|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
28-511 |
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: 681.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 28 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 107
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 108 QPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPtHI 187
Cdd:TIGR01438 82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 188 EGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 267
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 268 CAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIG 347
Cdd:TIGR01438 241 FVPIKVEQI-EAKVLVEFTDSTNGIE--EEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIYAVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 348 DVVEGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTV 427
Cdd:TIGR01438 318 DILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLEWTI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 428 AGRD-ASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDP 506
Cdd:TIGR01438 398 PSRDnHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSGQDI 477
|
....*
gi 62089028 507 TVTGC 511
Cdd:TIGR01438 478 LQQGC 482
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
28-510 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 544.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 28 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQ-DAPNYGWEV 106
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 107 AQPvpHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTH 186
Cdd:PTZ00052 85 SSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPSIPED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 187 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLR 266
Cdd:PTZ00052 162 VPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 267 GCAPSRVRRLPDgQLQVTWEDSTTGKedtgtFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDsrEATSVPHIYAI 346
Cdd:PTZ00052 242 GVVPINIEKMDD-KIKVLFSDGTTEL-----FDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN--DCTNIPNIFAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 347 GDVVEGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFT 426
Cdd:PTZ00052 314 GDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 427 VAGRD--------------ASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEE 492
Cdd:PTZ00052 394 AVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEV 473
|
490
....*....|....*...
gi 62089028 493 VVKLRISKRSGLDPTVTG 510
Cdd:PTZ00052 474 FMNLSVTRRSGESFAAKG 491
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
42-497 |
1.45e-145 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 424.95 E-value: 1.45e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 42 ACAKEAAQLGRKVSVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQD-APNYGWEVAQPVpHDWRKMAEA 120
Cdd:PRK06116 18 ASANRAAMYGAKVALIEAKR---------LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENK-FDWAKLIAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 121 VQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIIIATGGRPRYPThIEGAlEYGITSDDI 200
Cdd:PRK06116 88 RDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTV---EVNGERY--TADHILIATGGRPSIPD-IPGA-EYGITSDGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 201 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 279
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGdAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 280 QLQVTWEDsttGKEDTgtFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVvEGRPELTPT 359
Cdd:PRK06116 241 SLTLTLED---GETLT--VDCLIWAIGREPNTDGLGLENAGVKLN-EKGYIIVDEYQNTNVPGIYAVGDV-TGRVELTPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 360 AIMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDAsQCYVK 438
Cdd:PRK06116 314 AIAAGRRLSERLFNNKPDEkLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 62089028 439 MVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 497
Cdd:PRK06116 393 LVVVGKEEK-VVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
42-494 |
1.57e-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: 371.73 E-value: 1.57e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 42 ACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPvPHDWRKMAEAV 121
Cdd:COG1249 17 VAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAP-SVDWAALMARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 122 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGALEYGITSDDIF 201
Cdd:COG1249 87 DKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTV--EVTGGETL--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 202 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGq 280
Cdd:COG1249 163 ELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 281 LQVTWEDSttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPTA 360
Cdd:COG1249 242 VTVTLEDG--GGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGG-IKVDEYLRTSVPGIYAIGDVT-GGPQLAHVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 361 IMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDAsQCYVKMV 440
Cdd:COG1249 318 SAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGID--VKVGKFPFAANGRALALGET-EGFVKLI 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 62089028 441 CLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVV 494
Cdd:COG1249 395 ADAE-TGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALK 447
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
42-497 |
7.91e-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: 361.85 E-value: 7.91e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 42 ACAKEAAQLGRKVSVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 121
Cdd:TIGR01421 16 ASARRAAEHGAKALLVEAKK---------LGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 122 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTvcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGAlEYGITSDDIF 201
Cdd:TIGR01421 87 DAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGT---VEVNGRDY--TAPHILIATGGKPSFPENIPGA-ELGTDSDGFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 202 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQ 280
Cdd:TIGR01421 161 ALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 281 LQVTWEDSTTgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVeGRPELTPTA 360
Cdd:TIGR01421 241 LVIHFEDGKS----IDDVDELIWAIGRKPNTKGLGLENVGIKLN-EKGQIIVDEYQNTNVPGIYALGDVV-GKVELTPVA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 361 IMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVaGRDASQCYVKM 439
Cdd:TIGR01421 315 IAAGRKLSERLFNGKTDDkLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAM-TSEKQKCRMKL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 62089028 440 VCLrEPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 497
Cdd:TIGR01421 394 VCA-GKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
28-497 |
1.68e-110 |
|
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: 335.24 E-value: 1.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 28 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDyvEPSpqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 107
Cdd:TIGR01424 2 DYDLFVIGAGSGGVRAARLAAALGAKVAIAE--EFR-------VGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 108 QpVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKeilLSADHIIIATGGRPRYPThI 187
Cdd:TIGR01424 73 K-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKPA-L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 188 EGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLR 266
Cdd:TIGR01424 148 PGH-ELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRILP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 267 GCAPSRVRRLPDGQLQVtwedsTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAI 346
Cdd:TIGR01424 227 EDSITSISKDDDGRLKA-----TLSKHEEIVADVVLFATGRSPNTNGLGLEAAGVRLN-DLGAIAVDEYSRTSTPSIYAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 347 GDVVEgRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFT 426
Cdd:TIGR01424 301 GDVTD-RINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRPMKAT 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62089028 427 VAGRDaSQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 497
Cdd:TIGR01424 378 FSGRQ-EKTLMKLV-VDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
44-501 |
5.31e-94 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 294.80 E-value: 5.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 44 AKEAAQLGRKVSVVDY-VEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQ 122
Cdd:PLN02507 41 ARFSANFGAKVGICELpFHPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEINEKVDFNWKKLLQKKT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 123 NHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPThIEGAlEYGITSDDIFW 202
Cdd:PLN02507 121 DEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGSRAQRPN-IPGK-ELAITSDEALS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 203 LKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGqL 281
Cdd:PLN02507 199 LEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-I 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 282 QVTwedSTTGKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEgRPELTPTAI 361
Cdd:PLN02507 278 KVI---TDHGEEFVA--DVVLFATGRAPNTKRLNLEAVGVELD-KAGAVKVDEYSRTNIPSIWAIGDVTN-RINLTPVAL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 362 MAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEhVEVYHAHYKPLEFTVAGRDaSQCYVKMVC 441
Cdd:PLN02507 351 MEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGD-ILVFTSSFNPMKNTISGRQ-EKTVMKLIV 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 442 LREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKR 501
Cdd:PLN02507 429 DAETDK-VLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMRSVTR 487
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
70-501 |
3.27e-83 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 268.28 E-value: 3.27e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 70 GLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKAS 149
Cdd:PLN02546 122 GVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGK 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 150 FVDEHTVcgvAKGGKeiLLSADHIIIATGGRPRYPtHIEGaLEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI 229
Cdd:PLN02546 202 IVDPHTV---DVDGK--LYTARNILIAVGGRPFIP-DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 230 GLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTwedstTGKEDTGTFDTVLWAIGRV 308
Cdd:PLN02546 275 KSDVHVFIRQKKvLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLK-----TNKGTVEGFSHVMFATGRK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 309 PDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEgRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTV 388
Cdd:PLN02546 350 PNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVPSIWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAV 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 389 FTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREppQLVLGLHFLGPNAGEVTQGFAL 468
Cdd:PLN02546 428 FSQPPIGQVGLTEEQAIEEYGD--VDVFTANFRPLKATLSGLPDRVFMKLIVCAKT--NKVLGVHMCGEDAPEIIQGFAV 503
|
410 420 430
....*....|....*....|....*....|...
gi 62089028 469 GIKCGASYAQVMRTVGIHPTCSEEVVKLRISKR 501
Cdd:PLN02546 504 AVKAGLTKADFDATVGIHPTAAEEFVTMRTPTR 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
28-496 |
5.41e-82 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 265.33 E-value: 5.41e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 28 DYDLLVVGGGSGGLACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 107
Cdd:PTZ00058 48 VYDLIVIGGGSGGMAAARRAARNKAKVALVE---------KDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 108 QPVphDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVC--GVAKGGKEI------------------- 166
Cdd:PTZ00058 119 FSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLikKVSQVDGEAdesdddevtivsagvsqld 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 167 ---LLSADHIIIATGGRPRYPtHIEGaLEYGITSDDIFWLKEsPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPL 242
Cdd:PTZ00058 197 dgqVIEGKNILIAVGNKPIFP-DVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 243 RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSttGKEDtgTFDTVLWAIGRVPDTRSLNLEKAGVD 322
Cdd:PTZ00058 274 RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDG--RKYE--HFDYVIYCVGRSPNTEDLNLKALNIK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 323 TSPDTqkILVDSREATSVPHIYAIGDVVEGRP---------------------------------ELTPTAIMAGRLLVQ 369
Cdd:PTZ00058 350 TPKGY--IKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvQLTPVAINAGRLLAD 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 370 RLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDASQ---CYVKMVCLrEPP 446
Cdd:PTZ00058 428 RLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDMDPAQkekTYLKLVCV-GKE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 62089028 447 QLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 496
Cdd:PTZ00058 507 ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
47-497 |
1.11e-77 |
|
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: 251.82 E-value: 1.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 47 AAQL-GRKVSVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEV-AQPVPHDWRKMAEAVQNH 124
Cdd:TIGR01423 22 AATLyKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFdRSSVKANWKALIAAKNKA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 125 VKSLNWGHRVQLQDRK-VKYFNIKASFVDEHTVCgVAKGG------KEiLLSADHIIIATGGRPRYPThIEGaLEYGITS 197
Cdd:TIGR01423 102 VLDINKSYEGMFADTEgLTFFLGWGALEDKNVVL-VRESAdpksavKE-RLQAEHILLATGSWPQMLG-IPG-IEHCISS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 198 DDIFWLKESPGKTLVVGASYVALECAGFLTG---IGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRV 273
Cdd:TIGR01423 178 NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMiLRGFDSTLRKELTKQLRANGINIMTNENPAKV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 274 RRLPDGQLQVTWEdstTGKedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTqKILVDSREATSVPHIYAIGDVVeGR 353
Cdd:TIGR01423 258 TLNADGSKHVTFE---SGK--TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKG-AIQVDEFSRTNVPNIYAIGDVT-DR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 354 PELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHgqEHVEVYHAHYKPLEFTVAGRDAS 433
Cdd:TIGR01423 331 VMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYK 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62089028 434 QCYVKMVClREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 497
Cdd:TIGR01423 409 KFVAKIVT-NHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMR 471
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
43-491 |
4.32e-76 |
|
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: 246.79 E-value: 4.32e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 43 CAKEAAQLGRKVSVVDYVEpspqgtrwgLGGTCVNVGCIPKK-LMHQAALLGGlIQDAPNYGWEVAQpVPHDWRKMAEAV 121
Cdd:TIGR01350 16 AAIRAAQLGLKVALVEKEY---------LGGTCLNVGCIPTKaLLHSAEVYDE-IKHAKDLGIEVEN-VSVDWEKMQKRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 122 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRY-PTHIEGALEYGITSDDI 200
Cdd:TIGR01350 85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTV-SVTGENGEETLEAKNIIIATGSRPRSlPGPFDFDGKVVITSTGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 201 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPD 278
Cdd:TIGR01350 164 LNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 279 gqlQVTWEDSTtGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVVEGrPELTP 358
Cdd:TIGR01350 243 ---QVTYENKG-GETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIGG-PMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 359 TAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGqehvevyhaHYKPLEFTVA--GR----DA 432
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGY---------DVKIGKFPFAanGKalalGE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 62089028 433 SQCYVKMVCLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 491
Cdd:TIGR01350 388 TDGFVKIIADKK-TGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
42-496 |
1.66e-70 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 232.40 E-value: 1.66e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 42 ACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRK----M 117
Cdd:PRK06370 19 PLAARAAGLGMKVALIE---------RGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAvmarK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 118 AEAVQN-HVKSLNWghrvqLQDRK-VKYFNIKASFVDEHTVCgVAkggkEILLSADHIIIATGGRPRYPtHIEGALEYG- 194
Cdd:PRK06370 90 RRIRARsRHGSEQW-----LRGLEgVDVFRGHARFESPNTVR-VG----GETLRAKRIFINTGARAAIP-PIPGLDEVGy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 195 ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiP--LRGFDQQMSSMVIEHMASHGTRFLRGCAPSR 272
Cdd:PRK06370 159 LTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERG-PrlLPREDEDVAAAVREILEREGIDVRLNAECIR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 273 VRRLPDGqlqVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDvVEG 352
Cdd:PRK06370 238 VERDGDG---IAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGY-IKVDDQLRTTNPGIYAAGD-CNG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 353 RPELTPTAIMAGRLLVQRLFGGS----SDLmdydNVPTTVFTPLEYGCVGLSEEEAVARhGQEhVEVYHahykpLEFTVA 428
Cdd:PRK06370 313 RGAFTHTAYNDARIVAANLLDGGrrkvSDR----IVPYATYTDPPLARVGMTEAEARKS-GRR-VLVGT-----RPMTRV 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62089028 429 GR----DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 496
Cdd:PRK06370 382 GRavekGETQGFMKVV-VDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
27-491 |
2.85e-70 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 231.57 E-value: 2.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 27 RDYDLLVVGGGSGGLACAKEAAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEv 106
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 107 AQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTH 186
Cdd:PRK06416 73 AENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTV-RVMTEDGEQTYTAKNIILATGSRPRELPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 187 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRF 264
Cdd:PRK06416 152 IEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveALPRI-LPGEDKEISKLAERALKKRGIKI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 265 LRGcapSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTspDTQKILVDSREATSVPHIY 344
Cdd:PRK06416 231 KTG---AKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKT--DRGFIEVDEQLRTNVPNIY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 345 AIGDVVEGrPELTPTAIMAGRLLVQRLFGGSSDlMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYhahykplE 424
Cdd:PRK06416 306 AIGDIVGG-PMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVV-------K 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62089028 425 FTVAGR------DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 491
Cdd:PRK06416 375 FPFAGNgkalalGETDGFVKLI-FDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
42-495 |
3.08e-67 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 223.52 E-value: 3.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 42 ACAKEAAQLGRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPhDWRKMAEAV 121
Cdd:PRK06292 17 VAARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKI-DFKKVMARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 122 QNHVKSLNWGH-RVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIIIATGGR-PRYPThIEGALEYGI-TSD 198
Cdd:PRK06292 87 RRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTV---EVNGERI--EAKNIVIATGSRvPPIPG-VWLILGDRLlTSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 199 DIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHgTRFLRGCAPSRVRRL 276
Cdd:PRK06292 161 DAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVfeRGDRI-LPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 277 PDGQLQVTWEDsttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVeGRPEL 356
Cdd:PRK06292 239 GDEKVEELEKG---GKTETIEADYVLVATGRRPNTDGLGLENTGIELD-ERGRPVVDEHTQTSVPGIYAAGDVN-GKPPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 357 TPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARhGQEHVEvyhAHYkplEFTVAGR----DA 432
Cdd:PRK06292 314 LHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAA-GIDYVV---GEV---PFEAQGRarvmGK 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62089028 433 SQCYVKMVCLREPpQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTcSEEVVK 495
Cdd:PRK06292 387 NDGFVKVYADKKT-GRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPT-LSEGLR 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
42-491 |
4.45e-64 |
|
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: 215.36 E-value: 4.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 42 ACAKEAAQLGRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPnYGWEVAQPVPhDWRKMAEAV 121
Cdd:TIGR02053 14 AAAIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPP-FGGLAATVAV-DFGELLEGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 122 QNHVKSLnwghrvqlqdRKVKYFNI-----------KASFVDEHTVcgVAKGGKEIlLSADHIIIATGGRPRYPtHIEGA 190
Cdd:TIGR02053 83 REVVEEL----------RHEKYEDVlssygvdylrgRARFKDPKTV--KVDLGREV-RGAKRFLIATGARPAIP-PIPGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 191 LEYG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGC 268
Cdd:TIGR02053 149 KEAGyLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTSA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 269 APSRVRRLPDGQLQVTwedSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGD 348
Cdd:TIGR02053 229 QVKAVSVRGGGKIITV---EKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGG-ILVDETLRTSNPGIYAAGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 349 VVeGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAvarhgQEHVEVYHAHYKPLEFTVA 428
Cdd:TIGR02053 305 VT-GGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEA-----QKAGIECDCRTLPLTNVPR 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62089028 429 GR--DASQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 491
Cdd:TIGR02053 379 ARinRDTRGFIKLVAEPGTGK-VLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
42-364 |
3.68e-61 |
|
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: 202.93 E-value: 3.68e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 42 ACAKEAAQLGRKVSVVdyvepspqgtrwGLGGTCVNVGCIPKKLMHQAAllggliqdapnygwEVAQPVPHdWRKMAEAV 121
Cdd:pfam07992 14 AAALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAA--------------EAPEIASL-WADLYKRK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 122 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGvakggKEILLSADHIIIATGGRPRYPThIEGALEYG------I 195
Cdd:pfam07992 67 EEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDG-----DGETITYDRLVIATGARPRLPP-IPGVELNVgflvrtL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 196 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVR 274
Cdd:pfam07992 141 DSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 275 RLPDGQLQVTwedsttGKEDTGTFDTVLWAIGRVPDTRslNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVEGRP 354
Cdd:pfam07992 221 GDGDGVEVIL------KDGTEIDADLVVVAIGRRPNTE--LLEAAGLELDERGG-IVVDEYLRTSVPGIYAAGDCRVGGP 291
|
330
....*....|
gi 62089028 355 ELTPTAIMAG 364
Cdd:pfam07992 292 ELAQNAVAQG 301
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
44-461 |
8.06e-53 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 185.36 E-value: 8.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 44 AKEAAQLGRKVSVVDyvepspqgTRWGLGGTCVNVGCIPKKLMHQAAL-LGGLIQDA--PNYGwEVAQPVPHDWRKMAEA 120
Cdd:PRK05249 21 AMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlySSYR-VKLRITFADLLARADH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 121 VQNHVKSLnwgHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDI 200
Cdd:PRK05249 92 VINKQVEV---RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 201 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 279
Cdd:PRK05249 169 LSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTlINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 280 QLqVTWEDsttGKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPT 359
Cdd:PRK05249 249 VI-VHLKS---GKKIKA--DCLLYANGRTGNTDGLNLENAGLEADSRGQ-LKVNENYQTAVPHIYAVGDVI-GFPSLASA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 360 AIMAGRLLVQRLFGGSSDLMdYDNVPTTVFTPLEYGCVGLSEEEAVARHGqeHVEVYHAHYKPLeftvA-GRDASQCY-- 436
Cdd:PRK05249 321 SMDQGRIAAQHAVGEATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKV--PYEVGRARFKEL----ArAQIAGDNVgm 393
|
410 420
....*....|....*....|....*
gi 62089028 437 VKMVCLREPPQLvLGLHFLGPNAGE 461
Cdd:PRK05249 394 LKILFHRETLEI-LGVHCFGERATE 417
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
47-502 |
2.48e-45 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 165.48 E-value: 2.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 47 AAQLGRKVSVVDYVEpSPQGTRwGLGGTCVNVGCIPKK-LMHQAALLGGLIQDAPNYGWEVAQpVPHDWRKMAEAVQNHV 125
Cdd:PRK06327 23 AAQLGLKVACIEAWK-NPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGIHVDG-VKIDVAKMIARKDKVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 126 KSLNWGHRVQLQDRKVKYFNIKASFV---DEHTVCGVAKGGKEILlSADHIIIATGGRPRyptHIEGAL---EYGITSDD 199
Cdd:PRK06327 100 KKMTGGIEGLFKKNKITVLKGRGSFVgktDAGYEIKVTGEDETVI-TAKHVIIATGSEPR---HLPGVPfdnKIILDNTG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 200 IFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM--MRSIpLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLP 277
Cdd:PRK06327 176 ALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeaLPAF-LAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 278 DGqLQVTWEDSTtGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGrPELT 357
Cdd:PRK06327 255 KG-VSVAYTDAD-GEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLD-ERGFIPVDDHCRTNVPNVYAIGDVVRG-PMLA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 358 PTAIMAGrLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVArhgqEHVEvYHAHYKPleFTVAGR----DAS 433
Cdd:PRK06327 331 HKAEEEG-VAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKA----EGVE-YKAGKFP--FMANGRalamGEP 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62089028 434 QCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSeEVVK---LRISKRS 502
Cdd:PRK06327 403 DGFVKIIADAKTDE-ILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLS-EVWHeaaLAVDKRP 472
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
51-493 |
4.38e-43 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 158.58 E-value: 4.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 51 GRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVQNHVKSLN 129
Cdd:PRK07846 22 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 130 WG---HRVQLQDrKVKYFNIKASFVDEHTVCgVAKGGkeiLLSADHIIIATGGRPRYPTHI-EGALEYGiTSDDIFWLKE 205
Cdd:PRK07846 91 AGgeeYRGRDTP-NIDVYRGHARFIGPKTLR-TGDGE---EITADQVVIAAGSRPVIPPVIaDSGVRYH-TSDTIMRLPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 206 SPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMashGTRF-LR-GCAPSRVRRLPDGqLQ 282
Cdd:PRK07846 165 LPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISERFTELA---SKRWdVRlGRNVVGVSQDGSG-VT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 283 VTWEDSTtgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVveGRP-ELTPTAI 361
Cdd:PRK07846 241 LRLDDGS-----TVEADVLLVATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV--SSPyQLKHVAN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 362 MAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARhGQEHVeVYHAHYKPLEFTVAGRDASQCyVKMV 440
Cdd:PRK07846 313 HEARVVQHNLLHPDDLIaSDHRFVPAAVFTHPQIASVGLTENEARAA-GLDIT-VKVQNYGDVAYGWAMEDTTGF-VKLI 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 62089028 441 CLREPPQLvLGLHFLGPNAGEVTQGF----ALGIKcgasyAQVM--RTVGIHPTCSEEV 493
Cdd:PRK07846 390 ADRDTGRL-LGAHIIGPQASTLIQPLiqamSFGLD-----AREMarGQYWIHPALPEVV 442
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
42-471 |
1.88e-42 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 159.16 E-value: 1.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 42 ACAKEAAQLGRKVSVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 121
Cdd:PRK13748 112 AAALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 122 QNHVKSLnwghrvqlqdRKVKYFNI------------KASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPThIEG 189
Cdd:PRK13748 183 QARVDEL----------RHAKYEGIldgnpaitvlhgEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPP-IPG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 190 ALE--YGiTSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 267
Cdd:PRK13748 252 LKEtpYW-TSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEH 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 268 CAPSRVRRLpDGQLQVtwedsTTGKedtGTF--DTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYA 345
Cdd:PRK13748 331 TQASQVAHV-DGEFVL-----TTGH---GELraDKLLVATGRAPNTRSLALDAAGVTVNAQGA-IVIDQGMRTSVPHIYA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 346 IGDVVEgRPELTPTAIMAGRLLVQRLFGGSSDLmDYDNVPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEF 425
Cdd:PRK13748 401 AGDCTD-QPQFVYVAAAAGTRAAINMTGGDAAL-DLTAMPAVVFTDPQVATVGYSEAE--AHHDGIETDSRTLTLDNVPR 476
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 62089028 426 TVAGRDaSQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIK 471
Cdd:PRK13748 477 ALANFD-TRGFIKLV-IEEGSGRLIGVQAVAPEAGELIQTAALAIR 520
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
65-493 |
1.88e-40 |
|
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: 151.45 E-value: 1.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 65 QGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVqnhvkslnWGHRVQL------- 136
Cdd:TIGR03452 31 KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRV--------FGDRIDPiaagged 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 137 -----QDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHI-EGALEYgITSDDIFWLKESPGKT 210
Cdd:TIGR03452 98 yrrgdETPNIDVYDGHARFVGPRTL--RTGDGEEI--TGDQIVIAAGSRPYIPPAIaDSGVRY-HTNEDIMRLPELPESL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 211 LVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEhMASHGTRFLRGCAPSRVRRLPDGqLQVTWEDST 289
Cdd:TIGR03452 173 VIVGGGYIAAEFAHVFSALGTRVTIVNRSTKlLRHLDEDISDRFTE-IAKKKWDIRLGRNVTAVEQDGDG-VTLTLDDGS 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 290 tgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVveGRP-ELTPTAIMAGRLLV 368
Cdd:TIGR03452 251 -----TVTADVLLVATGRVPNGDLLDAEAAGVEVDED-GRIKVDEYGRTSARGVWALGDV--SSPyQLKHVANAEARVVK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 369 QRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVyhAHYKPLEFTVAGRDaSQCYVKMVCLREPPQ 447
Cdd:TIGR03452 323 HNLLHPNDlRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKI--QNYGDVAYGWAMED-TTGFCKLIADRDTGK 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 62089028 448 LvLGLHFLGPNAGEVTQGFALGIKCGASYAQVMR-TVGIHPTCSEEV 493
Cdd:TIGR03452 400 L-LGAHIIGPQASSLIQPLITAMAFGLDAREMARkQYWIHPALPEVV 445
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
384-496 |
1.96e-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: 130.75 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 384 VPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDASqCYVKMVCLREPpQLVLGLHFLGPNAGEVT 463
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADRET-GKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 62089028 464 QGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 496
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
44-491 |
6.38e-36 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 138.73 E-value: 6.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 44 AKEAAQLGRKVSVVdyvEPSPQGtrwgLGGTCVNVGCIPKKLMHQAAllggliqdapNYGWEVAQPVPHdwrkmAEAVQN 123
Cdd:PRK07251 19 AAKLASAGKKVALV---EESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQVMAT-----KNTVTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 124 HVKSLNWGhrvQLQDRKVKYFNIKASFVDEHTVCGVAkGGKEILLSADHIIIATGGRPRYPThIEGALE--YGITSDDIF 201
Cdd:PRK07251 77 RLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQA-GDEKIELTAETIVINTGAVSNVLP-IPGLADskHVYDSTGIQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 202 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQ 280
Cdd:PRK07251 152 SLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKN-DGDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 281 LQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDvVEGRPELTPTA 360
Cdd:PRK07251 231 VLVVTEDETY------RFDALLYATGRKPNTEPLGLENTDIELT-ERGAIKVDDYCQTSVPGVFAVGD-VNGGPQFTYIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 361 IMAGRLLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehvevyhahYKPLEFTVAG--RDASQCYV 437
Cdd:PRK07251 303 LDDFRIVFGYLTGDGSyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLP---------YAVKELLVAAmpRAHVNNDL 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 62089028 438 K---MVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 491
Cdd:PRK07251 374 RgafKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
47-491 |
1.63e-30 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 123.35 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 47 AAQLGRKVSVVDYVEPSPQGtrwgLGGTCVNVGCIPKKLmhqaallggLIQDApnygwEVAQPVPHDWRKMAEAVqNHVK 126
Cdd:NF040477 19 AATLAKAGWRVAIIEQSAQM----YGGTCINIGCIPTKT---------LVHDA-----EQHQDFSTAMQRKSSVV-GFLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 127 SLNWGHRVQLQDrkVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSDDIF 201
Cdd:NF040477 80 DKNYHNLADLDN--VDVINGRAEFIDNHTL-RVFQADGEQELRGEKIFINTGAQSVLPpipglTTTPGVYD----STGLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 202 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLpDGQ 280
Cdd:NF040477 153 NLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAeLFLPREDRDIAQAIATILQDQGVELILNAQVQRVSSH-EGE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 281 LQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGrPELTPTA 360
Cdd:NF040477 232 VQLETAEGVL------TVDALLVASGRKPATAGLQLQNAGVAVN-ERGAIVVDKYLRTTADNIWAMGDVTGG-LQFTYIS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 361 IMAGRLLVQRLFG-GSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVagrDASQCYVKM 439
Cdd:NF040477 304 LDDFRIVRDSLLGeGKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVM---NDTRGVLKA 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 62089028 440 VcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 491
Cdd:NF040477 381 V-VDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSE 431
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
152-398 |
3.71e-30 |
|
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: 119.92 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 152 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITS----DDIFWLKE-----SPGKTLVVGASYVALEC 222
Cdd:COG0446 65 EAKTV--TLRDGETL--SYDKLVLATGARPRPP-PIPGLDLPGVFTlrtlDDADALREalkefKGKRAVVIGGGPIGLEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 223 AGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGQLQVTWEDsttgkEDTGTFDTV 301
Cdd:COG0446 140 AEALRKRGLKVTLVeRAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTD-----GEEIPADLV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 302 LWAIGRVPDTrSLnLEKAGVDTSPdTQKILVDSREATSVPHIYAIGDVVE------GRPELTP---TAIMAGRLLVQRLF 372
Cdd:COG0446 213 VVAPGVRPNT-EL-AKDAGLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasAANKQGRVAAENIL 289
|
250 260
....*....|....*....|....*...
gi 62089028 373 GGSsdlMDYDNVPTTVFT--PLEYGCVG 398
Cdd:COG0446 290 GGP---APFPGLGTFISKvfDLCIASTG 314
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
42-491 |
6.76e-25 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 108.46 E-value: 6.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 42 ACAKEAAQLGRKVSVVDYVEPSpqgtrwgLGGTCVNVGCIPKKLMHQAA------------LLGGLIQDAPNYGWE---- 105
Cdd:PTZ00153 130 AAAINAMERGLKVIIFTGDDDS-------IGGTCVNVGCIPSKALLYATgkyrelknlaklYTYGIYTNAFKNGKNdpve 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 106 ----VAQPVPHDWRKMAEAVQNHVKSLNWG-------HRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEilLSADHII 174
Cdd:PTZ00153 203 rnqlVADTVQIDITKLKEYTQSVIDKLRGGienglksKKFCKNSEHVQVIYERGHIVDKNTI-KSEKSGKE--FKVKNII 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 175 IATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiplrgfdQQMSSMVI 254
Cdd:PTZ00153 280 IATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYS-------PQLLPLLD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 255 EHMASHGTRFLRGCAPSRVR--------RLPDGQLQVT--WEDSTTGKEDTGTF----------DTVLWAIGRVPDTRSL 314
Cdd:PTZ00153 353 ADVAKYFERVFLKSKPVRVHlntlieyvRAGKGNQPVIigHSERQTGESDGPKKnmndiketyvDSCLVATGRKPNTNNL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 315 NLEKAGVDTS----PDTQKILVDSREATSVPHIYAIGDvVEGRPELTPTA----------IMA--GRLLVQRLFGGSSDL 378
Cdd:PTZ00153 433 GLDKLKIQMKrgfvSVDEHLRVLREDQEVYDNIFCIGD-ANGKQMLAHTAshqalkvvdwIEGkgKENVNINVENWASKP 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 379 MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKP-------LEFTVAGRDASQCY--------------V 437
Cdd:PTZ00153 512 IIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEISFYKAnskvlceNNISFPNNSKNNSYnkgkyntvdntegmV 591
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 62089028 438 KMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 491
Cdd:PTZ00153 592 KIVYLKDTKE-ILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISE 644
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
47-490 |
1.51e-24 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 106.48 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 47 AAQLGRKVSVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHdwRKMAEAVQNHVK 126
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEA--RVDLPAVNARVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 127 SLNWGH----RVQLQDRKVKYFNIKASFVDE----HTVCGVAKGGKEILLSADHIIIATGGRPRYpthIEGALEYG---I 195
Cdd:PRK07845 89 ALAAAQsadiRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPRI---LPTAEPDGeriL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 196 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQmSSMVIEH-MASHGTRFLRGCAPSRV 273
Cdd:PRK07845 166 TWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDAD-AAEVLEEvFARRGMTVLKRSRAESV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 274 RRLPDGQLqVTWEDsttGKEDTGTFdtVLWAIGRVPDTRSLNLEKAGVDTSPdTQKILVD--SReaTSVPHIYAIGDVVE 351
Cdd:PRK07845 245 ERTGDGVV-VTLTD---GRTVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDrvSR--TSVPGIYAAGDCTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 352 GRPeLTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSeeEAVARHGQEHVEVY------HAHYKPLEF 425
Cdd:PRK07845 316 VLP-LASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVS--QAAIDSGEVPARTVmlplatNPRAKMSGL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62089028 426 tvagRDAsqcYVKMVClREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCS 490
Cdd:PRK07845 393 ----RDG---FVKLFC-RPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLS 449
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
72-496 |
3.41e-23 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 102.01 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 72 GGTCVNVGCIPKKLmhqaallggLIQDAPNYG-WEVAQPvphdwRKmaEAVQNHVKSLNWGHRVQLQDrkVKYFNIKASF 150
Cdd:PRK08010 40 GGTCINIGCIPTKT---------LVHDAQQHTdFVRAIQ-----RK--NEVVNFLRNKNFHNLADMPN--IDVIDGQAEF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 151 VDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSDDIFWLKESPGKTLVVGASYVALECAGF 225
Cdd:PRK08010 102 INNHSL-RVHRPEGNLEIHGEKIFINTGAQTVVPpipgiTTTPGVYD----STGLLNLKELPGHLGILGGGYIGVEFASM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 226 LTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDSTTgkedtgTFDTVLWA 304
Cdd:PRK08010 177 FANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISH-HENQVQVHSEHAQL------AVDALLIA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 305 IGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGRpELTPTAIMAGRLLVQRLFG-GSSDLMDYDN 383
Cdd:PRK08010 250 SGRQPATASLHPENAGIAVN-ERGAIVVDKYLHTTADNIWAMGDVTGGL-QFTYISLDDYRIVRDELLGeGKRSTDDRKN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 384 VPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREppQLVLGLHFLGPNAGEVT 463
Cdd:PRK08010 328 VPYSVFMTPPLSRVGMTEEQ--ARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKT--QRILGASLLCVDSHEMI 403
|
410 420 430
....*....|....*....|....*....|...
gi 62089028 464 QGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 496
Cdd:PRK08010 404 NIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
152-408 |
1.64e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 99.45 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 152 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPThIEGALEYGITS----DDIFWLKE--SPGKTLVV-GASYVALECAG 224
Cdd:COG1251 85 AARTV--TLADGETL--PYDKLVLATGSRPRVPP-IPGADLPGVFTlrtlDDADALRAalAPGKRVVViGGGLIGLEAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 225 FLTGIGLDTT-IMMRSIPL-RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDsttgkedtGTF---D 299
Cdd:COG1251 160 ALRKRGLEVTvVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLAD--------GEElpaD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 300 TVLWAIGRVPDTrSLnLEKAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE------GRP--ELTPTAIMAGRLLVQRL 371
Cdd:COG1251 231 LVVVAIGVRPNT-EL-ARAAGLAVD---RGIVVDDYLRTSDPDIYAAGDCAEhpgpvyGRRvlELVAPAYEQARVAAANL 305
|
250 260 270
....*....|....*....|....*....|....*....
gi 62089028 372 FGGSSDLMDYDNVPTTVFTPLEYGCVGLSE--EEAVARH 408
Cdd:COG1251 306 AGGPAAYEGSVPSTKLKVFGVDVASAGDAEgdEEVVVRG 344
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
159-366 |
2.53e-17 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 82.48 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 159 VAKGGKEILLSADHIIIATGGRPRYPThIEGALE-------YGITSDDIFWlkesPGKT-LVVGASYVALECAGFLTGIG 230
Cdd:COG0492 90 RVTTDDGTEYEAKAVIIATGAGPRKLG-LPGEEEfegrgvsYCATCDGFFF----RGKDvVVVGGGDSALEEALYLTKFA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 231 LDTTIMMRSIPLRGfdqqmSSMVIEHMASH-GTRFLRGCAPSRVrrLPDGQLQ-VTWEDSTTGKEDTGTFDTVLWAIGRV 308
Cdd:COG0492 165 SKVTLIHRRDELRA-----SKILVERLRANpKIEVLWNTEVTEI--EGDGRVEgVTLKNVKTGEEKELEVDGVFVAIGLK 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 62089028 309 PDTrSLnLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVVEGRPELTPTAIMAGRL 366
Cdd:COG0492 238 PNT-EL-LKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAI 292
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
127-440 |
5.91e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 83.17 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 127 SLNWGHRVQLQDRKVKYFNIKAsfvdehtvcgvAKGGKEILLSADHIIIATGGRPRYPTHIEGALE--YGITS-DDIFWL 203
Cdd:PRK09564 72 DVKTEHEVVKVDAKNKTITVKN-----------LKTGSIFNDTYDKLMIATGARPIIPPIKNINLEnvYTLKSmEDGLAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 204 KESPGKT-----LVVGASYVALECAGFLTGIGLDTTIMMRS--IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrl 276
Cdd:PRK09564 141 KELLKDEeikniVIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELHLNEFVKSL--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 277 pDGQLQVTWEDSTTGKEDTgtfDTVLWAIGRVPDTRSLnlEKAGVDTSpDTQKILVDSREATSVPHIYAIGD------VV 350
Cdd:PRK09564 218 -IGEDKVEGVVTDKGEYEA---DVVIVATGVKPNTEFL--EDTGLKTL-KNGAIIVDEYGETSIENIYAAGDcatiynIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 351 EGRPELTPTAIMA---GRLLVQRLFG---------GSSDLMDYDnvpttvftpLEYGCVGLSEEEAVArHGQEHVEVY-- 416
Cdd:PRK09564 291 SNKNVYVPLATTAnklGRMVGENLAGrhvsfkgtlGSACIKVLD---------LEAARTGLTEEEAKK-LGIDYKTVFik 360
|
330 340
....*....|....*....|....*..
gi 62089028 417 ---HAHYKPleftvagrDASQCYVKMV 440
Cdd:PRK09564 361 dknHTNYYP--------GQEDLYVKLI 379
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
209-284 |
1.20e-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: 69.16 E-value: 1.20e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62089028 209 KTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVT 284
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVeRRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
164-371 |
7.66e-11 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 63.47 E-value: 7.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 164 KEILLSADHIIIATGG-RPRYPThIEG--------ALEY---------GITSddifWLKESP---GKTLVVGASYVALEC 222
Cdd:PRK12770 113 EELVKKYDAVLIATGTwKSRKLG-IPGedlpgvysALEYlfriraaklGYLP----WEKVPPvegKKVVVVGAGLTAVDA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 223 A--GFLTGIGLDTTIMMRSIPlrgfDQQMSSMVIEHMASHGTRFLRGCAP------SRVRRLPDGQLQVTWEDST----- 289
Cdd:PRK12770 188 AleAVLLGAEKVYLAYRRTIN----EAPAGKYEIERLIARGVEFLELVTPvriigeGRVEGVELAKMRLGEPDESgrprp 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 290 ---TGKEDTGTFDTVLWAIGRVPdTRSLNLEKAGVDTSPDTqKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGRL 366
Cdd:PRK12770 264 vpiPGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKG-EIVVDEKHMTSREGVFAAGDVVTG-PSKIGKAIKSGLR 340
|
....*
gi 62089028 367 LVQRL 371
Cdd:PRK12770 341 AAQSI 345
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
152-406 |
1.23e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 63.23 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 152 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITSDDI-----FW----------LKESPGKTLVVGAS 216
Cdd:COG1252 84 EARTV--TLADGRTL--SYDYLVIATGSVTNFF-GIPGLAEHALPLKTLedalaLRerllaaferaERRRLLTIVVVGGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 217 Y----VALECAGFLTGIGLDTTIMMRSI----------PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGqlq 282
Cdd:COG1252 159 PtgveLAGELAELLRKLLRYPGIDPDKVritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADG--- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 283 VTWEDSTTGKedtgtFDTVLWAIG-RVPDTrslnLEKAGVDTSPDTQkILVDSR-EATSVPHIYAIGDVV-----EGRPe 355
Cdd:COG1252 234 VTLEDGEEIP-----ADTVIWAAGvKAPPL----LADLGLPTDRRGR-VLVDPTlQVPGHPNVFAIGDCAavpdpDGKP- 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 62089028 356 LTPTAIMA-------GRLLVQRLFGGssdlmdydnvPTTVFTPLEYGC-VGLSEEEAVA 406
Cdd:COG1252 303 VPKTAQAAvqqakvlAKNIAALLRGK----------PLKPFRYRDKGClASLGRGAAVA 351
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
209-422 |
1.51e-09 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 60.18 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 209 KTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrlpDGQLqVTWEd 287
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKiNKLMDADMNQPILDELDKREIPYRLNEEIDAI----NGNE-VTFK- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 288 stTGKEDtgTFDTVLWAIGRVPDTRSlnLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEG------RPELTPTAI 361
Cdd:PRK13512 224 --SGKVE--HYDMIIEGVGTHPNSKF--IESSNIKLD-DKGFIPVNDKFETNVPNIYAIGDIITShyrhvdLPASVPLAW 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62089028 362 MAGR---LLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEaVARHGQEHVEV---YHAHYKP 422
Cdd:PRK13512 297 GAHRaasIVAEQIAGNDTiEFKGFLGNNIVKFFDYTFASVGVKPNE-LKQFDYKMVEVtqgAHANYYP 363
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
171-365 |
2.32e-07 |
|
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: 53.22 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 171 DHIIIATG-GRPRyPTHIEG--------ALEY--GITSDDIFWLKESPGKTLVV-GASYVALECAGflTGIGL---DTTI 235
Cdd:COG0493 208 DAVFLATGaGKPR-DLGIPGedlkgvhsAMDFltAVNLGEAPDTILAVGKRVVViGGGNTAMDCAR--TALRLgaeSVTI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 236 MMRsiplRGFDQqMSSMV--IEHMASHGTRFLRGCAPSRVRRLPDGQL------QVTW-EDSTTGK----EDTGTF---- 298
Cdd:COG0493 285 VYR----RTREE-MPASKeeVEEALEEGVEFLFLVAPVEIIGDENGRVtglecvRMELgEPDESGRrrpvPIEGSEftlp 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62089028 299 -DTVLWAIGRVPDTRSLnLEKAGVDTSPDTqKILVDSRE-ATSVPHIYAIGDVVEGrPELTPTAIMAGR 365
Cdd:COG0493 360 aDLVILAIGQTPDPSGL-EEELGLELDKRG-TIVVDEETyQTSLPGVFAGGDAVRG-PSLVVWAIAEGR 425
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
171-365 |
5.45e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 48.64 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 171 DHIIIATG-GRPRyPTHIEG--------ALEYGITSDDIFWLKESP-GKTLVV-GASYVALECAGflTGIGL---DTTIM 236
Cdd:PRK11749 227 DAVFIGTGaGLPR-FLGIPGenlggvysAVDFLTRVNQAVADYDLPvGKRVVViGGGNTAMDAAR--TAKRLgaeSVTIV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 237 MRsiplRGFDQqMSSMV--IEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWE--------DSTTGKE----DTGTF--DT 300
Cdd:PRK11749 304 YR----RGREE-MPASEeeVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVrmelgepdASGRRRVpiegSEFTLpaDL 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62089028 301 VLWAIGRVPDTRSLNLEKaGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGR 365
Cdd:PRK11749 379 VIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTG-AATVVWAVGDGK 441
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
132-351 |
9.70e-06 |
|
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: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 132 HRVQLqdrkvkYFNIKASFVDEHTVCGVAKGGKeiLLSADHIIIATGGRPRYPThIEGALEYGITS-------DDIFWLK 204
Cdd:TIGR02374 67 HGITL------YTGETVIQIDTDQKQVITDAGR--TLSYDKLILATGSYPFILP-IPGADKKGVYVfrtiedlDAIMAMA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 205 ESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGcapsrvrrlpdgqlQ 282
Cdd:TIGR02374 138 QRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVihHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLE--------------K 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62089028 283 VTWEDSTTGKEDTGTF--------DTVLWAIGRVPDTRsLNLEkAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE 351
Cdd:TIGR02374 204 DTVEIVGATKADRIRFkdgssleaDLIVMAAGIRPNDE-LAVS-AGIKVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
211-378 |
2.54e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 46.45 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 211 LVVGASYVALECAGFLTGIGLDTTIMMRSiplrgfDQQMSSMV-------IEH-MASHGTRFLRGCAPSRVRRLPDGqLQ 282
Cdd:PRK04965 145 LVVGGGLIGTELAMDLCRAGKAVTLVDNA------ASLLASLMppevssrLQHrLTEMGVHLLLKSQLQGLEKTDSG-IR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62089028 283 VTWEDSttgkeDTGTFDTVLWAIGRVPDTrSLNLEkAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE--GR--PELTP 358
Cdd:PRK04965 218 ATLDSG-----RSIEVDAVIAAAGLRPNT-ALARR-AGLAVN---RGIVVDSYLQTSAPDIYALGDCAEinGQvlPFLQP 287
|
170 180
....*....|....*....|
gi 62089028 359 tAIMAGRLLVQRLFGGSSDL 378
Cdd:PRK04965 288 -IQLSAMALAKNLLGQNTPL 306
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
278-349 |
3.52e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 43.22 E-value: 3.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62089028 278 DGQlQVT---WEDSTTGKEDTGTFDTVLWAIGRVPDTRSLnleKAGVDTSPDTQkILVDSREATSVPHIYAIGDV 349
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 ... |
113-179 |
1.87e-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: 1.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62089028 113 DWRKMAEAVQNHVKSLNW--GHRVQLQDRKVKYFniKASFVDEHTvcgVAKGGKEILLSADHIIIATGG 179
Cdd:cd08704 6 DWSKSAEEIHNLIRALNPwpGAYTTLNGKRLKIL--KAEVLEESG---EAAPGTILAVDKKGLLVACGD 69
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
299-365 |
4.23e-03 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 39.76 E-value: 4.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62089028 299 DTVLWAIGRVPDTRSLnLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGR 365
Cdd:PRK12810 390 DLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNAYQTSNPKVFAAGDMRRG-QSLVVWAIAEGR 454
|
|
| |
