|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
110-598 |
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: 852.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 110 YDYDLIVIGGGSGGLACSKEAASFGKKVMVLDFVVPTPQGTSWGLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWEY 189
Cdd:TIGR01438 1 YDYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 190 EEQVKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHKIKATNKKGKESFFTAEKFVVATGERPRYLNI 269
Cdd:TIGR01438 81 EETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 270 PGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRSIFLRGFDQEMANRAGAYMETHGVKFIKQ 349
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 350 FVPIKVELLEEgtpgriKVTAKSTQGDQIIEDEYNTVLIAVGRDACTRNIGLEKIGVKINERNGKIPVSDEEQTSVPHVY 429
Cdd:TIGR01438 241 FVPIKVEQIEA------KVLVEFTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 430 AIGDILDGKLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYGEENLEVYHTLFWPLE 509
Cdd:TIGR01438 315 AVGDILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 510 WTVPSRDN-NTCFAKIICNKQDNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIFTTMDTSKSSG 588
Cdd:TIGR01438 395 WTIPSRDNhNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSG 474
|
490
....*....|
gi 1214874590 589 GDISQKGCUG 598
Cdd:TIGR01438 475 QDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
109-598 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 534.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 109 TYDYDLIVIGGGSGGLACSKEAASFGKKVMVLDFVVPTPQGTSWGLGGTCVNVGCIPKKLMHQAAILGQSLK-DSRKFGW 187
Cdd:PTZ00052 3 TFMYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 188 EYEEqvKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHKIkATNKKGKESFFTAEKFVVATGERPRYL 267
Cdd:PTZ00052 83 KTSS--SFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPSIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 268 -NIPGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRSIFLRGFDQEMANRAGAYMETHGVKF 346
Cdd:PTZ00052 160 eDVPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 347 IKQFVPIKVELLEEgtpgRIKV--TAKSTQgdqiiedEYNTVLIAVGRDACTRNIGLEKIGVKINERNGKIpvSDEEQTS 424
Cdd:PTZ00052 240 LEGVVPINIEKMDD----KIKVlfSDGTTE-------LFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKII--APNDCTN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 425 VPHVYAIGDILDGKLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYGEENLEVYHTL 504
Cdd:PTZ00052 307 IPNIFAVGDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 505 FWPLEWTVPSRD--------------NNTCFAKIICNKQDNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGI 570
Cdd:PTZ00052 387 FNTLEIAAVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGI 466
|
490 500
....*....|....*....|....*...
gi 1214874590 571 HPTCAEIFTTMDTSKSSGGDISQKGCUG 598
Cdd:PTZ00052 467 HPTDAEVFMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
109-581 |
3.54e-148 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 434.97 E-value: 3.54e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 109 TYDYDLIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpqgtSWGLGGTCVNVGCIPKKLMHQAAILGQSLKD-SRKFGW 187
Cdd:PRK06116 2 TKDYDLIVIGGGSGGIASANRAAMYGAKVALIE---------AKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 188 EYEEQvKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHKIKATNKKgkesfFTAEKFVVATGERPRYL 267
Cdd:PRK06116 73 DVTEN-KFDWAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGER-----YTADHILIATGGRPSIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 268 NIPGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRS-IFLRGFDQEMANRAGAYMETHGVKF 346
Cdd:PRK06116 147 DIPG-AEYGITSDGFFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGdAPLRGFDPDIRETLVEEMEKKGIRL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 347 IKQFVPIKVELLEEGTpgrikVTAKSTQGDQIIEDeynTVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQTSVP 426
Cdd:PRK06116 226 HTNAVPKAVEKNADGS-----LTLTLEDGETLTVD---CLIWAIGREPNTDGLGLENAGVKLNEK-GYIIVDEYQNTNVP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 427 HVYAIGDIlDGKLELTPVAIQAGRLLARRLYRG-SKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYGEENLEVYHTLF 505
Cdd:PRK06116 297 GIYAVGDV-TGRVELTPVAIAAGRRLSERLFNNkPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSF 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1214874590 506 WPLEWTVPSRDNnTCFAKIICNKQDnDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIFTTM 581
Cdd:PRK06116 376 TPMYTALTGHRQ-PCLMKLVVVGKE-EKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTM 449
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
109-581 |
5.97e-123 |
|
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: 370.57 E-value: 5.97e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 109 TYDYDLIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpqgtSWGLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWE 188
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 189 YEEqVKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHKIKATNKKgkesFFTAEKFVVATGERPRYLN 268
Cdd:COG1249 72 AGA-PSVDWAALMARKDKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTVEVTGGE----TLTADHIVIATGSRPRVPP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 269 IPG-DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRS-IFLRGFDQEMANRAGAYMETHGVKF 346
Cdd:COG1249 147 IPGlDEVRVLTSDEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGdRLLPGEDPEISEALEKALEKEGIDI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 347 IKQFVPIKVElleeGTPGRIKVTAKStqGDQIIEDEYNTVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQTSVP 426
Cdd:COG1249 227 LTGAKVTSVE----KTGDGVTVTLED--GGGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDER-GGIKVDEYLRTSVP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 427 HVYAIGDILdGKLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYgeENLEVYHTLFW 506
Cdd:COG1249 300 GIYAIGDVT-GGPQLAHVASAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAG--IDVKVGKFPFA 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1214874590 507 PLEWTVpSRDNNTCFAKIICNKqDNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIFTTM 581
Cdd:COG1249 377 ANGRAL-ALGETEGFVKLIADA-ETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEA 449
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
110-581 |
9.50e-111 |
|
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: 339.09 E-value: 9.50e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 110 YDYDLIVIGGGSGGLACSKEAASFGKKVMV--LDFVvptpqgtswglGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGW 187
Cdd:TIGR01424 1 FDYDLFVIGAGSGGVRAARLAAALGAKVAIaeEFRV-----------GGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 188 EYEEqVKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHKIKATNKKGKesfFTAEKFVVATGERPRYL 267
Cdd:TIGR01424 70 TVGK-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 268 NIPGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVR-SIFLRGFDQEMANRAGAYMETHGVKF 346
Cdd:TIGR01424 146 ALPG-HELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 347 IKQFVPIKVELLEEgtpGRIKVTakSTQGDQIIEDeynTVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQTSVP 426
Cdd:TIGR01424 225 LPEDSITSISKDDD---GRLKAT--LSKHEEIVAD---VVLFATGRSPNTNGLGLEAAGVRLNDL-GAIAVDEYSRTSTP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 427 HVYAIGDILDgKLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYGEenLEVYHTLFW 506
Cdd:TIGR01424 296 SIYAVGDVTD-RINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1214874590 507 PLEWTVPSRDNNtCFAKIICNkQDNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIFTTM 581
Cdd:TIGR01424 373 PMKATFSGRQEK-TLMKLVVD-AKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTM 445
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
112-581 |
1.10e-110 |
|
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: 339.12 E-value: 1.10e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpqgtSWGLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWEYEE 191
Cdd:TIGR01421 3 YDYLVIGGGSGGIASARRAAEHGAKALLVE---------AKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQND 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 192 QVKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHKIKATNKKgkesfFTAEKFVVATGERPRYL-NIP 270
Cdd:TIGR01421 74 ENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRD-----YTAPHILIATGGKPSFPeNIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 271 GdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVR-SIFLRGFDQEMANRAGAYMETHGVKFIKQ 349
Cdd:TIGR01421 149 G-AELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 350 FVPIKVELLEEGtpgriKVTAKSTQGDQIieDEYNTVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQTSVPHVY 429
Cdd:TIGR01421 228 SKPVKVEKTVEG-----KLVIHFEDGKSI--DDVDELIWAIGRKPNTKGLGLENVGIKLNEK-GQIIVDEYQNTNVPGIY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 430 AIGDILdGKLELTPVAIQAGRLLARRLYRGSK-VKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYGEENLEVYHTLFWPL 508
Cdd:TIGR01421 300 ALGDVV-GKVELTPVAIAAGRKLSERLFNGKTdDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPM 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1214874590 509 EWTVPSRDNNTCFaKIICNKQdNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIFTTM 581
Cdd:TIGR01421 379 YYAMTSEKQKCRM-KLVCAGK-EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTM 449
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
105-583 |
6.42e-103 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 322.60 E-value: 6.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 105 DNSVTYDYDLIVIGGGSGGLACSKEAASFGKKVMVLDFVVPT-PQGTSWGLGGTCVNVGCIPKKLMHQAAILGQSLKDSR 183
Cdd:PLN02546 73 ESERHYDFDLFTIGAGSGGVRASRFASNFGASAAVCELPFATiSSDTLGGVGGTCVLRGCVPKKLLVYASKYSHEFEESR 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 184 KFGWEYEEQVKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHKIKATNKkgkesFFTAEKFVVATGER 263
Cdd:PLN02546 153 GFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGK-----LYTARNILIAVGGR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 264 PRYLNIPGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRSI-FLRGFDQEMANRAGAYMETH 342
Cdd:PLN02546 228 PFIPDIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKkVLRGFDEEVRDFVAEQMSLR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 343 GVKFIKQFVPIKVELLEEGTPGrIKVTAKSTQGdqiiedeYNTVLIAVGRDACTRNIGLEKIGVKINErNGKIPVSDEEQ 422
Cdd:PLN02546 307 GIEFHTEESPQAIIKSADGSLS-LKTNKGTVEG-------FSHVMFATGRKPNTKNLGLEEVGVKMDK-NGAIEVDEYSR 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 423 TSVPHVYAIGDILDgKLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYGEenLEVYH 502
Cdd:PLN02546 378 TSVPSIWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD--VDVFT 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 503 TLFWPLEWTVPSRDNNTCFAKIICNKqdNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIFTTMD 582
Cdd:PLN02546 455 ANFRPLKATLSGLPDRVFMKLIVCAK--TNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMR 532
|
.
gi 1214874590 583 T 583
Cdd:PLN02546 533 T 533
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
95-583 |
7.20e-102 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 317.91 E-value: 7.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 95 KDGSLAKLLDD--NSVTYDYDLIVIGGGSGGLACSKEAASFGKKVMVLDFVV-PTPQGTSWGLGGTCVNVGCIPKKLMHQ 171
Cdd:PLN02507 7 IDGEVAKVNADeaNATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICELPFhPISSESIGGVGGTCVIRGCVPKKILVY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 172 AAILGQSLKDSRKFGWEYEEQVKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHKIKATNKKGKESFF 251
Cdd:PLN02507 87 GATFGGEFEDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 252 TAEKFVVATGERPRYLNIPGdKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVR-SIFLRGFDQE 330
Cdd:PLN02507 167 TAKHILIATGSRAQRPNIPG-KELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 331 MANRAGAYMETHGVKFIKQFVPIKVELLEEGtpgrIKVTakSTQGDQIIEDeynTVLIAVGRDACTRNIGLEKIGVKInE 410
Cdd:PLN02507 246 MRAVVARNLEGRGINLHPRTNLTQLTKTEGG----IKVI--TDHGEEFVAD---VVLFATGRAPNTKRLNLEAVGVEL-D 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 411 RNGKIPVSDEEQTSVPHVYAIGDILDgKLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAI 490
Cdd:PLN02507 316 KAGAVKVDEYSRTNIPSIWAIGDVTN-RINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 491 EiYGEENLEVYHTLFWPLEWTVPSRDNNTcFAKIICNKQDnDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGI 570
Cdd:PLN02507 395 E-QAKGDILVFTSSFNPMKNTISGRQEKT-VMKLIVDAET-DKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGI 471
|
490
....*....|...
gi 1214874590 571 HPTCAEIFTTMDT 583
Cdd:PLN02507 472 HPSAAEEFVTMRS 484
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
111-581 |
1.90e-90 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 289.98 E-value: 1.90e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 111 DYDLIVIGGGSGGLACSKEAASFGKKVMVLDFVVptpqgtswgLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWEYE 190
Cdd:PTZ00058 48 VYDLIVIGGGSGGMAAARRAARNKAKVALVEKDY---------LGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 191 EQVkhNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHK--IKATNKKGKES------------------- 249
Cdd:PTZ00058 119 FSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQvlIKKVSQVDGEAdesdddevtivsagvsqld 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 250 ---FFTAEKFVVATGERPRYLNIPGdKEYCITSDDLFSLPYcPGKTLVVGASYVALECAGFLAGIGLDATVMVR-SIFLR 325
Cdd:PTZ00058 197 dgqVIEGKNILIAVGNKPIFPDVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLR 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 326 GFDQEMANRAGAYMETHGVKFIKQFVPIKVELLEEGTpgrikVTAKSTQGDQIIEDEYntVLIAVGRDACTRNIGLEkiG 405
Cdd:PTZ00058 275 KFDETIINELENDMKKNNINIITHANVEEIEKVKEKN-----LTIYLSDGRKYEHFDY--VIYCVGRSPNTEDLNLK--A 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 406 VKINERNGKIPVSDEEQTSVPHVYAIGDILDGK---------------------------------LELTPVAIQAGRLL 452
Cdd:PTZ00058 346 LNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKknqeiedlnllklyneepylkkkentsgesyynVQLTPVAINAGRLL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 453 ARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYGEENLEVYHTLFWPLEWTV----PSRDNNTcFAKIICNK 528
Cdd:PTZ00058 426 ADRLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVydmdPAQKEKT-YLKLVCVG 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1214874590 529 QDnDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIFTTM 581
Cdd:PTZ00058 505 KE-ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
112-583 |
2.37e-84 |
|
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: 271.85 E-value: 2.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAAS-FGKKVMVLDfvVPTPQGTSW--GLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWE 188
Cdd:TIGR01423 4 FDLVVIGAGSGGLEAGWNAATlYKKRVAVVD--VQTHHGPPFyaALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 189 YE-EQVKHNWETMREAIQNYIGSLNWGYRVALRDKQ-VRYENAYGEFVESHKI----KATNKKGKESFFTAEKFVVATGE 262
Cdd:TIGR01423 82 FDrSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVlvreSADPKSAVKERLQAEHILLATGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 263 RPRYLNIPGDkEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAG---IGLDATVMVR-SIFLRGFDQEMANRAGAY 338
Cdd:TIGR01423 162 WPQMLGIPGI-EHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRnNMILRGFDSTLRKELTKQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 339 METHGVKFIKQFVPIKVELLEEGTPgriKVTAKSTQgdqiiEDEYNTVLIAVGRDACTRNIGLEKIGVKINErNGKIPVS 418
Cdd:TIGR01423 241 LRANGINIMTNENPAKVTLNADGSK---HVTFESGK-----TLDVDVVMMAIGRVPRTQTLQLDKVGVELTK-KGAIQVD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 419 DEEQTSVPHVYAIGDILDgKLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYgeENL 498
Cdd:TIGR01423 312 EFSRTNVPNIYAIGDVTD-RVMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKV 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 499 EVYHTLFWPLEWTVPSRDNNTCFAKIICNKQDNDrVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIF 578
Cdd:TIGR01423 389 AVYESSFTPLMHNISGSKYKKFVAKIVTNHADGT-VLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEEL 467
|
....*
gi 1214874590 579 TTMDT 583
Cdd:TIGR01423 468 CSMRT 472
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
112-577 |
1.15e-82 |
|
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: 266.43 E-value: 1.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAASFGKKVMVldfvVPTPQgtswgLGGTCVNVGCIPKK-LMHQAAILGQsLKDSRKFGWEYE 190
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVAL----VEKEY-----LGGTCLNVGCIPTKaLLHSAEVYDE-IKHAKDLGIEVE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 191 EqVKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHKIKATNKKGKESFfTAEKFVVATGERPRYLNIP 270
Cdd:TIGR01350 72 N-VSVDWEKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTVSVTGENGEETL-EAKNIIIATGSRPRSLPGP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 271 --GDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATV--MVRSIfLRGFDQEMANRAGAYMETHGVKF 346
Cdd:TIGR01350 150 fdFDGKVVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 347 IKQfvpIKVELLEEGtpGRIKVTAKSTQGDQIIEDEYntVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQTSVP 426
Cdd:TIGR01350 229 LTN---TKVTAVEKN--DDQVTYENKGGETETLTGEK--VLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 427 HVYAIGDILdGKLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAieiyGEENLEVYHTLFw 506
Cdd:TIGR01350 301 GIYAIGDVI-GGPMLAHVASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQA----KEAGYDVKIGKF- 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1214874590 507 PLEWTVPSR--DNNTCFAKIICNKQDnDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEI 577
Cdd:TIGR01350 375 PFAANGKALalGETDGFVKIIADKKT-GEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSEA 446
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
111-580 |
2.87e-73 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 242.01 E-value: 2.87e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 111 DYDLIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpQGTswgLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWEYE 190
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHAD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 191 EqVKHNWETMREAIQNYIGSLNWGYRVALRDK-QVRYENAYGEFVESHKIKAtnkkgKESFFTAEKFVVATGErpRYLNI 269
Cdd:PRK06292 74 G-PKIDFKKVMARVRRERDRFVGGVVEGLEKKpKIDKIKGTARFVDPNTVEV-----NGERIEAKNIVIATGS--RVPPI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 270 PG----DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRS-IFLRGFDQEMANRAGAYMEthgv 344
Cdd:PRK06292 146 PGvwliLGDRLLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGdRILPLEDPEVSKQAQKILS---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 345 KFIKQFVPIKVELLEEGtpGRIKVTAKSTQGD-QIIEDEYntVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQT 423
Cdd:PRK06292 222 KEFKIKLGAKVTSVEKS--GDEKVEELEKGGKtETIEADY--VLVATGRRPNTDGLGLENTGIELDER-GRPVVDEHTQT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 424 SVPHVYAIGDIlDGKLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYGEenlevYHT 503
Cdd:PRK06292 297 SVPGIYAAGDV-NGKPPLLHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAAGID-----YVV 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1214874590 504 LFWPLEWTVPSR--DNNTCFAKIICNKqDNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIFTT 580
Cdd:PRK06292 371 GEVPFEAQGRARvmGKNDGFVKVYADK-KTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSEGLRT 448
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
111-577 |
4.24e-68 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 228.11 E-value: 4.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 111 DYDLIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpqgtSWGLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWEYE 190
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 191 EqVKHNWetmrEAIQNY----IGSLNWGYRVALRDKQVRYENAYGEFVESHKIKATNKKGKESfFTAEKFVVATGERPRy 266
Cdd:PRK06416 75 N-VGIDF----KKVQEWkngvVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTVRVMTEDGEQT-YTAKNIILATGSRPR- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 267 lNIPG---DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATV--MVRSIfLRGFDQEMANRAGAYMET 341
Cdd:PRK06416 148 -ELPGieiDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveALPRI-LPGEDKEISKLAERALKK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 342 HGVKFIkqfVPIKVELLEEGTPGrIKVTAKSTQGDQIIEDEYntVLIAVGRDACTRNIGLEKIGVKInERnGKIPVSDEE 421
Cdd:PRK06416 226 RGIKIK---TGAKAKKVEQTDDG-VTVTLEDGGKEETLEADY--VLVAVGRRPNTENLGLEELGVKT-DR-GFIEVDEQL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 422 QTSVPHVYAIGDILdGKLELTPVAIQAGRLLARRLyRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYGEenLEVY 501
Cdd:PRK06416 298 RTNVPNIYAIGDIV-GGPMLAHKASAEGIIAAEAI-AGNPHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVV 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 502 HTLFwplewTVPSR----DNNTCFAKIICNKQDNdRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEI 577
Cdd:PRK06416 374 KFPF-----AGNGKalalGETDGFVKLIFDKKDG-EVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEA 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
112-598 |
6.51e-68 |
|
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: 227.69 E-value: 6.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpQGTswgLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWEYEE 191
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPPFGGLAATV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 192 QVkhNWETMREAIQNYIGSL-NWGYRVALRDKQVRYENAYGEFVESHKIKAtnkKGKESFFTAEKFVVATGERPRYLNIP 270
Cdd:TIGR02053 72 AV--DFGELLEGKREVVEELrHEKYEDVLSSYGVDYLRGRARFKDPKTVKV---DLGREVRGAKRFLIATGARPAIPPIP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 271 GDKE--YcITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRS-IFLRGFDQEMANRAGAYMETHGVKFI 347
Cdd:TIGR02053 147 GLKEagY-LTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 348 KQfVPIKVELLEEgtpGRIKVTAKSTQGDQIIEDEYntVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQTSVPH 427
Cdd:TIGR02053 226 TS-AQVKAVSVRG---GGKIITVEKPGGQGEVEADE--LLVATGRRPNTDGLGLEKAGVKLDER-GGILVDETLRTSNPG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 428 VYAIGDILDGkLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEIYGEENLEVYHTLFWP 507
Cdd:TIGR02053 299 IYAAGDVTGG-LQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 508 LEWTvpsRDNNTCFAKIICNkQDNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAE-------IFTT 580
Cdd:TIGR02053 378 RARI---NRDTRGFIKLVAE-PGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEglklaaqTFYR 453
|
490
....*....|....*...
gi 1214874590 581 mdtskssggDISQKGCUG 598
Cdd:TIGR02053 454 ---------DVSKLSCCA 462
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
112-449 |
6.79e-62 |
|
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: 206.79 E-value: 6.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpqgtswgLGGTCVNVGCIPKKLMHQAAILGQSLKDsrkfgweyee 191
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE------------DEGTCPYGGCVLSKALLGAAEAPEIASL---------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 192 qvkhnWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVESHKikatnKKGKESFFTAEKFVVATGERPRYLNIPG 271
Cdd:pfam07992 59 -----WADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEEL-----VDGDGETITYDRLVIATGARPRLPPIPG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 272 DKEYC------ITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRS-IFLRGFDQEMANRAGAYMETHGV 344
Cdd:pfam07992 129 VELNVgflvrtLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALdRLLRAFDEEISAALEKALEKNGV 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 345 KFIKQFVPIKVElleeGTPGRIKVTAKstQGDQIiedEYNTVLIAVGRDACTRniGLEKIGVKINERNGkIPVSDEEQTS 424
Cdd:pfam07992 209 EVRLGTSVKEII----GDGDGVEVILK--DGTEI---DADLVVVAIGRRPNTE--LLEAAGLELDERGG-IVVDEYLRTS 276
|
330 340
....*....|....*....|....*
gi 1214874590 425 VPHVYAIGDILDGKLELTPVAIQAG 449
Cdd:pfam07992 277 VPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
112-576 |
6.15e-59 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 203.90 E-value: 6.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAASFGKKVMVLdfvvptpqGTSWgLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWEYEE 191
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALI--------ERGL-LGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 192 QVKHNWETMREAIQNYIGSLNWGYRVALRDkqvrYENA---YGE--FVESHKIKATNKKgkesfFTAEKFVVATGERPRY 266
Cdd:PRK06370 77 PVSVDFKAVMARKRRIRARSRHGSEQWLRG----LEGVdvfRGHarFESPNTVRVGGET-----LRAKRIFINTGARAAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 267 LNIPG--DKEYcITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRS-IFLRGFDQEMANRAGAYMETHG 343
Cdd:PRK06370 148 PPIPGldEVGY-LTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGpRLLPREDEDVAAAVREILEREG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 344 VKFIKQFVPIKVelleEGTPGRIKVTAKSTQGDQIIE-DEyntVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQ 422
Cdd:PRK06370 227 IDVRLNAECIRV----ERDGDGIAVGLDCNGGAPEITgSH---ILVAVGRVPNTDDLGLEAAGVETDAR-GYIKVDDQLR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 423 TSVPHVYAIGDIlDGKLELTPVAIQAGRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEiYGeENLEVYh 502
Cdd:PRK06370 299 TTNPGIYAAGDC-NGRGAFTHTAYNDARIVAANLLDGGRRKVSDRIVPYATYTDPPLARVGMTEAEARK-SG-RRVLVG- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 503 tlfwplewTVPSRD--------NNTCFAKIICnKQDNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTC 574
Cdd:PRK06370 375 --------TRPMTRvgravekgETQGFMKVVV-DADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTV 445
|
..
gi 1214874590 575 AE 576
Cdd:PRK06370 446 SE 447
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
111-577 |
1.27e-50 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 181.66 E-value: 1.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 111 DYDLIVIGGGSGGLACSKEAASFGKKVMVLDfVVPTPQGTSwGLGGTCVNVGCIPKK-LMHQAAILGQSLKDSRKFGWEY 189
Cdd:PRK06327 4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIE-AWKNPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGIHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 190 EEqVKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFV----ESHKIKATNKKGKEsfFTAEKFVVATGERPR 265
Cdd:PRK06327 82 DG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktdAGYEIKVTGEDETV--ITAKHVIIATGSEPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 266 YL-NIPGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVM-VRSIFLRGFDQEMANRAGAYMETHG 343
Cdd:PRK06327 159 HLpGVPFDNKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeALPAFLAAADEQVAKEAAKAFTKQG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 344 VKFIkqfVPIKVELLEEGTPGrIKVTAKSTQGDQIIEdEYNTVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQT 423
Cdd:PRK06327 239 LDIH---LGVKIGEIKTGGKG-VSVAYTDADGEAQTL-EVDKLIVSIGRVPNTDGLGLEAVGLKLDER-GFIPVDDHCRT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 424 SVPHVYAIGDILDGKLeLTPVAIQAGRLLARRLyRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEiygeENLEVYHT 503
Cdd:PRK06327 313 NVPNVYAIGDVVRGPM-LAHKAEEEGVAVAERI-AGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKA----EGVEYKAG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 504 LFwplewtvPSRDNN--------TCFAKIICNKQdNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCA 575
Cdd:PRK06327 387 KF-------PFMANGralamgepDGFVKIIADAK-TDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLS 458
|
..
gi 1214874590 576 EI 577
Cdd:PRK06327 459 EV 460
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
111-577 |
9.23e-45 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 165.13 E-value: 9.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 111 DYDLIVIGGGSGGLACSKEAAsfGKKVMVLDfvvptpQGTswgLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGweYE 190
Cdd:PRK07846 1 HYDLIIIGTGSGNSILDERFA--DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 191 EQVKH-NWETMREAIQNYIGSLNWG---YRvALRDKQVRYENAYGEFVESHKIKAtnkkGKESFFTAEKFVVATGERPRY 266
Cdd:PRK07846 68 AELDGvRWPDIVSRVFGRIDPIAAGgeeYR-GRDTPNIDVYRGHARFIGPKTLRT----GDGEEITADQVVIAAGSRPVI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 267 LNIPGDKE--YcITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRSIF-LRGFDQEMANRagaYMETHG 343
Cdd:PRK07846 143 PPVIADSGvrY-HTSDTIMRLPELPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRlLRHLDDDISER---FTELAS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 344 VKFikqfvpiKVELLE-----EGTPGRIKVTaksTQGDQIIEDEynTVLIAVGRDACTRNIGLEKIGVKINErNGKIPVS 418
Cdd:PRK07846 219 KRW-------DVRLGRnvvgvSQDGSGVTLR---LDDGSTVEAD--VLLVATGRVPNGDLLDAAAAGVDVDE-DGRVVVD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 419 DEEQTSVPHVYAIGDILDgKLELTPVAIQAGRLLARRLYRGSK-VKCDYINVPTTVFTPLEYGCCGYAEEKAIEI----- 492
Cdd:PRK07846 286 EYQRTSAEGVFALGDVSS-PYQLKHVANHEARVVQHNLLHPDDlIASDHRFVPAAVFTHPQIASVGLTENEARAAgldit 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 493 ----------YGeenlevyhtlfWPLEWTvpsrdnnTCFAKIICNKqDNDRVIGFHVLGPNAGEITQGFGAAMKCGLT-K 561
Cdd:PRK07846 365 vkvqnygdvaYG-----------WAMEDT-------TGFVKLIADR-DTGRLLGAHIIGPQASTLIQPLIQAMSFGLDaR 425
|
490
....*....|....*.
gi 1214874590 562 EKLDETIGIHPTCAEI 577
Cdd:PRK07846 426 EMARGQYWIHPALPEV 441
|
|
| GRX_GRXh_1_2_like |
cd03419 |
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of ... |
21-102 |
2.04e-41 |
|
Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.
Pssm-ID: 239511 [Multi-domain] Cd Length: 82 Bit Score: 144.22 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 21 RVMVFSKSFCPYCDRVKDLFSSLGAEYHSLELDECDDGSDIQEALQELTGQKTVPNVFVNKTHVGGCDKTLQAHKDGSLA 100
Cdd:cd03419 1 PVVVFSKSYCPYCKRAKSLLKELGVKPAVVELDQHEDGSEIQDYLQELTGQRTVPNVFIGGKFIGGCDDLMALHKSGKLV 80
|
..
gi 1214874590 101 KL 102
Cdd:cd03419 81 KL 82
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
109-576 |
5.01e-41 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 154.93 E-value: 5.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 109 TYDYDLIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpqgTSWGLGGTCVNVGCIPKKlmhqaailgqslkdsrkfgwe 188
Cdd:PRK05249 3 MYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSK--------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 189 yeeqvkhnweTMREAIQNYIG----SLNWGYRVALR--------------DKQVRY-ENAY-----------GEFVESHK 238
Cdd:PRK05249 54 ----------ALREAVLRLIGfnqnPLYSSYRVKLRitfadllaradhviNKQVEVrRGQYernrvdliqgrARFVDPHT 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 239 IKATNKKGKESFFTAEKFVVATGERP-RYLNIPGDKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATV 317
Cdd:PRK05249 124 VEVECPDGEVETLTADKIVIATGSRPyRPPDVDFDHPRIYDSDSILSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 318 MVRSIFLRGF-DQEMANRAGAYMETHGVKFI-KQfvpiKVELLEEGTPGRIkVTAKStqGDQIIEDeynTVLIAVGRDAC 395
Cdd:PRK05249 204 INTRDRLLSFlDDEISDALSYHLRDSGVTIRhNE----EVEKVEGGDDGVI-VHLKS--GKKIKAD---CLLYANGRTGN 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 396 TRNIGLEKIGVKINERnGKIPVSDEEQTSVPHVYAIGDILdGKLELTPVAIQAGRLLARRLYRGSKVKcdYIN-VPTTVF 474
Cdd:PRK05249 274 TDGLNLENAGLEADSR-GQLKVNENYQTAVPHIYAVGDVI-GFPSLASASMDQGRIAAQHAVGEATAH--LIEdIPTGIY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 475 TPLEYGCCGYAEEKAIEI---YgeenlEVYHTLFWPLewtvpSRDN----NTCFAKIICNKqDNDRVIGFHVLGPNAGE- 546
Cdd:PRK05249 350 TIPEISSVGKTEQELTAAkvpY-----EVGRARFKEL-----ARAQiagdNVGMLKILFHR-ETLEILGVHCFGERATEi 418
|
490 500 510
....*....|....*....|....*....|..
gi 1214874590 547 --ITQgfgAAMKCGLTKEKLDETIGIHPTCAE 576
Cdd:PRK05249 419 ihIGQ---AIMEQKGTIEYFVNTTFNYPTMAE 447
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
112-576 |
1.66e-39 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 149.90 E-value: 1.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAASFGKKVMVLdfvvptpQGTSWGLGGTCVNVGCIPKKLMHQAAilgqslkdsrKFGWEYEE 191
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVALV-------EESKAMYGGTCINIGCIPTKTLLVAA----------EKNLSFEQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 192 QVKHnwetmREAIQNYIGSLNWGyrvALRDKQVRYENAYGEFVESHKIKATNKKGKESfFTAEKFVVATGERPRYLNIPG 271
Cdd:PRK07251 67 VMAT-----KNTVTSRLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIE-LTAETIVINTGAVSNVLPIPG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 272 --DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVM-VRSIFLRGFDQEMANRAGAYMETHGVKFIK 348
Cdd:PRK07251 138 laDSKHVYDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 349 QfvpikvelleegtpgrIKVTAKSTQGDQII---EDE---YNTVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQ 422
Cdd:PRK07251 218 N----------------AHTTEVKNDGDQVLvvtEDEtyrFDALLYATGRKPNTEPLGLENTDIELTER-GAIKVDDYCQ 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 423 TSVPHVYAIGDIlDGKLELTPVAIQAGRLLARRLY-RGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEI---YGEENL 498
Cdd:PRK07251 281 TSVPGVFAVGDV-NGGPQFTYISLDDFRIVFGYLTgDGSYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAglpYAVKEL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 499 EVYhtlfwplewTVPSRDNNTCFA---KIICNKqDNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCA 575
Cdd:PRK07251 360 LVA---------AMPRAHVNNDLRgafKVVVNT-ETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMA 429
|
.
gi 1214874590 576 E 576
Cdd:PRK07251 430 E 430
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
111-577 |
2.36e-38 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 147.21 E-value: 2.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 111 DYDLIVIGGGSGGLACSKEAAsfGKKVMVLDfvvptpQGTswgLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWEYE 190
Cdd:TIGR03452 2 HYDLIIIGTGSGNSIPDPRFA--DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLGIDAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 191 EQvKHNWETMREAI-QNYIGSLNWG---YRVALRDKQVRYENAYGEFVESHKIKAtnkkGKESFFTAEKFVVATGERPR- 265
Cdd:TIGR03452 71 ID-SVRWPDIVSRVfGDRIDPIAAGgedYRRGDETPNIDVYDGHARFVGPRTLRT----GDGEEITGDQIVIAAGSRPYi 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 266 --YLNIPGDKEYciTSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRS-IFLRGFDQEMANRagaYMETH 342
Cdd:TIGR03452 146 ppAIADSGVRYH--TNEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRStKLLRHLDEDISDR---FTEIA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 343 GVKFikqfvpikvelleEGTPGRiKVTAKSTQGDQI---IED----EYNTVLIAVGRDACTRNIGLEKIGVKINErNGKI 415
Cdd:TIGR03452 221 KKKW-------------DIRLGR-NVTAVEQDGDGVtltLDDgstvTADVLLVATGRVPNGDLLDAEAAGVEVDE-DGRI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 416 PVSDEEQTSVPHVYAIGDIlDGKLELTPVAIQAGRLLARRLYR-GSKVKCDYINVPTTVFTPLEYGCCGYAEEKA----- 489
Cdd:TIGR03452 286 KVDEYGRTSARGVWALGDV-SSPYQLKHVANAEARVVKHNLLHpNDLRKMPHDFVPSAVFTHPQIATVGLTEQEAreagh 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 490 -----IEIYGeenlEVYHTlfWPLEWTvpsrdnnTCFAKIICNKqDNDRVIGFHVLGPNAGEITQGFGAAMKCGLT-KEK 563
Cdd:TIGR03452 365 ditvkIQNYG----DVAYG--WAMEDT-------TGFCKLIADR-DTGKLLGAHIIGPQASSLIQPLITAMAFGLDaREM 430
|
490
....*....|....
gi 1214874590 564 LDETIGIHPTCAEI 577
Cdd:TIGR03452 431 ARKQYWIHPALPEV 444
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
469-581 |
1.15e-36 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 132.29 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 469 VPTTVFTPLEYGCCGYAEEKAIEIYGEenLEVYHTLFWPLEWTVPSRDNNtCFAKIICNKQDnDRVIGFHVLGPNAGEIT 548
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADRET-GKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 1214874590 549 QGFGAAMKCGLTKEKLDETIGIHPTCAEIFTTM 581
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| GRX_euk |
TIGR02180 |
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize ... |
22-103 |
8.22e-35 |
|
Glutaredoxin; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model represents eukaryotic glutaredoxins and includes sequences from fungi, plants and metazoans as well as viruses.
Pssm-ID: 274016 [Multi-domain] Cd Length: 83 Bit Score: 126.21 E-value: 8.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 22 VMVFSKSFCPYCDRVKDLFSSLGAE-YHSLELDECDDGSDIQEALQELTGQKTVPNVFVNKTHVGGCDKTLQAHKDGSLA 100
Cdd:TIGR02180 1 VVVFSKSYCPYCKKAKEILAKLNVKpYEVVELDQLSNGSEIQDYLEEITGQRTVPNIFINGKFIGGCSDLLALYKNGKLA 80
|
...
gi 1214874590 101 KLL 103
Cdd:TIGR02180 81 ELL 83
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
116-597 |
8.53e-35 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 138.75 E-value: 8.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 116 VIGGGSGGLACSKEAASFGKKVMVLDfvvptpQGTswgLGGTCVNVGCIPKKLMHQAAILGQSLKDSrkfgweyeeqvkh 195
Cdd:PRK13748 103 VIGSGGAAMAAALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRES------------- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 196 nweTMREAIQNYIGSLNwgyRVALRDKQ---------VRYEN------------AYGEFVESHKIKATNKKGKESFFTAE 254
Cdd:PRK13748 161 ---PFDGGIAATVPTID---RSRLLAQQqarvdelrhAKYEGildgnpaitvlhGEARFKDDQTLIVRLNDGGERVVAFD 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 255 KFVVATGERPRYLNIPGDKE--YCITSDDLFSlPYCPGKTLVVGASYVALECAGFLAGIGLDATVMVRSIFLRGFDQEMA 332
Cdd:PRK13748 235 RCLIATGASPAVPPIPGLKEtpYWTSTEALVS-DTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIG 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 333 NRAGAYMETHGVKFIKQFVPIKV-----ELLEEGTPGRIKvtakstqGDQIiedeyntvLIAVGRDACTRNIGLEKIGVK 407
Cdd:PRK13748 314 EAVTAAFRAEGIEVLEHTQASQVahvdgEFVLTTGHGELR-------ADKL--------LVATGRAPNTRSLALDAAGVT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 408 INERnGKIPVSDEEQTSVPHVYAIGDILDgKLELTPVAIQAGRLLARRLyRGSKVKCDYINVPTTVFTPLEYGCCGYAEE 487
Cdd:PRK13748 379 VNAQ-GAIVIDQGMRTSVPHIYAAGDCTD-QPQFVYVAAAAGTRAAINM-TGGDAALDLTAMPAVVFTDPQVATVGYSEA 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 488 KAieiyGEENLE-VYHTLfwPLEwTVPSRDNN---TCFAKIICNKQdNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEK 563
Cdd:PRK13748 456 EA----HHDGIEtDSRTL--TLD-NVPRALANfdtRGFIKLVIEEG-SGRLIGVQAVAPEAGELIQTAALAIRNRMTVQE 527
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1214874590 564 LDETIGIHPT-------CAEIFTTmdtskssggDISQKGCU 597
Cdd:PRK13748 528 LADQLFPYLTmveglklAAQTFNK---------DVKQLSCC 559
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
110-578 |
5.03e-29 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 119.88 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 110 YDYDLIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpQGTSWgLGGTCVNVGCIP-KKLMHQAailgqslkdsrkfgwe 188
Cdd:NF040477 2 NHYQAIIIGFGKAGKTLAATLAKAGWRVAIIE------QSAQM-YGGTCINIGCIPtKTLVHDA---------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 189 yeeQVKHNWETmreAIQNYIGSLNWgyrvaLRDK---------QVRYENAYGEFVESHKIKATNKKGkESFFTAEKFVVA 259
Cdd:NF040477 59 ---EQHQDFST---AMQRKSSVVGF-----LRDKnyhnladldNVDVINGRAEFIDNHTLRVFQADG-EQELRGEKIFIN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 260 TGERPRYLNIPGDKEY--CITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVM-VRSIFLRGFDQEMANRAG 336
Cdd:NF040477 127 TGAQSVLPPIPGLTTTpgVYDSTGLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFeAAELFLPREDRDIAQAIA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 337 AYMETHGVKFIkqfVPIKVELLEEgTPGRIKVtakSTQGDQIIEDeynTVLIAVGRDACTRNIGLEKIGVKINERnGKIP 416
Cdd:NF040477 207 TILQDQGVELI---LNAQVQRVSS-HEGEVQL---ETAEGVLTVD---ALLVASGRKPATAGLQLQNAGVAVNER-GAIV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 417 VSDEEQTSVPHVYAIGDIlDGKLELTPVAIQAGRLLARRLY-RGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAIEiYGE 495
Cdd:NF040477 276 VDKYLRTTADNIWAMGDV-TGGLQFTYISLDDFRIVRDSLLgEGKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARA-SGA 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 496 ENLEVyhTLfwPLEwTVPS----RDNNTCFAKIICNKqdNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIH 571
Cdd:NF040477 354 DIQVV--TL--PVA-AIPRarvmNDTRGVLKAVVDNK--TQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTH 426
|
....*..
gi 1214874590 572 PTCAEIF 578
Cdd:NF040477 427 PTMSESL 433
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
112-580 |
1.77e-28 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 120.40 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAASFGKKVMVLdfvvptpQGTSWGLGGTCVNVGCIPKKLMHQAAILGQSLKDSRK------- 184
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIF-------TGDDDSIGGTCVNVGCIPSKALLYATGKYRELKNLAKlytygiy 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 185 ---FGWEYEEQVKHNWET----------MREAIQNYIGSLNWGYRVALRDK---------QVRYENayGEFVESHKIKAt 242
Cdd:PTZ00153 190 tnaFKNGKNDPVERNQLVadtvqiditkLKEYTQSVIDKLRGGIENGLKSKkfcknsehvQVIYER--GHIVDKNTIKS- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 243 NKKGKEsfFTAEKFVVATGERPrylNIPG----DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDAT-V 317
Cdd:PTZ00153 267 EKSGKE--FKVKNIIIATGSTP---NIPDnievDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVsF 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 318 MVRSIFLRGFDQEMANragaYMEThgvKFIKQfVPIKVELLEE---------GTPGRIKVTAKSTQGD--------QIIE 380
Cdd:PTZ00153 342 EYSPQLLPLLDADVAK----YFER---VFLKS-KPVRVHLNTLieyvragkgNQPVIIGHSERQTGESdgpkknmnDIKE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 381 DEYNTVLIAVGRDACTRNIGLEKIGVKINErnGKIPVSD------EEQTSVPHVYAIGDIlDGKLELTPVA-IQAGRLLA 453
Cdd:PTZ00153 414 TYVDSCLVATGRKPNTNNLGLDKLKIQMKR--GFVSVDEhlrvlrEDQEVYDNIFCIGDA-NGKQMLAHTAsHQALKVVD 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 454 RRLYRGSK-VKCD----------YINVPTTVFTPLEYGCCGYAEEKAIEIYGEENL--EVYH-----TLFWPLEWTVPSR 515
Cdd:PTZ00153 491 WIEGKGKEnVNINvenwaskpiiYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVgvEISFykansKVLCENNISFPNN 570
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1214874590 516 DNNTCFAKIICN-------------KQDNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIFTT 580
Cdd:PTZ00153 571 SKNNSYNKGKYNtvdntegmvkivyLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVLDA 648
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
112-458 |
1.97e-27 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 112.52 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAASFGKKVMVLDFVVPTPQGTSWglggTCV-NVGCIPKKLMhqaailgqslkdsrkfGWEYE 190
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATT----KEIeNYPGFPEGIS----------------GPELA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 191 EQvkhnwetMREAIQNYigslnwgyrvalrDKQVRYENAYGEFVESHKIKATNKKGKEsfFTAEKFVVATGERPRYLNIP 270
Cdd:COG0492 61 ER-------LREQAERF-------------GAEILLEEVTSVDKDDGPFRVTTDDGTE--YEAKAVIIATGAGPRKLGLP 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 271 GDKE-------YCITSDdlfsLPYCPGKT-LVVGASYVALECAGFLAGIGLDATVMVRSIFLRGfDQEMANRAgayMETH 342
Cdd:COG0492 119 GEEEfegrgvsYCATCD----GFFFRGKDvVVVGGGDSALEEALYLTKFASKVTLIHRRDELRA-SKILVERL---RANP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 343 GVKFIKQFVPIKVElleeGTpGRI-KVTAKSTQGDQIIEDEYNTVLIAVGRDACTRniGLEKIGVKINErNGKIPVSDEE 421
Cdd:COG0492 191 KIEVLWNTEVTEIE----GD-GRVeGVTLKNVKTGEEKELEVDGVFVAIGLKPNTE--LLKGLGLELDE-DGYIVVDEDM 262
|
330 340 350
....*....|....*....|....*....|....*..
gi 1214874590 422 QTSVPHVYAIGDILDGKLELTPVAIQAGRLLARRLYR 458
Cdd:COG0492 263 ETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAAR 299
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
112-576 |
2.04e-25 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 109.33 E-value: 2.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpQGTSWgLGGTCVNVGCIPKK-LMHQAAILGQSLKDSRKfgweye 190
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIE------QSNAM-YGGTCINIGCIPTKtLVHDAQQHTDFVRAIQR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 191 eqvkhnwetmREAIQNYIGSLNWGYRVALRDKQVRYENAygEFVESHKIKaTNKKGKESFFTAEKFVVATGERPRYLNIP 270
Cdd:PRK08010 71 ----------KNEVVNFLRNKNFHNLADMPNIDVIDGQA--EFINNHSLR-VHRPEGNLEIHGEKIFINTGAQTVVPPIP 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 271 G--DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDATVM-VRSIFLRGFDQEMANRAGAYMETHGVKFI 347
Cdd:PRK08010 138 GitTTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDII 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 348 kqfVPIKVELL--EEGtpgriKVTAKSTQGDQIIEdeynTVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQTSV 425
Cdd:PRK08010 218 ---LNAHVERIshHEN-----QVQVHSEHAQLAVD----ALLIASGRQPATASLHPENAGIAVNER-GAIVVDKYLHTTA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 426 PHVYAIGDILDGkLELTPVAIQAGRLLARRLY-RGSKVKCDYINVPTTVFTPLEYGCCGYAEEKAieiygEENLEVYHTL 504
Cdd:PRK08010 285 DNIWAMGDVTGG-LQFTYISLDDYRIVRDELLgEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQA-----RESGADIQVV 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1214874590 505 FWPLEWTVPSR---DNNTCFAKIICNKqdNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAE 576
Cdd:PRK08010 359 TLPVAAIPRARvmnDTRGVLKAIVDNK--TQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSE 431
|
|
| GRX_family |
cd02066 |
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ... |
21-95 |
2.54e-24 |
|
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: 96.38 E-value: 2.54e-24
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1214874590 21 RVMVFSKSFCPYCDRVKDLFSSLGAEYHslELDECDDGsDIQEALQELTGQKTVPNVFVNKTHVGGCDKTLQAHK 95
Cdd:cd02066 1 KVVVFSKSTCPYCKRAKRLLESLGIEFE--EIDILEDG-ELREELKELSGWPTVPQIFINGEFIGGYDDLKALHE 72
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
114-572 |
2.35e-21 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 97.24 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 114 LIVIGGGSGGLACSKEAASFGKKVMVLDfvvptpqgtSWGLGGTCVNVGCIPKKLMHQAAILGQSLKDSRKFGWEYE--E 191
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIddG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 192 QVKHNWETMREAIQNYIGSLNWGYRVALRDKQVRYENAYGEFVE----SHKIKATNKKGKESFFTAEKFVVATGERPRYL 267
Cdd:PRK07845 75 EARVDLPAVNARVKALAAAQSADIRARLEREGVRVIAGRGRLIDpglgPHRVKVTTADGGEETLDADVVLIATGASPRIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 268 niPG---DKEYCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDAT-VMVRSIFLRGFDQEMANRAGAYMETHG 343
Cdd:PRK07845 155 --PTaepDGERILTWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDADAAEVLEEVFARRG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 344 VKFIKQFVPIKVELLEEGtpgrikVTAKSTQGDQIiedEYNTVLIAVGRDACTRNIGLEKIGVKINERnGKIPVSDEEQT 423
Cdd:PRK07845 233 MTVLKRSRAESVERTGDG------VVVTLTDGRTV---EGSHALMAVGSVPNTAGLGLEEAGVELTPS-GHITVDRVSRT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 424 SVPHVYAIGDIlDGKLELTPVAIQAGRL-LARRLyrGSKVK-CDYINVPTTVFTPLEYGCCGYAeEKAIEiYGEENLEVY 501
Cdd:PRK07845 303 SVPGIYAAGDC-TGVLPLASVAAMQGRIaMYHAL--GEAVSpLRLKTVASNVFTRPEIATVGVS-QAAID-SGEVPARTV 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1214874590 502 htlfwplewTVPSRDN--------NTCFAKIICnKQDNDRVIGFHVLGPNAGEITQGFGAAMKCGLTKEKLDETIGIHP 572
Cdd:PRK07845 378 ---------MLPLATNprakmsglRDGFVKLFC-RPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYP 446
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
257-456 |
9.48e-21 |
|
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: 93.34 E-value: 9.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 257 VVATGERPRYLNIPGdkeycITSDDLFSL------PYC--------PGKTLVVGASYVALECAGFLAGIGLDATVMVRS- 321
Cdd:COG0446 83 VLATGARPRPPPIPG-----LDLPGVFTLrtlddaDALrealkefkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAp 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 322 IFLRGFDQEMANRAGAYMETHGVKFIKQFVPIKVElleegtpGRIKVTAKSTQGDQIiedEYNTVLIAVGrdacTR-NIG 400
Cdd:COG0446 158 RLLGVLDPEMAALLEEELREHGVELRLGETVVAID-------GDDKVAVTLTDGEEI---PADLVVVAPG----VRpNTE 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1214874590 401 L-EKIGVKINERNGkIPVSDEEQTSVPHVYAIGD------ILDGK---LELTPVAIQAGRLLARRL 456
Cdd:COG0446 224 LaKDAGLALGERGW-IKVDETLQTSDPDVYAAGDcaevphPVTGKtvyIPLASAANKQGRVAAENI 288
|
|
| Glutaredoxin |
pfam00462 |
Glutaredoxin; |
22-84 |
7.80e-18 |
|
Glutaredoxin;
Pssm-ID: 425695 [Multi-domain] Cd Length: 60 Bit Score: 77.54 E-value: 7.80e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1214874590 22 VMVFSKSFCPYCDRVKDLFSSLGAEYHSLELDEcddGSDIQEALQELTGQKTVPNVFVNKTHV 84
Cdd:pfam00462 1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDVDE---DPEIREELKELSGWPTVPQVFIDGEHI 60
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
257-460 |
1.14e-17 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 85.19 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 257 VVATGERPRYLNIPG-DKEYCI---TSDDLFSL-PYCPGKT--LVVGASYVALECAGFLAGIGLDATVMVRS--IFLRGF 327
Cdd:COG1251 103 VLATGSRPRVPPIPGaDLPGVFtlrTLDDADALrAALAPGKrvVVIGGGLIGLEAAAALRKRGLEVTVVERAprLLPRQL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 328 DQEMANRAGAYMETHGVKFIKQfvpikVELLE-EGTPGRIKVTAKStqGDQIIEDeynTVLIAVGrdacTR-NIGL-EKI 404
Cdd:COG1251 183 DEEAGALLQRLLEALGVEVRLG-----TGVTEiEGDDRVTGVRLAD--GEELPAD---LVVVAIG----VRpNTELaRAA 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 405 GVKINerNGkIPVSDEEQTSVPHVYAIGDI------LDGK--LELTPVAIQAGRLLARRL------YRGS 460
Cdd:COG1251 249 GLAVD--RG-IVVDDYLRTSDPDIYAAGDCaehpgpVYGRrvLELVAPAYEQARVAAANLaggpaaYEGS 315
|
|
| GRX_bact |
TIGR02181 |
Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
22-103 |
3.25e-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: 76.53 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 22 VMVFSKSFCPYCDRVKDLFSSLGAEYHSLELDecDDGSDIQEaLQELTGQKTVPNVFVNKTHVGGCDKTLQAHKDGSLAK 101
Cdd:TIGR02181 1 VTIYTKPYCPYCTRAKALLSSKGVTFTEIRVD--GDPALRDE-MMQRSGRRTVPQIFIGDVHVGGCDDLYALDREGKLDP 77
|
..
gi 1214874590 102 LL 103
Cdd:TIGR02181 78 LL 79
|
|
| GrxC |
COG0695 |
Glutaredoxin [Posttranslational modification, protein turnover, chaperones]; |
21-104 |
9.11e-16 |
|
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440459 [Multi-domain] Cd Length: 74 Bit Score: 72.15 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 21 RVMVFSKSFCPYCDRVKDLFSSLGAEYHSLELDEcdDGSDIQEaLQELTGQKTVPNVFVNKTHVGGCDktlqahkDGSLA 100
Cdd:COG0695 1 KVTLYTTPGCPYCARAKRLLDEKGIPYEEIDVDE--DPEAREE-LRERSGRRTVPVIFIGGEHLGGFD-------EGELD 70
|
....
gi 1214874590 101 KLLD 104
Cdd:COG0695 71 ALLA 74
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
291-367 |
3.07e-15 |
|
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: 70.70 E-value: 3.07e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1214874590 291 KTLVVGASYVALECAGFLAGIGLDATVMVRSI-FLRGFDQEMANRAGAYMETHGVKFIKQFVPIKVELLEEGTPGRIK 367
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDrLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLT 78
|
|
| GlrX-like_plant |
TIGR02189 |
Glutaredoxin-like family; This family of glutaredoxin-like proteins is aparrently limited to ... |
13-103 |
4.18e-15 |
|
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: 71.33 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 13 VKELIDSNRVMVFSKSFCPYCDRVKDLFSSLGAEYHSLELDECDDGSDIQEALQELTGQKTVPNVFVNKTHVGGCDKTLQ 92
Cdd:TIGR02189 1 VRRMVSEKAVVIFSRSSCCMCHVVKRLLLTLGVNPAVHEIDKEPAGKDIENALSRLGCSPAVPAVFVGGKLVGGLENVMA 80
|
90
....*....|.
gi 1214874590 93 AHKDGSLAKLL 103
Cdd:TIGR02189 81 LHISGSLVPML 91
|
|
| GRX_GRXb_1_3_like |
cd03418 |
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ... |
22-88 |
2.43e-14 |
|
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: 68.00 E-value: 2.43e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1214874590 22 VMVFSKSFCPYCDRVKDLFSSLGAEYhslELDECDDGSDIQEALQELTGQ-KTVPNVFVNKTHVGGCD 88
Cdd:cd03418 2 VEIYTKPNCPYCVRAKALLDKKGVDY---EEIDVDGDPALREEMINRSGGrRTVPQIFIGDVHIGGCD 66
|
|
| PRK10638 |
PRK10638 |
glutaredoxin 3; Provisional |
22-103 |
2.25e-12 |
|
glutaredoxin 3; Provisional
Pssm-ID: 182607 [Multi-domain] Cd Length: 83 Bit Score: 62.91 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 22 VMVFSKSFCPYCDRVKDLFSSLGAEYHSLELDecdDGSDIQEALQELTGQKTVPNVFVNKTHVGGCDKTLQAHKDGSLAK 101
Cdd:PRK10638 4 VEIYTKATCPFCHRAKALLNSKGVSFQEIPID---GDAAKREEMIKRSGRTTVPQIFIDAQHIGGCDDLYALDARGGLDP 80
|
..
gi 1214874590 102 LL 103
Cdd:PRK10638 81 LL 82
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
257-481 |
1.31e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 63.61 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 257 VVATGERPRYLNIPGDKEYCI---TSDDLFSL------------PYCPGKTLVVGASYVALECAGFLAGIgLDATVMVRS 321
Cdd:COG1252 102 VIATGSVTNFFGIPGLAEHALplkTLEDALALrerllaaferaeRRRLLTIVVVGGGPTGVELAGELAEL-LRKLLRYPG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 322 I---------------FLRGFDQEMANRAGAYMETHGVKFIKQFvpiKVElleEGTPGRIKVTakstQGDQIiedEYNTV 386
Cdd:COG1252 181 IdpdkvritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGT---RVT---EVDADGVTLE----DGEEI---PADTV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 387 LIAVGRDA--CTRNIGLEKigvkinERNGKIPVsDEEQTSV--PHVYAIGD---ILDGKLELTP----VAIQAGRLLARR 455
Cdd:COG1252 248 IWAAGVKAppLLADLGLPT------DRRGRVLV-DPTLQVPghPNVFAIGDcaaVPDPDGKPVPktaqAAVQQAKVLAKN 320
|
250 260
....*....|....*....|....*.
gi 1214874590 456 LYRGSKVKcdyinvPTTVFTPLEYGC 481
Cdd:COG1252 321 IAALLRGK------PLKPFRYRDKGC 340
|
|
| GRX_PICOT_like |
cd03028 |
Glutaredoxin (GRX) family, PKC-interacting cousin of TRX (PICOT)-like subfamily; composed of ... |
13-100 |
3.48e-10 |
|
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: 56.73 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 13 VKELIDSNRVMVFSKS-----FCPYCDRVKDLFSSLGAEYHS---LElDEcddgsDIQEALQELTGQKTVPNVFVNKTHV 84
Cdd:cd03028 1 IKKLIKENPVVLFMKGtpeepRCGFSRKVVQILNQLGVDFGTfdiLE-DE-----EVRQGLKEYSNWPTFPQLYVNGELV 74
|
90
....*....|....*.
gi 1214874590 85 GGCDKTLQAHKDGSLA 100
Cdd:cd03028 75 GGCDIVKEMHESGELQ 90
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
254-598 |
2.39e-09 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 60.23 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 254 EKFVVATGERPRYLNIPG-DKEYCI---TSDDLFSLPYCPGKTL---VVGASYVALECAGFLAGIGLDATVMVRSIFL-- 324
Cdd:TIGR02374 98 DKLILATGSYPFILPIPGaDKKGVYvfrTIEDLDAIMAMAQRFKkaaVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLma 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 325 RGFDQEMANRAGAYMETHGVKFI--KQfvpiKVELLEEGTPGRIKVTakstQGDQIiedEYNTVLIAVG---RDACTRNI 399
Cdd:TIGR02374 178 KQLDQTAGRLLQRELEQKGLTFLleKD----TVEIVGATKADRIRFK----DGSSL---EADLIVMAAGirpNDELAVSA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 400 GLEKigvkinerNGKIPVSDEEQTSVPHVYAIGDildgkleltpVAIQAGRL--LARRLYRGSKVKCDYI-NVPTTVF-- 474
Cdd:TIGR02374 247 GIKV--------NRGIIVNDSMQTSDPDIYAVGE----------CAEHNGRVygLVAPLYEQAKVLADHIcGVECEEYeg 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 475 ----TPL-----EYGCCGYAEE----KAIEIYGEENlEVYHTLFWplewtvpsRDNNTCFAKIICNKQDNDRVigFHVLG 541
Cdd:TIGR02374 309 sdlsAKLkllgvDVWSAGDAQEtertTSIKIYDEQK-GIYKKLVL--------SDDKLLGAVLFGDTSDYGRL--LDMVL 377
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1214874590 542 pNAGEITQGFGAAMKCGLTKEKLDETIGIHPTCAEIFTTMDTSKSSGGDISQKGCUG 598
Cdd:TIGR02374 378 -KQADISEDPAIIKPQISGPEAGGPGVEAMPDSEQICSCNTVTKGAIIDAIHTGSCT 433
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
291-435 |
4.28e-09 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 59.03 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 291 KTLVVGASYVALECAGFLAGIGLDATVMVRSI-FLRGFDQEMANRAGAYMETHGV--KFIKQFVPIKVELleegtpgrik 367
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDkINKLMDADMNQPILDELDKREIpyRLNEEIDAINGNE---------- 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1214874590 368 VTAKStqGDQiieDEYNTVLIAVGRDACTRNIglEKIGVKINERnGKIPVSDEEQTSVPHVYAIGDIL 435
Cdd:PRK13512 220 VTFKS--GKV---EHYDMIIEGVGTHPNSKFI--ESSNIKLDDK-GFIPVNDKFETNVPNIYAIGDII 279
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
257-456 |
1.28e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 56.92 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 257 VVATGE-RPRYLNIPGDKEYCITS--DDLFS-----LPYCP---------GKTLVVGASYVALECAGFLAGIGLDATVMV 319
Cdd:PRK12770 123 LIATGTwKSRKLGIPGEDLPGVYSalEYLFRiraakLGYLPwekvppvegKKVVVVGAGLTAVDAALEAVLLGAEKVYLA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 320 --RSIflrgfdQEMAnrAGAYM----ETHGVKFIKQFVPikVELLEEGTPGRIK-VTAKSTQGDQ-------IIED---- 381
Cdd:PRK12770 203 yrRTI------NEAP--AGKYEierlIARGVEFLELVTP--VRIIGEGRVEGVElAKMRLGEPDEsgrprpvPIPGsefv 272
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1214874590 382 -EYNTVLIAVGRDAcTRNIGLEKIGVKINeRNGKIPVSDEEQTSVPHVYAIGDILDGKLELTPvAIQAGRLLARRL 456
Cdd:PRK12770 273 lEADTVVFAIGEIP-TPPFAKECLGIELN-RKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGK-AIKSGLRAAQSI 345
|
|
| GRX_hybridPRX5 |
cd03029 |
Glutaredoxin (GRX) family, PRX5 hybrid subfamily; composed of hybrid proteins containing ... |
22-88 |
1.50e-08 |
|
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: 51.75 E-value: 1.50e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1214874590 22 VMVFSKSFCPYCDRVKDLFSSLGAEYHSLELDECDDGSdiqeALQELTGQKTVPNVFVNKTHVGGCD 88
Cdd:cd03029 3 VSLFTKPGCPFCARAKAALQENGISYEEIPLGKDITGR----SLRAVTGAMTVPQVFIDGELIGGSD 65
|
|
| GRX_DEP |
cd03027 |
Glutaredoxin (GRX) family, Dishevelled, Egl-10, and Pleckstrin (DEP) subfamily; composed of ... |
21-86 |
3.00e-08 |
|
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: 50.87 E-value: 3.00e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1214874590 21 RVMVFSKSFCPYCDRVKDLFSSLGAEYHSLELDECddgSDIQEALQELTGQKTVPNVFVNKTHVGG 86
Cdd:cd03027 2 RVTIYSRLGCEDCTAVRLFLREKGLPYVEINIDIF---PERKAELEERTGSSVVPQIFFNEKLVGG 64
|
|
| PHA03050 |
PHA03050 |
glutaredoxin; Provisional |
13-103 |
4.79e-08 |
|
glutaredoxin; Provisional
Pssm-ID: 165343 [Multi-domain] Cd Length: 108 Bit Score: 51.56 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 13 VKELIDSNRVMVFSKSFCPYCDRVKDL---FSSLGAEYHSLELDECDDGSDIQEALQELTGQKTVPNVFVNKTHVGGCDK 89
Cdd:PHA03050 6 VQQRLANNKVTIFVKFTCPFCRNALDIlnkFSFKRGAYEIVDIKEFKPENELRDYFEQITGGRTVPRIFFGKTSIGGYSD 85
|
90
....*....|....
gi 1214874590 90 TLQAHKDGSLAKLL 103
Cdd:PHA03050 86 LLEIDNMDALGDIL 99
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
257-453 |
1.99e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 53.64 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 257 VVATG-ERPRYLNIPGDK--------EYcITS----DDLFSLPycPGKTLVV-GASYVALECAGflAGIGLDA---TVMV 319
Cdd:PRK11749 230 FIGTGaGLPRFLGIPGENlggvysavDF-LTRvnqaVADYDLP--VGKRVVViGGGNTAMDAAR--TAKRLGAesvTIVY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 320 RsiflRGFDqEMANRAG--AYMETHGVKFIKQFVPikVELLEEGtPGRIKVTA---------KSTQGDQIIEDEY----- 383
Cdd:PRK11749 305 R----RGRE-EMPASEEevEHAKEEGVEFEWLAAP--VEILGDE-GRVTGVEFvrmelgepdASGRRRVPIEGSEftlpa 376
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 384 NTVLIAVGRDACTRNIGLEKiGVKINERNGKIPVSDEEQTSVPHVYAIGDILDGKlELTPVAIQAGRLLA 453
Cdd:PRK11749 377 DLVIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTGA-ATVVWAVGDGKDAA 444
|
|
| grxA |
PRK11200 |
glutaredoxin 1; Provisional |
22-88 |
5.50e-07 |
|
glutaredoxin 1; Provisional
Pssm-ID: 183036 [Multi-domain] Cd Length: 85 Bit Score: 47.72 E-value: 5.50e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1214874590 22 VMVFSKSFCPYCDRVKDLfsslgAEYHSLELDECD-DGSDIQEA------LQELTGQ--KTVPNVFVNKTHVGGCD 88
Cdd:PRK11200 3 VVIFGRPGCPYCVRAKEL-----AEKLSEERDDFDyRYVDIHAEgiskadLEKTVGKpvETVPQIFVDQKHIGGCT 73
|
|
| NrdH |
cd02976 |
NrdH-redoxin (NrdH) family; NrdH is a small monomeric protein with a conserved redox active ... |
21-86 |
8.71e-07 |
|
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: 46.83 E-value: 8.71e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1214874590 21 RVMVFSKSFCPYCDRVKDLFSSLGAEYHSLELDEcddGSDIQEALQELTGQKTVPNVFVNKTHVGG 86
Cdd:cd02976 1 EVTVYTKPDCPYCKATKRFLDERGIPFEEVDVDE---DPEALEELKKLNGYRSVPVVVIGDEHLSG 63
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
253-437 |
2.07e-06 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 50.90 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 253 AEKF---VVATGE-RPRYLNIPGDKEYCITS--------------DDLFSLPYCPGK-TLVVGASYVALECAGFLAGIGL 313
Cdd:PRK12778 515 EEGFkgiFIASGAgLPNFMNIPGENSNGVMSsneyltrvnlmdaaSPDSDTPIKFGKkVAVVGGGNTAMDSARTAKRLGA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 314 DaTVMVrsIFLRGfDQEMANRAGAY--METHGVKF----------------IKQFVPIKVELLEEGTPGRIKVTAksTQG 375
Cdd:PRK12778 595 E-RVTI--VYRRS-EEEMPARLEEVkhAKEEGIEFltlhnpieyladekgwVKQVVLQKMELGEPDASGRRRPVA--IPG 668
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1214874590 376 DQIIEDeYNTVLIAVGrdaCTRNIGLEKI--GVKINeRNGKIPVSDEEQTSVPHVYAIGDILDG 437
Cdd:PRK12778 669 STFTVD-VDLVIVSVG---VSPNPLVPSSipGLELN-RKGTIVVDEEMQSSIPGIYAGGDIVRG 727
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
193-456 |
2.78e-06 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 50.71 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 193 VKHNWE-TMREAIQNYIGSLNWG---YRVA--LRDKQVRYENAYGEFVESHKI--------KATNKKGKESFFTAekfvV 258
Cdd:PRK12775 450 VKYGVDvTVYEALHVVGGVLQYGipsFRLPrdIIDREVQRLVDIGVKIETNKVigktftvpQLMNDKGFDAVFLG----V 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 259 ATGErPRYLNIPGDKEYCITSDDLF---------------SLPYCPGKTLVV-GASYVALECAGFLAGIGldaTVMVRSI 322
Cdd:PRK12775 526 GAGA-PTFLGIPGEFAGQVYSANEFltrvnlmggdkfpflDTPISLGKSVVViGAGNTAMDCLRVAKRLG---APTVRCV 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 323 FLRGfDQEMANRAGA--YMETHGVKFIKQFVPIKVELLEEGTPGRIKVTA------------KSTQGDQIIEDEYNTVLI 388
Cdd:PRK12775 602 YRRS-EAEAPARIEEirHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKVEEmelgepdekgrrKPMPTGEFKDLECDTVIY 680
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1214874590 389 AVGRDA------CTRNIGLEKIGvKINERNGKIpvSDEEQTSVPHVYAIGDILDGKLELTpVAIQAGRLLARRL 456
Cdd:PRK12775 681 ALGTKAnpiitqSTPGLALNKWG-NIAADDGKL--ESTQSTNLPGVFAGGDIVTGGATVI-LAMGAGRRAARSI 750
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
235-489 |
4.38e-06 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 49.27 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 235 ESHKIKATNKKGKESF-FTAEKFVVATGERPRYLNIPGdkeycITSDDLFSL-PYCPGKTL-------------VVGASY 299
Cdd:PRK09564 85 KNKTITVKNLKTGSIFnDTYDKLMIATGARPIIPPIKN-----INLENVYTLkSMEDGLALkellkdeeiknivIIGAGF 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 300 VALECAGFLAGIGLDATVMVRS--IFLRGFDQEMANRAGAYMETHGVKF-IKQFVpikVELLEEGtpgriKVTAKSTQGD 376
Cdd:PRK09564 160 IGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELhLNEFV---KSLIGED-----KVEGVVTDKG 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 377 QIiedEYNTVLIAVGRDACT---RNIGLEKIGvkinerNGKIPVSDEEQTSVPHVYAIGD------ILDGKLELTPVAIQ 447
Cdd:PRK09564 232 EY---EADVVIVATGVKPNTeflEDTGLKTLK------NGAIIVDEYGETSIENIYAAGDcatiynIVSNKNVYVPLATT 302
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1214874590 448 A---GRLLARRLYRGSKVKCDYINVPTTVFTPLEYGCCGYAEEKA 489
Cdd:PRK09564 303 AnklGRMVGENLAGRHVSFKGTLGSACIKVLDLEAARTGLTEEEA 347
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
264-454 |
2.67e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 46.93 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 264 PRYLNIPGD--------KEYcITSDDL-------FSLPYCPGK-TLVVGASYVALECAGFLAGIGLDATVMVRsiflRGf 327
Cdd:PRK12831 241 PKFMGIPGEnlngvfsaNEF-LTRVNLmkaykpeYDTPIKVGKkVAVVGGGNVAMDAARTALRLGAEVHIVYR----RS- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 328 DQEMANRAGAY--METHGVKF----------------IKQFVPIKVELLEEGTPGRIKVTAkstqgdqiIEDEY-----N 384
Cdd:PRK12831 315 EEELPARVEEVhhAKEEGVIFdlltnpveilgdengwVKGMKCIKMELGEPDASGRRRPVE--------IEGSEfvlevD 386
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1214874590 385 TVLIAVGRDAcTRNIGLEKIGVKINERnGKIpVSDEE--QTSVPHVYAIGDILDGklELTPV-AIQAGRLLAR 454
Cdd:PRK12831 387 TVIMSLGTSP-NPLISSTTKGLKINKR-GCI-VADEEtgLTSKEGVFAGGDAVTG--AATVIlAMGAGKKAAK 454
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
246-436 |
4.29e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 45.82 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 246 GKESFFTAEKFVVATGERPRYLNIPGDKEY-------CITSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDATVM 318
Cdd:PRK10262 99 GDSGEYTCDALIIATGASARYLGLPSEEAFkgrgvsaCATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 319 VR-------SIFLRGFDQEMANrAGAYMETHgvkfikqfvpikvELLEEGTPGRIKVTA---KSTQGDQIIED-EYNTVL 387
Cdd:PRK10262 176 HRrdgfraeKILIKRLMDKVEN-GNIILHTN-------------RTLEEVTGDQMGVTGvrlRDTQNSDNIESlDVAGLF 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1214874590 388 IAVGRDACTrniglEKIGVKINERNGKIPVS-----DEEQTSVPHVYAIGDILD 436
Cdd:PRK10262 242 VAIGHSPNT-----AIFEGQLELENGYIKVQsgihgNATQTSIPGVFAAGDVMD 290
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
257-454 |
7.96e-05 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 45.51 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 257 VVATG-ERPRYLNIPG-DKEYCIT----------SDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGlDATVMVrsIFL 324
Cdd:COG0493 211 FLATGaGKPRDLGIPGeDLKGVHSamdfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLG-AESVTI--VYR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 325 RGFDqEMANRAGAYMETH--GVKFI-----KQFVP-----------IKVELLEEGTPGRIKVTAKStqG-DQIIE-Deyn 384
Cdd:COG0493 288 RTRE-EMPASKEEVEEALeeGVEFLflvapVEIIGdengrvtglecVRMELGEPDESGRRRPVPIE--GsEFTLPaD--- 361
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1214874590 385 TVLIAVGRDACTRNIgLEKIGVKINERnGKIPVSDEE-QTSVPHVYAIGDILDGklELTPV-AIQAGRLLAR 454
Cdd:COG0493 362 LVILAIGQTPDPSGL-EEELGLELDKR-GTIVVDEETyQTSLPGVFAGGDAVRG--PSLVVwAIAEGRKAAR 429
|
|
| PRK12839 |
PRK12839 |
FAD-dependent oxidoreductase; |
105-155 |
1.54e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237223 [Multi-domain] Cd Length: 572 Bit Score: 44.82 E-value: 1.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1214874590 105 DNSVTYDYDLIVIGGGSGGLACSKEAASFGKKVMVLDFVVPTPQGTSWGLG 155
Cdd:PRK12839 2 TPSMTHTYDVVVVGSGAGGLSAAVAAAYGGAKVLVVEKASTCGGATAWSGG 52
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
113-159 |
4.66e-04 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 42.66 E-value: 4.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1214874590 113 DLIVIGGGSGGLACSKEAASFGKKVMVLDFVVPTPQGTSWGLGGTCV 159
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWSSGGIDA 47
|
|
| GRXA |
TIGR02183 |
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which ... |
22-96 |
7.06e-04 |
|
Glutaredoxin, GrxA family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the E. coli glyutaredoxin GrxA which appears to have primary responsibility for the reduction of ribonucleotide reductase.
Pssm-ID: 131238 [Multi-domain] Cd Length: 86 Bit Score: 39.04 E-value: 7.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1214874590 22 VMVFSKSFCPYCDRVKDLFSSLGAEYHSLELDECDDGSD--IQEALQELTGQ--KTVPNVFVNKTHVGGCDKTLQAHKD 96
Cdd:TIGR02183 2 VVIFGRPGCPYCVRAKQLAEKLAIERADFEFRYIDIHAEgiSKADLEKTVGKpvETVPQIFVDEKHVGGCTDFEQLVKE 80
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
109-141 |
8.16e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 42.19 E-value: 8.16e-04
10 20 30
....*....|....*....|....*....|...
gi 1214874590 109 TYDYDLIVIGGGSGGLACSKEAASFGKKVMVLD 141
Cdd:PRK12834 2 AMDADVIVVGAGLAGLVAAAELADAGKRVLLLD 34
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
109-141 |
9.41e-04 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 42.09 E-value: 9.41e-04
10 20 30
....*....|....*....|....*....|...
gi 1214874590 109 TYDYDLIVIGGGSGGLACSKEAASFGKKVMVLD 141
Cdd:COG3573 3 AMDADVIVVGAGLAGLVAAAELADAGRRVLLLD 35
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
112-141 |
1.14e-03 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 41.80 E-value: 1.14e-03
10 20 30
....*....|....*....|....*....|
gi 1214874590 112 YDLIVIGGGSGGLACSKEAASFGKKVMVLD 141
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIE 30
|
|
| PTZ00062 |
PTZ00062 |
glutaredoxin; Provisional |
4-109 |
2.39e-03 |
|
glutaredoxin; Provisional
Pssm-ID: 240250 [Multi-domain] Cd Length: 204 Bit Score: 39.78 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214874590 4 TGRDLLQARVKELIDSNRVMVFSKS-----FCPYCDRVKDLFSSLGAEYHSLELdeCDDgSDIQEALQELTGQKTVPNVF 78
Cdd:PTZ00062 97 GSSEDTVEKIERLIRNHKILLFMKGsktfpFCRFSNAVVNMLNSSGVKYETYNI--FED-PDLREELKVYSNWPTYPQLY 173
|
90 100 110
....*....|....*....|....*....|.
gi 1214874590 79 VNKTHVGGCDKTLQAHKDGSLAKLLDDNSVT 109
Cdd:PTZ00062 174 VNGELIGGHDIIKELYESNSLRKVIPDDCFE 204
|
|
| GRX_GRX_like |
cd03031 |
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of ... |
33-103 |
2.64e-03 |
|
Glutaredoxin (GRX) family, GRX-like domain containing protein subfamily; composed of uncharacterized eukaryotic proteins containing a GRX-like domain having only one conserved cysteine, aligning to the C-terminal cysteine of the CXXC motif of GRXs. This subfamily is predominantly composed of plant proteins. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins via a redox active CXXC motif using a similar dithiol mechanism employed by TRXs. GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. Proteins containing only the C-terminal cysteine are generally redox inactive.
Pssm-ID: 239329 [Multi-domain] Cd Length: 147 Bit Score: 38.76 E-value: 2.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1214874590 33 CDRVKDLFSSLGAEY-------HSLELDEcddgsdIQEALQELTGQKTVPNVFVNKTHVGGCDKTLQAHKDGSLAKLL 103
Cdd:cd03031 19 CNNVRAILESFRVKFderdvsmDSGFREE------LRELLGAELKAVSLPRVFVDGRYLGGAEEVLRLNESGELRKLL 90
|
|
| TLE_N |
pfam03920 |
Groucho/TLE N-terminal Q-rich domain; The N-terminal domain of the Grouch/TLE co-repressor ... |
33-56 |
2.84e-03 |
|
Groucho/TLE N-terminal Q-rich domain; The N-terminal domain of the Grouch/TLE co-repressor proteins are involved in oligomerization.
Pssm-ID: 461094 Cd Length: 117 Bit Score: 37.79 E-value: 2.84e-03
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
111-156 |
4.43e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 39.50 E-value: 4.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1214874590 111 DYDLIVIGGGSGGLACSKEAASFGKKVMVLDFVVPTpQGTSWGLGG 156
Cdd:COG0665 2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPG-SGASGRNAG 46
|
|
| PTZ00367 |
PTZ00367 |
squalene epoxidase; Provisional |
96-141 |
5.48e-03 |
|
squalene epoxidase; Provisional
Pssm-ID: 240384 [Multi-domain] Cd Length: 567 Bit Score: 39.83 E-value: 5.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1214874590 96 DGSLAKLLDDNSVT-YDYDLIVIGGGSGGLACSKEAASFGKKVMVLD 141
Cdd:PTZ00367 17 NRILSRLRFKPARTnYDYDVIIVGGSIAGPVLAKALSKQGRKVLMLE 63
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
111-139 |
6.37e-03 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 39.32 E-value: 6.37e-03
10 20
....*....|....*....|....*....
gi 1214874590 111 DYDLIVIGGGSGGLACSKEAASFGKKVMV 139
Cdd:PRK06134 12 ECDVLVIGSGAAGLSAAVTAAWHGLKVIV 40
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
109-140 |
7.29e-03 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 39.05 E-value: 7.29e-03
10 20 30
....*....|....*....|....*....|..
gi 1214874590 109 TYDYDLIVIGGGSGGLACSKEAASFGKKVMVL 140
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVL 32
|
|
| |
