIGR01421 313 VAIAAGRKLSERLFnGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAM-TSEKQKCRM 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 577 KIIC-NKfdNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 635
Cdd:TIGR01421 392 KLVCaGK--EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
181-635 |
7.53e-97 |
|
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: 304.81 E-value: 7.53e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 181 AKEAANLGKKVMV--LDFVvpspqgttwglGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEyNQQVKHNWEAMTEAI 258
Cdd:TIGR01424 18 ARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWT-VGKARFDWKKLLAAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 259 QSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQetfYTASKFVIATGERPRYLGIQGdKEYCITSDDLFS 338
Cdd:TIGR01424 86 DQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKPALPG-HELGITSNEAFH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 339 LPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFDQEMAEKVGSYLEQQGVKFQRKftpILVQQLEKGLP 417
Cdd:TIGR01424 162 LPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRILPE---DSITSISKDDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 418 GKLKVVAKSTEgpetvEGIYNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILDgKPELTP 497
Cdd:TIGR01424 239 GRLKATLSKHE-----EIVADVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTPSIYAVGDVTD-RINLTP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 498 VAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFWPLEWTVAGRDNNtCYAK 577
Cdd:TIGR01424 312 VAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARR--KFGDIEVYRAEFRPMKATFSGRQEK-TLMK 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 510120858 578 IICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 635
Cdd:TIGR01424 389 LVVDA-KDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
164-635 |
1.33e-94 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 302.57 E-value: 1.33e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 164 HDYDLIIIGGGSGGLSCAKEAANLGKKVMV--LDFVVPSPQgTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGW 241
Cdd:PLN02546 78 YDFDLFTIGAGSGGVRASRFASNFGASAAVceLPFATISSD-TLGGVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGW 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 242 EYNQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKkgqetFYTASKFVIATGERPRYL 321
Cdd:PLN02546 157 KYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGK-----LYTARNILIAVGGRPFIP 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 322 GIQGdKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSV-LLRGFDQEMAEKVGSYLEQQGVKF 400
Cdd:PLN02546 232 DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAEQMSLRGIEF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 401 QRKFTPilvQQLEKGLPGKLKVvaKSTEGpeTVEGiYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVP 480
Cdd:PLN02546 311 HTEESP---QAIIKSADGSLSL--KTNKG--TVEG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 481 HVYAIGDILDgKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKkeNLEVYHTLFW 560
Cdd:PLN02546 382 SIWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYG--DVDVFTANFR 458
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510120858 561 PLEWTVAGRDNNTCYAKIICNKfdNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 635
Cdd:PLN02546 459 PLKATLSGLPDRVFMKLIVCAK--TNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTM 531
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
160-635 |
7.58e-94 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 298.65 E-value: 7.58e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 160 DDSAHDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVV-PSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKK 238
Cdd:PLN02507 20 NATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICELPFhPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 239 YGWEYNQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETFYTASKFVIATGERP 318
Cdd:PLN02507 100 YGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 319 RYLGIQGdKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVL-LRGFDQEMAEKVGSYLEQQG 397
Cdd:PLN02507 180 QRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMRAVVARNLEGRG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 398 VKFQRKFTpilVQQLEKgLPGKLKVVAKSTEgpetvEGIYNTVLLAIGRDSCTRKIGLEKIGVKInEKNGKIPVNDVEQT 477
Cdd:PLN02507 259 INLHPRTN---LTQLTK-TEGGIKVITDHGE-----EFVADVVLFATGRAPNTKRLNLEAVGVEL-DKAGAVKVDEYSRT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 478 NVPHVYAIGDILDgKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLeVYHT 557
Cdd:PLN02507 329 NIPSIWAIGDVTN-RINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGDIL-VFTS 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510120858 558 LFWPLEWTVAGRDNNTCYAKIICNKFDneRVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 635
Cdd:PLN02507 407 SFNPMKNTISGRQEKTVMKLIVDAETD--KVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTM 482
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
180-631 |
4.51e-83 |
|
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: 269.13 E-value: 4.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 180 CAKEAANLGKKVMVldfvVPSPQgttwgLGGTCVNVGCIPKK-LMHQAALLgHALQDAKKYGWEYNQqVKHNWEAMTEAI 258
Cdd:TIGR01350 16 AAIRAAQLGLKVAL----VEKEY-----LGGTCLNVGCIPTKaLLHSAEVY-DEIKHAKDLGIEVEN-VSVDWEKMQKRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 259 QSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETfYTASKFVIATGERPRYL--GIQGDKEYCITSDDL 336
Cdd:TIGR01350 85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLpgPFDFDGKVVITSTGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 337 FSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTV---MVRsvLLRGFDQEMAEKVGSYLEQQGVKFqrkFTPILVQQLE 413
Cdd:TIGR01350 164 LNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTViemLDR--ILPGEDAEVSKVLQKALKKKGVKI---LTNTKVTAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 414 KGlpGKLKVVAKSTEGPETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILdGKP 493
Cdd:TIGR01350 239 KN--DDQVTYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDE-RGRIVVDEYMRTNVPGIYAIGDVI-GGP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 494 ELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAiemyKKENLEVYHTLFwPLewTVAGR---- 569
Cdd:TIGR01350 313 MLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF-PF--AANGKalal 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510120858 570 DNNTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 631
Cdd:TIGR01350 386 GETDGFVKIIADK-KTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
208-635 |
2.72e-75 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 251.84 E-value: 2.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 208 LGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGweYNQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEF 287
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYG--FDTQFSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 288 VDLHKIKATNKKGQETFY------------------------TASKFVIATGERPRYLGIQGdKEYCITSDDLFSLPYcP 343
Cdd:PTZ00058 160 LSENQVLIKKVSQVDGEAdesdddevtivsagvsqlddgqviEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 344 GCTLVVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKglPGKLKV 422
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKE--KNLTIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 423 VAKSTEgpetvEGIYNTVLLAIGRDSCTRKIGLEkiGVKINEKNGKIPVNDVEQTNVPHVYAIGDILDGKP--------- 493
Cdd:PTZ00058 316 LSDGRK-----YEHFDYVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 494 ------------------------ELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKK 549
Cdd:PTZ00058 389 lklyneepylkkkentsgesyynvQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGK 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 550 ENLEVYHTLFWPLEWTV---AGRDNNTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHP 626
Cdd:PTZ00058 469 ENVKIYESRFTNLFFSVydmDPAQKEKTYLKLVCVG-KEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHP 547
|
....*....
gi 510120858 627 TCGEVFTTL 635
Cdd:PTZ00058 548 TAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
184-630 |
3.76e-74 |
|
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: 246.42 E-value: 3.76e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 184 AANL-GKKVMVLDfvVPSPQGTTW--GLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQ-VKHNWEAMTEAIQ 259
Cdd:TIGR01423 22 AATLyKKRVAVVD--VQTHHGPPFyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDRSsVKANWKALIAAKN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 260 SHIGSLNWGYRVTLRE-KGVTYVNSFGEFVDLHKIKA-----TNKKGQETFyTASKFVIATGERPRYLGIQGDkEYCITS 333
Cdd:TIGR01423 100 KAVLDINKSYEGMFADtEGLTFFLGWGALEDKNVVLVresadPKSAVKERL-QAEHILLATGSWPQMLGIPGI-EHCISS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 334 DDLFSLPYCPGCTLVVGASYVGLECAGFLAG---LGLDVTVMVR-SVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPilv 409
Cdd:TIGR01423 178 NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTKQLRANGINIMTNENP--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 410 QQLEKGLPGKLKVVAKSTEgpetvEGIYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDIL 489
Cdd:TIGR01423 255 AKVTLNADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELT-KKGAIQVDEFSRTNVPNIYAIGDVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 490 DgKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKenLEVYHTLFWPLEWTVAGR 569
Cdd:TIGR01423 329 D-RVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEK--VAVYESSFTPLMHNISGS 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510120858 570 DNNTCYAKIICNKFDNErVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGE 630
Cdd:TIGR01423 406 KYKKFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
180-631 |
4.64e-69 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 231.96 E-value: 4.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 180 CAKEAANLGKKVMVL--DFvvpspqgttwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYnQQVKHNWEAMTEA 257
Cdd:PRK06416 19 AAIRAAQLGLKVAIVekEK-----------LGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKA-ENVGIDFKKVQEW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 258 IQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETfYTASKFVIATGERPRYL-GIQGDKEYCITSDDL 336
Cdd:PRK06416 87 KNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQT-YTAKNIILATGSRPRELpGIEIDGRVIWTSDEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 337 FSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTV---MVRsvLLRGFDQEMAEKVGSYLEQQGVKFqrkFTPILVQQLE 413
Cdd:PRK06416 166 LNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALKKRGIKI---KTGAKAKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 414 KGLPGkLKVVAKSTEGPETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEknGKIPVNDVEQTNVPHVYAIGDILdGKP 493
Cdd:PRK06416 241 QTDDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIV-GGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 494 ELTPVAIQAGKLLARRLFGVSLEkCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFwplewtvAGR---- 569
Cdd:PRK06416 315 MLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKE--EGFDVKVVKFPF-------AGNgkal 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510120858 570 --DNNTCYAKIICNKFDNErVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 631
Cdd:PRK06416 385 alGETDGFVKLIFDKKDGE-VLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
165-634 |
3.27e-66 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 224.67 E-value: 3.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 165 DYDLIIIGGGSGGLSCAKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYn 244
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 245 QQVKHNWEAMTEAIQSHIGSLNWGYRVTLREK-GVTYVNSFGEFVDLHKIKATnkkgqETFYTASKFVIATGER-PRYLG 322
Cdd:PRK06292 73 DGPKIDFKKVMARVRRERDRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEVN-----GERIEAKNIVIATGSRvPPIPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 323 I-QGDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQgVKF 400
Cdd:PRK06292 148 VwLILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-FKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 401 qrkFTPILVQQLEKGlpGKLKVVAKSTEG-PETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNV 479
Cdd:PRK06292 227 ---KLGAKVTSVEKS--GDEKVEELEKGGkTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 480 PHVYAIGDIlDGKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKenlevYHTLF 559
Cdd:PRK06292 299 PGIYAAGDV-NGKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGID-----YVVGE 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510120858 560 WPLEWTVAGR-DNNTCYA-KIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLT-KQLLdDTIGIHPTCGEVFTT 634
Cdd:PRK06292 373 VPFEAQGRARvMGKNDGFvKVYADK-KTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTvEDLL-RMPFYHPTLSEGLRT 448
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
181-652 |
1.51e-62 |
|
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: 214.98 E-value: 1.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 181 AKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGweYNQQVKHNWEAMTEAIQS 260
Cdd:TIGR02053 16 AIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGG--LAATVAVDFGELLEGKRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 261 HIGSL-NWGYRVTLREKGVTYVNSFGEFVDLHKIKAtnKKGQETFYtASKFVIATGERPRYLGIQGDKE--YcITSDDLF 337
Cdd:TIGR02053 85 VVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGREVRG-AKRFLIATGARPAIPPIPGLKEagY-LTSEEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 338 SLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKFQrkfTPILVQQLEKGL 416
Cdd:TIGR02053 161 ALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVV---TSAQVKAVSVRG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 417 PGKLKVVAKStEGPETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDGkPELT 496
Cdd:TIGR02053 238 GGKIITVEKP-GGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDE-RGGILVDETLRTSNPGIYAAGDVTGG-LQLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 497 PVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIemykkENLEVYHTLFWPLEWTVAGRDN--NTC 574
Cdd:TIGR02053 313 YVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQ-----KAGIECDCRTLPLTNVPRARINrdTRG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510120858 575 YAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSglDITQKGCUG 652
Cdd:TIGR02053 388 FIKLVAEP-GTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFYR--DVSKLSCCA 462
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
180-635 |
9.60e-55 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 193.50 E-value: 9.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 180 CAKEAANLGKKVMVLdfvvpspqGTTWgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQ 259
Cdd:PRK06370 20 LAARAAGLGMKVALI--------ERGL-LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAVMARKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 260 SHIGSLNWGYRVTLRE-KGVTYVNSFGEFVDLHKIKATNKKgqetfYTASKFVIATGERPRYLGIQG--DKEYcITSDDL 336
Cdd:PRK06370 91 RIRARSRHGSEQWLRGlEGVDVFRGHARFESPNTVRVGGET-----LRAKRIFINTGARAAIPPIPGldEVGY-LTNETI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 337 FSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSV-LLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKG 415
Cdd:PRK06370 165 FSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPrLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGDG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 416 lpgkLKVVAKSTEGPETVEGiyNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDIlDGKPEL 495
Cdd:PRK06370 245 ----IAVGLDCNGGAPEITG--SHILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRGAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 496 TPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFwplewTVAGR----DN 571
Cdd:PRK06370 317 THTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARK--SGRRVLVGTRPM-----TRVGRavekGE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510120858 572 NTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 635
Cdd:PRK06370 390 TQGFMKVVVDA-DTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
180-503 |
1.76e-52 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 182.90 E-value: 1.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 180 CAKEAANLGKKVMVLDfvvpspqgttwgLGGTCVNVGCIPKKLMHQAALLGHALqdakkygweynqqvkHNWEAMTEAIQ 259
Cdd:pfam07992 15 AALTLAQLGGKVTLIE------------DEGTCPYGGCVLSKALLGAAEAPEIA---------------SLWADLYKRKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 260 SHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKikatnKKGQETFYTASKFVIATGERPRYLGIQGDKEYC------ITS 333
Cdd:pfam07992 68 EVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEEL-----VDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtLDS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 334 DDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKFQrkfTPILVQQL 412
Cdd:pfam07992 143 AEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGVEVR---LGTSVKEI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 413 EkGLPGKLKVVaksTEGPETVEgiYNTVLLAIGRDSCTRkiGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDGK 492
Cdd:pfam07992 220 I-GDGDGVEVI---LKDGTEID--ADLVVVAIGRRPNTE--LLEAAGLELDE-RGGIVVDEYLRTSVPGIYAAGDCRVGG 290
|
330
....*....|.
gi 510120858 493 PELTPVAIQAG 503
Cdd:pfam07992 291 PELAQNAVAQG 301
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
184-631 |
1.44e-43 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 163.17 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 184 AANLGKKVMVLDfVVPSPQGTTwGLGGTCVNVGCIPKK-LMHQAALLGHALQDAKKYGWEYNQqVKHNWEAMTEAIQSHI 262
Cdd:PRK06327 23 AAQLGLKVACIE-AWKNPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGIHVDG-VKIDVAKMIARKDKVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 263 GSLNWGYRVTLREKGVTYVNSFGEFV----DLHKIKATNKKGQETfyTASKFVIATGERPRYL-GIQGDKEYCITSDDLF 337
Cdd:PRK06327 100 KKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDETVI--TAKHVIIATGSEPRHLpGVPFDNKIILDNTGAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 338 SLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFQrkfTPILVQQLEKGl 416
Cdd:PRK06327 178 NFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTKQGLDIH---LGVKIGEIKTG- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 417 pGKLKVVAKSTEGPETVEGIYNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILdGKPELT 496
Cdd:PRK06327 254 -GKGVSVAYTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDE-RGFIPVDDHCRTNVPNVYAIGDVV-RGPMLA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 497 PVAIQAGKLLARRLFGVSlEKCDYINIPTTVFTPLEYGCCGLSEEKAiemyKKENLEVYHTLFwPleWTVAGR----DNN 572
Cdd:PRK06327 331 HKAEEEGVAVAERIAGQK-GHIDYNTIPWVIYTSPEIAWVGKTEQQL----KAEGVEYKAGKF-P--FMANGRalamGEP 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 510120858 573 TCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 631
Cdd:PRK06327 403 DGFVKIIADA-KTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEV 460
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
188-631 |
6.66e-42 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 157.81 E-value: 6.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 188 GKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGweYNQQVKH-NWEAMTEAIQSHIGSLN 266
Cdd:PRK07846 22 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 267 WG---YRVtLREKGVTYVNSFGEFVDLHKIKAtnkkGQETFYTASKFVIATGERPRYLGIQGDKE--YcITSDDLFSLPY 341
Cdd:PRK07846 91 AGgeeYRG-RDTPNIDVYRGHARFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSGvrY-HTSDTIMRLPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 342 CPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKvgsYLEQQGVKFQRKF--TPILVQQLEKGlpg 418
Cdd:PRK07846 165 LPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISER---FTELASKRWDVRLgrNVVGVSQDGSG--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 419 klkvVAKSTEGPETVEGiyNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDgKPELTPV 498
Cdd:PRK07846 239 ----VTLRLDDGSTVEA--DVLLVATGRVPNGDLLDAAAAGVDVDE-DGRVVVDEYQRTSAEGVFALGDVSS-PYQLKHV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 499 AIQAGKLLARRLF-GVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLF------WPLEWTvagrdn 571
Cdd:PRK07846 311 ANHEARVVQHNLLhPDDLIASDHRFVPAAVFTHPQIASVGLTENEARA--AGLDITVKVQNYgdvaygWAMEDT------ 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510120858 572 nTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLT-KQLLDDTIGIHPTCGEV 631
Cdd:PRK07846 383 -TGFVKLIADR-DTGRLLGAHIIGPQASTLIQPLIQAMSFGLDaREMARGQYWIHPALPEV 441
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
181-630 |
2.15e-38 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 148.00 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 181 AKEAANLGKKVMVLDfvvpspqgTTWGLGGTCVNVGCIPKKLMHQAALlghalqdakkYGWEYNQ-------QVKHN--W 251
Cdd:PRK05249 21 AMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVL----------RLIGFNQnplyssyRVKLRitF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 252 EAMTEAIQSHIGSlnwgyRVTLREK-----GVTYVNSFGEFVDLHKIKATNKKGQETFYTASKFVIATGERP-RYLGIQG 325
Cdd:PRK05249 83 ADLLARADHVINK-----QVEVRRGqyernRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPyRPPDVDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 326 DKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKF 404
Cdd:PRK05249 158 DHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRDSGVTIRHNE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 405 TPILVQQLEKGL-----PGKlKVVAkstegpetvegiyNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNV 479
Cdd:PRK05249 238 EVEKVEGGDDGVivhlkSGK-KIKA-------------DCLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNENYQTAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 480 PHVYAIGDILdGKPELTPVAIQAGKLLARRLFGVSLEKcdYIN-IPTTVFTPLEYGCCGLSEEKAIEM---YkkenlEVY 555
Cdd:PRK05249 303 PHIYAVGDVI-GFPSLASASMDQGRIAAQHAVGEATAH--LIEdIPTGIYTIPEISSVGKTEQELTAAkvpY-----EVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 556 HTLFwplewtvagRDN--------NTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPT 627
Cdd:PRK05249 375 RARF---------KELaraqiagdNVGMLKILFHR-ETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPT 444
|
...
gi 510120858 628 CGE 630
Cdd:PRK05249 445 MAE 447
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
523-635 |
4.99e-37 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 133.83 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 523 IPTTVFTPLEYGCCGLSEEKAIEMYKKenLEVYHTLFWPLEWTVAGRDNNtCYAKIICNKfDNERVVGFHLLGPNAGEIT 602
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADR-ETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 510120858 603 QGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 635
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
202-631 |
8.04e-37 |
|
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: 143.36 E-value: 8.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 202 QGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGweYNQQVKH-NWEAMTEAIQSH----IGSLNWGYRVTLREK 276
Cdd:TIGR03452 31 KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRVFGDridpIAAGGEDYRRGDETP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 277 GVTYVNSFGEFVDlhkiKATNKKGQETFYTASKFVIATGERPR---YLGIQGDKEYciTSDDLFSLPYCPGCTLVVGASY 353
Cdd:TIGR03452 106 NIDVYDGHARFVG----PRTLRTGDGEEITGDQIVIAAGSRPYippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 354 VGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKvgsYLEQQGVKF--QRKFTPILVQQLEKGlpgklkvVAKSTEGP 430
Cdd:TIGR03452 180 IAAEFAHVFSALGTRVTIVNRStKLLRHLDEDISDR---FTEIAKKKWdiRLGRNVTAVEQDGDG-------VTLTLDDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 431 ETVEGiyNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDIldGKP-ELTPVAIQAGKLLARR 509
Cdd:TIGR03452 250 STVTA--DVLLVATGRVPNGDLLDAEAAGVEVDE-DGRIKVDEYGRTSARGVWALGDV--SSPyQLKHVANAEARVVKHN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 510 LFG-VSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEV--YHTLF--WPLEWTvagrdnnTCYAKIICNKfD 584
Cdd:TIGR03452 325 LLHpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIqnYGDVAygWAMEDT-------TGFCKLIADR-D 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 510120858 585 NERVVGFHLLGPNAGEITQGFAAAMKCGLT-KQLLDDTIGIHPTCGEV 631
Cdd:TIGR03452 397 TGKLLGAHIIGPQASSLIQPLITAMAFGLDaREMARKQYWIHPALPEV 444
|
|
| GRX_GRXh_1_2_like |
cd03419 |
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ... |
76-157 |
5.87e-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: 129.58 E-value: 5.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 76 RVMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQ 155
Cdd:cd03419 1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
|
..
gi 510120858 156 KL 157
Cdd:cd03419 81 KL 82
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
181-630 |
2.40e-33 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 132.95 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 181 AKEAANLGKKVMVLDfvvPSPQGttwgLGGTCVNVGCIPKKLMHQAAllghalqdakKYGWEYNQQVKHNweamtEAIQS 260
Cdd:PRK07251 19 AAKLASAGKKVALVE---ESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQVMATK-----NTVTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 261 HIGSLNWGyrvTLREKGVTYVNSFGEFVDLHKIKATNKKGQETFyTASKFVIATGERPRYLGIQG--DKEYCITSDDLFS 338
Cdd:PRK07251 77 RLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIEL-TAETIVINTGAVSNVLPIPGlaDSKHVYDSTGIQS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 339 LPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKglp 417
Cdd:PRK07251 153 LETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKNDGD--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 418 gklKVVAKSTEGPETvegiYNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDIlDGKPELTP 497
Cdd:PRK07251 230 ---QVLVVTEDETYR----FDALLYATGRKPNTEPLGLENTDIELTE-RGAIKVDDYCQTSVPGVFAVGDV-NGGPQFTY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 498 VAIQAGKLLARRLFGVS---LEkcDYINIPTTVFTPLEYGCCGLSEEKAIEM---YKKENLevyhtlfwPLEWTVAGRDN 571
Cdd:PRK07251 301 ISLDDFRIVFGYLTGDGsytLE--DRGNVPTTMFITPPLSQVGLTEKEAKEAglpYAVKEL--------LVAAMPRAHVN 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510120858 572 NTCYA--KIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGE 630
Cdd:PRK07251 371 NDLRGafKVVVNT-ETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| GRX_euk |
TIGR02180 |
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ... |
77-158 |
6.61e-33 |
|
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.
Pssm-ID: 274016 [Multi-domain] Cd Length: 83 Bit Score: 121.20 E-value: 6.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 77 VMIFSKSYCPHSTRVKELFSSLGV-VYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQ 155
Cdd:TIGR02180 1 VVVFSKSYCPYCKKAKEILAKLNVkPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKLA 80
|
...
gi 510120858 156 KLL 158
Cdd:TIGR02180 81 ELL 83
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
180-651 |
4.07e-32 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 131.43 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 180 CAKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQ 259
Cdd:PRK13748 113 AALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 260 SHIGSLnwgyRVTLREK------GVTYVNSFGEFVDLHKIKATNKKGQETFYTASKFVIATGERPRYLGIQGDKE--YCI 331
Cdd:PRK13748 184 ARVDEL----RHAKYEGildgnpAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKEtpYWT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 332 TSDDLFSlPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQ 411
Cdd:PRK13748 260 STEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAH 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 412 LEKglpgklKVVAKSTEGpetvEGIYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDILDg 491
Cdd:PRK13748 339 VDG------EFVLTTGHG----ELRADKLLVATGRAPNTRSLALDAAGVTVN-AQGAIVIDQGMRTSVPHIYAAGDCTD- 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 492 KPELTPVAIQAGKLLARRLFGVSlEKCDYINIPTTVFTPLEYGCCGLSEEKAiemyKKENLEVyhtlfwplEWTVAGRDN 571
Cdd:PRK13748 407 QPQFVYVAAAAGTRAAINMTGGD-AALDLTAMPAVVFTDPQVATVGYSEAEA----HHDGIET--------DSRTLTLDN 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 572 ntcYAKIICNkFDNE------------RVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPT-------CGEVF 632
Cdd:PRK13748 474 ---VPRALAN-FDTRgfiklvieegsgRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTmveglklAAQTF 549
|
490
....*....|....*....
gi 510120858 633 TTleitkssglDITQKGCU 651
Cdd:PRK13748 550 NK---------DVKQLSCC 559
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
209-635 |
6.81e-32 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 128.74 E-value: 6.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 209 GGTCVNVGCIP-KKLMHqaallghalqDAKKYGweynqqvkhnweAMTEAIQ--SHIGSLnwgyrvtLREKG-------- 277
Cdd:NF040477 40 GGTCINIGCIPtKTLVH----------DAEQHQ------------DFSTAMQrkSSVVGF-------LRDKNyhnladld 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 278 -VTYVNSFGEFVDLHKIKATNKKGQETFYtASKFVIATGERPRYLGIQGDKEY--CITSDDLFSLPYCPGCTLVVGASYV 354
Cdd:NF040477 91 nVDVINGRAEFIDNHTLRVFQADGEQELR-GEKIFINTGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 355 GLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFqrkftpILVQQLEKGLPGKLKVVAKSTEGPETV 433
Cdd:NF040477 170 GVEFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVEL------ILNAQVQRVSSHEGEVQLETAEGVLTV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 434 EGiyntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDIlDGKPELTPVAIQAGKLLARRLFGV 513
Cdd:NF040477 244 DA----LLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLGE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 514 SLEKC-DYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYhTLfwPLEWTVAGR---DNNTCYAKIICNKfdNERVV 589
Cdd:NF040477 318 GKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARA--SGADIQVV-TL--PVAAIPRARvmnDTRGVLKAVVDNK--TQRIL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 510120858 590 GFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 635
Cdd:NF040477 391 GVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDL 436
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
209-635 |
2.48e-25 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 109.33 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 209 GGTCVNVGCIPKKLMhqaallghaLQDAKKYGweynqqvkhnweAMTEAIQSHIGSLNWgyrvtLREK---------GVT 279
Cdd:PRK08010 40 GGTCINIGCIPTKTL---------VHDAQQHT------------DFVRAIQRKNEVVNF-----LRNKnfhnladmpNID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 280 YVNSFGEFVDLHKIKaTNKKGQETFYTASKFVIATGERPRYLGIQG--DKEYCITSDDLFSLPYCPGCTLVVGASYVGLE 357
Cdd:PRK08010 94 VIDGQAEFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIPGitTTPGVYDSTGLLNLKELPGHLGILGGGYIGVE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 358 CAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFqrkftpILVQQLEKGLPGKLKVVAKSTEGPETVEGI 436
Cdd:PRK08010 173 FASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDI------ILNAHVERISHHENQVQVHSEHAQLAVDAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 437 yntvLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILDGKpELTPVAIQAGKLLARRLFGVSLE 516
Cdd:PRK08010 247 ----LIASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNIWAMGDVTGGL-QFTYISLDDYRIVRDELLGEGKR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 517 KC-DYINIPTTVFTPLEYGCCGLSEEKAiemykKENLEVYHTLFWPLEWTVAGR---DNNTCYAKIICNKfdNERVVGFH 592
Cdd:PRK08010 321 STdDRKNVPYSVFMTPPLSRVGMTEEQA-----RESGADIQVVTLPVAAIPRARvmnDTRGVLKAIVDNK--TQRILGAS 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 510120858 593 LLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 635
Cdd:PRK08010 394 LLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
181-634 |
9.49e-25 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 109.23 E-value: 9.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 181 AKEAANLGKKVMVLdfvvpspQGTTWGLGGTCVNVGCIPKKLMHQAA----------------LLGHALQDAKKYGWEYN 244
Cdd:PTZ00153 132 AINAMERGLKVIIF-------TGDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVERN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 245 Q----QVKHNWEAMTEAIQSHIGSLNWGYRVTLREKG-------VTYVNSFGEFVDLHKIKAtNKKGQEtfYTASKFVIA 313
Cdd:PTZ00153 205 QlvadTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKfcknsehVQVIYERGHIVDKNTIKS-EKSGKE--FKVKNIIIA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 314 TGERPRY-LGIQGDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVT-VMVRSVLLRGFDQEMAekvgS 391
Cdd:PTZ00153 282 TGSTPNIpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLLPLLDADVA----K 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 392 YLEQQGVKFQ--RKFTPILVQQLEKGLPGKLKVVAKS--TEGPETVEGIYNT---------VLLAIGRDSCTRKIGLEKI 458
Cdd:PTZ00153 358 YFERVFLKSKpvRVHLNTLIEYVRAGKGNQPVIIGHSerQTGESDGPKKNMNdiketyvdsCLVATGRKPNTNNLGLDKL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 459 GVKINEknGKIPVND---VEQTN---VPHVYAIGDIlDGKPELTPVA-IQA-----------GKLLARRLFGVSLEKCDY 520
Cdd:PTZ00153 438 KIQMKR--GFVSVDEhlrVLREDqevYDNIFCIGDA-NGKQMLAHTAsHQAlkvvdwiegkgKENVNINVENWASKPIIY 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 521 INIPTTVFTPLEYGCCGLSEEKAIEMYKKENL--EVYH-----TLFWPLEWTVAGRDNNTCYAKIICNKFDN-------- 585
Cdd:PTZ00153 515 KNIPSVCYTTPELAFIGLTEKEAKELYPPDNVgvEISFykansKVLCENNISFPNNSKNNSYNKGKYNTVDNtegmvkiv 594
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 510120858 586 -----ERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTT 634
Cdd:PTZ00153 595 ylkdtKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
184-487 |
4.92e-23 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 102.63 E-value: 4.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 184 AANLGKKVMVLDFVvpspqgttwGLGGTCVNVGCIPKK----------LMHQAALLGHALQDAKKYGWEY---NQQVKhn 250
Cdd:PRK07845 20 AAQLGADVTVIERD---------GLGGAAVLTDCVPSKtliataevrtELRRAAELGIRFIDDGEARVDLpavNARVK-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 251 weAMTEAiQSHigslnwGYRVTLREKGVTYVNSFGEFVDL----HKIKATNKKGQETFYTASKFVIATGERPRYL-GIQG 325
Cdd:PRK07845 89 --ALAAA-QSA------DIRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPRILpTAEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 326 DKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVT-VMVRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKF 404
Cdd:PRK07845 160 DGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 405 TPILVQQLEKGlpgklkVVAKSTEGpETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYA 484
Cdd:PRK07845 240 RAESVERTGDG------VVVTLTDG-RTVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIYA 309
|
...
gi 510120858 485 IGD 487
Cdd:PRK07845 310 AGD 312
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
311-536 |
6.92e-23 |
|
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: 99.89 E-value: 6.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 311 VIATGERPRYLGIQGdkeycITSDDLFSL------PYC-------PGCTLVV-GASYVGLECAGFLAGLGLDVTVMVRS- 375
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddaDALrealkefKGKRAVViGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 376 VLLRGFDQEMAEKVGSYLEQQGVKFQRKFTpilVQQLEkglpGKLKVVAKSTEGpETVEgiYNTVLLAIGrdsctrkIG- 454
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGET---VVAID----GDDKVAVTLTDG-EEIP--ADLVVVAPG-------VRp 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 455 ----LEKIGVKINEKNGkIPVNDVEQTNVPHVYAIGD------ILDGKPELTP---VAIQAGKLLARRLFGVSLEkcdYI 521
Cdd:COG0446 221 ntelAKDAGLALGERGW-IKVDETLQTSDPDVYAAGDcaevphPVTGKTVYIPlasAANKQGRVAAENILGGPAP---FP 296
|
250
....*....|....*
gi 510120858 522 NIPTTVFTPleYGCC 536
Cdd:COG0446 297 GLGTFISKV--FDLC 309
|
|
| GRX_family |
cd02066 |
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
76-150 |
1.30e-22 |
|
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.
Pssm-ID: 239017 [Multi-domain] Cd Length: 72 Bit Score: 91.76 E-value: 1.30e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510120858 76 RVMIFSKSYCPHSTRVKELFSSLGVVYniLELDQVDDGAsVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQ 150
Cdd:cd02066 1 KVVVFSKSTCPYCKRAKRLLESLGIEF--EEIDILEDGE-LREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
311-512 |
1.29e-19 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 91.36 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 311 VIATGERPRYLGIQG-DKEYCI---TSDDLFSL-PYCPGCT--LVVGASYVGLECAGFLAGLGLDVTVMVRS--VLLRGF 381
Cdd:COG1251 103 VLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 382 DQEMAEKVGSYLEQQGVKFQrkftpilvqqlekglpgkLKVVAKSTEGPETVEGIY---------NTVLLAIG---RDSC 449
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVR------------------LGTGVTEIEGDDRVTGVRladgeelpaDLVVVAIGvrpNTEL 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510120858 450 TRKIGLEkigvkINekNGkIPVNDVEQTNVPHVYAIGDI------LDGKP--ELTPVAIQAGKLLARRLFG 512
Cdd:COG1251 245 ARAAGLA-----VD--RG-IVVDDYLRTSDPDIYAAGDCaehpgpVYGRRvlELVAPAYEQARVAAANLAG 307
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
303-503 |
1.13e-17 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 84.02 E-value: 1.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 303 TFYTASKFVIATGERPRYLGIQGDKE-------YCITSDdlfsLPYCPGCT-LVVGASYVGLECAGFLAGLGLDVTVMVR 374
Cdd:COG0492 97 TEYEAKAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEALYLTKFASKVTLIHR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 375 SVLLRGfDQEMAEKVgsyLEQQGVKFQRKFTPILVQqLEKGLPGkLKVVAKSTEGPETVEgiYNTVLLAIGRDSCTRkiG 454
Cdd:COG0492 173 RDELRA-SKILVERL---RANPKIEVLWNTEVTEIE-GDGRVEG-VTLKNVKTGEEKELE--VDGVFVAIGLKPNTE--L 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510120858 455 LEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDGKPELTPVAIQAG 503
Cdd:COG0492 243 LKGLGLELDE-DGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEG 290
|
|
| GRX_bact |
TIGR02181 |
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
77-158 |
1.67e-17 |
|
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]
Pssm-ID: 274017 [Multi-domain] Cd Length: 79 Bit Score: 77.30 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 77 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDqvDDGASVQEVLtEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQK 156
Cdd:TIGR02181 1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVD--GDPALRDEMM-QRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDP 77
|
..
gi 510120858 157 LL 158
Cdd:TIGR02181 78 LL 79
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
347-421 |
1.79e-16 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 74.55 E-value: 1.79e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510120858 347 LVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKGLPGKLK 421
Cdd:pfam00070 3 VVVGGGYIGLELAGALARLGSKVTVVERRdRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| Glutaredoxin |
pfam00462 |
Glutaredoxin; |
77-139 |
5.22e-16 |
|
Glutaredoxin;
Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 72.54 E-value: 5.22e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510120858 77 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDgasVQEVLTEISNQKTVPNIFVNKVHV 139
Cdd:pfam00462 1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDEDPE---IREELKELSGWPTVPQVFIDGEHI 60
|
|
| GRX_GRXb_1_3_like |
cd03418 |
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ... |
77-143 |
1.12e-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: 66.46 E-value: 1.12e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510120858 77 VMIFSKSYCPHSTRVKELFSSLGVVYnilELDQVDDGASVQEVLTEISNQ-KTVPNIFVNKVHVGGCD 143
Cdd:cd03418 2 VEIYTKPNCPYCVRAKALLDKKGVDY---EEIDVDGDPALREEMINRSGGrRTVPQIFIGDVHIGGCD 66
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
292-618 |
1.83e-13 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 72.77 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 292 KIKATNKKGQETF-YTASKFVIATGER---PRYLGIQGDKEYCITS-DD------LFSLPYCPGCTlVVGASYVGLECAG 360
Cdd:PRK09564 88 TITVKNLKTGSIFnDTYDKLMIATGARpiiPPIKNINLENVYTLKSmEDglalkeLLKDEEIKNIV-IIGAGFIGLEAVE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 361 FLAGLGLDVTVMVRS--VLLRGFDQEMAEKVGSYLEQQGVKFQrkftpilVQQLEKGLPGKLKVvakstEGPETVEGIYN 438
Cdd:PRK09564 167 AAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELH-------LNEFVKSLIGEDKV-----EGVVTDKGEYE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 439 T--VLLAIGRDSCTRKI---GLEKIgvkineKNGKIPVNDVEQTNVPHVYAIGD------ILDGKPELTPVAIQAGKLla 507
Cdd:PRK09564 235 AdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKNVYVPLATTANKL-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 508 RRLFGVSLEKCDYINIPT------TVFTpLEYGCCGLSEEKAiemyKKENLEVY--------HTLFWPlewtvagrDNNT 573
Cdd:PRK09564 307 GRMVGENLAGRHVSFKGTlgsaciKVLD-LEAARTGLTEEEA----KKLGIDYKtvfikdknHTNYYP--------GQED 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 510120858 574 CYAKIICNKfDNERVVGFHLLGPNAGEI-TQGFAAAMKCGLTKQLL 618
Cdd:PRK09564 374 LYVKLIYEA-DTKVILGGQIIGKKGAVLrIDALAVAIYAKLTTQEL 418
|
|
| GlrX-like_plant |
TIGR02189 |
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ... |
70-158 |
4.34e-12 |
|
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to plants. Multiple isoforms are found in A. thaliana and O.sativa.
Pssm-ID: 274023 [Multi-domain] Cd Length: 99 Bit Score: 62.86 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 70 DLIEGNRVMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAH 149
Cdd:TIGR02189 3 RMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALH 82
|
....*....
gi 510120858 150 QNGLLQKLL 158
Cdd:TIGR02189 83 ISGSLVPML 91
|
|
| GrxC |
COG0695 |
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
76-143 |
7.08e-12 |
|
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 61.37 E-value: 7.08e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510120858 76 RVMIFSKSYCPHSTRVKELFSSLGVVYNilELDqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCD 143
Cdd:COG0695 1 KVTLYTTPGCPYCARAKRLLDEKGIPYE--EID-VDEDPEAREELRERSGRRTVPVIFIGGEHLGGFD 65
|
|
| PRK10638 |
PRK10638 |
glutaredoxin 3; Provisional |
77-159 |
1.67e-11 |
|
glutaredoxin 3; Provisional
Pssm-ID: 182607 [Multi-domain] Cd Length: 83 Bit Score: 60.60 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 77 VMIFSKSYCPHSTRVKELFSSLGVVYNILEldqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQK 156
Cdd:PRK10638 4 VEIYTKATCPFCHRAKALLNSKGVSFQEIP---IDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80
|
...
gi 510120858 157 LLQ 159
Cdd:PRK10638 81 LLK 83
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
269-544 |
5.70e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 64.77 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 269 YRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETFYtaSKFVIATGERPRYLGIQGDKEYCI---TSDDLFSL------ 339
Cdd:COG1252 62 LRELLRRAGVRFIQGEVTGIDPEARTVTLADGRTLSY--DYLVIATGSVTNFFGIPGLAEHALplkTLEDALALrerlla 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 340 ------PYCPGCTLVVGASYVGLECAGFLAGL--------GLD--------VTVMVRsvLLRGFDQEMAEKVGSYLEQQG 397
Cdd:COG1252 140 aferaeRRRLLTIVVVGGGPTGVELAGELAELlrkllrypGIDpdkvritlVEAGPR--ILPGLGEKLSEAAEKELEKRG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 398 VKFQRKFTpilVQQLEKGlpgklKVVaksTEGPETVEgiYNTVLLAIG-------RDSctrkiGLEKigvkinEKNGKIP 470
Cdd:COG1252 218 VEVHTGTR---VTEVDAD-----GVT---LEDGEEIP--ADTVIWAAGvkappllADL-----GLPT------DRRGRVL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 471 VNDVEQT-NVPHVYAIGD---ILDGKPELTP----VAIQAGKLLARRLFGVSLEKcdyiniPTTVFTPLEYGC-CGLSEE 541
Cdd:COG1252 274 VDPTLQVpGHPNVFAIGDcaaVPDPDGKPVPktaqAAVQQAKVLAKNIAALLRGK------PLKPFRYRDKGClASLGRG 347
|
...
gi 510120858 542 KAI 544
Cdd:COG1252 348 AAV 350
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
300-516 |
3.59e-10 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 63.31 E-value: 3.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 300 GQETFYtaSKFVIATGERPRYLGIQG-DKEYCI---TSDDLFSLPYCPGCTL---VVGASYVGLECAGFLAGLGLDVTV- 371
Cdd:TIGR02374 92 GRTLSY--DKLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMDVSVi 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 372 -MVRSVLLRGFDQEMAEKVGSYLEQQGVKFQ-RKFTPILVQQlekglpGKLKVVaKSTEGPETVEGIyntVLLAIG---R 446
Cdd:TIGR02374 170 hHAPGLMAKQLDQTAGRLLQRELEQKGLTFLlEKDTVEIVGA------TKADRI-RFKDGSSLEADL---IVMAAGirpN 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510120858 447 DSCTRKIGLekigvkinEKNGKIPVNDVEQTNVPHVYAIGDI--LDGKP-ELTPVAIQAGKLLARRLFGVSLE 516
Cdd:TIGR02374 240 DELAVSAGI--------KVNRGIIVNDSMQTSDPDIYAVGECaeHNGRVyGLVAPLYEQAKVLADHICGVECE 304
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
347-512 |
9.01e-10 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 61.34 E-value: 9.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 347 LVVGASYVGLECAGFLAGLGLDVTVMVRSV-LLRGFDQEMAEKVGSYLEQQGVKFQrkftpiLVQQLEKgLPGKLkVVAK 425
Cdd:PRK13512 152 LVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREIPYR------LNEEIDA-INGNE-VTFK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 426 STEgpetVEGiYNTVLLAIGRDSCTRKIglEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILDG------KPELTPVA 499
Cdd:PRK13512 224 SGK----VEH-YDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIITShyrhvdLPASVPLA 295
|
170
....*....|....*.
gi 510120858 500 I---QAGKLLARRLFG 512
Cdd:PRK13512 296 WgahRAASIVAEQIAG 311
|
|
| GRX_PICOT_like |
cd03028 |
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ... |
70-155 |
5.58e-09 |
|
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: 53.65 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 70 DLIEGNRVMIFSKSY-----CPHSTRVKELFSSLGVVY---NILEldqvDDgaSVQEVLTEISNQKTVPNIFVNKVHVGG 141
Cdd:cd03028 3 KLIKENPVVLFMKGTpeeprCGFSRKVVQILNQLGVDFgtfDILE----DE--EVRQGLKEYSNWPTFPQLYVNGELVGG 76
|
90
....*....|....
gi 510120858 142 CDRTFQAHQNGLLQ 155
Cdd:cd03028 77 CDIVKEMHESGELQ 90
|
|
| GRX_hybridPRX5 |
cd03029 |
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ... |
77-143 |
1.41e-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: 49.05 E-value: 1.41e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510120858 77 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVlteiSNQKTVPNIFVNKVHVGGCD 143
Cdd:cd03029 3 VSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRAV----TGAMTVPQVFIDGELIGGSD 65
|
|
| GRX_DEP |
cd03027 |
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ... |
76-141 |
5.77e-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: 5.77e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510120858 76 RVMIFSKSYCPHSTRVKELFSSLGVVYniLELDqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGG 141
Cdd:cd03027 2 RVTIYSRLGCEDCTAVRLFLREKGLPY--VEIN-IDIFPERKAELEERTGSSVVPQIFFNEKLVGG 64
|
|
| grxA |
PRK11200 |
glutaredoxin 1; Provisional |
77-149 |
7.29e-06 |
|
glutaredoxin 1; Provisional
Pssm-ID: 183036 [Multi-domain] Cd Length: 85 Bit Score: 44.64 E-value: 7.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510120858 77 VMIFSKSYCPHSTRVKELFSSLGVV---YNILELDQVDDGASVQEVLTEISNQ-KTVPNIFVNKVHVGGCDRtFQAH 149
Cdd:PRK11200 3 VVIFGRPGCPYCVRAKELAEKLSEErddFDYRYVDIHAEGISKADLEKTVGKPvETVPQIFVDQKHIGGCTD-FEAY 78
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
348-508 |
1.73e-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: 47.82 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 348 VVGASYVGLECAGFLAGLG-LDVTVMVRsvllRGFDqEM---AEKVgSYLEQQGVKFQ-----RKF--------TPILVQ 410
Cdd:COG0493 260 VIGGGNTAMDCARTALRLGaESVTIVYR----RTRE-EMpasKEEV-EEALEEGVEFLflvapVEIigdengrvTGLECV 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 411 QLEKGLP---GKLKVVAKstEGPE-TVEGiyNTVLLAIGRDSCTRKIgLEKIGVKINeKNGKIPVNDVE-QTNVPHVYAI 485
Cdd:COG0493 334 RMELGEPdesGRRRPVPI--EGSEfTLPA--DLVILAIGQTPDPSGL-EEELGLELD-KRGTIVVDEETyQTSLPGVFAG 407
|
170 180
....*....|....*....|...
gi 510120858 486 GDILDGkPELTPVAIQAGKLLAR 508
Cdd:COG0493 408 GDAVRG-PSLVVWAIAEGRKAAR 429
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
311-510 |
3.30e-05 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 46.52 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 311 VIATGE-RPRYLGIQGDKEYCITS--DDLFS-----LPYCP---------GCTLVVGASYVGLECAGFLAGLGLDVTVMV 373
Cdd:PRK12770 123 LIATGTwKSRKLGIPGEDLPGVYSalEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAALEAVLLGAEKVYLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 374 -RsvllRGFDQEMAekvGSY----LEQQGVKFQRKFTPILVQQlEKGLPG----KLKVVAKSTEG---PETVEGI----- 436
Cdd:PRK12770 203 yR----RTINEAPA---GKYeierLIARGVEFLELVTPVRIIG-EGRVEGvelaKMRLGEPDESGrprPVPIPGSefvle 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510120858 437 YNTVLLAIGrDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDILDGkPELTPVAIQAGKLLARRL 510
Cdd:PRK12770 275 ADTVVFAIG-EIPTPPFAKECLGIELN-RKGEIVVDEKHMTSREGVFAAGDVVTG-PSKIGKAIKSGLRAAQSI 345
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
299-487 |
4.69e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 46.65 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 299 KGQETFYtaSKFVIATGERPRYLGIQG-DKEYCI---TSDDLFSLPYCPGCT---LVVGASYVGLECAGFLAGLGLDVTV 371
Cdd:PRK14989 96 AGRTVFY--DKLIMATGSYPWIPPIKGsETQDCFvyrTIEDLNAIEACARRSkrgAVVGGGLLGLEAAGALKNLGVETHV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 372 MVRSVLLRG--FDQEMAEKVGSYLEQQGVKFQ-RKFTPILVQQLEKGlpGKLKVVAKSTEgPETVEGIYNTVLLAigRDS 448
Cdd:PRK14989 174 IEFAPMLMAeqLDQMGGEQLRRKIESMGVRVHtSKNTLEIVQEGVEA--RKTMRFADGSE-LEVDFIVFSTGIRP--QDK 248
|
170 180 190
....*....|....*....|....*....|....*....
gi 510120858 449 CTRKIGLEkIGvkineKNGKIPVNDVEQTNVPHVYAIGD 487
Cdd:PRK14989 249 LATQCGLA-VA-----PRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
311-507 |
9.20e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 45.56 E-value: 9.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 311 VIATG-ERPRYLGIQGDK--------EYcITSDDLFSLPYCPGC---TLVVGASYVGLECAGFLAGLG-LDVTVMVRsvl 377
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDF-LTRVNQAVADYDLPVgkrVVVIGGGNTAMDAARTAKRLGaESVTIVYR--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 378 lRGFDqEM---AEKVgSYLEQQGVKFQRKFTPILVQQLEKGLPG------KLKVVAKSTEGPETVEGIY-----NTVLLA 443
Cdd:PRK11749 306 -RGRE-EMpasEEEV-EHAKEEGVEFEWLAAPVEILGDEGRVTGvefvrmELGEPDASGRRRVPIEGSEftlpaDLVIKA 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510120858 444 IGRDSCTRKIGLEKiGVKINEKNGKIPVNDVEQTNVPHVYAIGDILDGkPELTPVAIQAGKLLA 507
Cdd:PRK11749 383 IGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTG-AATVVWAVGDGKDAA 444
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
300-490 |
2.60e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 43.51 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 300 GQETFYTASKFVIATGERPRYLGIQGDKEY-------CITSDDLFslpYCPGCTLVVGASYVGLECAGFLAGLGLDVTVM 372
Cdd:PRK10262 99 GDSGEYTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 373 VRSVLLRGfDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKGLPGkLKVvaKSTEGPETVEGI-YNTVLLAIGRDSCTr 451
Cdd:PRK10262 176 HRRDGFRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTG-VRL--RDTQNSDNIESLdVAGLFVAIGHSPNT- 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 510120858 452 kiglEKIGVKINEKNGKIPVN-----DVEQTNVPHVYAIGDILD 490
Cdd:PRK10262 251 ----AIFEGQLELENGYIKVQsgihgNATQTSIPGVFAAGDVMD 290
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
269-512 |
3.43e-04 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 43.37 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 269 YRVTLREKgvTYVNSFGefVDLHKIKAtnkKGQEtfYTASKFVIATGERPRYLGIQGDkEYCITsddLFSLPYCPGC--- 345
Cdd:PRK04965 71 FNLRLFPH--TWVTDID--AEAQVVKS---QGNQ--WQYDKLVLATGASAFVPPIPGR-ELMLT---LNSQQEYRAAetq 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 346 ------TLVVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFdqeMAEKVGSYLE----QQGVKFQRKFTpilVQQLEK 414
Cdd:PRK04965 138 lrdaqrVLVVGGGLIGTELAMDLCRAGKAVTLVDNaASLLASL---MPPEVSSRLQhrltEMGVHLLLKSQ---LQGLEK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 415 GLPGklkVVAKSTEGpETVEgiYNTVLLAIGRDSCT---RKIGLEKigvkinekNGKIPVNDVEQTNVPHVYAIGDI--L 489
Cdd:PRK04965 212 TDSG---IRATLDSG-RSIE--VDAVIAAAGLRPNTalaRRAGLAV--------NRGIVVDSYLQTSAPDIYALGDCaeI 277
|
250 260
....*....|....*....|....*
gi 510120858 490 DGK--PELTPVAIQAgKLLARRLFG 512
Cdd:PRK04965 278 NGQvlPFLQPIQLSA-MALAKNLLG 301
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
309-510 |
3.44e-04 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 43.60 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 309 KFVIATGERPRYLGIQGDKEY-------------------CITSDDLFSLPYCPGCTL----VVGASYVGLECAGFLAGL 365
Cdd:PTZ00318 116 KLVVAHGARPNTFNIPGVEERafflkevnhargirkrivqCIERASLPTTSVEERKRLlhfvVVGGGPTGVEFAAELADF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 366 GLD--------------VTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEkglpgklkVVAKSTEGP 430
Cdd:PTZ00318 196 FRDdvrnlnpelveeckVTVLeAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKE--------VVLKDGEVI 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 431 ETVEGIYNTvllAIGRDSCTRKIGLEKigvkinEKNGKIPVND-VEQTNVPHVYAIGDILDGK----PELTPVAIQAGKL 505
Cdd:PTZ00318 268 PTGLVVWST---GVGPGPLTKQLKVDK------TSRGRISVDDhLRVKPIPNVFALGDCAANEerplPTLAQVASQQGVY 338
|
....*
gi 510120858 506 LARRL 510
Cdd:PTZ00318 339 LAKEF 343
|
|
| NrdH |
cd02976 |
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
76-141 |
4.97e-04 |
|
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: 39.13 E-value: 4.97e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510120858 76 RVMIFSKSYCPHSTRVKELFSSLGVVYNilELDqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGG 141
Cdd:cd02976 1 EVTVYTKPDCPYCKATKRFLDERGIPFE--EVD-VDEDPEALEELKKLNGYRSVPVVVIGDEHLSG 63
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
305-486 |
9.61e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 41.83 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 305 YTASKFVIATGE--RPRYLGIqgdKEYCITSDDLFSL-PYCPGCTLVVGASYVGLECAGFLAGLGLDVTVmvrsvLLRGF 381
Cdd:pfam13738 117 YQARYVIIATGEfdFPNKLGV---PELPKHYSYVKDFhPYAGQKVVVIGGYNSAVDAALELVRKGARVTV-----LYRGS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 382 DQEMAEKVGSYleqqGVKfqrkftPILVQQLEKGL-PGKLKVVAKS---------------TEGPETVEgIYNTVLLAIG 445
Cdd:pfam13738 189 EWEDRDSDPSY----SLS------PDTLNRLEELVkNGKIKAHFNAevkeitevdvsykvhTEDGRKVT-SNDDPILATG 257
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510120858 446 RDSCTRKigLEKIGVKINEkNGKIPVND-VEQTNVPHVYAIG 486
Cdd:pfam13738 258 YHPDLSF--LKKGLFELDE-DGRPVLTEeTESTNVPGLFLAG 296
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
348-508 |
2.80e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 40.77 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 348 VVGASYVGLECAGFLAGLGLDVTVMVRsvllRGfDQEM---AEKVGsYLEQQGVKFQRKFTPILVQQLEKGLPGKLKVV- 423
Cdd:PRK12831 286 VVGGGNVAMDAARTALRLGAEVHIVYR----RS-EEELparVEEVH-HAKEEGVIFDLLTNPVEILGDENGWVKGMKCIk 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 424 -------AKSTEGPETVEGIY-----NTVLLAIGRdSCTRKIGLEKIGVKINeKNGKIPVN-DVEQTNVPHVYAIGDILD 490
Cdd:PRK12831 360 melgepdASGRRRPVEIEGSEfvlevDTVIMSLGT-SPNPLISSTTKGLKIN-KRGCIVADeETGLTSKEGVFAGGDAVT 437
|
170
....*....|....*....
gi 510120858 491 GkpELTPV-AIQAGKLLAR 508
Cdd:PRK12831 438 G--AATVIlAMGAGKKAAK 454
|
|
| GRXA |
TIGR02183 |
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
77-142 |
3.49e-03 |
|
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: 37.11 E-value: 3.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 77 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVD---DGASVQEVLTEISNQ-KTVPNIFVNKVHVGGC 142
Cdd:TIGR02183 2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEFRYIDihaEGISKADLEKTVGKPvETVPQIFVDEKHVGGC 71
|
|
| PTZ00062 |
PTZ00062 |
glutaredoxin; Provisional |
71-161 |
5.22e-03 |
|
glutaredoxin; Provisional
Pssm-ID: 240250 [Multi-domain] Cd Length: 204 Bit Score: 38.62 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510120858 71 LIEGNRVMIFSKS-----YCPHSTRVKELFSSLGV---VYNILElDQvddgaSVQEVLTEISNQKTVPNIFVNKVHVGGC 142
Cdd:PTZ00062 109 LIRNHKILLFMKGsktfpFCRFSNAVVNMLNSSGVkyeTYNIFE-DP-----DLREELKVYSNWPTYPQLYVNGELIGGH 182
|
90
....*....|....*....
gi 510120858 143 DRTFQAHQNGLLQKLLQDD 161
Cdd:PTZ00062 183 DIIKELYESNSLRKVIPDD 201
|
|
| PHA03050 |
PHA03050 |
glutaredoxin; Provisional |
72-141 |
8.04e-03 |
|
glutaredoxin; Provisional
Pssm-ID: 165343 [Multi-domain] Cd Length: 108 Bit Score: 36.53 E-value: 8.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510120858 72 IEGNRVMIFSKSYCPHSTRVKELFSSLGV---VYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGG 141
Cdd:PHA03050 10 LANNKVTIFVKFTCPFCRNALDILNKFSFkrgAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGG 82
|
|
| |
