|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
14-485 |
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: 687.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 93
Cdd:TIGR01438 16 AAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEETVKHDWKRLVEAV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 94 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPtHIEGALEYGITSDDIF 173
Cdd:TIGR01438 96 QNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GIPGAKELCITSDDLF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 174 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLpDGQL 253
Cdd:TIGR01438 175 SLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQI-EAKV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 254 QVTWEDSTTGKEdtGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGRPELTPIAI 333
Cdd:TIGR01438 254 LVEFTDSTNGIE--EEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIYAVGDILEDKPELTPVAI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 334 MAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRD-ASQCYVKMV 412
Cdd:TIGR01438 332 QAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLEWTIPSRDnHNKCYAKLV 411
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48257067 413 CLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG 485
Cdd:TIGR01438 412 CNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSGQDILQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
14-485 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 549.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQ-DAPNYGWEVAQPvpHDWRKMAEA 92
Cdd:PTZ00052 19 AAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKTSSS--FNWGKLVTT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 93 VQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDI 172
Cdd:PTZ00052 97 VQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPSIPEDVPGAKEYSITSDDI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 173 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDgQ 252
Cdd:PTZ00052 176 FSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDD-K 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 253 LQVTWEDSTTGKedtgtFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDsrEATSVPHIYAIGDVVEGRPELTPIA 332
Cdd:PTZ00052 255 IKVLFSDGTTEL-----FDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN--DCTNIPNIFAVGDVVEGRPELTPVA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 333 IMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRD--------- 403
Cdd:PTZ00052 328 IKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIAAVHREkherarkde 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 404 -----ASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDP 478
Cdd:PTZ00052 408 ydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVFMNLSVTRRSGESF 487
|
....*..
gi 48257067 479 TVTGCUG 485
Cdd:PTZ00052 488 AAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
14-469 |
3.21e-146 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 425.72 E-value: 3.21e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQD-APNYGWEVAQPVpHDWRKMAEA 92
Cdd:PRK06116 18 ASANRAAMYGAKVALIEAKR---------LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENK-FDWAKLIAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 93 VQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIIIATGGRPRYPThIEGAlEYGITSDDI 172
Cdd:PRK06116 88 RDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTV---EVNGERY--TADHILIATGGRPSIPD-IPGA-EYGITSDGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 173 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 251
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGdAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 252 QLQVTWEDsttGKEDTgtFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVvEGRPELTPI 331
Cdd:PRK06116 241 SLTLTLED---GETLT--VDCLIWAIGREPNTDGLGLENAGVKLN-EKGYIIVDEYQNTNVPGIYAVGDV-TGRVELTPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 332 AIMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDAsQCYVK 410
Cdd:PRK06116 314 AIAAGRRLSERLFNNKPDEkLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 48257067 411 MVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 469
Cdd:PRK06116 393 LVVVGKEEK-VVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
14-466 |
2.00e-124 |
|
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: 370.19 E-value: 2.00e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPvPHDWRKMAEAV 93
Cdd:COG1249 17 VAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAP-SVDWAALMARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 94 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGALEYGITSDDIF 173
Cdd:COG1249 87 DKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTV--EVTGGETL--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 174 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGq 252
Cdd:COG1249 163 ELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 253 LQVTWEDSttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPIA 332
Cdd:COG1249 242 VTVTLEDG--GGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGG-IKVDEYLRTSVPGIYAIGDVT-GGPQLAHVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 333 IMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDAsQCYVKMV 412
Cdd:COG1249 318 SAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGID--VKVGKFPFAANGRALALGET-EGFVKLI 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 48257067 413 CLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVV 466
Cdd:COG1249 395 ADAE-TGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALK 447
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
14-469 |
2.62e-121 |
|
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: 362.24 E-value: 2.62e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 93
Cdd:TIGR01421 16 ASARRAAEHGAKALLVEAKK---------LGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 94 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTvcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGAlEYGITSDDIF 173
Cdd:TIGR01421 87 DAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGT---VEVNGRDY--TAPHILIATGGKPSFPENIPGA-ELGTDSDGFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 174 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQ 252
Cdd:TIGR01421 161 ALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 253 LQVTWEDSTTgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVeGRPELTPIA 332
Cdd:TIGR01421 241 LVIHFEDGKS----IDDVDELIWAIGRKPNTKGLGLENVGIKLN-EKGQIIVDEYQNTNVPGIYALGDVV-GKVELTPVA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 333 IMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVaGRDASQCYVKM 411
Cdd:TIGR01421 315 IAAGRKLSERLFNGKTDDkLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAM-TSEKQKCRMKL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 48257067 412 VCLrEPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 469
Cdd:TIGR01421 394 VCA-GKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
14-469 |
6.51e-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: 335.63 E-value: 6.51e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDyvEPSpqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQpVPHDWRKMAEAV 93
Cdd:TIGR01424 16 RAARLAAALGAKVAIAE--EFR-------VGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVGK-ARFDWKKLLAAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 94 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKeilLSADHIIIATGGRPRYPThIEGAlEYGITSDDIF 173
Cdd:TIGR01424 86 DQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKPA-LPGH-ELGITSNEAF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 174 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQ 252
Cdd:TIGR01424 161 HLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRILPEDSITSISKDDDGR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 253 LQVtwedsTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEgRPELTPIA 332
Cdd:TIGR01424 241 LKA-----TLSKHEEIVADVVLFATGRSPNTNGLGLEAAGVRLN-DLGAIAVDEYSRTSTPSIYAVGDVTD-RINLTPVA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 333 IMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDaSQCYVKMV 412
Cdd:TIGR01424 314 IHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRPMKATFSGRQ-EKTLMKLV 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 48257067 413 cLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 469
Cdd:TIGR01424 391 -VDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
16-473 |
1.22e-94 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 295.57 E-value: 1.22e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 16 AKEAAQLGRKVSVVDY-VEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQ 94
Cdd:PLN02507 41 ARFSANFGAKVGICELpFHPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEINEKVDFNWKKLLQKKT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 95 NHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPThIEGAlEYGITSDDIFW 174
Cdd:PLN02507 121 DEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPN-IPGK-ELAITSDEALS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 175 LKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGqL 253
Cdd:PLN02507 199 LEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-I 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 254 QVTwedSTTGKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEgRPELTPIAI 333
Cdd:PLN02507 278 KVI---TDHGEEFVA--DVVLFATGRAPNTKRLNLEAVGVELD-KAGAVKVDEYSRTNIPSIWAIGDVTN-RINLTPVAL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 334 MAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEhVEVYHAHYKPLEFTVAGRDaSQCYVKMVC 413
Cdd:PLN02507 351 MEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGD-ILVFTSSFNPMKNTISGRQ-EKTVMKLIV 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 414 LREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKR 473
Cdd:PLN02507 429 DAETDK-VLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMRSVTR 487
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
42-473 |
3.85e-84 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 269.82 E-value: 3.85e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 42 GLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKAS 121
Cdd:PLN02546 122 GVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGK 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 122 FVDEHTVcgvAKGGKeiLLSADHIIIATGGRPRYPtHIEGaLEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI 201
Cdd:PLN02546 202 IVDPHTV---DVDGK--LYTARNILIAVGGRPFIP-DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 202 GLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTwedstTGKEDTGTFDTVLWAIGRV 280
Cdd:PLN02546 275 KSDVHVFIRQKKvLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLK-----TNKGTVEGFSHVMFATGRK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 281 PDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEgRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTV 360
Cdd:PLN02546 350 PNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVPSIWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAV 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 361 FTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREppQLVLGLHFLGPNAGEVTQGFAL 440
Cdd:PLN02546 428 FSQPPIGQVGLTEEQAIEEYGD--VDVFTANFRPLKATLSGLPDRVFMKLIVCAKT--NKVLGVHMCGEDAPEIIQGFAV 503
|
410 420 430
....*....|....*....|....*....|...
gi 48257067 441 GIKCGASYAQVMRTVGIHPTCSEEVVKLRISKR 473
Cdd:PLN02546 504 AVKAGLTKADFDATVGIHPTAAEEFVTMRTPTR 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
14-468 |
2.15e-82 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 265.33 E-value: 2.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVphDWRKMAEAV 93
Cdd:PTZ00058 62 AAARRAARNKAKVALVE---------KDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFSF--NLPLLVERR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 94 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVC--GVAKGGKEI----------------------LLSADHIIIAT 149
Cdd:PTZ00058 131 DKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLikKVSQVDGEAdesdddevtivsagvsqlddgqVIEGKNILIAV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 150 GGRPRYPtHIEGaLEYGITSDDIFWLKEsPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEH 228
Cdd:PTZ00058 211 GNKPIFP-DVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLLRKFDETIINELEND 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 229 MASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSttGKEDtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTqkILVDSRE 308
Cdd:PTZ00058 288 MKKNNINIITHANVEEIEKVKEKNLTIYLSDG--RKYE--HFDYVIYCVGRSPNTEDLNLKALNIKTPKGY--IKVDDNQ 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 309 ATSVPHIYAIGDVVEGRP---------------------------------ELTPIAIMAGRLLVQRLFGGSSDLMDYDN 355
Cdd:PTZ00058 362 RTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvQLTPVAINAGRLLADRLFGPFSRTTNYKL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 356 VPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDASQ---CYVKMVCLrEPPQLVLGLHFLGPNAG 432
Cdd:PTZ00058 442 IPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDMDPAQkekTYLKLVCV-GKEELIKGLHIVGLNAD 520
|
490 500 510
....*....|....*....|....*....|....*.
gi 48257067 433 EVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 468
Cdd:PTZ00058 521 EILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
19-469 |
1.99e-78 |
|
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: 252.97 E-value: 1.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 19 AAQL-GRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEV-AQPVPHDWRKMAEAVQNH 96
Cdd:TIGR01423 22 AATLyKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFdRSSVKANWKALIAAKNKA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 97 VKSLNWGHRVQLQDRK-VKYFNIKASFVDEHTVCgVAKGG------KEiLLSADHIIIATGGRPRYPThIEGaLEYGITS 169
Cdd:TIGR01423 102 VLDINKSYEGMFADTEgLTFFLGWGALEDKNVVL-VRESAdpksavKE-RLQAEHILLATGSWPQMLG-IPG-IEHCISS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 170 DDIFWLKESPGKTLVVGASYVALECAGFLTG---IGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRV 245
Cdd:TIGR01423 178 NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMiLRGFDSTLRKELTKQLRANGINIMTNENPAKV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 246 RRLPDGQLQVTWEdstTGKedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTqKILVDSREATSVPHIYAIGDVVeGR 325
Cdd:TIGR01423 258 TLNADGSKHVTFE---SGK--TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKG-AIQVDEFSRTNVPNIYAIGDVT-DR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 326 PELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHgqEHVEVYHAHYKPLEFTVAGRDAS 405
Cdd:TIGR01423 331 VMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYK 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48257067 406 QCYVKMVClREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 469
Cdd:TIGR01423 409 KFVAKIVT-NHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMR 471
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
15-463 |
1.76e-75 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 244.47 E-value: 1.76e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 15 CAKEAAQLGRKVSVVDYVEpspqgtrwgLGGTCVNVGCIPKK-LMHQAALLGGlIQDAPNYGWEVAQpVPHDWRKMAEAV 93
Cdd:TIGR01350 16 AAIRAAQLGLKVALVEKEY---------LGGTCLNVGCIPTKaLLHSAEVYDE-IKHAKDLGIEVEN-VSVDWEKMQKRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 94 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRY-PTHIEGALEYGITSDDI 172
Cdd:TIGR01350 85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTV-SVTGENGEETLEAKNIIIATGSRPRSlPGPFDFDGKVVITSTGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 173 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPD 250
Cdd:TIGR01350 164 LNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 251 gqlQVTWEDSTtGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVVEGrPELTP 330
Cdd:TIGR01350 243 ---QVTYENKG-GETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIGG-PMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 331 IAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGqehvevyhaHYKPLEFTVA--GR----DA 404
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGY---------DVKIGKFPFAanGKalalGE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 48257067 405 SQCYVKMVCLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 463
Cdd:TIGR01350 388 TDGFVKIIADKK-TGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
14-468 |
3.81e-70 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 230.47 E-value: 3.81e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRK----M 89
Cdd:PRK06370 19 PLAARAAGLGMKVALIE---------RGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAvmarK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 90 AEAVQN-HVKSLNWghrvqLQDRK-VKYFNIKASFVDEHTVCgVAkggkEILLSADHIIIATGGRPRYPtHIEGALEYG- 166
Cdd:PRK06370 90 RRIRARsRHGSEQW-----LRGLEgVDVFRGHARFESPNTVR-VG----GETLRAKRIFINTGARAAIP-PIPGLDEVGy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 167 ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiP--LRGFDQQMSSMVIEHMASHGTRFLRGCAPSR 244
Cdd:PRK06370 159 LTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERG-PrlLPREDEDVAAAVREILEREGIDVRLNAECIR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 245 VRRLPDGqlqVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDvVEG 324
Cdd:PRK06370 238 VERDGDG---IAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGY-IKVDDQLRTTNPGIYAAGD-CNG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 325 RPELTPIAIMAGRLLVQRLFGGS----SDLmdydNVPTTVFTPLEYGCVGLSEEEAVARhGQEhVEVYHahykpLEFTVA 400
Cdd:PRK06370 313 RGAFTHTAYNDARIVAANLLDGGrrkvSDR----IVPYATYTDPPLARVGMTEAEARKS-GRR-VLVGT-----RPMTRV 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48257067 401 GR----DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 468
Cdd:PRK06370 382 GRavekGETQGFMKVV-VDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
8-463 |
9.73e-69 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 226.95 E-value: 9.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 8 GGSGGLACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEvAQPVPHDWR 87
Cdd:PRK06416 12 AGPGGYVAAIRAAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIK-AENVGIDFK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 88 KMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGI 167
Cdd:PRK06416 82 KVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTV-RVMTEDGEQTYTAKNIILATGSRPRELPGIEIDGRVIW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 168 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRFLRGcapSRV 245
Cdd:PRK06416 161 TSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveALPRI-LPGEDKEISKLAERALKKRGIKIKTG---AKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 246 RRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTspDTQKILVDSREATSVPHIYAIGDVVEGr 325
Cdd:PRK06416 237 KKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKT--DRGFIEVDEQLRTNVPNIYAIGDIVGG- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 326 PELTPIAIMAGRLLVQRLFGGSSDlMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYhahykplEFTVAGR--- 402
Cdd:PRK06416 314 PMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVV-------KFPFAGNgka 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 48257067 403 ---DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 463
Cdd:PRK06416 384 lalGETDGFVKLI-FDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
14-467 |
5.07e-67 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 222.36 E-value: 5.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPhDWRKMAEAV 93
Cdd:PRK06292 17 VAARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKI-DFKKVMARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 94 QNHVKSLNWGH-RVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIIIATGGR-PRYPThIEGALEYGI-TSD 170
Cdd:PRK06292 87 RRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTV---EVNGERI--EAKNIVIATGSRvPPIPG-VWLILGDRLlTSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 171 DIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHgTRFLRGCAPSRVRRL 248
Cdd:PRK06292 161 DAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVfeRGDRI-LPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 249 PDGQLQVTWEDsttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVeGRPEL 328
Cdd:PRK06292 239 GDEKVEELEKG---GKTETIEADYVLVATGRRPNTDGLGLENTGIELD-ERGRPVVDEHTQTSVPGIYAAGDVN-GKPPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 329 TPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARhGQEHVEvyhAHYkplEFTVAGR----DA 404
Cdd:PRK06292 314 LHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAA-GIDYVV---GEV---PFEAQGRarvmGK 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 48257067 405 SQCYVKMVCLREPpQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTcSEEVVK 467
Cdd:PRK06292 387 NDGFVKVYADKKT-GRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPT-LSEGLR 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
14-485 |
5.06e-65 |
|
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: 217.29 E-value: 5.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPnYGWEVAQPVPhDWRKMAEAV 93
Cdd:TIGR02053 14 AAAIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPP-FGGLAATVAV-DFGELLEGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 94 QNHVKSLnwghrvqlqdRKVKYFNI-----------KASFVDEHTVcgVAKGGKEIlLSADHIIIATGGRPRYPtHIEGA 162
Cdd:TIGR02053 83 REVVEEL----------RHEKYEDVlssygvdylrgRARFKDPKTV--KVDLGREV-RGAKRFLIATGARPAIP-PIPGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 163 LEYG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGC 240
Cdd:TIGR02053 149 KEAGyLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTSA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 241 APSRVRRLPDGQLQVTwedSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGD 320
Cdd:TIGR02053 229 QVKAVSVRGGGKIITV---EKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGG-ILVDETLRTSNPGIYAAGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 321 VVeGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAvarhgQEHVEVYHAHYKPLEFTVA 400
Cdd:TIGR02053 305 VT-GGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEA-----QKAGIECDCRTLPLTNVPR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 401 GR--DASQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEevvKLRISKRSGL-D 477
Cdd:TIGR02053 379 ARinRDTRGFIKLVAEPGTGK-VLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE---GLKLAAQTFYrD 454
|
....*...
gi 48257067 478 PTVTGCUG 485
Cdd:TIGR02053 455 VSKLSCCA 462
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
14-336 |
1.06e-60 |
|
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: 201.01 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVdyvepspqgtrwGLGGTCVNVGCIPKKLMHQAAllggliqdapnygwEVAQPVPHdWRKMAEAV 93
Cdd:pfam07992 14 AAALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAA--------------EAPEIASL-WADLYKRK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 94 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGvakggKEILLSADHIIIATGGRPRYPThIEGALEYG------I 167
Cdd:pfam07992 67 EEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDG-----DGETITYDRLVIATGARPRLPP-IPGVELNVgflvrtL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 168 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVR 246
Cdd:pfam07992 141 DSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 247 RLPDGQLQVTwedsttGKEDTGTFDTVLWAIGRVPDTRslNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVEGRP 326
Cdd:pfam07992 221 GDGDGVEVIL------KDGTEIDADLVVVAIGRRPNTE--LLEAAGLELDERGG-IVVDEYLRTSVPGIYAAGDCRVGGP 291
|
330
....*....|
gi 48257067 327 ELTPIAIMAG 336
Cdd:pfam07992 292 ELAQNAVAQG 301
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
16-433 |
8.94e-52 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 181.89 E-value: 8.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 16 AKEAAQLGRKVSVVDyvepspqgTRWGLGGTCVNVGCIPKKLMHQAAL-LGGLIQDA--PNYGwEVAQPVPHDWRKMAEA 92
Cdd:PRK05249 21 AMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlySSYR-VKLRITFADLLARADH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 93 VQNHVKSLnwgHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDI 172
Cdd:PRK05249 92 VINKQVEV---RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 173 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 251
Cdd:PRK05249 169 LSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTlINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 252 QLqVTWEDsttGKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPI 331
Cdd:PRK05249 249 VI-VHLKS---GKKIKA--DCLLYANGRTGNTDGLNLENAGLEADSRGQ-LKVNENYQTAVPHIYAVGDVI-GFPSLASA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 332 AIMAGRLLVQRLFGGSSDLMdYDNVPTTVFTPLEYGCVGLSEEEAVARHGqeHVEVYHAHYKPLeftvA-GRDASQCY-- 408
Cdd:PRK05249 321 SMDQGRIAAQHAVGEATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKV--PYEVGRARFKEL----ArAQIAGDNVgm 393
|
410 420
....*....|....*....|....*
gi 48257067 409 VKMVCLREPPQLvLGLHFLGPNAGE 433
Cdd:PRK05249 394 LKILFHRETLEI-LGVHCFGERATE 417
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
19-474 |
3.18e-45 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 164.71 E-value: 3.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 19 AAQLGRKVSVVDYVEpSPQGTRwGLGGTCVNVGCIPKK-LMHQAALLGGLIQDAPNYGWEVAQpVPHDWRKMAEAVQNHV 97
Cdd:PRK06327 23 AAQLGLKVACIEAWK-NPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGIHVDG-VKIDVAKMIARKDKVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 98 KSLNWGHRVQLQDRKVKYFNIKASFV---DEHTVCGVAKGGKEILlSADHIIIATGGRPRyptHIEGAL---EYGITSDD 171
Cdd:PRK06327 100 KKMTGGIEGLFKKNKITVLKGRGSFVgktDAGYEIKVTGEDETVI-TAKHVIIATGSEPR---HLPGVPfdnKIILDNTG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 172 IFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM--MRSIpLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLP 249
Cdd:PRK06327 176 ALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeaLPAF-LAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 250 DGqLQVTWEDSTtGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGrPELT 329
Cdd:PRK06327 255 KG-VSVAYTDAD-GEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLD-ERGFIPVDDHCRTNVPNVYAIGDVVRG-PMLA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 330 PIAIMAGrLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVArhgqEHVEvYHAHYKPleFTVAGR----DAS 405
Cdd:PRK06327 331 HKAEEEG-VAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKA----EGVE-YKAGKFP--FMANGRalamGEP 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48257067 406 QCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSeEVVK---LRISKRS 474
Cdd:PRK06327 403 DGFVKIIADAKTDE-ILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLS-EVWHeaaLAVDKRP 472
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
23-465 |
4.65e-44 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 160.89 E-value: 4.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 23 GRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVQNHVKSLN 101
Cdd:PRK07846 22 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 102 WG---HRVQLQDrKVKYFNIKASFVDEHTVCgVAKGGkeiLLSADHIIIATGGRPRYPTHI-EGALEYGiTSDDIFWLKE 177
Cdd:PRK07846 91 AGgeeYRGRDTP-NIDVYRGHARFIGPKTLR-TGDGE---EITADQVVIAAGSRPVIPPVIaDSGVRYH-TSDTIMRLPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 178 SPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMashGTRF-LR-GCAPSRVRRLPDGqLQ 254
Cdd:PRK07846 165 LPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISERFTELA---SKRWdVRlGRNVVGVSQDGSG-VT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 255 VTWEDSTtgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVveGRP-ELTPIAI 333
Cdd:PRK07846 241 LRLDDGS-----TVEADVLLVATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV--SSPyQLKHVAN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 334 MAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARhGQEHVeVYHAHYKPLEFTVAGRDASQCyVKMV 412
Cdd:PRK07846 313 HEARVVQHNLLHPDDLIaSDHRFVPAAVFTHPQIASVGLTENEARAA-GLDIT-VKVQNYGDVAYGWAMEDTTGF-VKLI 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 48257067 413 CLREPPQLvLGLHFLGPNAGEVTQGF----ALGIKcgasyAQVM--RTVGIHPTCSEEV 465
Cdd:PRK07846 390 ADRDTGRL-LGAHIIGPQASTLIQPLiqamSFGLD-----AREMarGQYWIHPALPEVV 442
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
14-443 |
5.27e-43 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 159.93 E-value: 5.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 93
Cdd:PRK13748 112 AAALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 94 QNHVKSLnwghrvqlqdRKVKYFNI------------KASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPThIEG 161
Cdd:PRK13748 183 QARVDEL----------RHAKYEGIldgnpaitvlhgEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPP-IPG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 162 ALE--YGiTSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 239
Cdd:PRK13748 252 LKEtpYW-TSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEH 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 240 CAPSRVRRLpDGQLQVtwedsTTGKedtGTF--DTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYA 317
Cdd:PRK13748 331 TQASQVAHV-DGEFVL-----TTGH---GELraDKLLVATGRAPNTRSLALDAAGVTVNAQGA-IVIDQGMRTSVPHIYA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 318 IGDVVEgRPELTPIAIMAGRLLVQRLFGGSSDLmDYDNVPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEF 397
Cdd:PRK13748 401 AGDCTD-QPQFVYVAAAAGTRAAINMTGGDAAL-DLTAMPAVVFTDPQVATVGYSEAE--AHHDGIETDSRTLTLDNVPR 476
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 48257067 398 TVAGRDaSQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIK 443
Cdd:PRK13748 477 ALANFD-TRGFIKLV-IEEGSGRLIGVQAVAPEAGELIQTAALAIR 520
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
37-465 |
4.38e-41 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 152.60 E-value: 4.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 37 QGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVqnhvkslnWGHRVQL------- 108
Cdd:TIGR03452 31 KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRV--------FGDRIDPiaagged 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 109 -----QDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHI-EGALEYgITSDDIFWLKESPGKT 182
Cdd:TIGR03452 98 yrrgdETPNIDVYDGHARFVGPRTL--RTGDGEEI--TGDQIVIAAGSRPYIPPAIaDSGVRY-HTNEDIMRLPELPESL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 183 LVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEhMASHGTRFLRGCAPSRVRRLPDGqLQVTWEDST 261
Cdd:TIGR03452 173 VIVGGGYIAAEFAHVFSALGTRVTIVNRSTKlLRHLDEDISDRFTE-IAKKKWDIRLGRNVTAVEQDGDG-VTLTLDDGS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 262 tgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVveGRP-ELTPIAIMAGRLLV 340
Cdd:TIGR03452 251 -----TVTADVLLVATGRVPNGDLLDAEAAGVEVDED-GRIKVDEYGRTSARGVWALGDV--SSPyQLKHVANAEARVVK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 341 QRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVyhAHYKPLEFTVAGRDaSQCYVKMVCLREPPQ 419
Cdd:TIGR03452 323 HNLLHPNDlRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKI--QNYGDVAYGWAMED-TTGFCKLIADRDTGK 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 48257067 420 LvLGLHFLGPNAGEVTQGFALGIKCGASYAQVMR-TVGIHPTCSEEV 465
Cdd:TIGR03452 400 L-LGAHIIGPQASSLIQPLITAMAFGLDAREMARkQYWIHPALPEVV 445
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
356-468 |
2.58e-36 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 129.98 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 356 VPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDASqCYVKMVCLREPpQLVLGLHFLGPNAGEVT 435
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADRET-GKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 48257067 436 QGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 468
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
16-463 |
2.73e-36 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 139.11 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 16 AKEAAQLGRKVSVVdyvEPSPQGtrwgLGGTCVNVGCIPKKLMHQAAllggliqdapNYGWEVAQPVPHdwrkmAEAVQN 95
Cdd:PRK07251 19 AAKLASAGKKVALV---EESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQVMAT-----KNTVTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 96 HVKSLNWGhrvQLQDRKVKYFNIKASFVDEHTVCGVAkGGKEILLSADHIIIATGGRPRYPThIEGALE--YGITSDDIF 173
Cdd:PRK07251 77 RLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQA-GDEKIELTAETIVINTGAVSNVLP-IPGLADskHVYDSTGIQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 174 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQ 252
Cdd:PRK07251 152 SLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKN-DGDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 253 LQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDvVEGRPELTPIA 332
Cdd:PRK07251 231 VLVVTEDETY------RFDALLYATGRKPNTEPLGLENTDIELT-ERGAIKVDDYCQTSVPGVFAVGD-VNGGPQFTYIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 333 IMAGRLLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehvevyhahYKPLEFTVAG--RDASQCYV 409
Cdd:PRK07251 303 LDDFRIVFGYLTGDGSyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLP---------YAVKELLVAAmpRAHVNNDL 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 48257067 410 K---MVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 463
Cdd:PRK07251 374 RgafKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
19-463 |
8.15e-32 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 126.82 E-value: 8.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 19 AAQLGRKVSVVDYVEPSPQGtrwgLGGTCVNVGCIPKKLmhqaallggLIQDApnygwEVAQPVPHDWRKMAEAVqNHVK 98
Cdd:NF040477 19 AATLAKAGWRVAIIEQSAQM----YGGTCINIGCIPTKT---------LVHDA-----EQHQDFSTAMQRKSSVV-GFLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 99 SLNWGHRVQLQDrkVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSDDIF 173
Cdd:NF040477 80 DKNYHNLADLDN--VDVINGRAEFIDNHTL-RVFQADGEQELRGEKIFINTGAQSVLPpipglTTTPGVYD----STGLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 174 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLpDGQ 252
Cdd:NF040477 153 NLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAeLFLPREDRDIAQAIATILQDQGVELILNAQVQRVSSH-EGE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 253 LQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGrPELTPIA 332
Cdd:NF040477 232 VQLETAEGVL------TVDALLVASGRKPATAGLQLQNAGVAVN-ERGAIVVDKYLRTTADNIWAMGDVTGG-LQFTYIS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 333 IMAGRLLVQRLFG-GSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVagrDASQCYVKM 411
Cdd:NF040477 304 LDDFRIVRDSLLGeGKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVM---NDTRGVLKA 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 48257067 412 VcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 463
Cdd:NF040477 381 V-VDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSE 431
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
124-370 |
1.53e-29 |
|
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: 117.99 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 124 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITS----DDIFWLKE-----SPGKTLVVGASYVALEC 194
Cdd:COG0446 65 EAKTV--TLRDGETL--SYDKLVLATGARPRPP-PIPGLDLPGVFTlrtlDDADALREalkefKGKRAVVIGGGPIGLEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 195 AGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGQLQVTWEDsttgkEDTGTFDTV 273
Cdd:COG0446 140 AEALRKRGLKVTLVeRAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTD-----GEEIPADLV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 274 LWAIGRVPDTrSLnLEKAGVDTSPdTQKILVDSREATSVPHIYAIGDVVE------GRPELTP---IAIMAGRLLVQRLF 344
Cdd:COG0446 213 VVAPGVRPNT-EL-AKDAGLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasAANKQGRVAAENIL 289
|
250 260
....*....|....*....|....*...
gi 48257067 345 GGSsdlMDYDNVPTTVFT--PLEYGCVG 370
Cdd:COG0446 290 GGP---APFPGLGTFISKvfDLCIASTG 314
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
19-462 |
5.57e-25 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 107.25 E-value: 5.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 19 AAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHdwRKMAEAVQNHVK 98
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEA--RVDLPAVNARVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 99 SLNWGH----RVQLQDRKVKYFNIKASFVDE----HTVCGVAKGGKEILLSADHIIIATGGRPRYpthIEGALEYG---I 167
Cdd:PRK07845 89 ALAAAQsadiRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPRI---LPTAEPDGeriL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 168 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQmSSMVIEH-MASHGTRFLRGCAPSRV 245
Cdd:PRK07845 166 TWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDAD-AAEVLEEvFARRGMTVLKRSRAESV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 246 RRLPDGQLqVTWEDsttGKEDTGTFdtVLWAIGRVPDTRSLNLEKAGVDTSPdTQKILVD--SReaTSVPHIYAIGDVVE 323
Cdd:PRK07845 245 ERTGDGVV-VTLTD---GRTVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDrvSR--TSVPGIYAAGDCTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 324 GRPeLTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSeeEAVARHGQEHVEVY------HAHYKPLEF 397
Cdd:PRK07845 316 VLP-LASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVS--QAAIDSGEVPARTVmlplatNPRAKMSGL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48257067 398 tvagRDAsqcYVKMVClREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCS 462
Cdd:PRK07845 393 ----RDG---FVKLFC-RPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLS 449
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
14-463 |
1.44e-24 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 107.31 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 14 ACAKEAAQLGRKVSVVDYVEPSpqgtrwgLGGTCVNVGCIPKKLMHQAA------------LLGGLIQDAPNYGWE---- 77
Cdd:PTZ00153 130 AAAINAMERGLKVIIFTGDDDS-------IGGTCVNVGCIPSKALLYATgkyrelknlaklYTYGIYTNAFKNGKNdpve 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 78 ----VAQPVPHDWRKMAEAVQNHVKSLNWG-------HRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEilLSADHII 146
Cdd:PTZ00153 203 rnqlVADTVQIDITKLKEYTQSVIDKLRGGienglksKKFCKNSEHVQVIYERGHIVDKNTI-KSEKSGKE--FKVKNII 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 147 IATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiplrgfdQQMSSMVI 226
Cdd:PTZ00153 280 IATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYS-------PQLLPLLD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 227 EHMASHGTRFLRGCAPSRVR--------RLPDGQLQVT--WEDSTTGKEDTGTF----------DTVLWAIGRVPDTRSL 286
Cdd:PTZ00153 353 ADVAKYFERVFLKSKPVRVHlntlieyvRAGKGNQPVIigHSERQTGESDGPKKnmndiketyvDSCLVATGRKPNTNNL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 287 NLEKAGVDTS----PDTQKILVDSREATSVPHIYAIGDvVEGRPELTP------------IAIMAGRLLVQRLFGGSSDL 350
Cdd:PTZ00153 433 GLDKLKIQMKrgfvSVDEHLRVLREDQEVYDNIFCIGD-ANGKQMLAHtashqalkvvdwIEGKGKENVNINVENWASKP 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 351 MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKP-------LEFTVAGRDASQCY--------------V 409
Cdd:PTZ00153 512 IIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEISFYKAnskvlceNNISFPNNSKNNSYnkgkyntvdntegmV 591
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 48257067 410 KMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 463
Cdd:PTZ00153 592 KIVYLKDTKE-ILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISE 644
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
44-468 |
4.65e-24 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 104.33 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 44 GGTCVNVGCIPKKLmhqaallggLIQDAPNYG-WEVAQPvphdwRKmaEAVQNHVKSLNWGHRVQLQDrkVKYFNIKASF 122
Cdd:PRK08010 40 GGTCINIGCIPTKT---------LVHDAQQHTdFVRAIQ-----RK--NEVVNFLRNKNFHNLADMPN--IDVIDGQAEF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 123 VDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSDDIFWLKESPGKTLVVGASYVALECAGF 197
Cdd:PRK08010 102 INNHSL-RVHRPEGNLEIHGEKIFINTGAQTVVPpipgiTTTPGVYD----STGLLNLKELPGHLGILGGGYIGVEFASM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 198 LTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDSTTgkedtgTFDTVLWA 276
Cdd:PRK08010 177 FANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISH-HENQVQVHSEHAQL------AVDALLIA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 277 IGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGRpELTPIAIMAGRLLVQRLFG-GSSDLMDYDN 355
Cdd:PRK08010 250 SGRQPATASLHPENAGIAVN-ERGAIVVDKYLHTTADNIWAMGDVTGGL-QFTYISLDDYRIVRDELLGeGKRSTDDRKN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 356 VPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREppQLVLGLHFLGPNAGEVT 435
Cdd:PRK08010 328 VPYSVFMTPPLSRVGMTEEQ--ARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKT--QRILGASLLCVDSHEMI 403
|
410 420 430
....*....|....*....|....*....|...
gi 48257067 436 QGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 468
Cdd:PRK08010 404 NIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
124-380 |
4.55e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 97.90 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 124 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPThIEGALEYGITS----DDIFWLKE--SPGKTLVV-GASYVALECAG 196
Cdd:COG1251 85 AARTV--TLADGETL--PYDKLVLATGSRPRVPP-IPGADLPGVFTlrtlDDADALRAalAPGKRVVViGGGLIGLEAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 197 FLTGIGLDTT-IMMRSIPL-RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDsttgkedtGTF---D 271
Cdd:COG1251 160 ALRKRGLEVTvVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLAD--------GEElpaD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 272 TVLWAIGRVPDTrSLnLEKAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE------GRP--ELTPIAIMAGRLLVQRL 343
Cdd:COG1251 231 LVVVAIGVRPNT-EL-ARAAGLAVD---RGIVVDDYLRTSDPDIYAAGDCAEhpgpvyGRRvlELVAPAYEQARVAAANL 305
|
250 260 270
....*....|....*....|....*....|....*....
gi 48257067 344 FGGSSDLMDYDNVPTTVFTPLEYGCVGLSE--EEAVARH 380
Cdd:COG1251 306 AGGPAAYEGSVPSTKLKVFGVDVASAGDAEgdEEVVVRG 344
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
99-412 |
2.17e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 84.32 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 99 SLNWGHRVQLQDRKVKYFNIKAsfvdehtvcgvAKGGKEILLSADHIIIATGGRPRYPTHIEGALE--YGITS-DDIFWL 175
Cdd:PRK09564 72 DVKTEHEVVKVDAKNKTITVKN-----------LKTGSIFNDTYDKLMIATGARPIIPPIKNINLEnvYTLKSmEDGLAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 176 KESPGKT-----LVVGASYVALECAGFLTGIGLDTTIMMRS--IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrl 248
Cdd:PRK09564 141 KELLKDEeikniVIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELHLNEFVKSL--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 249 pDGQLQVTWEDSTTGKEDTgtfDTVLWAIGRVPDTRSLnlEKAGVDTSpDTQKILVDSREATSVPHIYAIGD------VV 322
Cdd:PRK09564 218 -IGEDKVEGVVTDKGEYEA---DVVIVATGVKPNTEFL--EDTGLKTL-KNGAIIVDEYGETSIENIYAAGDcatiynIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 323 EGRPELTPIAIMA---GRLLVQRLFG---------GSSDLMDYDnvpttvftpLEYGCVGLSEEEAVArHGQEHVEVY-- 388
Cdd:PRK09564 291 SNKNVYVPLATTAnklGRMVGENLAGrhvsfkgtlGSACIKVLD---------LEAARTGLTEEEAKK-LGIDYKTVFik 360
|
330 340
....*....|....*....|....*..
gi 48257067 389 ---HAHYKPleftvagrDASQCYVKMV 412
Cdd:PRK09564 361 dknHTNYYP--------GQEDLYVKLI 379
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
131-338 |
1.96e-16 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 79.78 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 131 VAKGGKEILLSADHIIIATGGRPRYPThIEGALE-------YGITSDDIFWlkesPGKT-LVVGASYVALECAGFLTGIG 202
Cdd:COG0492 90 RVTTDDGTEYEAKAVIIATGAGPRKLG-LPGEEEfegrgvsYCATCDGFFF----RGKDvVVVGGGDSALEEALYLTKFA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 203 LDTTIMMRSIPLRGfdqqmSSMVIEHMASH-GTRFLRGCAPSRVrrLPDGQLQ-VTWEDSTTGKEDTGTFDTVLWAIGRV 280
Cdd:COG0492 165 SKVTLIHRRDELRA-----SKILVERLRANpKIEVLWNTEVTEI--EGDGRVEgVTLKNVKTGEEKELEVDGVFVAIGLK 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 48257067 281 PDTrSLnLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVVEGRPELTPIAIMAGRL 338
Cdd:COG0492 238 PNT-EL-LKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAI 292
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
181-256 |
1.40e-14 |
|
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: 68.77 E-value: 1.40e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48257067 181 KTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVT 256
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVeRRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
124-378 |
4.33e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 61.30 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 124 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITSDDI-----FW----------LKESPGKTLVVGAS 188
Cdd:COG1252 84 EARTV--TLADGRTL--SYDYLVIATGSVTNFF-GIPGLAEHALPLKTLedalaLRerllaaferaERRRLLTIVVVGGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 189 Y----VALECAGFLTGIGLDTTIMMRSI----------PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGqlq 254
Cdd:COG1252 159 PtgveLAGELAELLRKLLRYPGIDPDKVritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADG--- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 255 VTWEDSTTGKedtgtFDTVLWAIG-RVPDTrslnLEKAGVDTSPDTQkILVDSR-EATSVPHIYAIGDVV-----EGRPe 327
Cdd:COG1252 234 VTLEDGEEIP-----ADTVIWAAGvKAPPL----LADLGLPTDRRGR-VLVDPTlQVPGHPNVFAIGDCAavpdpDGKP- 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 48257067 328 LTPIAIMA-------GRLLVQRLFGGssdlmdydnvPTTVFTPLEYGC-VGLSEEEAVA 378
Cdd:COG1252 303 VPKTAQAAvqqakvlAKNIAALLRGK----------PLKPFRYRDKGClASLGRGAAVA 351
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
136-343 |
4.66e-10 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 61.16 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 136 KEILLSADHIIIATGG-RPRYPThIEG--------ALEY---------GITSddifWLKESP---GKTLVVGASYVALEC 194
Cdd:PRK12770 113 EELVKKYDAVLIATGTwKSRKLG-IPGedlpgvysALEYlfriraaklGYLP----WEKVPPvegKKVVVVGAGLTAVDA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 195 A--GFLTGIGLDTTIMMRSIPlrgfDQQMSSMVIEHMASHGTRFLRGCAP------SRVRRLPDGQLQVTWEDST----- 261
Cdd:PRK12770 188 AleAVLLGAEKVYLAYRRTIN----EAPAGKYEIERLIARGVEFLELVTPvriigeGRVEGVELAKMRLGEPDESgrprp 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 262 ---TGKEDTGTFDTVLWAIGRVPdTRSLNLEKAGVDTSPDTqKILVDSREATSVPHIYAIGDVVEGrPELTPIAIMAGRL 338
Cdd:PRK12770 264 vpiPGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKG-EIVVDEKHMTSREGVFAAGDVVTG-PSKIGKAIKSGLR 340
|
....*
gi 48257067 339 LVQRL 343
Cdd:PRK12770 341 AAQSI 345
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
181-394 |
5.88e-10 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 61.34 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 181 KTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrlpDGQLqVTWEd 259
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKiNKLMDADMNQPILDELDKREIPYRLNEEIDAI----NGNE-VTFK- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 260 stTGKEDtgTFDTVLWAIGRVPDTRSlnLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEG------RPELTPIAI 333
Cdd:PRK13512 224 --SGKVE--HYDMIIEGVGTHPNSKF--IESSNIKLD-DKGFIPVNDKFETNVPNIYAIGDIITShyrhvdLPASVPLAW 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 48257067 334 MAGR---LLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEaVARHGQEHVEV---YHAHYKP 394
Cdd:PRK13512 297 GAHRaasIVAEQIAGNDTiEFKGFLGNNIVKFFDYTFASVGVKPNE-LKQFDYKMVEVtqgAHANYYP 363
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
143-337 |
1.59e-06 |
|
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: 50.52 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 143 DHIIIATG-GRPRyPTHIEG--------ALEY--GITSDDIFWLKESPGKTLVV-GASYVALECAGflTGIGL---DTTI 207
Cdd:COG0493 208 DAVFLATGaGKPR-DLGIPGedlkgvhsAMDFltAVNLGEAPDTILAVGKRVVViGGGNTAMDCAR--TALRLgaeSVTI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 208 MMRsiplRGFDQqMSSMV--IEHMASHGTRFLRGCAPSRVRRLPDGQL------QVTW-EDSTTGK----EDTGTF---- 270
Cdd:COG0493 285 VYR----RTREE-MPASKeeVEEALEEGVEFLFLVAPVEIIGDENGRVtglecvRMELgEPDESGRrrpvPIEGSEftlp 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48257067 271 -DTVLWAIGRVPDTRSLnLEKAGVDTSPDTqKILVDSRE-ATSVPHIYAIGDVVEGrPELTPIAIMAGR 337
Cdd:COG0493 360 aDLVILAIGQTPDPSGL-EEELGLELDKRG-TIVVDEETyQTSLPGVFAGGDAVRG-PSLVVWAIAEGR 425
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
183-350 |
4.60e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 48.76 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 183 LVVGASYVALECAGFLTGIGLDTTIMMRSiplrgfDQQMSSMV-------IEH-MASHGTRFLRGCAPSRVRRLPDGqLQ 254
Cdd:PRK04965 145 LVVGGGLIGTELAMDLCRAGKAVTLVDNA------ASLLASLMppevssrLQHrLTEMGVHLLLKSQLQGLEKTDSG-IR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 255 VTWEDSttgkeDTGTFDTVLWAIGRVPDTrSLNLEkAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE--GR--PELTP 330
Cdd:PRK04965 218 ATLDSG-----RSIEVDAVIAAAGLRPNT-ALARR-AGLAVN---RGIVVDSYLQTSAPDIYALGDCAEinGQvlPFLQP 287
|
170 180
....*....|....*....|
gi 48257067 331 IaIMAGRLLVQRLFGGSSDL 350
Cdd:PRK04965 288 I-QLSAMALAKNLLGQNTPL 306
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
104-323 |
1.01e-05 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 48.29 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 104 HRVQLqdrkvkYFNIKASFVDEHTVCGVAKGGKeiLLSADHIIIATGGRPRYPThIEGALEYGITS-------DDIFWLK 176
Cdd:TIGR02374 67 HGITL------YTGETVIQIDTDQKQVITDAGR--TLSYDKLILATGSYPFILP-IPGADKKGVYVfrtiedlDAIMAMA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 177 ESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGcapsrvrrlpdgqlQ 254
Cdd:TIGR02374 138 QRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVihHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLE--------------K 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48257067 255 VTWEDSTTGKEDTGTF--------DTVLWAIGRVPDTRsLNLEkAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE 323
Cdd:TIGR02374 204 DTVEIVGATKADRIRFkdgssleaDLIVMAAGIRPNDE-LAVS-AGIKVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
143-324 |
1.78e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 47.10 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 143 DHIIIATG-GRPRyPTHIEG--------ALEYGITSDDIFWLKESP-GKTLVV-GASYVALECAGflTGIGL---DTTIM 208
Cdd:PRK11749 227 DAVFIGTGaGLPR-FLGIPGenlggvysAVDFLTRVNQAVADYDLPvGKRVVViGGGNTAMDAAR--TAKRLgaeSVTIV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 209 MRsiplRGFDQqMSSMV--IEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWE--------DSTTGKE----DTGTF--DT 272
Cdd:PRK11749 304 YR----RGREE-MPASEeeVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVrmelgepdASGRRRVpiegSEFTLpaDL 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 48257067 273 VLWAIGRVPDTRSLNLEKaGVDTSPDTQKILVDSREATSVPHIYAIGDVVEG 324
Cdd:PRK11749 379 VIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTG 429
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
250-321 |
3.40e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 43.22 E-value: 3.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 48257067 250 DGQlQVT---WEDSTTGKEDTGTFDTVLWAIGRVPDTRSLnleKAGVDTSPDTQkILVDSREATSVPHIYAIGDV 321
Cdd:PRK15317 416 DGD-KVTgltYKDRTTGEEHHLELEGVFVQIGLVPNTEWL---KGTVELNRRGE-IIVDARGATSVPGVFAAGDC 485
|
|
| Met_tRNA_FMT_C |
cd08704 |
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl ... |
85-151 |
1.72e-03 |
|
C-terminal domain of Formyltransferase and other enzymes; C-terminal domain of formyl transferase and other proteins with diverse enzymatic activities. Proteins found in this family include methionyl-tRNA formyltransferase, ArnA, and 10-formyltetrahydrofolate dehydrogenase. Methionyl-tRNA formyltransferases constitute the majority of the family and also demonstrate greater sequence diversity. Although most proteins with formyltransferase activity contain the C-terminal domain, some formyltransferases ( for example, prokaryotic glycinamide ribonucleotide transformylase (GART)) only have the core catalytic domain, indicating that the C-terminal domain is not a requirement for catalytic activity and may be involved in substrate binding. For example, the C-terminal domain of methionyl-tRNA formyltransferase is involved in the tRNA binding.
Pssm-ID: 187732 [Multi-domain] Cd Length: 87 Bit Score: 37.51 E-value: 1.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 48257067 85 DWRKMAEAVQNHVKSLNW--GHRVQLQDRKVKYFniKASFVDEHTvcgVAKGGKEILLSADHIIIATGG 151
Cdd:cd08704 6 DWSKSAEEIHNLIRALNPwpGAYTTLNGKRLKIL--KAEVLEESG---EAAPGTILAVDKKGLLVACGD 69
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
181-337 |
2.03e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 40.39 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 181 KTLVVGASYVALECAGFLTGIGLDTTIMMRsiplRGfDQQMSSMV--IEHMASHGTRFLRGCAPsrVRRLPDG------- 251
Cdd:PRK12831 283 KVAVVGGGNVAMDAARTALRLGAEVHIVYR----RS-EEELPARVeeVHHAKEEGVIFDLLTNP--VEILGDEngwvkgm 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48257067 252 ---QLQVTWEDST--------TGKEDTGTFDTVLWAIGRVPDtRSLNLEKAGVDTSPDtQKILVDSRE-ATSVPHIYAIG 319
Cdd:PRK12831 356 kciKMELGEPDASgrrrpveiEGSEFVLEVDTVIMSLGTSPN-PLISSTTKGLKINKR-GCIVADEETgLTSKEGVFAGG 433
|
170
....*....|....*....
gi 48257067 320 DVVEGrpELTPIAIM-AGR 337
Cdd:PRK12831 434 DAVTG--AATVILAMgAGK 450
|
|
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