|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
127-615 |
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 110735449 127 HDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEY 206
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 207 NQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETFYTASKFVIATGERPRYLGI 286
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 287 QGDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGFDQEMAEKVGSYLEQQGVKFQRK 366
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 367 FTPILVQQLEKglpgklKVVAKSTEGPETVEGIYNTVLLAIGRDSCTRKIGLEKIGVKINEKNGKIPVNDVEQTNVPHVY 446
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 447 AIGDILDGKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLE 526
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 527 WTVAGRDN-NTCYAKIICNKFDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSG 605
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 110735449 606 LDITQKGCUG 615
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
124-615 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 525.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 124 DSAHDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVVPSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQ-DAKKY 202
Cdd:PTZ00052 1 HLTFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 203 GWEYNQqvKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIkATNKKGQETFYTASKFVIATGERPR 282
Cdd:PTZ00052 81 GWKTSS--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 283 YL-GIQGDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGFDQEMAEKVGSYLEQQGV 361
Cdd:PTZ00052 158 IPeDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 362 KFQRKFTPILVQQLEKglpgKLKVV--AKSTEgpetvegIYNTVLLAIGRDSCTRKIGLEKIGVKINEKNGKIPVNDVeq 439
Cdd:PTZ00052 238 LFLEGVVPINIEKMDD----KIKVLfsDGTTE-------LFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPNDC-- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 440 TNVPHVYAIGDILDGKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYH 519
Cdd:PTZ00052 305 TNIPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 520 TLFWPLEWTVAGRD--------------NNTCYAKIICNKFDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTI 585
Cdd:PTZ00052 385 QEFNTLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMI 464
|
490 500 510
....*....|....*....|....*....|
gi 110735449 586 GIHPTCGEVFTTLEITKSSGLDITQKGCUG 615
Cdd:PTZ00052 465 GIHPTDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
144-598 |
1.30e-129 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 387.98 E-value: 1.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 144 AKEAANLGKKVMVLDfvvpspqgtTWGLGGTCVNVGCIPKKLMHQAALLGHALQD-AKKYGWEYNQQvKHNWEAMTEAIQ 222
Cdd:PRK06116 20 ANRAAMYGAKVALIE---------AKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTEN-KFDWAKLIANRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 223 SHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKgqetfYTASKFVIATGERPRYLGIQGdKEYCITSDDLFSL 302
Cdd:PRK06116 90 AYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIPDIPG-AEYGITSDGFFAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 303 PYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVL-LRGFDQEMAEKVGSYLEQQGVKFQRKFTPilvQQLEKGLPG 381
Cdd:PRK06116 164 EELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDApLRGFDPDIRETLVEEMEKKGIRLHTNAVP---KAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 382 KLKVvakSTEGPETVEgiYNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDIlDGKPELTPV 461
Cdd:PRK06116 241 SLTL---TLEDGETLT--VDCLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVPGIYAVGDV-TGRVELTPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 462 AIQAGKLLARRLF-GVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLEWTVAGRDNnTCYAK 540
Cdd:PRK06116 314 AIAAGRRLSERLFnNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 110735449 541 IICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 598
Cdd:PRK06116 393 LVVVG-KEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
143-598 |
4.39e-119 |
|
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: 361.33 E-value: 4.39e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 143 CAKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYnQQVKHNWEAMTEAIQ 222
Cdd:COG1249 18 AAIRAAQLGLKVALVE------KGR---LGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISA-GAPSVDWAALMARKD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 223 SHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATnkkGQETfYTASKFVIATGERPRYLGIQG-DKEYCITSDDLFS 301
Cdd:COG1249 88 KVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVT---GGET-LTADHIVIATGSRPRVPPIPGlDEVRVLTSDEALE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 302 LPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKFQRKFTpilVQQLEKGlP 380
Cdd:COG1249 164 LEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDILTGAK---VTSVEKT-G 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 381 GKLKVVAKSTEGPETVEGiyNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILdGKPELTP 460
Cdd:COG1249 240 DGVTVTLEDGGGEEAVEA--DKVLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVPGIYAIGDVT-GGPQLAH 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 461 VAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFWPLEWTVAGRDNnTCYAK 540
Cdd:COG1249 316 VASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEARE--AGIDVKVGKFPFAANGRALALGET-EGFVK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 110735449 541 IICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 598
Cdd:COG1249 393 LIADA-ETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
144-598 |
6.88e-101 |
|
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: 314.09 E-value: 6.88e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 144 AKEAANLGKKVMVLDfvvpspqgtTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQS 223
Cdd:TIGR01421 18 ARRAAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKRDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 224 HIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKgqetfYTASKFVIATGERPRYL-GIQGdKEYCITSDDLFSL 302
Cdd:TIGR01421 89 YVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIPG-AELGTDSDGFFAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 303 PYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPIlvqQLEKGLPG 381
Cdd:TIGR01421 163 EELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPV---KVEKTVEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 382 KLKV-VAKSTEGPETVEgiyntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILdGKPELTP 460
Cdd:TIGR01421 240 KLVIhFEDGKSIDDVDE-----LIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIYALGDVV-GKVELTP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 461 VAIQAGKLLARRLF-GVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEVYHTLFWPLEWTVaGRDNNTCYA 539
Cdd:TIGR01421 313 VAIAAGRKLSERLFnGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAM-TSEKQKCRM 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 540 KIIC-NKfdNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 598
Cdd:TIGR01421 392 KLVCaGK--EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
144-598 |
9.26e-98 |
|
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: 305.97 E-value: 9.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 144 AKEAANLGKKVMV--LDFVvpspqgttwglGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEyNQQVKHNWEAMTEAI 221
Cdd:TIGR01424 18 ARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWT-VGKARFDWKKLLAAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 222 QSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQetfYTASKFVIATGERPRYLGIQGdKEYCITSDDLFS 301
Cdd:TIGR01424 86 DQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKPALPG-HELGITSNEAFH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 302 LPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFDQEMAEKVGSYLEQQGVKFQRKftpILVQQLEKGLP 380
Cdd:TIGR01424 162 LPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRILPE---DSITSISKDDD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 381 GKLKVVAKSTEgpetvEGIYNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILDgKPELTP 460
Cdd:TIGR01424 239 GRLKATLSKHE-----EIVADVVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTPSIYAVGDVTD-RINLTP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 461 VAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFWPLEWTVAGRDNNtCYAK 540
Cdd:TIGR01424 312 VAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARR--KFGDIEVYRAEFRPMKATFSGRQEK-TLMK 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 110735449 541 IICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 598
Cdd:TIGR01424 389 LVVDA-KDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
147-598 |
5.04e-95 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 302.57 E-value: 5.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 147 AANLGKKVMV--LDFVVPSPQgTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQSH 224
Cdd:PLN02546 98 ASNFGASAAVceLPFATISSD-TLGGVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 225 IGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKkgqetFYTASKFVIATGERPRYLGIQGdKEYCITSDDLFSLPY 304
Cdd:PLN02546 177 LQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGK-----LYTARNILIAVGGRPFIPDIPG-IEHAIDSDAALDLPS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 305 CPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSV-LLRGFDQEMAEKVGSYLEQQGVKFQRKFTPilvQQLEKGLPGKL 383
Cdd:PLN02546 251 KPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAEQMSLRGIEFHTEESP---QAIIKSADGSL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 384 KVvaKSTEGpeTVEGiYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDILDgKPELTPVAI 463
Cdd:PLN02546 328 SL--KTNKG--TVEG-FSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVPSIWAVGDVTD-RINLTPVAL 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 464 QAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKkeNLEVYHTLFWPLEWTVAGRDNNTCYAKIIC 543
Cdd:PLN02546 401 MEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYG--DVDVFTANFRPLKATLSGLPDRVFMKLIVC 478
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 110735449 544 NKfdNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 598
Cdd:PLN02546 479 AK--TNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTM 531
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
123-598 |
1.60e-94 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 299.42 E-value: 1.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 123 DDSAHDYDLIIIGGGSGGLSCAKEAANLGKKVMVLDFVV-PSPQGTTWGLGGTCVNVGCIPKKLMHQAALLGHALQDAKK 201
Cdd:PLN02507 20 NATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICELPFhPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 202 YGWEYNQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETFYTASKFVIATGERP 281
Cdd:PLN02507 100 YGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 282 RYLGIQGdKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVL-LRGFDQEMAEKVGSYLEQQG 360
Cdd:PLN02507 180 QRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELpLRGFDDEMRAVVARNLEGRG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 361 VKFQRKFTpilVQQLEKgLPGKLKVVAKSTEgpetvEGIYNTVLLAIGRDSCTRKIGLEKIGVKInEKNGKIPVNDVEQT 440
Cdd:PLN02507 259 INLHPRTN---LTQLTK-TEGGIKVITDHGE-----EFVADVVLFATGRAPNTKRLNLEAVGVEL-DKAGAVKVDEYSRT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 441 NVPHVYAIGDILDgKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLeVYHT 520
Cdd:PLN02507 329 NIPSIWAIGDVTN-RINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGDIL-VFTS 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110735449 521 LFWPLEWTVAGRDNNTCYAKIICNKFDneRVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 598
Cdd:PLN02507 407 SFNPMKNTISGRQEKTVMKLIVDAETD--KVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTM 482
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
143-594 |
1.30e-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: 269.51 E-value: 1.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 143 CAKEAANLGKKVMVldfvVPSPQgttwgLGGTCVNVGCIPKK-LMHQAALLgHALQDAKKYGWEYNQqVKHNWEAMTEAI 221
Cdd:TIGR01350 16 AAIRAAQLGLKVAL----VEKEY-----LGGTCLNVGCIPTKaLLHSAEVY-DEIKHAKDLGIEVEN-VSVDWEKMQKRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 222 QSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETfYTASKFVIATGERPRYL--GIQGDKEYCITSDDL 299
Cdd:TIGR01350 85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEET-LEAKNIIIATGSRPRSLpgPFDFDGKVVITSTGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 300 FSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTV---MVRsvLLRGFDQEMAEKVGSYLEQQGVKFqrkFTPILVQQLE 376
Cdd:TIGR01350 164 LNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTViemLDR--ILPGEDAEVSKVLQKALKKKGVKI---LTNTKVTAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 377 KGlpGKLKVVAKSTEGPETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILdGKP 456
Cdd:TIGR01350 239 KN--DDQVTYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDE-RGRIVVDEYMRTNVPGIYAIGDVI-GGP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 457 ELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAiemyKKENLEVYHTLFwPLewTVAGR---- 532
Cdd:TIGR01350 313 MLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF-PF--AANGKalal 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110735449 533 DNNTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 594
Cdd:TIGR01350 386 GETDGFVKIIADK-KTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
171-598 |
1.17e-75 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 251.84 E-value: 1.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 171 LGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGweYNQQVKHNWEAMTEAIQSHIGSLNWGYRVTLREKGVTYVNSFGEF 250
Cdd:PTZ00058 82 LGGTCVNVGCVPKKIMFNAASIHDILENSRHYG--FDTQFSFNLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 251 VDLHKIKATNKKGQETFY------------------------TASKFVIATGERPRYLGIQGdKEYCITSDDLFSLPYcP 306
Cdd:PTZ00058 160 LSENQVLIKKVSQVDGEAdesdddevtivsagvsqlddgqviEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-A 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 307 GCTLVVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKglPGKLKV 385
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKE--KNLTIY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 386 VAKSTEgpetvEGIYNTVLLAIGRDSCTRKIGLEkiGVKINEKNGKIPVNDVEQTNVPHVYAIGDILDGKP--------- 456
Cdd:PTZ00058 316 LSDGRK-----YEHFDYVIYCVGRSPNTEDLNLK--ALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnl 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 457 ------------------------ELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKK 512
Cdd:PTZ00058 389 lklyneepylkkkentsgesyynvQLTPVAINAGRLLADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGK 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 513 ENLEVYHTLFWPLEWTV---AGRDNNTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHP 589
Cdd:PTZ00058 469 ENVKIYESRFTNLFFSVydmDPAQKEKTYLKLVCVG-KEELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHP 547
|
....*....
gi 110735449 590 TCGEVFTTL 598
Cdd:PTZ00058 548 TAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
147-593 |
1.64e-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: 1.64e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 147 AANL-GKKVMVLDfvVPSPQGTTW--GLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQ-VKHNWEAMTEAIQ 222
Cdd:TIGR01423 22 AATLyKKRVAVVD--VQTHHGPPFyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFDRSsVKANWKALIAAKN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 223 SHIGSLNWGYRVTLRE-KGVTYVNSFGEFVDLHKIKA-----TNKKGQETFyTASKFVIATGERPRYLGIQGDkEYCITS 296
Cdd:TIGR01423 100 KAVLDINKSYEGMFADtEGLTFFLGWGALEDKNVVLVresadPKSAVKERL-QAEHILLATGSWPQMLGIPGI-EHCISS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 297 DDLFSLPYCPGCTLVVGASYVGLECAGFLAG---LGLDVTVMVR-SVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPilv 372
Cdd:TIGR01423 178 NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTKQLRANGINIMTNENP--- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 373 QQLEKGLPGKLKVVAKSTEgpetvEGIYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDIL 452
Cdd:TIGR01423 255 AKVTLNADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELT-KKGAIQVDEFSRTNVPNIYAIGDVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 453 DgKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKenLEVYHTLFWPLEWTVAGR 532
Cdd:TIGR01423 329 D-RVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKFEK--VAVYESSFTPLMHNISGS 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110735449 533 DNNTCYAKIICNKFDNErVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGE 593
Cdd:TIGR01423 406 KYKKFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
143-594 |
1.09e-69 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 232.73 E-value: 1.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 143 CAKEAANLGKKVMVL--DFvvpspqgttwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYnQQVKHNWEAMTEA 220
Cdd:PRK06416 19 AAIRAAQLGLKVAIVekEK-----------LGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKA-ENVGIDFKKVQEW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 221 IQSHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETfYTASKFVIATGERPRYL-GIQGDKEYCITSDDL 299
Cdd:PRK06416 87 KNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQT-YTAKNIILATGSRPRELpGIEIDGRVIWTSDEA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 300 FSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTV---MVRsvLLRGFDQEMAEKVGSYLEQQGVKFqrkFTPILVQQLE 376
Cdd:PRK06416 166 LNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveaLPR--ILPGEDKEISKLAERALKKRGIKI---KTGAKAKKVE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 377 KGLPGkLKVVAKSTEGPETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEknGKIPVNDVEQTNVPHVYAIGDILdGKP 456
Cdd:PRK06416 241 QTDDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKTDR--GFIEVDEQLRTNVPNIYAIGDIV-GGP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 457 ELTPVAIQAGKLLARRLFGVSLEkCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFwplewtvAGR---- 532
Cdd:PRK06416 315 MLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKE--EGFDVKVVKFPF-------AGNgkal 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110735449 533 --DNNTCYAKIICNKFDNErVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 594
Cdd:PRK06416 385 alGETDGFVKLIFDKKDGE-VLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
128-597 |
8.97e-67 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 225.06 E-value: 8.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 128 DYDLIIIGGGSGGLSCAKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYn 207
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 208 QQVKHNWEAMTEAIQSHIGSLNWGYRVTLREK-GVTYVNSFGEFVDLHKIKATnkkgqETFYTASKFVIATGER-PRYLG 285
Cdd:PRK06292 73 DGPKIDFKKVMARVRRERDRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEVN-----GERIEAKNIVIATGSRvPPIPG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 286 I-QGDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQgVKF 363
Cdd:PRK06292 148 VwLILGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILSKE-FKI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 364 qrkFTPILVQQLEKGlpGKLKVVAKSTEG-PETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNV 442
Cdd:PRK06292 227 ---KLGAKVTSVEKS--GDEKVEELEKGGkTETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQTSV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 443 PHVYAIGDIlDGKPELTPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKenlevYHTLF 522
Cdd:PRK06292 299 PGIYAAGDV-NGKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGID-----YVVGE 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110735449 523 WPLEWTVAGR-DNNTCYA-KIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLT-KQLLdDTIGIHPTCGEVFTT 597
Cdd:PRK06292 373 VPFEAQGRARvMGKNDGFvKVYADK-KTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTvEDLL-RMPFYHPTLSEGLRT 448
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
144-615 |
2.13e-63 |
|
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: 216.13 E-value: 2.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 144 AKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGweYNQQVKHNWEAMTEAIQS 223
Cdd:TIGR02053 16 AIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGG--LAATVAVDFGELLEGKRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 224 HIGSL-NWGYRVTLREKGVTYVNSFGEFVDLHKIKAtnKKGQETFYtASKFVIATGERPRYLGIQGDKE--YcITSDDLF 300
Cdd:TIGR02053 85 VVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV--DLGREVRG-AKRFLIATGARPAIPPIPGLKEagY-LTSEEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 301 SLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKFQrkfTPILVQQLEKGL 379
Cdd:TIGR02053 161 ALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVV---TSAQVKAVSVRG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 380 PGKLKVVAKStEGPETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDGkPELT 459
Cdd:TIGR02053 238 GGKIITVEKP-GGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDE-RGGILVDETLRTSNPGIYAAGDVTGG-LQLE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 460 PVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIemykkENLEVYHTLFWPLEWTVAGRDN--NTC 537
Cdd:TIGR02053 313 YVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQ-----KAGIECDCRTLPLTNVPRARINrdTRG 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110735449 538 YAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTLEITKSSglDITQKGCUG 615
Cdd:TIGR02053 388 FIKLVAEP-GTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGLKLAAQTFYR--DVSKLSCCA 462
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
143-598 |
2.86e-55 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 194.27 E-value: 2.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 143 CAKEAANLGKKVMVLdfvvpspqGTTWgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQ 222
Cdd:PRK06370 20 LAARAAGLGMKVALI--------ERGL-LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAVMARKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 223 SHIGSLNWGYRVTLRE-KGVTYVNSFGEFVDLHKIKATNKKgqetfYTASKFVIATGERPRYLGIQG--DKEYcITSDDL 299
Cdd:PRK06370 91 RIRARSRHGSEQWLRGlEGVDVFRGHARFESPNTVRVGGET-----LRAKRIFINTGARAAIPPIPGldEVGY-LTNETI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 300 FSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSV-LLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKG 378
Cdd:PRK06370 165 FSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPrLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGDG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 379 lpgkLKVVAKSTEGPETVEGiyNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDIlDGKPEL 458
Cdd:PRK06370 245 ----IAVGLDCNGGAPEITG--SHILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLRTTNPGIYAAGDC-NGRGAF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 459 TPVAIQAGKLLARRLFGVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLFwplewTVAGR----DN 534
Cdd:PRK06370 317 THTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARK--SGRRVLVGTRPM-----TRVGRavekGE 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110735449 535 NTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 598
Cdd:PRK06370 390 TQGFMKVVVDA-DTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
143-466 |
3.60e-53 |
|
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: 184.06 E-value: 3.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 143 CAKEAANLGKKVMVLdfvvpspqgttwGLGGTCVNVGCIPKKLMHQAALLGHALqdakkygweynqqvkHNWEAMTEAIQ 222
Cdd:pfam07992 15 AALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAAEAPEIA---------------SLWADLYKRKE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 223 SHIGSLNWGYRVTLREKGVTYVNSFGEFVDLHKikatnKKGQETFYTASKFVIATGERPRYLGIQGDKEYC------ITS 296
Cdd:pfam07992 68 EVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEEL-----VDGDGETITYDRLVIATGARPRLPPIPGVELNVgflvrtLDS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 297 DDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKFQrkfTPILVQQL 375
Cdd:pfam07992 143 AEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGVEVR---LGTSVKEI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 376 EkGLPGKLKVVaksTEGPETVEgiYNTVLLAIGRDSCTRkiGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDGK 455
Cdd:pfam07992 220 I-GDGDGVEVI---LKDGTEID--ADLVVVAIGRRPNTE--LLEAAGLELDE-RGGIVVDEYLRTSVPGIYAAGDCRVGG 290
|
330
....*....|.
gi 110735449 456 PELTPVAIQAG 466
Cdd:pfam07992 291 PELAQNAVAQG 301
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
147-594 |
5.45e-44 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 163.56 E-value: 5.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 147 AANLGKKVMVLDfVVPSPQGTTwGLGGTCVNVGCIPKK-LMHQAALLGHALQDAKKYGWEYNQqVKHNWEAMTEAIQSHI 225
Cdd:PRK06327 23 AAQLGLKVACIE-AWKNPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGIHVDG-VKIDVAKMIARKDKVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 226 GSLNWGYRVTLREKGVTYVNSFGEFV----DLHKIKATNKKGQETfyTASKFVIATGERPRYL-GIQGDKEYCITSDDLF 300
Cdd:PRK06327 100 KKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDETVI--TAKHVIIATGSEPRHLpGVPFDNKIILDNTGAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 301 SLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFQrkfTPILVQQLEKGl 379
Cdd:PRK06327 178 NFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTKQGLDIH---LGVKIGEIKTG- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 380 pGKLKVVAKSTEGPETVEGIYNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILdGKPELT 459
Cdd:PRK06327 254 -GKGVSVAYTDADGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDE-RGFIPVDDHCRTNVPNVYAIGDVV-RGPMLA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 460 PVAIQAGKLLARRLFGVSlEKCDYINIPTTVFTPLEYGCCGLSEEKAiemyKKENLEVYHTLFwPleWTVAGR----DNN 535
Cdd:PRK06327 331 HKAEEEGVAVAERIAGQK-GHIDYNTIPWVIYTSPEIAWVGKTEQQL----KAEGVEYKAGKF-P--FMANGRalamGEP 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 110735449 536 TCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEV 594
Cdd:PRK06327 403 DGFVKIIADA-KTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSEV 460
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
151-594 |
4.40e-42 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 157.81 E-value: 4.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 151 GKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGweYNQQVKH-NWEAMTEAIQSHIGSLN 229
Cdd:PRK07846 22 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 230 WG---YRVtLREKGVTYVNSFGEFVDLHKIKAtnkkGQETFYTASKFVIATGERPRYLGIQGDKE--YcITSDDLFSLPY 304
Cdd:PRK07846 91 AGgeeYRG-RDTPNIDVYRGHARFIGPKTLRT----GDGEEITADQVVIAAGSRPVIPPVIADSGvrY-HTSDTIMRLPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 305 CPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKvgsYLEQQGVKFQRKF--TPILVQQLEKGlpg 381
Cdd:PRK07846 165 LPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISER---FTELASKRWDVRLgrNVVGVSQDGSG--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 382 klkvVAKSTEGPETVEGiyNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDgKPELTPV 461
Cdd:PRK07846 239 ----VTLRLDDGSTVEA--DVLLVATGRVPNGDLLDAAAAGVDVDE-DGRVVVDEYQRTSAEGVFALGDVSS-PYQLKHV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 462 AIQAGKLLARRLF-GVSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYHTLF------WPLEWTvagrdn 534
Cdd:PRK07846 311 ANHEARVVQHNLLhPDDLIASDHRFVPAAVFTHPQIASVGLTENEARA--AGLDITVKVQNYgdvaygWAMEDT------ 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110735449 535 nTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLT-KQLLDDTIGIHPTCGEV 594
Cdd:PRK07846 383 -TGFVKLIADR-DTGRLLGAHIIGPQASTLIQPLIQAMSFGLDaREMARGQYWIHPALPEV 441
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
144-593 |
1.51e-38 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 148.00 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 144 AKEAANLGKKVMVLDfvvpspqgTTWGLGGTCVNVGCIPKKLMHQAALlghalqdakkYGWEYNQ-------QVKHN--W 214
Cdd:PRK05249 21 AMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVL----------RLIGFNQnplyssyRVKLRitF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 215 EAMTEAIQSHIGSlnwgyRVTLREK-----GVTYVNSFGEFVDLHKIKATNKKGQETFYTASKFVIATGERP-RYLGIQG 288
Cdd:PRK05249 83 ADLLARADHVINK-----QVEVRRGqyernRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPyRPPDVDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 289 DKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKF 367
Cdd:PRK05249 158 DHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLInTRDRLLSFLDDEISDALSYHLRDSGVTIRHNE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 368 TPILVQQLEKGL-----PGKlKVVAkstegpetvegiyNTVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNV 442
Cdd:PRK05249 238 EVEKVEGGDDGVivhlkSGK-KIKA-------------DCLLYANGRTGNTDGLNLENAGLEADSR-GQLKVNENYQTAV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 443 PHVYAIGDILdGKPELTPVAIQAGKLLARRLFGVSLEKcdYIN-IPTTVFTPLEYGCCGLSEEKAIEM---YkkenlEVY 518
Cdd:PRK05249 303 PHIYAVGDVI-GFPSLASASMDQGRIAAQHAVGEATAH--LIEdIPTGIYTIPEISSVGKTEQELTAAkvpY-----EVG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 519 HTLFwplewtvagRDN--------NTCYAKIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPT 590
Cdd:PRK05249 375 RARF---------KELaraqiagdNVGMLKILFHR-ETLEILGVHCFGERATEIIHIGQAIMEQKGTIEYFVNTTFNYPT 444
|
...
gi 110735449 591 CGE 593
Cdd:PRK05249 445 MAE 447
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
486-598 |
3.87e-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: 3.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 486 IPTTVFTPLEYGCCGLSEEKAIEMYKKenLEVYHTLFWPLEWTVAGRDNNtCYAKIICNKfDNERVVGFHLLGPNAGEIT 565
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADR-ETGKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 110735449 566 QGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 598
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
165-594 |
5.83e-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: 5.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 165 QGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGweYNQQVKH-NWEAMTEAIQSH----IGSLNWGYRVTLREK 239
Cdd:TIGR03452 31 KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRVFGDridpIAAGGEDYRRGDETP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 240 GVTYVNSFGEFVDlhkiKATNKKGQETFYTASKFVIATGERPR---YLGIQGDKEYciTSDDLFSLPYCPGCTLVVGASY 316
Cdd:TIGR03452 106 NIDVYDGHARFVG----PRTLRTGDGEEITGDQIVIAAGSRPYippAIADSGVRYH--TNEDIMRLPELPESLVIVGGGY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 317 VGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKvgsYLEQQGVKF--QRKFTPILVQQLEKGlpgklkvVAKSTEGP 393
Cdd:TIGR03452 180 IAAEFAHVFSALGTRVTIVNRStKLLRHLDEDISDR---FTEIAKKKWdiRLGRNVTAVEQDGDG-------VTLTLDDG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 394 ETVEGiyNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDIldGKP-ELTPVAIQAGKLLARR 472
Cdd:TIGR03452 250 STVTA--DVLLVATGRVPNGDLLDAEAAGVEVDE-DGRIKVDEYGRTSARGVWALGDV--SSPyQLKHVANAEARVVKHN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 473 LFG-VSLEKCDYINIPTTVFTPLEYGCCGLSEEKAIEMYKKENLEV--YHTLF--WPLEWTvagrdnnTCYAKIICNKfD 547
Cdd:TIGR03452 325 LLHpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKIqnYGDVAygWAMEDT-------TGFCKLIADR-D 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 110735449 548 NERVVGFHLLGPNAGEITQGFAAAMKCGLT-KQLLDDTIGIHPTCGEV 594
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 ... |
39-120 |
5.32e-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: 5.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 39 RVMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQ 118
Cdd:cd03419 1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
|
..
gi 110735449 119 KL 120
Cdd:cd03419 81 KL 82
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
144-593 |
1.82e-33 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 132.95 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 144 AKEAANLGKKVMVLDfvvPSPQGttwgLGGTCVNVGCIPKKLMHQAAllghalqdakKYGWEYNQQVKHNweamtEAIQS 223
Cdd:PRK07251 19 AAKLASAGKKVALVE---ESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQVMATK-----NTVTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 224 HIGSLNWGyrvTLREKGVTYVNSFGEFVDLHKIKATNKKGQETFyTASKFVIATGERPRYLGIQG--DKEYCITSDDLFS 301
Cdd:PRK07251 77 RLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIEL-TAETIVINTGAVSNVLPIPGlaDSKHVYDSTGIQS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 302 LPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKglp 380
Cdd:PRK07251 153 LETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKNDGD--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 381 gklKVVAKSTEGPETvegiYNTVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDIlDGKPELTP 460
Cdd:PRK07251 230 ---QVLVVTEDETYR----FDALLYATGRKPNTEPLGLENTDIELTE-RGAIKVDDYCQTSVPGVFAVGDV-NGGPQFTY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 461 VAIQAGKLLARRLFGVS---LEkcDYINIPTTVFTPLEYGCCGLSEEKAIEM---YKKENLevyhtlfwPLEWTVAGRDN 534
Cdd:PRK07251 301 ISLDDFRIVFGYLTGDGsytLE--DRGNVPTTMFITPPLSQVGLTEKEAKEAglpYAVKEL--------LVAAMPRAHVN 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110735449 535 NTCYA--KIICNKfDNERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGE 593
Cdd:PRK07251 371 NDLRGafKVVVNT-ETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| GRX_euk |
TIGR02180 |
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ... |
40-121 |
8.00e-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: 120.81 E-value: 8.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 40 VMIFSKSYCPHSTRVKELFSSLGV-VYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQ 118
Cdd:TIGR02180 1 VVVFSKSYCPYCKKAKEILAKLNVkPYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKLA 80
|
...
gi 110735449 119 KLL 121
Cdd:TIGR02180 81 ELL 83
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
143-614 |
3.13e-32 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 131.43 E-value: 3.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 143 CAKEAANLGKKVMVLDfvvpspQGTtwgLGGTCVNVGCIPKKLMHQAALLGHALQDAKKYGWEYNQQVKHNWEAMTEAIQ 222
Cdd:PRK13748 113 AALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 223 SHIGSLnwgyRVTLREK------GVTYVNSFGEFVDLHKIKATNKKGQETFYTASKFVIATGERPRYLGIQGDKE--YCI 294
Cdd:PRK13748 184 ARVDEL----RHAKYEGildgnpAITVLHGEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPPIPGLKEtpYWT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 295 TSDDLFSlPYCPGCTLVVGASYVGLECAGFLAGLGLDVTVMVRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQ 374
Cdd:PRK13748 260 STEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVAH 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 375 LEKglpgklKVVAKSTEGpetvEGIYNTVLLAIGRDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDILDg 454
Cdd:PRK13748 339 VDG------EFVLTTGHG----ELRADKLLVATGRAPNTRSLALDAAGVTVN-AQGAIVIDQGMRTSVPHIYAAGDCTD- 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 455 KPELTPVAIQAGKLLARRLFGVSlEKCDYINIPTTVFTPLEYGCCGLSEEKAiemyKKENLEVyhtlfwplEWTVAGRDN 534
Cdd:PRK13748 407 QPQFVYVAAAAGTRAAINMTGGD-AALDLTAMPAVVFTDPQVATVGYSEAEA----HHDGIET--------DSRTLTLDN 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 535 ntcYAKIICNkFDNE------------RVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPT-------CGEVF 595
Cdd:PRK13748 474 ---VPRALAN-FDTRgfiklvieegsgRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPYLTmveglklAAQTF 549
|
490
....*....|....*....
gi 110735449 596 TTleitkssglDITQKGCU 614
Cdd:PRK13748 550 NK---------DVKQLSCC 559
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
172-598 |
5.39e-32 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 128.74 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 172 GGTCVNVGCIP-KKLMHqaallghalqDAKKYGweynqqvkhnweAMTEAIQ--SHIGSLnwgyrvtLREKG-------- 240
Cdd:NF040477 40 GGTCINIGCIPtKTLVH----------DAEQHQ------------DFSTAMQrkSSVVGF-------LRDKNyhnladld 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 241 -VTYVNSFGEFVDLHKIKATNKKGQETFYtASKFVIATGERPRYLGIQGDKEY--CITSDDLFSLPYCPGCTLVVGASYV 317
Cdd:NF040477 91 nVDVINGRAEFIDNHTLRVFQADGEQELR-GEKIFINTGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 318 GLECAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFqrkftpILVQQLEKGLPGKLKVVAKSTEGPETV 396
Cdd:NF040477 170 GVEFASMFARFGSKVTIFeAAELFLPREDRDIAQAIATILQDQGVEL------ILNAQVQRVSSHEGEVQLETAEGVLTV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 397 EGiyntVLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDIlDGKPELTPVAIQAGKLLARRLFGV 476
Cdd:NF040477 244 DA----LLVASGRKPATAGLQLQNAGVAVNER-GAIVVDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLGE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 477 SLEKC-DYINIPTTVFTPLEYGCCGLSEEKAIEmyKKENLEVYhTLfwPLEWTVAGR---DNNTCYAKIICNKfdNERVV 552
Cdd:NF040477 318 GKRSTdDRQNVPYSVFMTPPLSRIGMTEEQARA--SGADIQVV-TL--PVAAIPRARvmnDTRGVLKAVVDNK--TQRIL 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 110735449 553 GFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 598
Cdd:NF040477 391 GVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSESLNDL 436
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
172-598 |
2.14e-25 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 109.33 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 172 GGTCVNVGCIPKKLMhqaallghaLQDAKKYGweynqqvkhnweAMTEAIQSHIGSLNWgyrvtLREK---------GVT 242
Cdd:PRK08010 40 GGTCINIGCIPTKTL---------VHDAQQHT------------DFVRAIQRKNEVVNF-----LRNKnfhnladmpNID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 243 YVNSFGEFVDLHKIKaTNKKGQETFYTASKFVIATGERPRYLGIQG--DKEYCITSDDLFSLPYCPGCTLVVGASYVGLE 320
Cdd:PRK08010 94 VIDGQAEFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIPGitTTPGVYDSTGLLNLKELPGHLGILGGGYIGVE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 321 CAGFLAGLGLDVTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFqrkftpILVQQLEKGLPGKLKVVAKSTEGPETVEGI 399
Cdd:PRK08010 173 FASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDI------ILNAHVERISHHENQVQVHSEHAQLAVDAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 400 yntvLLAIGRDSCTRKIGLEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILDGKpELTPVAIQAGKLLARRLFGVSLE 479
Cdd:PRK08010 247 ----LIASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTADNIWAMGDVTGGL-QFTYISLDDYRIVRDELLGEGKR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 480 KC-DYINIPTTVFTPLEYGCCGLSEEKAiemykKENLEVYHTLFWPLEWTVAGR---DNNTCYAKIICNKfdNERVVGFH 555
Cdd:PRK08010 321 STdDRKNVPYSVFMTPPLSRVGMTEEQA-----RESGADIQVVTLPVAAIPRARvmnDTRGVLKAIVDNK--TQRILGAS 393
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 110735449 556 LLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTTL 598
Cdd:PRK08010 394 LLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
144-597 |
6.84e-25 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 109.62 E-value: 6.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 144 AKEAANLGKKVMVLdfvvpspQGTTWGLGGTCVNVGCIPKKLMHQAA----------------LLGHALQDAKKYGWEYN 207
Cdd:PTZ00153 132 AINAMERGLKVIIF-------TGDDDSIGGTCVNVGCIPSKALLYATgkyrelknlaklytygIYTNAFKNGKNDPVERN 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 208 Q----QVKHNWEAMTEAIQSHIGSLNWGYRVTLREKG-------VTYVNSFGEFVDLHKIKAtNKKGQEtfYTASKFVIA 276
Cdd:PTZ00153 205 QlvadTVQIDITKLKEYTQSVIDKLRGGIENGLKSKKfcknsehVQVIYERGHIVDKNTIKS-EKSGKE--FKVKNIIIA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 277 TGERPRY-LGIQGDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVT-VMVRSVLLRGFDQEMAekvgS 354
Cdd:PTZ00153 282 TGSTPNIpDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsFEYSPQLLPLLDADVA----K 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 355 YLEQQGVKFQ--RKFTPILVQQLEKGLPGKLKVVAKS--TEGPETVEGIYNT---------VLLAIGRDSCTRKIGLEKI 421
Cdd:PTZ00153 358 YFERVFLKSKpvRVHLNTLIEYVRAGKGNQPVIIGHSerQTGESDGPKKNMNdiketyvdsCLVATGRKPNTNNLGLDKL 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 422 GVKINEknGKIPVND---VEQTN---VPHVYAIGDIlDGKPELTPVA-IQA-----------GKLLARRLFGVSLEKCDY 483
Cdd:PTZ00153 438 KIQMKR--GFVSVDEhlrVLREDqevYDNIFCIGDA-NGKQMLAHTAsHQAlkvvdwiegkgKENVNINVENWASKPIIY 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 484 INIPTTVFTPLEYGCCGLSEEKAIEMYKKENL--EVYH-----TLFWPLEWTVAGRDNNTCYAKIICNKFDN-------- 548
Cdd:PTZ00153 515 KNIPSVCYTTPELAFIGLTEKEAKELYPPDNVgvEISFykansKVLCENNISFPNNSKNNSYNKGKYNTVDNtegmvkiv 594
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 110735449 549 -----ERVVGFHLLGPNAGEITQGFAAAMKCGLTKQLLDDTIGIHPTCGEVFTT 597
Cdd:PTZ00153 595 ylkdtKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
147-450 |
3.15e-23 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 103.02 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 147 AANLGKKVMVLDFVvpspqgttwGLGGTCVNVGCIPKK----------LMHQAALLGHALQDAKKYGWEY---NQQVKhn 213
Cdd:PRK07845 20 AAQLGADVTVIERD---------GLGGAAVLTDCVPSKtliataevrtELRRAAELGIRFIDDGEARVDLpavNARVK-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 214 weAMTEAiQSH-IgslnwgyRVTLREKGVTYVNSFGEFVDL----HKIKATNKKGQETFYTASKFVIATGERPRYL-GIQ 287
Cdd:PRK07845 89 --ALAAA-QSAdI-------RARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPRILpTAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 288 GDKEYCITSDDLFSLPYCPGCTLVVGASYVGLECAGFLAGLGLDVT-VMVRSVLLRGFDQEMAEKVGSYLEQQGVKFQRK 366
Cdd:PRK07845 159 PDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 367 FTPILVQQLEKGlpgklkVVAKSTEGpETVEGIYntVLLAIGRDSCTRKIGLEKIGVKINEkNGKIPVNDVEQTNVPHVY 446
Cdd:PRK07845 239 SRAESVERTGDG------VVVTLTDG-RTVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDRVSRTSVPGIY 308
|
....
gi 110735449 447 AIGD 450
Cdd:PRK07845 309 AAGD 312
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
274-499 |
3.92e-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: 100.66 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 274 VIATGERPRYLGIQGdkeycITSDDLFSL------PYC-------PGCTLVV-GASYVGLECAGFLAGLGLDVTVMVRS- 338
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddaDALrealkefKGKRAVViGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 339 VLLRGFDQEMAEKVGSYLEQQGVKFQRKFTpilVQQLEkglpGKLKVVAKSTEGpETVEgiYNTVLLAIGrdsctrkIG- 417
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGET---VVAID----GDDKVAVTLTDG-EEIP--ADLVVVAPG-------VRp 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 418 ----LEKIGVKINEKNGkIPVNDVEQTNVPHVYAIGD------ILDGKPELTP---VAIQAGKLLARRLFGVSLEkcdYI 484
Cdd:COG0446 221 ntelAKDAGLALGERGW-IKVDETLQTSDPDVYAAGDcaevphPVTGKTVYIPlasAANKQGRVAAENILGGPAP---FP 296
|
250
....*....|....*
gi 110735449 485 NIPTTVFTPleYGCC 499
Cdd:COG0446 297 GLGTFISKV--FDLC 309
|
|
| GRX_family |
cd02066 |
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
39-113 |
1.46e-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: 91.37 E-value: 1.46e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110735449 39 RVMIFSKSYCPHSTRVKELFSSLGVVYniLELDQVDDGAsVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQ 113
Cdd:cd02066 1 KVVVFSKSTCPYCKRAKRLLESLGIEF--EEIDILEDGE-LREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
274-475 |
5.55e-20 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 92.51 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 274 VIATGERPRYLGIQG-DKEYCI---TSDDLFSL-PYCPGCT--LVVGASYVGLECAGFLAGLGLDVTVMVRS--VLLRGF 344
Cdd:COG1251 103 VLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 345 DQEMAEKVGSYLEQQGVKFQrkftpilvqqlekglpgkLKVVAKSTEGPETVEGIY---------NTVLLAIG---RDSC 412
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVR------------------LGTGVTEIEGDDRVTGVRladgeelpaDLVVVAIGvrpNTEL 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110735449 413 TRKIGLEkigvkINekNGkIPVNDVEQTNVPHVYAIGDI------LDGKP--ELTPVAIQAGKLLARRLFG 475
Cdd:COG1251 245 ARAAGLA-----VD--RG-IVVDDYLRTSDPDIYAAGDCaehpgpVYGRRvlELVAPAYEQARVAAANLAG 307
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
266-466 |
8.13e-18 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 84.40 E-value: 8.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 266 TFYTASKFVIATGERPRYLGIQGDKE-------YCITSDdlfsLPYCPGCT-LVVGASYVGLECAGFLAGLGLDVTVMVR 337
Cdd:COG0492 97 TEYEAKAVIIATGAGPRKLGLPGEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEALYLTKFASKVTLIHR 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 338 SVLLRGfDQEMAEKVgsyLEQQGVKFQRKFTPILVQqLEKGLPGkLKVVAKSTEGPETVEgiYNTVLLAIGRDSCTRkiG 417
Cdd:COG0492 173 RDELRA-SKILVERL---RANPKIEVLWNTEVTEIE-GDGRVEG-VTLKNVKTGEEKELE--VDGVFVAIGLKPNTE--L 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110735449 418 LEKIGVKINEkNGKIPVNDVEQTNVPHVYAIGDILDGKPELTPVAIQAG 466
Cdd:COG0492 243 LKGLGLELDE-DGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEG 290
|
|
| GRX_bact |
TIGR02181 |
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
40-121 |
1.51e-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: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 40 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDqvDDGASVQEVLtEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQK 119
Cdd:TIGR02181 1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVD--GDPALRDEMM-QRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDP 77
|
..
gi 110735449 120 LL 121
Cdd:TIGR02181 78 LL 79
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
310-384 |
1.22e-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: 74.93 E-value: 1.22e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110735449 310 LVVGASYVGLECAGFLAGLGLDVTVMVRS-VLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKGLPGKLK 384
Cdd:pfam00070 3 VVVGGGYIGLELAGALARLGSKVTVVERRdRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| Glutaredoxin |
pfam00462 |
Glutaredoxin; |
40-102 |
6.21e-16 |
|
Glutaredoxin;
Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 72.15 E-value: 6.21e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735449 40 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDgasVQEVLTEISNQKTVPNIFVNKVHV 102
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 ... |
40-106 |
1.11e-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: 1.11e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110735449 40 VMIFSKSYCPHSTRVKELFSSLGVVYnilELDQVDDGASVQEVLTEISNQ-KTVPNIFVNKVHVGGCD 106
Cdd:cd03418 2 VEIYTKPNCPYCVRAKALLDKKGVDY---EEIDVDGDPALREEMINRSGGrRTVPQIFIGDVHIGGCD 66
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
255-581 |
1.73e-13 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 72.77 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 255 KIKATNKKGQETF-YTASKFVIATGER---PRYLGIQGDKEYCITS-DD------LFSLPYCPGCTlVVGASYVGLECAG 323
Cdd:PRK09564 88 TITVKNLKTGSIFnDTYDKLMIATGARpiiPPIKNINLENVYTLKSmEDglalkeLLKDEEIKNIV-IIGAGFIGLEAVE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 324 FLAGLGLDVTVMVRS--VLLRGFDQEMAEKVGSYLEQQGVKFQrkftpilVQQLEKGLPGKLKVvakstEGPETVEGIYN 401
Cdd:PRK09564 167 AAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELH-------LNEFVKSLIGEDKV-----EGVVTDKGEYE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 402 T--VLLAIGRDSCTRKI---GLEKIgvkineKNGKIPVNDVEQTNVPHVYAIGD------ILDGKPELTPVAIQAGKLla 470
Cdd:PRK09564 235 AdvVIVATGVKPNTEFLedtGLKTL------KNGAIIVDEYGETSIENIYAAGDcatiynIVSNKNVYVPLATTANKL-- 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 471 RRLFGVSLEKCDYINIPT------TVFTpLEYGCCGLSEEKAiemyKKENLEVY--------HTLFWPlewtvagrDNNT 536
Cdd:PRK09564 307 GRMVGENLAGRHVSFKGTlgsaciKVLD-LEAARTGLTEEEA----KKLGIDYKtvfikdknHTNYYP--------GQED 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 110735449 537 CYAKIICNKfDNERVVGFHLLGPNAGEI-TQGFAAAMKCGLTKQLL 581
Cdd:PRK09564 374 LYVKLIYEA-DTKVILGGQIIGKKGAVLrIDALAVAIYAKLTTQEL 418
|
|
| GlrX-like_plant |
TIGR02189 |
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ... |
33-121 |
3.39e-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: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 33 DLIEGNRVMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAH 112
Cdd:TIGR02189 3 RMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMALH 82
|
....*....
gi 110735449 113 QNGLLQKLL 121
Cdd:TIGR02189 83 ISGSLVPML 91
|
|
| GrxC |
COG0695 |
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
39-106 |
7.64e-12 |
|
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 60.98 E-value: 7.64e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110735449 39 RVMIFSKSYCPHSTRVKELFSSLGVVYNilELDqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCD 106
Cdd:COG0695 1 KVTLYTTPGCPYCARAKRLLDEKGIPYE--EID-VDEDPEAREELRERSGRRTVPVIFIGGEHLGGFD 65
|
|
| PRK10638 |
PRK10638 |
glutaredoxin 3; Provisional |
40-122 |
1.57e-11 |
|
glutaredoxin 3; Provisional
Pssm-ID: 182607 [Multi-domain] Cd Length: 83 Bit Score: 60.60 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 40 VMIFSKSYCPHSTRVKELFSSLGVVYNILEldqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGGCDRTFQAHQNGLLQK 119
Cdd:PRK10638 4 VEIYTKATCPFCHRAKALLNSKGVSFQEIP---IDGDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80
|
...
gi 110735449 120 LLQ 122
Cdd:PRK10638 81 LLK 83
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
232-507 |
2.86e-11 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 65.54 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 232 YRVTLREKGVTYVNSFGEFVDLHKIKATNKKGQETFYtaSKFVIATGERPRYLGIQGDKEYCI---TSDDLFSL------ 302
Cdd:COG1252 62 LRELLRRAGVRFIQGEVTGIDPEARTVTLADGRTLSY--DYLVIATGSVTNFFGIPGLAEHALplkTLEDALALrerlla 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 303 ------PYCPGCTLVVGASYVGLECAGFLAGL--------GLD--------VTVMVRsvLLRGFDQEMAEKVGSYLEQQG 360
Cdd:COG1252 140 aferaeRRRLLTIVVVGGGPTGVELAGELAELlrkllrypGIDpdkvritlVEAGPR--ILPGLGEKLSEAAEKELEKRG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 361 VKFQRKFTpilVQQLEKGlpgklKVVaksTEGPETVEgiYNTVLLAIG-------RDSctrkiGLEKigvkinEKNGKIP 433
Cdd:COG1252 218 VEVHTGTR---VTEVDAD-----GVT---LEDGEEIP--ADTVIWAAGvkappllADL-----GLPT------DRRGRVL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 434 VNDVEQT-NVPHVYAIGD---ILDGKPELTP----VAIQAGKLLARRLFGVSLEKcdyiniPTTVFTPLEYGC-CGLSEE 504
Cdd:COG1252 274 VDPTLQVpGHPNVFAIGDcaaVPDPDGKPVPktaqAAVQQAKVLAKNIAALLRGK------PLKPFRYRDKGClASLGRG 347
|
...
gi 110735449 505 KAI 507
Cdd:COG1252 348 AAV 350
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
263-479 |
2.84e-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: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 263 GQETFYtaSKFVIATGERPRYLGIQG-DKEYCI---TSDDLFSLPYCPGCTL---VVGASYVGLECAGFLAGLGLDVTV- 334
Cdd:TIGR02374 92 GRTLSY--DKLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMDVSVi 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 335 -MVRSVLLRGFDQEMAEKVGSYLEQQGVKFQ-RKFTPILVQQlekglpGKLKVVaKSTEGPETVEGIyntVLLAIG---R 409
Cdd:TIGR02374 170 hHAPGLMAKQLDQTAGRLLQRELEQKGLTFLlEKDTVEIVGA------TKADRI-RFKDGSSLEADL---IVMAAGirpN 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735449 410 DSCTRKIGLekigvkinEKNGKIPVNDVEQTNVPHVYAIGDI--LDGKP-ELTPVAIQAGKLLARRLFGVSLE 479
Cdd:TIGR02374 240 DELAVSAGI--------KVNRGIIVNDSMQTSDPDIYAVGECaeHNGRVyGLVAPLYEQAKVLADHICGVECE 304
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
310-475 |
8.23e-10 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 61.34 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 310 LVVGASYVGLECAGFLAGLGLDVTVMVRSV-LLRGFDQEMAEKVGSYLEQQGVKFQrkftpiLVQQLEKgLPGKLkVVAK 388
Cdd:PRK13512 152 LVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREIPYR------LNEEIDA-INGNE-VTFK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 389 STEgpetVEGiYNTVLLAIGRDSCTRKIglEKIGVKINEKnGKIPVNDVEQTNVPHVYAIGDILDG------KPELTPVA 462
Cdd:PRK13512 224 SGK----VEH-YDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDIITShyrhvdLPASVPLA 295
|
170
....*....|....*.
gi 110735449 463 I---QAGKLLARRLFG 475
Cdd:PRK13512 296 WgahRAASIVAEQIAG 311
|
|
| GRX_PICOT_like |
cd03028 |
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ... |
33-118 |
5.84e-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: 53.27 E-value: 5.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 33 DLIEGNRVMIFSKSY-----CPHSTRVKELFSSLGVVY---NILEldqvDDgaSVQEVLTEISNQKTVPNIFVNKVHVGG 104
Cdd:cd03028 3 KLIKENPVVLFMKGTpeeprCGFSRKVVQILNQLGVDFgtfDILE----DE--EVRQGLKEYSNWPTFPQLYVNGELVGG 76
|
90
....*....|....
gi 110735449 105 CDRTFQAHQNGLLQ 118
Cdd:cd03028 77 CDIVKEMHESGELQ 90
|
|
| GRX_hybridPRX5 |
cd03029 |
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ... |
40-106 |
1.24e-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: 1.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110735449 40 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVDDGASVQEVlteiSNQKTVPNIFVNKVHVGGCD 106
Cdd:cd03029 3 VSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGRSLRAV----TGAMTVPQVFIDGELIGGSD 65
|
|
| GRX_DEP |
cd03027 |
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ... |
39-104 |
5.43e-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: 5.43e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110735449 39 RVMIFSKSYCPHSTRVKELFSSLGVVYniLELDqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGG 104
Cdd:cd03027 2 RVTIYSRLGCEDCTAVRLFLREKGLPY--VEIN-IDIFPERKAELEERTGSSVVPQIFFNEKLVGG 64
|
|
| grxA |
PRK11200 |
glutaredoxin 1; Provisional |
40-112 |
7.48e-06 |
|
glutaredoxin 1; Provisional
Pssm-ID: 183036 [Multi-domain] Cd Length: 85 Bit Score: 44.25 E-value: 7.48e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110735449 40 VMIFSKSYCPHSTRVKELFSSLGVV---YNILELDQVDDGASVQEVLTEISNQ-KTVPNIFVNKVHVGGCDRtFQAH 112
Cdd:PRK11200 3 VVIFGRPGCPYCVRAKELAEKLSEErddFDYRYVDIHAEGISKADLEKTVGKPvETVPQIFVDQKHIGGCTD-FEAY 78
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
311-471 |
1.29e-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: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 311 VVGASYVGLECAGFLAGLG-LDVTVMVRsvllRGFDqEM---AEKVgSYLEQQGVKFQ-----RKF--------TPILVQ 373
Cdd:COG0493 260 VIGGGNTAMDCARTALRLGaESVTIVYR----RTRE-EMpasKEEV-EEALEEGVEFLflvapVEIigdengrvTGLECV 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 374 QLEKGLP---GKLKVVAKstEGPE-TVEGiyNTVLLAIGRDSCTRKIgLEKIGVKINeKNGKIPVNDVE-QTNVPHVYAI 448
Cdd:COG0493 334 RMELGEPdesGRRRPVPI--EGSEfTLPA--DLVILAIGQTPDPSGL-EEELGLELD-KRGTIVVDEETyQTSLPGVFAG 407
|
170 180
....*....|....*....|...
gi 110735449 449 GDILDGkPELTPVAIQAGKLLAR 471
Cdd:COG0493 408 GDAVRG-PSLVVWAIAEGRKAAR 429
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
274-473 |
1.90e-05 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 47.29 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 274 VIATGE-RPRYLGIQGDKEYCITS--DDLFS-----LPYCP---------GCTLVVGASYVGLECAGFLAGLGLDVTVMV 336
Cdd:PRK12770 123 LIATGTwKSRKLGIPGEDLPGVYSalEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAALEAVLLGAEKVYLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 337 -RsvllRGFDQEMAekvGSY----LEQQGVKFQRKFTPILVQQlEKGLPG----KLKVVAKSTEG---PETVEGI----- 399
Cdd:PRK12770 203 yR----RTINEAPA---GKYeierLIARGVEFLELVTPVRIIG-EGRVEGvelaKMRLGEPDESGrprPVPIPGSefvle 274
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110735449 400 YNTVLLAIGrDSCTRKIGLEKIGVKINeKNGKIPVNDVEQTNVPHVYAIGDILDGkPELTPVAIQAGKLLARRL 473
Cdd:PRK12770 275 ADTVVFAIG-EIPTPPFAKECLGIELN-RKGEIVVDEKHMTSREGVFAAGDVVTG-PSKIGKAIKSGLRAAQSI 345
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
262-450 |
4.04e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 46.65 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 262 KGQETFYtaSKFVIATGERPRYLGIQG-DKEYCI---TSDDLFSLPYCPGCT---LVVGASYVGLECAGFLAGLGLDVTV 334
Cdd:PRK14989 96 AGRTVFY--DKLIMATGSYPWIPPIKGsETQDCFvyrTIEDLNAIEACARRSkrgAVVGGGLLGLEAAGALKNLGVETHV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 335 MVRSVLLRG--FDQEMAEKVGSYLEQQGVKFQ-RKFTPILVQQLEKGlpGKLKVVAKSTEgPETVEGIYNTVLLAigRDS 411
Cdd:PRK14989 174 IEFAPMLMAeqLDQMGGEQLRRKIESMGVRVHtSKNTLEIVQEGVEA--RKTMRFADGSE-LEVDFIVFSTGIRP--QDK 248
|
170 180 190
....*....|....*....|....*....|....*....
gi 110735449 412 CTRKIGLEkIGvkineKNGKIPVNDVEQTNVPHVYAIGD 450
Cdd:PRK14989 249 LATQCGLA-VA-----PRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
274-470 |
6.67e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 45.56 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 274 VIATG-ERPRYLGIQGDK--------EYcITSDDLFSLPYCPGC---TLVVGASYVGLECAGFLAGLGL-DVTVMVRsvl 340
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDF-LTRVNQAVADYDLPVgkrVVVIGGGNTAMDAARTAKRLGAeSVTIVYR--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 341 lRGFDqEM---AEKVgSYLEQQGVKFQRKFTPILVQQLEKGLPG------KLKVVAKSTEGPETVEGIY-----NTVLLA 406
Cdd:PRK11749 306 -RGRE-EMpasEEEV-EHAKEEGVEFEWLAAPVEILGDEGRVTGvefvrmELGEPDASGRRRVPIEGSEftlpaDLVIKA 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110735449 407 IGRDSCTRKIGLEKiGVKINEKNGKIPVNDVEQTNVPHVYAIGDILDGkPELTPVAIQAGKLLA 470
Cdd:PRK11749 383 IGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTG-AATVVWAVGDGKDAA 444
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
263-453 |
2.07e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 43.90 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 263 GQETFYTASKFVIATGERPRYLGIQGDKEY-------CITSDDLFslpYCPGCTLVVGASYVGLECAGFLAGLGLDVTVM 335
Cdd:PRK10262 99 GDSGEYTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 336 VRSVLLRGfDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEKGLPGkLKVvaKSTEGPETVEGI-YNTVLLAIGRDSCTr 414
Cdd:PRK10262 176 HRRDGFRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTG-VRL--RDTQNSDNIESLdVAGLFVAIGHSPNT- 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 110735449 415 kiglEKIGVKINEKNGKIPVN-----DVEQTNVPHVYAIGDILD 453
Cdd:PRK10262 251 ----AIFEGQLELENGYIKVQsgihgNATQTSIPGVFAAGDVMD 290
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
232-475 |
3.17e-04 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 43.37 E-value: 3.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 232 YRVTLREKgvTYVNSFGefVDLHKIKAtnkKGQEtfYTASKFVIATGERPRYLGIQGDkEYCITsddLFSLPYCPGC--- 308
Cdd:PRK04965 71 FNLRLFPH--TWVTDID--AEAQVVKS---QGNQ--WQYDKLVLATGASAFVPPIPGR-ELMLT---LNSQQEYRAAetq 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 309 ------TLVVGASYVGLECAGFLAGLGLDVTVMVR-SVLLRGFdqeMAEKVGSYLE----QQGVKFQRKFTpilVQQLEK 377
Cdd:PRK04965 138 lrdaqrVLVVGGGLIGTELAMDLCRAGKAVTLVDNaASLLASL---MPPEVSSRLQhrltEMGVHLLLKSQ---LQGLEK 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 378 GLPGklkVVAKSTEGpETVEgiYNTVLLAIGRDSCT---RKIGLEKigvkinekNGKIPVNDVEQTNVPHVYAIGDI--L 452
Cdd:PRK04965 212 TDSG---IRATLDSG-RSIE--VDAVIAAAGLRPNTalaRRAGLAV--------NRGIVVDSYLQTSAPDIYALGDCaeI 277
|
250 260
....*....|....*....|....*
gi 110735449 453 DGK--PELTPVAIQAgKLLARRLFG 475
Cdd:PRK04965 278 NGQvlPFLQPIQLSA-MALAKNLLG 301
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
272-473 |
3.19e-04 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 43.60 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 272 KFVIATGERPRYLGIQGDKEY-------------------CITSDDLFSLPYCPGCTL----VVGASYVGLECAGFLAGL 328
Cdd:PTZ00318 116 KLVVAHGARPNTFNIPGVEERafflkevnhargirkrivqCIERASLPTTSVEERKRLlhfvVVGGGPTGVEFAAELADF 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 329 GLD--------------VTVM-VRSVLLRGFDQEMAEKVGSYLEQQGVKFQRKFTPILVQQLEkglpgklkVVAKSTEGP 393
Cdd:PTZ00318 196 FRDdvrnlnpelveeckVTVLeAGSEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKE--------VVLKDGEVI 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 394 ETVEGIYNTvllAIGRDSCTRKIGLEKigvkinEKNGKIPVND-VEQTNVPHVYAIGDILDGK----PELTPVAIQAGKL 468
Cdd:PTZ00318 268 PTGLVVWST---GVGPGPLTKQLKVDK------TSRGRISVDDhLRVKPIPNVFALGDCAANEerplPTLAQVASQQGVY 338
|
....*
gi 110735449 469 LARRL 473
Cdd:PTZ00318 339 LAKEF 343
|
|
| NrdH |
cd02976 |
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
39-104 |
4.81e-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: 38.75 E-value: 4.81e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110735449 39 RVMIFSKSYCPHSTRVKELFSSLGVVYNilELDqVDDGASVQEVLTEISNQKTVPNIFVNKVHVGG 104
Cdd:cd02976 1 EVTVYTKPDCPYCKATKRFLDERGIPFE--EVD-VDEDPEALEELKKLNGYRSVPVVVIGDEHLSG 63
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
268-449 |
8.92e-04 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 41.83 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 268 YTASKFVIATGE--RPRYLGIqgdKEYCITSDDLFSL-PYCPGCTLVVGASYVGLECAGFLAGLGLDVTVmvrsvLLRGF 344
Cdd:pfam13738 117 YQARYVIIATGEfdFPNKLGV---PELPKHYSYVKDFhPYAGQKVVVIGGYNSAVDAALELVRKGARVTV-----LYRGS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 345 DQEMAEKVGSYleqqGVKfqrkftPILVQQLEKGL-PGKLKVVAKS---------------TEGPETVEgIYNTVLLAIG 408
Cdd:pfam13738 189 EWEDRDSDPSY----SLS------PDTLNRLEELVkNGKIKAHFNAevkeitevdvsykvhTEDGRKVT-SNDDPILATG 257
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 110735449 409 RDSCTRKigLEKIGVKINEkNGKIPVND-VEQTNVPHVYAIG 449
Cdd:pfam13738 258 YHPDLSF--LKKGLFELDE-DGRPVLTEeTESTNVPGLFLAG 296
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
311-471 |
1.97e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 41.16 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 311 VVGASYVGLECAGFLAGLGLDVTVMVRsvllRGfDQEM---AEKVGsYLEQQGVKFQRKFTPILVQQLEKGLPGKLKVV- 386
Cdd:PRK12831 286 VVGGGNVAMDAARTALRLGAEVHIVYR----RS-EEELparVEEVH-HAKEEGVIFDLLTNPVEILGDENGWVKGMKCIk 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 387 -------AKSTEGPETVEGIY-----NTVLLAIGRdSCTRKIGLEKIGVKINeKNGKIPVN-DVEQTNVPHVYAIGDILD 453
Cdd:PRK12831 360 melgepdASGRRRPVEIEGSEfvlevDTVIMSLGT-SPNPLISSTTKGLKIN-KRGCIVADeETGLTSKEGVFAGGDAVT 437
|
170
....*....|....*....
gi 110735449 454 GkpELTPV-AIQAGKLLAR 471
Cdd:PRK12831 438 G--AATVIlAMGAGKKAAK 454
|
|
| GRXA |
TIGR02183 |
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
40-105 |
3.80e-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: 36.73 E-value: 3.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 40 VMIFSKSYCPHSTRVKELFSSLGVVYNILELDQVD---DGASVQEVLTEISNQ-KTVPNIFVNKVHVGGC 105
Cdd:TIGR02183 2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEFRYIDihaEGISKADLEKTVGKPvETVPQIFVDEKHVGGC 71
|
|
| PTZ00062 |
PTZ00062 |
glutaredoxin; Provisional |
34-124 |
5.79e-03 |
|
glutaredoxin; Provisional
Pssm-ID: 240250 [Multi-domain] Cd Length: 204 Bit Score: 38.62 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110735449 34 LIEGNRVMIFSKS-----YCPHSTRVKELFSSLGV---VYNILElDQvddgaSVQEVLTEISNQKTVPNIFVNKVHVGGC 105
Cdd:PTZ00062 109 LIRNHKILLFMKGsktfpFCRFSNAVVNMLNSSGVkyeTYNIFE-DP-----DLREELKVYSNWPTYPQLYVNGELIGGH 182
|
90
....*....|....*....
gi 110735449 106 DRTFQAHQNGLLQKLLQDD 124
Cdd:PTZ00062 183 DIIKELYESNSLRKVIPDD 201
|
|
| PHA03050 |
PHA03050 |
glutaredoxin; Provisional |
35-104 |
8.40e-03 |
|
glutaredoxin; Provisional
Pssm-ID: 165343 [Multi-domain] Cd Length: 108 Bit Score: 36.53 E-value: 8.40e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110735449 35 IEGNRVMIFSKSYCPHSTRVKELFSSLGV---VYNILELDQVDDGASVQEVLTEISNQKTVPNIFVNKVHVGG 104
Cdd:PHA03050 10 LANNKVTIFVKFTCPFCRNALDILNKFSFkrgAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGG 82
|
|
| |
