|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
38-523 |
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: 690.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 38 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 117
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 118 QPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPtHI 197
Cdd:TIGR01438 82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 198 EGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 277
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 278 CAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIG 357
Cdd:TIGR01438 241 FVPIKVEQI-EAKVLVEFTDSTNGIE--EEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIYAVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 358 DVVEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTV 437
Cdd:TIGR01438 318 DILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLEWTI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 438 AGRD-ASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDP 516
Cdd:TIGR01438 398 PSRDnHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSGQDI 477
|
....*..
gi 1205913878 517 TVTGCUG 523
Cdd:TIGR01438 478 LQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
38-523 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 552.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 38 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQ-DAPNYGWEV 116
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 117 AQPvpHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTH 196
Cdd:PTZ00052 85 SSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPSIPED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 197 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLR 276
Cdd:PTZ00052 162 VPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 277 GCAPSRVRRLPDgQLQVTWEDSTTGKedtgtFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDsrEATSVPHIYAI 356
Cdd:PTZ00052 242 GVVPINIEKMDD-KIKVLFSDGTTEL-----FDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN--DCTNIPNIFAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 357 GDVVEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFT 436
Cdd:PTZ00052 314 GDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 437 VAGRD--------------ASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEE 502
Cdd:PTZ00052 394 AVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEV 473
|
490 500
....*....|....*....|.
gi 1205913878 503 VVKLRISKRSGLDPTVTGCUG 523
Cdd:PTZ00052 474 FMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
52-507 |
1.08e-145 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 425.72 E-value: 1.08e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 52 ACAKEAAQLGRKVAVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQD-APNYGWEVAQPVpHDWRKMAEA 130
Cdd:PRK06116 18 ASANRAAMYGAKVALIEAKR---------LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENK-FDWAKLIAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 131 VQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIIIATGGRPRYPThIEGAlEYGITSDDI 210
Cdd:PRK06116 88 RDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTV---EVNGERY--TADHILIATGGRPSIPD-IPGA-EYGITSDGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 211 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 289
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGdAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 290 QLQVTWEDsttGKEDTgtFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVvEGRPELTPI 369
Cdd:PRK06116 241 SLTLTLED---GETLT--VDCLIWAIGREPNTDGLGLENAGVKLN-EKGYIIVDEYQNTNVPGIYAVGDV-TGRVELTPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 370 AIMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDAsQCYVK 448
Cdd:PRK06116 314 AIAAGRRLSERLFNNKPDEkLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1205913878 449 MVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 507
Cdd:PRK06116 393 LVVVGKEEK-VVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
52-504 |
1.46e-123 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 369.42 E-value: 1.46e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 52 ACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPvPHDWRKMAEAV 131
Cdd:COG1249 17 VAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAP-SVDWAALMARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 132 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGALEYGITSDDIF 211
Cdd:COG1249 87 DKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTV--EVTGGETL--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 212 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGq 290
Cdd:COG1249 163 ELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 291 LQVTWEDSttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPIA 370
Cdd:COG1249 242 VTVTLEDG--GGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGG-IKVDEYLRTSVPGIYAIGDVT-GGPQLAHVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 371 IMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDAsQCYVKMV 450
Cdd:COG1249 318 SAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGID--VKVGKFPFAANGRALALGET-EGFVKLI 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1205913878 451 CLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVV 504
Cdd:COG1249 395 ADAE-TGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALK 447
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
37-507 |
3.59e-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: 363.39 E-value: 3.59e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 37 RDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEV 116
Cdd:TIGR01421 1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKK---------LGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 117 AQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTvcgVAKGGKEIllSADHIIIATGGRPRYPTH 196
Cdd:TIGR01421 72 NDENTFNWPELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGT---VEVNGRDY--TAPHILIATGGKPSFPEN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 197 IEGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFL 275
Cdd:TIGR01421 147 IPGA-ELGTDSDGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVH 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 276 RGCAPSRVRRLPDGQLQVTWEDSTTgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYA 355
Cdd:TIGR01421 226 KLSKPVKVEKTVEGKLVIHFEDGKS----IDDVDELIWAIGRKPNTKGLGLENVGIKLN-EKGQIIVDEYQNTNVPGIYA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 356 IGDVVeGRPELTPIAIMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLE 434
Cdd:TIGR01421 301 LGDVV-GKVELTPVAIAAGRKLSERLFNGKTDDkLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMY 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205913878 435 FTVaGRDASQCYVKMVCLrEPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 507
Cdd:TIGR01421 380 YAM-TSEKQKCRMKLVCA-GKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
38-507 |
5.94e-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: 334.47 E-value: 5.94e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 38 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDyvEPSpqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 117
Cdd:TIGR01424 2 DYDLFVIGAGSGGVRAARLAAALGAKVAIAE--EFR-------VGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 118 QpVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKeilLSADHIIIATGGRPRYPThI 197
Cdd:TIGR01424 73 K-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKPA-L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 198 EGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLR 276
Cdd:TIGR01424 148 PGH-ELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRILP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 277 GCAPSRVRRLPDGQLQVtwedsTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAI 356
Cdd:TIGR01424 227 EDSITSISKDDDGRLKA-----TLSKHEEIVADVVLFATGRSPNTNGLGLEAAGVRLN-DLGAIAVDEYSRTSTPSIYAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 357 GDVVEgRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFT 436
Cdd:TIGR01424 301 GDVTD-RINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRPMKAT 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1205913878 437 VAGRDaSQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 507
Cdd:TIGR01424 378 FSGRQ-EKTLMKLV-VDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
28-511 |
3.90e-94 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 295.19 E-value: 3.90e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 28 GAARGAAGQRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDY-VEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLI 106
Cdd:PLN02507 15 NADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICELpFHPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 107 QDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIA 186
Cdd:PLN02507 95 EDAKNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 187 TGGRPRYPThIEGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIE 265
Cdd:PLN02507 175 TGSRAQRPN-IPGK-ELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDEMRAVVAR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 266 HMASHGTRFLRGCAPSRVRRLPDGqLQVTwedSTTGKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSR 345
Cdd:PLN02507 253 NLEGRGINLHPRTNLTQLTKTEGG-IKVI---TDHGEEFVA--DVVLFATGRAPNTKRLNLEAVGVELD-KAGAVKVDEY 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 346 EATSVPHIYAIGDVVEgRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEhVEV 425
Cdd:PLN02507 326 SRTNIPSIWAIGDVTN-RINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGD-ILV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 426 YHAHYKPLEFTVAGRDaSQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVK 505
Cdd:PLN02507 404 FTSSFNPMKNTISGRQ-EKTVMKLIVDAETDK-VLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVT 481
|
....*.
gi 1205913878 506 LRISKR 511
Cdd:PLN02507 482 MRSVTR 487
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
29-511 |
1.77e-84 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 272.13 E-value: 1.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 29 AARGAAGQR--DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDY-VEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGL 105
Cdd:PLN02546 68 APNGAESERhyDFDLFTIGAGSGGVRASRFASNFGASAAVCELpFATISSDTLGGVGGTCVLRGCVPKKLLVYASKYSHE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 106 IQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKeiLLSADHIII 185
Cdd:PLN02546 148 FEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTV---DVDGK--LYTARNILI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 186 ATGGRPRYPtHIEGaLEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVI 264
Cdd:PLN02546 223 AVGGRPFIP-DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKvLRGFDEEVRDFVA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 265 EHMASHGTRFLRGCAPSRVRRLPDGQLQVTwedstTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDS 344
Cdd:PLN02546 301 EQMSLRGIEFHTEESPQAIIKSADGSLSLK-----TNKGTVEGFSHVMFATGRKPNTKNLGLEEVGVKMD-KNGAIEVDE 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 345 REATSVPHIYAIGDVVEgRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVE 424
Cdd:PLN02546 375 YSRTSVPSIWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD--VD 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 425 VYHAHYKPLEFTVAGRDASQCYVKMVCLREppQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVV 504
Cdd:PLN02546 452 VFTANFRPLKATLSGLPDRVFMKLIVCAKT--NKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFV 529
|
....*..
gi 1205913878 505 KLRISKR 511
Cdd:PLN02546 530 TMRTPTR 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
38-506 |
7.68e-83 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 268.02 E-value: 7.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 38 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 117
Cdd:PTZ00058 48 VYDLIVIGGGSGGMAAARRAARNKAKVALVE---------KDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 118 QPVphDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVC--GVAKGGKEI------------------- 176
Cdd:PTZ00058 119 FSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLikKVSQVDGEAdesdddevtivsagvsqld 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 177 ---LLSADHIIIATGGRPRYPtHIEGaLEYGITSDDIFWLKEsPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPL 252
Cdd:PTZ00058 197 dgqVIEGKNILIAVGNKPIFP-DVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 253 RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSttGKEDtgTFDTVLWAIGRVPDTRSLNLEKAGVD 332
Cdd:PTZ00058 274 RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDG--RKYE--HFDYVIYCVGRSPNTEDLNLKALNIK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 333 TSPDTqkILVDSREATSVPHIYAIGDVVEGRP---------------------------------ELTPIAIMAGRLLVQ 379
Cdd:PTZ00058 350 TPKGY--IKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvQLTPVAINAGRLLAD 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 380 RLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDASQ---CYVKMVCLrEPP 456
Cdd:PTZ00058 428 RLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDMDPAQkekTYLKLVCV-GKE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1205913878 457 QLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 506
Cdd:PTZ00058 507 ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
57-507 |
1.46e-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: 254.51 E-value: 1.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 57 AAQL-GRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEV-AQPVPHDWRKMAEAVQNH 134
Cdd:TIGR01423 22 AATLyKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFdRSSVKANWKALIAAKNKA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 135 VKSLNWGHRVQLQDRK-VKYFNIKASFVDEHTVCgVAKGG------KEiLLSADHIIIATGGRPRYPThIEGaLEYGITS 207
Cdd:TIGR01423 102 VLDINKSYEGMFADTEgLTFFLGWGALEDKNVVL-VRESAdpksavKE-RLQAEHILLATGSWPQMLG-IPG-IEHCISS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 208 DDIFWLKESPGKTLVVGASYVALECAGFLTG---IGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRV 283
Cdd:TIGR01423 178 NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMiLRGFDSTLRKELTKQLRANGINIMTNENPAKV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 284 RRLPDGQLQVTWEdstTGKedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTqKILVDSREATSVPHIYAIGDVVeGR 363
Cdd:TIGR01423 258 TLNADGSKHVTFE---SGK--TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKG-AIQVDEFSRTNVPNIYAIGDVT-DR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 364 PELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHgqEHVEVYHAHYKPLEFTVAGRDAS 443
Cdd:TIGR01423 331 VMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYK 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1205913878 444 QCYVKMVClREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 507
Cdd:TIGR01423 409 KFVAKIVT-NHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMR 471
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
53-501 |
1.79e-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: 245.63 E-value: 1.79e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 53 CAKEAAQLGRKVAVVDYVEpspqgtrwgLGGTCVNVGCIPKK-LMHQAALLGGlIQDAPNYGWEVAQpVPHDWRKMAEAV 131
Cdd:TIGR01350 16 AAIRAAQLGLKVALVEKEY---------LGGTCLNVGCIPTKaLLHSAEVYDE-IKHAKDLGIEVEN-VSVDWEKMQKRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 132 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRY-PTHIEGALEYGITSDDI 210
Cdd:TIGR01350 85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTV-SVTGENGEETLEAKNIIIATGSRPRSlPGPFDFDGKVVITSTGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 211 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPD 288
Cdd:TIGR01350 164 LNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 289 gqlQVTWEDSTtGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVVEGrPELTP 368
Cdd:TIGR01350 243 ---QVTYENKG-GETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIGG-PMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 369 IAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGqehvevyhaHYKPLEFTVA--GR----DA 442
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGY---------DVKIGKFPFAanGKalalGE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1205913878 443 SQCYVKMVCLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 501
Cdd:TIGR01350 388 TDGFVKIIADKK-TGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
37-501 |
2.73e-69 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 229.26 E-value: 2.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 37 RDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEv 116
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 117 AQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTH 196
Cdd:PRK06416 73 AENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTV-RVMTEDGEQTYTAKNIILATGSRPRELPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 197 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRF 274
Cdd:PRK06416 152 IEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveALPRI-LPGEDKEISKLAERALKKRGIKI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 275 LRGcapSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTspDTQKILVDSREATSVPHIY 354
Cdd:PRK06416 231 KTG---AKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKT--DRGFIEVDEQLRTNVPNIY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 355 AIGDVVEGrPELTPIAIMAGRLLVQRLFGGSSDlMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYhahykplE 434
Cdd:PRK06416 306 AIGDIVGG-PMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVV-------K 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205913878 435 FTVAGR------DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 501
Cdd:PRK06416 375 FPFAGNgkalalGETDGFVKLI-FDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
52-506 |
5.51e-69 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 228.55 E-value: 5.51e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 52 ACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRK----M 127
Cdd:PRK06370 19 PLAARAAGLGMKVALIE---------RGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAvmarK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 128 AEAVQN-HVKSLNWghrvqLQDRK-VKYFNIKASFVDEHTVCgVAkggkEILLSADHIIIATGGRPRYPtHIEGALEYG- 204
Cdd:PRK06370 90 RRIRARsRHGSEQW-----LRGLEgVDVFRGHARFESPNTVR-VG----GETLRAKRIFINTGARAAIP-PIPGLDEVGy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 205 ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiP--LRGFDQQMSSMVIEHMASHGTRFLRGCAPSR 282
Cdd:PRK06370 159 LTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERG-PrlLPREDEDVAAAVREILEREGIDVRLNAECIR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 283 VRRLPDGqlqVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDvVEG 362
Cdd:PRK06370 238 VERDGDG---IAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGY-IKVDDQLRTTNPGIYAAGD-CNG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 363 RPELTPIAIMAGRLLVQRLFGGS----SDLmdydNVPTTVFTPLEYGCVGLSEEEAVARhGQEhVEVYHahykpLEFTVA 438
Cdd:PRK06370 313 RGAFTHTAYNDARIVAANLLDGGrrkvSDR----IVPYATYTDPPLARVGMTEAEARKS-GRR-VLVGT-----RPMTRV 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1205913878 439 GR----DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 506
Cdd:PRK06370 382 GRavekGETQGFMKVV-VDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
52-505 |
7.81e-67 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 222.75 E-value: 7.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 52 ACAKEAAQLGRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPhDWRKMAEAV 131
Cdd:PRK06292 17 VAARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKI-DFKKVMARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 132 QNHVKSLNWGH-RVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIIIATGGR-PRYPThIEGALEYGI-TSD 208
Cdd:PRK06292 87 RRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTV---EVNGERI--EAKNIVIATGSRvPPIPG-VWLILGDRLlTSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 209 DIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHgTRFLRGCAPSRVRRL 286
Cdd:PRK06292 161 DAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVfeRGDRI-LPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 287 PDGQLQVTWEDsttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVeGRPEL 366
Cdd:PRK06292 239 GDEKVEELEKG---GKTETIEADYVLVATGRRPNTDGLGLENTGIELD-ERGRPVVDEHTQTSVPGIYAAGDVN-GKPPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 367 TPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARhGQEHVEVYHahykplEFTVAGR----DA 442
Cdd:PRK06292 314 LHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAA-GIDYVVGEV------PFEAQGRarvmGK 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1205913878 443 SQCYVKMVCLREPpQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTcSEEVVK 505
Cdd:PRK06292 387 NDGFVKVYADKKT-GRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPT-LSEGLR 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
52-523 |
1.10e-63 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 214.59 E-value: 1.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 52 ACAKEAAQLGRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPnYGWEVAQPVPhDWRKMAEAV 131
Cdd:TIGR02053 14 AAAIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPP-FGGLAATVAV-DFGELLEGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 132 QNHVKSLnwghrvqlqdRKVKYFNI-----------KASFVDEHTVcgVAKGGKEIlLSADHIIIATGGRPRYPtHIEGA 200
Cdd:TIGR02053 83 REVVEEL----------RHEKYEDVlssygvdylrgRARFKDPKTV--KVDLGREV-RGAKRFLIATGARPAIP-PIPGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 201 LEYG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGC 278
Cdd:TIGR02053 149 KEAGyLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTSA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 279 APSRVRRLPDGQLQVTwedSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGD 358
Cdd:TIGR02053 229 QVKAVSVRGGGKIITV---EKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGG-ILVDETLRTSNPGIYAAGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 359 VVeGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAvarhgQEHVEVYHAHYKPLEFTVA 438
Cdd:TIGR02053 305 VT-GGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEA-----QKAGIECDCRTLPLTNVPR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 439 GR--DASQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEevvKLRISKRSGL-D 515
Cdd:TIGR02053 379 ARinRDTRGFIKLVAEPGTGK-VLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE---GLKLAAQTFYrD 454
|
....*...
gi 1205913878 516 PTVTGCUG 523
Cdd:TIGR02053 455 VSKLSCCA 462
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
52-374 |
1.50e-59 |
|
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: 198.70 E-value: 1.50e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 52 ACAKEAAQLGRKVAVVdyvepspqgtrwGLGGTCVNVGCIPKKLMHQAAllggliqdapnygwEVAQPVPHdWRKMAEAV 131
Cdd:pfam07992 14 AAALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAA--------------EAPEIASL-WADLYKRK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 132 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGvakggKEILLSADHIIIATGGRPRYPThIEGALEYG------I 205
Cdd:pfam07992 67 EEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDG-----DGETITYDRLVIATGARPRLPP-IPGVELNVgflvrtL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 206 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVR 284
Cdd:pfam07992 141 DSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 285 RLPDGQLQVTwedsttGKEDTGTFDTVLWAIGRVPDTRslNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVEGRP 364
Cdd:pfam07992 221 GDGDGVEVIL------KDGTEIDADLVVVAIGRRPNTE--LLEAAGLELDERGG-IVVDEYLRTSVPGIYAAGDCRVGGP 291
|
330
....*....|
gi 1205913878 365 ELTPIAIMAG 374
Cdd:pfam07992 292 ELAQNAVAQG 301
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
54-471 |
4.86e-52 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 183.43 E-value: 4.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 54 AKEAAQLGRKVAVVDyvepspqgTRWGLGGTCVNVGCIPKKLMHQAAL-LGGLIQDA--PNYGwEVAQPVPHDWRKMAEA 130
Cdd:PRK05249 21 AMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlySSYR-VKLRITFADLLARADH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 131 VQNHVKSLnwgHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDI 210
Cdd:PRK05249 92 VINKQVEV---RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 211 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 289
Cdd:PRK05249 169 LSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTlINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 290 QLqVTWEDsttGKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPI 369
Cdd:PRK05249 249 VI-VHLKS---GKKIKA--DCLLYANGRTGNTDGLNLENAGLEADSRGQ-LKVNENYQTAVPHIYAVGDVI-GFPSLASA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 370 AIMAGRLLVQRLFGGSSDLMdYDNVPTTVFTPLEYGCVGLSEEEAVARHGqeHVEVYHAHYKPLeftvA-GRDASQCY-- 446
Cdd:PRK05249 321 SMDQGRIAAQHAVGEATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKV--PYEVGRARFKEL----ArAQIAGDNVgm 393
|
410 420
....*....|....*....|....*
gi 1205913878 447 VKMVCLREPPQLvLGLHFLGPNAGE 471
Cdd:PRK05249 394 LKILFHRETLEI-LGVHCFGERATE 417
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
61-503 |
1.31e-43 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 160.50 E-value: 1.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 61 GRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVQNHVKSLN 139
Cdd:PRK07846 22 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 140 WG---HRVQLQDrKVKYFNIKASFVDEHTVCgVAKGGkeiLLSADHIIIATGGRPRYPTHI-EGALEYGiTSDDIFWLKE 215
Cdd:PRK07846 91 AGgeeYRGRDTP-NIDVYRGHARFIGPKTLR-TGDGE---EITADQVVIAAGSRPVIPPVIaDSGVRYH-TSDTIMRLPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 216 SPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMashGTRF-LR-GCAPSRVRRLPDGqLQ 292
Cdd:PRK07846 165 LPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISERFTELA---SKRWdVRlGRNVVGVSQDGSG-VT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 293 VTWEDSTtgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVveGRP-ELTPIAI 371
Cdd:PRK07846 241 LRLDDGS-----TVEADVLLVATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV--SSPyQLKHVAN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 372 MAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARhGQEHVeVYHAHYKPLEFTVAGRDASQCyVKMV 450
Cdd:PRK07846 313 HEARVVQHNLLHPDDLIaSDHRFVPAAVFTHPQIASVGLTENEARAA-GLDIT-VKVQNYGDVAYGWAMEDTTGF-VKLI 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1205913878 451 CLREPPQLvLGLHFLGPNAGEVTQGF----ALGIKcgasyAQVM--RTVGIHPTCSEEV 503
Cdd:PRK07846 390 ADRDTGRL-LGAHIIGPQASTLIQPLiqamSFGLD-----AREMarGQYWIHPALPEVV 442
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
36-512 |
2.67e-42 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 157.39 E-value: 2.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 36 QRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEpSPQGTRwGLGGTCVNVGCIPKK-LMHQAALLGGLIQDAPNYGW 114
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWK-NPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 115 EVAQpVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFV---DEHTVCGVAKGGKEIlLSADHIIIATGGRP 191
Cdd:PRK06327 80 HVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktDAGYEIKVTGEDETV-ITAKHVIIATGSEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 192 RyptHIEGAL---EYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM--MRSIpLRGFDQQMSSMVIEH 266
Cdd:PRK06327 158 R---HLPGVPfdnKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeaLPAF-LAAADEQVAKEAAKA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 267 MASHGTRFLRGCAPSRVRRLPDGqLQVTWEDStTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSRE 346
Cdd:PRK06327 234 FTKQGLDIHLGVKIGEIKTGGKG-VSVAYTDA-DGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLD-ERGFIPVDDHC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 347 ATSVPHIYAIGDVVEGrPELTPIAIMAGrLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVArhgqEHVEvY 426
Cdd:PRK06327 311 RTNVPNVYAIGDVVRG-PMLAHKAEEEG-VAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKA----EGVE-Y 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 427 HAHYKPleFTVAGR----DASQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSeE 502
Cdd:PRK06327 384 KAGKFP--FMANGRalamGEPDGFVKIIADAKTDE-ILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLS-E 459
|
490
....*....|...
gi 1205913878 503 VVK---LRISKRS 512
Cdd:PRK06327 460 VWHeaaLAVDKRP 472
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
52-481 |
3.26e-41 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 156.08 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 52 ACAKEAAQLGRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 131
Cdd:PRK13748 112 AAALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 132 QNHVKSLnwghrvqlqdRKVKYFNI------------KASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPThIEG 199
Cdd:PRK13748 183 QARVDEL----------RHAKYEGIldgnpaitvlhgEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPP-IPG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 200 ALE--YGiTSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 277
Cdd:PRK13748 252 LKEtpYW-TSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEH 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 278 CAPSRVRRLpDGQLQVtwedsTTGKedtGTF--DTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYA 355
Cdd:PRK13748 331 TQASQVAHV-DGEFVL-----TTGH---GELraDKLLVATGRAPNTRSLALDAAGVTVNAQGA-IVIDQGMRTSVPHIYA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 356 IGDVVEgRPELTPIAIMAGRLLVQRLFGGSSDLmDYDNVPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEF 435
Cdd:PRK13748 401 AGDCTD-QPQFVYVAAAAGTRAAINMTGGDAAL-DLTAMPAVVFTDPQVATVGYSEAE--AHHDGIETDSRTLTLDNVPR 476
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1205913878 436 TVAGRDaSQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIK 481
Cdd:PRK13748 477 ALANFD-TRGFIKLV-IEEGSGRLIGVQAVAPEAGELIQTAALAIR 520
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
61-503 |
1.56e-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: 151.83 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 61 GRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVqnhvksln 139
Cdd:TIGR03452 23 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRV-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 140 WGHRVQL------------QDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGALEYGITS 207
Cdd:TIGR03452 84 FGDRIDPiaaggedyrrgdETPNIDVYDGHARFVGPRTL--RTGDGEEI--TGDQIVIAAGSRPYIPPAIADSGVRYHTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 208 DDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEhMASHGTRFLRGCAPSRVRRL 286
Cdd:TIGR03452 160 EDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKlLRHLDEDISDRFTE-IAKKKWDIRLGRNVTAVEQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 287 PDGqLQVTWEDSTtgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVveGRP-E 365
Cdd:TIGR03452 239 GDG-VTLTLDDGS-----TVTADVLLVATGRVPNGDLLDAEAAGVEVDED-GRIKVDEYGRTSARGVWALGDV--SSPyQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 366 LTPIAIMAGRLLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVyhAHYKPLEFTVAGRDaSQ 444
Cdd:TIGR03452 310 LKHVANAEARVVKHNLLHPNDlRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKI--QNYGDVAYGWAMED-TT 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 445 CYVKMVCLREPPQLvLGLHFLGPNAGEVTQGFALGIKCGASYAQVMR-TVGIHPTCSEEV 503
Cdd:TIGR03452 387 GFCKLIADRDTGKL-LGAHIIGPQASSLIQPLITAMAFGLDAREMARkQYWIHPALPEVV 445
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
54-501 |
8.96e-37 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 141.43 E-value: 8.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 54 AKEAAQLGRKVAVVdyvEPSPQGtrwgLGGTCVNVGCIPKKLMHQAAllggliqdapNYGWEVAQPVPHdwrkmAEAVQN 133
Cdd:PRK07251 19 AAKLASAGKKVALV---EESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQVMAT-----KNTVTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 134 HVKSLNWGhrvQLQDRKVKYFNIKASFVDEHTVCGVAkGGKEILLSADHIIIATGGRPRYPThIEGALE--YGITSDDIF 211
Cdd:PRK07251 77 RLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQA-GDEKIELTAETIVINTGAVSNVLP-IPGLADskHVYDSTGIQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 212 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQ 290
Cdd:PRK07251 152 SLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKN-DGDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 291 LQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDvVEGRPELTPIA 370
Cdd:PRK07251 231 VLVVTEDETY------RFDALLYATGRKPNTEPLGLENTDIELT-ERGAIKVDDYCQTSVPGVFAVGD-VNGGPQFTYIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 371 IMAGRLLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehvevyhahYKPLEFTVAG--RDASQCYV 447
Cdd:PRK07251 303 LDDFRIVFGYLTGDGSyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLP---------YAVKELLVAAmpRAHVNNDL 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1205913878 448 K---MVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 501
Cdd:PRK07251 374 RgafKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
394-506 |
1.05e-35 |
|
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: 128.83 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 394 VPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDASqCYVKMVCLREPpQLVLGLHFLGPNAGEVT 473
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADRET-GKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 1205913878 474 QGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 506
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
54-501 |
5.94e-31 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 124.89 E-value: 5.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 54 AKEAAQLGRKVAVVdyvEPSPQGtrwgLGGTCVNVGCIPKKLmhqaallggLIQDApnygwEVAQPVPHDWRKMAEAVqN 133
Cdd:NF040477 19 AATLAKAGWRVAII---EQSAQM----YGGTCINIGCIPTKT---------LVHDA-----EQHQDFSTAMQRKSSVV-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 134 HVKSLNWGHRVQLQDrkVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSD 208
Cdd:NF040477 77 FLRDKNYHNLADLDN--VDVINGRAEFIDNHTL-RVFQADGEQELRGEKIFINTGAQSVLPpipglTTTPGVYD----ST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 209 DIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLp 287
Cdd:NF040477 150 GLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAeLFLPREDRDIAQAIATILQDQGVELILNAQVQRVSSH- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 288 DGQLQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGrPELT 367
Cdd:NF040477 229 EGEVQLETAEGVL------TVDALLVASGRKPATAGLQLQNAGVAVN-ERGAIVVDKYLRTTADNIWAMGDVTGG-LQFT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 368 PIAIMAGRLLVQRLFG-GSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVagrDASQCY 446
Cdd:NF040477 301 YISLDDFRIVRDSLLGeGKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVM---NDTRGV 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1205913878 447 VKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 501
Cdd:NF040477 378 LKAV-VDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSE 431
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
162-408 |
1.10e-28 |
|
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: 116.06 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 162 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITS----DDIFWLKE-----SPGKTLVVGASYVALEC 232
Cdd:COG0446 65 EAKTV--TLRDGETL--SYDKLVLATGARPRPP-PIPGLDLPGVFTlrtlDDADALREalkefKGKRAVVIGGGPIGLEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 233 AGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGQLQVTWEDsttgkEDTGTFDTV 311
Cdd:COG0446 140 AEALRKRGLKVTLVeRAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTD-----GEEIPADLV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 312 LWAIGRVPDTrSLnLEKAGVDTSPdTQKILVDSREATSVPHIYAIGDVVE------GRPELTP---IAIMAGRLLVQRLF 382
Cdd:COG0446 213 VVAPGVRPNT-EL-AKDAGLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasAANKQGRVAAENIL 289
|
250 260
....*....|....*....|....*...
gi 1205913878 383 GGSsdlMDYDNVPTTVFT--PLEYGCVG 408
Cdd:COG0446 290 GGP---APFPGLGTFISKvfDLCIASTG 314
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
17-501 |
3.86e-25 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 109.62 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 17 WRTQAVAGGVRGAARGAAGQ------RDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSpqgtrwgLGGTCVNVGC 90
Cdd:PTZ00153 89 SSPQPRSEKSLRANGFATSQsmnfsdEEYDVGIIGCGVGGHAAAINAMERGLKVIIFTGDDDS-------IGGTCVNVGC 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 91 IPKKLMHQAA------------LLGGLIQDAPNYGWE--------VAQPVPHDWRKMAEAVQNHVKSLNWG-------HR 143
Cdd:PTZ00153 162 IPSKALLYATgkyrelknlaklYTYGIYTNAFKNGKNdpvernqlVADTVQIDITKLKEYTQSVIDKLRGGienglksKK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 144 VQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEilLSADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVV 223
Cdd:PTZ00153 242 FCKNSEHVQVIYERGHIVDKNTI-KSEKSGKE--FKVKNIIIATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 224 GASYVALECAGFLTGIGLDTTIMMRSiplrgfdQQMSSMVIEHMASHGTRFLRGCAPSRVR--------RLPDGQLQVT- 294
Cdd:PTZ00153 319 GMGIIGLEFMDIYTALGSEVVSFEYS-------PQLLPLLDADVAKYFERVFLKSKPVRVHlntlieyvRAGKGNQPVIi 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 295 -WEDSTTGKEDTGTF----------DTVLWAIGRVPDTRSLNLEKAGVDTS----PDTQKILVDSREATSVPHIYAIGDv 359
Cdd:PTZ00153 392 gHSERQTGESDGPKKnmndiketyvDSCLVATGRKPNTNNLGLDKLKIQMKrgfvSVDEHLRVLREDQEVYDNIFCIGD- 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 360 VEGRPELTP------------IAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYH 427
Cdd:PTZ00153 471 ANGKQMLAHtashqalkvvdwIEGKGKENVNINVENWASKPIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEI 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 428 AHYKP-------LEFTVAGRDASQCY--------------VKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASY 486
Cdd:PTZ00153 551 SFYKAnskvlceNNISFPNNSKNNSYnkgkyntvdntegmVKIVYLKDTKE-ILGMFIVGSYASILIHEGVLAINLKLSV 629
|
570
....*....|....*
gi 1205913878 487 AQVMRTVGIHPTCSE 501
Cdd:PTZ00153 630 KDLAHMVHSHPTISE 644
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
82-506 |
6.22e-24 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 104.33 E-value: 6.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 82 GGTCVNVGCIPKKLmhqaallggLIQDAPNYG-WEVAQPvphdwRKmaEAVQNHVKSLNWGHRVQLQDrkVKYFNIKASF 160
Cdd:PRK08010 40 GGTCINIGCIPTKT---------LVHDAQQHTdFVRAIQ-----RK--NEVVNFLRNKNFHNLADMPN--IDVIDGQAEF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 161 VDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSDDIFWLKESPGKTLVVGASYVALECAGF 235
Cdd:PRK08010 102 INNHSL-RVHRPEGNLEIHGEKIFINTGAQTVVPpipgiTTTPGVYD----STGLLNLKELPGHLGILGGGYIGVEFASM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 236 LTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDSTTgkedtgTFDTVLWA 314
Cdd:PRK08010 177 FANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISH-HENQVQVHSEHAQL------AVDALLIA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 315 IGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGRpELTPIAIMAGRLLVQRLFG-GSSDLMDYDN 393
Cdd:PRK08010 250 SGRQPATASLHPENAGIAVN-ERGAIVVDKYLHTTADNIWAMGDVTGGL-QFTYISLDDYRIVRDELLGeGKRSTDDRKN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 394 VPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREppQLVLGLHFLGPNAGEVT 473
Cdd:PRK08010 328 VPYSVFMTPPLSRVGMTEEQ--ARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKT--QRILGASLLCVDSHEMI 403
|
410 420 430
....*....|....*....|....*....|...
gi 1205913878 474 QGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 506
Cdd:PRK08010 404 NIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
57-413 |
1.05e-23 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 103.79 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 57 AAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHdwRKMAEAVQNHVK 136
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEA--RVDLPAVNARVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 137 SLNWGH----RVQLQDRKVKYFNIKASFVDE----HTVCGVAKGGKEILLSADHIIIATGGRPRYpthIEGALEYG---I 205
Cdd:PRK07845 89 ALAAAQsadiRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPRI---LPTAEPDGeriL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 206 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQmSSMVIEH-MASHGTRFLRGCAPSRV 283
Cdd:PRK07845 166 TWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDAD-AAEVLEEvFARRGMTVLKRSRAESV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 284 RRLPDGQLqVTWEDsttGKEDTGTFdtVLWAIGRVPDTRSLNLEKAGVDTSPdTQKILVD--SReaTSVPHIYAIGDVVE 361
Cdd:PRK07845 245 ERTGDGVV-VTLTD---GRTVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDrvSR--TSVPGIYAAGDCTG 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1205913878 362 GRPeLTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEE 413
Cdd:PRK07845 316 VLP-LASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVSQAA 366
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
162-418 |
7.06e-21 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 94.82 E-value: 7.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 162 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPThIEGALEYGITS----DDIFWLKE--SPGKTLVV-GASYVALECAG 234
Cdd:COG1251 85 AARTV--TLADGETL--PYDKLVLATGSRPRVPP-IPGADLPGVFTlrtlDDADALRAalAPGKRVVViGGGLIGLEAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 235 FLTGIGLDTT-IMMRSIPL-RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDsttgkedtGTF---D 309
Cdd:COG1251 160 ALRKRGLEVTvVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLAD--------GEElpaD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 310 TVLWAIGRVPDTrSLnLEKAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE------GRP--ELTPIAIMAGRLLVQRL 381
Cdd:COG1251 231 LVVVAIGVRPNT-EL-ARAAGLAVD---RGIVVDDYLRTSDPDIYAAGDCAEhpgpvyGRRvlELVAPAYEQARVAAANL 305
|
250 260 270
....*....|....*....|....*....|....*....
gi 1205913878 382 FGGSSDLMDYDNVPTTVFTPLEYGCVGLSE--EEAVARH 418
Cdd:COG1251 306 AGGPAAYEGSVPSTKLKVFGVDVASAGDAEgdEEVVVRG 344
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
137-450 |
2.63e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 84.32 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 137 SLNWGHRVQLQDRKVKYFNIKAsfvdehtvcgvAKGGKEILLSADHIIIATGGRPRYPTHIEGALE--YGITS-DDIFWL 213
Cdd:PRK09564 72 DVKTEHEVVKVDAKNKTITVKN-----------LKTGSIFNDTYDKLMIATGARPIIPPIKNINLEnvYTLKSmEDGLAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 214 KESPGKT-----LVVGASYVALECAGFLTGIGLDTTIMMRS--IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrl 286
Cdd:PRK09564 141 KELLKDEeikniVIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELHLNEFVKSL--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 287 pDGQLQVTWEDSTTGKEDTgtfDTVLWAIGRVPDTRSLnlEKAGVDTSpDTQKILVDSREATSVPHIYAIGD------VV 360
Cdd:PRK09564 218 -IGEDKVEGVVTDKGEYEA---DVVIVATGVKPNTEFL--EDTGLKTL-KNGAIIVDEYGETSIENIYAAGDcatiynIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 361 EGRPELTPIAIMA---GRLLVQRLFG---------GSSDLMDYDnvpttvftpLEYGCVGLSEEEAVArHGQEHVEVY-- 426
Cdd:PRK09564 291 SNKNVYVPLATTAnklGRMVGENLAGrhvsfkgtlGSACIKVLD---------LEAARTGLTEEEAKK-LGIDYKTVFik 360
|
330 340
....*....|....*....|....*..
gi 1205913878 427 ---HAHYKPleftvagrDASQCYVKMV 450
Cdd:PRK09564 361 dknHTNYYP--------GQEDLYVKLI 379
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
169-376 |
6.96e-16 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 78.24 E-value: 6.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 169 VAKGGKEILLSADHIIIATGGRPRYPThIEGALE-------YGITSDDIFWlkesPGKT-LVVGASYVALECAGFLTGIG 240
Cdd:COG0492 90 RVTTDDGTEYEAKAVIIATGAGPRKLG-LPGEEEfegrgvsYCATCDGFFF----RGKDvVVVGGGDSALEEALYLTKFA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 241 LDTTIMMRSIPLRGfdqqmSSMVIEHMASH-GTRFLRGCAPSRVrrLPDGQLQ-VTWEDSTTGKEDTGTFDTVLWAIGRV 318
Cdd:COG0492 165 SKVTLIHRRDELRA-----SKILVERLRANpKIEVLWNTEVTEI--EGDGRVEgVTLKNVKTGEEKELEVDGVFVAIGLK 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1205913878 319 PDTrSLnLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVVEGRPELTPIAIMAGRL 376
Cdd:COG0492 238 PNT-EL-LKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAI 292
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
219-294 |
2.37e-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: 68.00 E-value: 2.37e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205913878 219 KTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVT 294
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVeRRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
219-432 |
6.75e-10 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 61.34 E-value: 6.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 219 KTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrlpDGQLqVTWEd 297
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKiNKLMDADMNQPILDELDKREIPYRLNEEIDAI----NGNE-VTFK- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 298 stTGKEDtgTFDTVLWAIGRVPDTRSlnLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEG------RPELTPIAI 371
Cdd:PRK13512 224 --SGKVE--HYDMIIEGVGTHPNSKF--IESSNIKLD-DKGFIPVNDKFETNVPNIYAIGDIITShyrhvdLPASVPLAW 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1205913878 372 MAGR---LLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEaVARHGQEHVEV---YHAHYKP 432
Cdd:PRK13512 297 GAHRaasIVAEQIAGNDTiEFKGFLGNNIVKFFDYTFASVGVKPNE-LKQFDYKMVEVtqgAHANYYP 363
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
174-381 |
1.17e-09 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 60.00 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 174 KEILLSADHIIIATGG-RPRYPThIEG--------ALEY---------GITSddifWLKESP---GKTLVVGASYVALEC 232
Cdd:PRK12770 113 EELVKKYDAVLIATGTwKSRKLG-IPGedlpgvysALEYlfriraaklGYLP----WEKVPPvegKKVVVVGAGLTAVDA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 233 A--GFLTGIGLDTTIMMRSIPlrgfDQQMSSMVIEHMASHGTRFLRGCAP------SRVRRLPDGQLQVTWEDST----- 299
Cdd:PRK12770 188 AleAVLLGAEKVYLAYRRTIN----EAPAGKYEIERLIARGVEFLELVTPvriigeGRVEGVELAKMRLGEPDESgrprp 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 300 ---TGKEDTGTFDTVLWAIGRVPdTRSLNLEKAGVDTSPDTqKILVDSREATSVPHIYAIGDVVEGrPELTPIAIMAGRL 376
Cdd:PRK12770 264 vpiPGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKG-EIVVDEKHMTSREGVFAAGDVVTG-PSKIGKAIKSGLR 340
|
....*
gi 1205913878 377 LVQRL 381
Cdd:PRK12770 341 AAQSI 345
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
162-416 |
3.13e-09 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 58.99 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 162 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITSDDI-----FW----------LKESPGKTLVVGAS 226
Cdd:COG1252 84 EARTV--TLADGRTL--SYDYLVIATGSVTNFF-GIPGLAEHALPLKTLedalaLRerllaaferaERRRLLTIVVVGGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 227 Y----VALECAGFLTGIGLDTTIMMRSI----------PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGqlq 292
Cdd:COG1252 159 PtgveLAGELAELLRKLLRYPGIDPDKVritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADG--- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 293 VTWEDSTTGKedtgtFDTVLWAIG-RVPDTrslnLEKAGVDTSPDTQkILVDSR-EATSVPHIYAIGDVV-----EGRPe 365
Cdd:COG1252 234 VTLEDGEEIP-----ADTVIWAAGvKAPPL----LADLGLPTDRRGR-VLVDPTlQVPGHPNVFAIGDCAavpdpDGKP- 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1205913878 366 LTPIAIMA-------GRLLVQRLFGGssdlmdydnvPTTVFTPLEYGC-VGLSEEEAVA 416
Cdd:COG1252 303 VPKTAQAAvqqakvlAKNIAALLRGK----------PLKPFRYRDKGClASLGRGAAVA 351
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
181-375 |
5.61e-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: 48.59 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 181 DHIIIATG-GRPRyPTHIEG--------ALEY--GITSDDIFWLKESPGKTLVV-GASYVALECAGflTGIGL---DTTI 245
Cdd:COG0493 208 DAVFLATGaGKPR-DLGIPGedlkgvhsAMDFltAVNLGEAPDTILAVGKRVVViGGGNTAMDCAR--TALRLgaeSVTI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 246 MMRsiplRGFDQqMSSMV--IEHMASHGTRFLRGCAPSRVRRLPDGQL------QVTW-EDSTTGK----EDTGTF---- 308
Cdd:COG0493 285 VYR----RTREE-MPASKeeVEEALEEGVEFLFLVAPVEIIGDENGRVtglecvRMELgEPDESGRrrpvPIEGSEftlp 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205913878 309 -DTVLWAIGRVPDTRSLnLEKAGVDTSPDTqKILVDSRE-ATSVPHIYAIGDVVEGrPELTPIAIMAGR 375
Cdd:COG0493 360 aDLVILAIGQTPDPSGL-EEELGLELDKRG-TIVVDEETyQTSLPGVFAGGDAVRG-PSLVVWAIAEGR 425
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
221-388 |
8.09e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 47.99 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 221 LVVGASYVALECAGFLTGIGLDTTIMMRSiplrgfDQQMSSMV-------IEH-MASHGTRFLRGCAPSRVRRLPDGqLQ 292
Cdd:PRK04965 145 LVVGGGLIGTELAMDLCRAGKAVTLVDNA------ASLLASLMppevssrLQHrLTEMGVHLLLKSQLQGLEKTDSG-IR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 293 VTWEDSttgkeDTGTFDTVLWAIGRVPDTrSLNLEkAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE--GR--PELTP 368
Cdd:PRK04965 218 ATLDSG-----RSIEVDAVIAAAGLRPNT-ALARR-AGLAVN---RGIVVDSYLQTSAPDIYALGDCAEinGQvlPFLQP 287
|
170 180
....*....|....*....|
gi 1205913878 369 IaIMAGRLLVQRLFGGSSDL 388
Cdd:PRK04965 288 I-QLSAMALAKNLLGQNTPL 306
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
142-361 |
1.39e-05 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 47.90 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 142 HRVQLqdrkvkYFNIKASFVDEHTVCGVAKGGKeiLLSADHIIIATGGRPRYPThIEGALEYGITS-------DDIFWLK 214
Cdd:TIGR02374 67 HGITL------YTGETVIQIDTDQKQVITDAGR--TLSYDKLILATGSYPFILP-IPGADKKGVYVfrtiedlDAIMAMA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 215 ESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGcapsrvrrlpdgqlQ 292
Cdd:TIGR02374 138 QRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVihHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLE--------------K 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1205913878 293 VTWEDSTTGKEDTGTF--------DTVLWAIGRVPDTRsLNLEkAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE 361
Cdd:TIGR02374 204 DTVEIVGATKADRIRFkdgssleaDLIVMAAGIRPNDE-LAVS-AGIKVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
181-362 |
5.53e-05 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 45.56 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 181 DHIIIATG-GRPRyPTHIEG--------ALEYGITSDDIFWLKESP-GKTLVV-GASYVALECAGflTGIGL---DTTIM 246
Cdd:PRK11749 227 DAVFIGTGaGLPR-FLGIPGenlggvysAVDFLTRVNQAVADYDLPvGKRVVViGGGNTAMDAAR--TAKRLgaeSVTIV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 247 MRsiplRGFDQqMSSMV--IEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWE--------DSTTGKE----DTGTF--DT 310
Cdd:PRK11749 304 YR----RGREE-MPASEeeVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVrmelgepdASGRRRVpiegSEFTLpaDL 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1205913878 311 VLWAIGRVPDTRSLNLEKaGVDTSPDTQKILVDSREATSVPHIYAIGDVVEG 362
Cdd:PRK11749 379 VIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTG 429
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
288-359 |
4.64e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 42.84 E-value: 4.64e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1205913878 288 DGQlQVT---WEDSTTGKEDTGTFDTVLWAIGRVPDTRSLnleKAGVDTSPDTQkILVDSREATSVPHIYAIGDV 359
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 ... |
123-189 |
2.45e-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: 37.13 E-value: 2.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1205913878 123 DWRKMAEAVQNHVKSLNW--GHRVQLQDRKVKYFniKASFVDEHTvcgVAKGGKEILLSADHIIIATGG 189
Cdd:cd08704 6 DWSKSAEEIHNLIRALNPwpGAYTTLNGKRLKIL--KAEVLEESG---EAAPGTILAVDKKGLLVACGD 69
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
219-375 |
2.96e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 40.00 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 219 KTLVVGASYVALECAGFLTGIGLDTTIMMRsiplRGfDQQMSSMV--IEHMASHGTRFLRGCAPsrVRRLPDG------- 289
Cdd:PRK12831 283 KVAVVGGGNVAMDAARTALRLGAEVHIVYR----RS-EEELPARVeeVHHAKEEGVIFDLLTNP--VEILGDEngwvkgm 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1205913878 290 ---QLQVTWEDST--------TGKEDTGTFDTVLWAIGRVPDtRSLNLEKAGVDTSPDtQKILVDSRE-ATSVPHIYAIG 357
Cdd:PRK12831 356 kciKMELGEPDASgrrrpveiEGSEFVLEVDTVIMSLGTSPN-PLISSTTKGLKINKR-GCIVADEETgLTSKEGVFAGG 433
|
170
....*....|....*....
gi 1205913878 358 DVVEGrpELTPIAIM-AGR 375
Cdd:PRK12831 434 DAVTG--AATVILAMgAGK 450
|
|
| |
