|
Name |
Accession |
Description |
Interval |
E-value |
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
9-494 |
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: 688.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 9 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 88
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPTPLGTRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 89 QPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPtHI 168
Cdd:TIGR01438 82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNKKGKEKIYSAERFLIATGERPRYP-GI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 169 EGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 248
Cdd:TIGR01438 161 PGAKELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDCANKVGEHMEEHGVKFKRQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 249 CAPSRVRRLpDGQLQVTWEDSTTGKEdtGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIG 328
Cdd:TIGR01438 241 FVPIKVEQI-EAKVLVEFTDSTNGIE--EEYDTVLLAIGRDACTRKLNLENVGVKINKKTGKIPADEEEQTNVPYIYAVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 329 DVVEGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTV 408
Cdd:TIGR01438 318 DILEDKPELTPVAIQAGRLLAQRLFKGSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLEWTI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 409 AGRD-ASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDP 487
Cdd:TIGR01438 398 PSRDnHNKCYAKLVCNKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTLSVTKRSGQDI 477
|
....*..
gi 13486927 488 TVTGCUG 494
Cdd:TIGR01438 478 LQQGCCG 484
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
9-494 |
0e+00 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 550.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 9 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQ-DAPNYGWEV 87
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPSTQGTKWGLGGTCVNVGCVPKKLMHYAANIGSIFHhDSQMYGWKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 88 AQPvpHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTH 167
Cdd:PTZ00052 85 SSS--FNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTV-SYGDNSQEETITAKYILIATGGRPSIPED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 168 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLR 247
Cdd:PTZ00052 162 VPGAKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGFDRQCSEKVVEYMKEQGTLFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 248 GCAPSRVRRLPDgQLQVTWEDSTTGKedtgtFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDsrEATSVPHIYAI 327
Cdd:PTZ00052 242 GVVPINIEKMDD-KIKVLFSDGTTEL-----FDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN--DCTNIPNIFAV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 328 GDVVEGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFT 407
Cdd:PTZ00052 314 GDVVEGRPELTPVAIKAGILLARRLFKQSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 408 VAGRD--------------ASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEE 473
Cdd:PTZ00052 394 AVHREkherarkdeydfdvSSNCLAKLVCVKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEV 473
|
490 500
....*....|....*....|.
gi 13486927 474 VVKLRISKRSGLDPTVTGCUG 494
Cdd:PTZ00052 474 FMNLSVTRRSGESFAAKGGCG 494
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
23-478 |
1.11e-146 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 427.27 E-value: 1.11e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 23 ACAKEAAQLGRKVAVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQD-APNYGWEVAQPVpHDWRKMAEA 101
Cdd:PRK06116 18 ASANRAAMYGAKVALIEAKR---------LGGTCVNVGCVPKKLMWYGAQIAEAFHDyAPGYGFDVTENK-FDWAKLIAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 102 VQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIIIATGGRPRYPThIEGAlEYGITSDDI 181
Cdd:PRK06116 88 RDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTV---EVNGERY--TADHILIATGGRPSIPD-IPGA-EYGITSDGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 182 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 260
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGdAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 261 QLQVTWEDsttGKEDTgtFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVvEGRPELTPT 340
Cdd:PRK06116 241 SLTLTLED---GETLT--VDCLIWAIGREPNTDGLGLENAGVKLN-EKGYIIVDEYQNTNVPGIYAVGDV-TGRVELTPV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 341 AIMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDAsQCYVK 419
Cdd:PRK06116 314 AIAAGRRLSERLFNNKPDEkLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQ-PCLMK 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 13486927 420 MVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 478
Cdd:PRK06116 393 LVVVGKEEK-VVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
23-475 |
4.48e-126 |
|
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: 374.81 E-value: 4.48e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 23 ACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPvPHDWRKMAEAV 102
Cdd:COG1249 17 VAAIRAAQLGLKVALVE---------KGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAP-SVDWAALMARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 103 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGALEYGITSDDIF 182
Cdd:COG1249 87 DKVVDRLRGGVEELLKKNGVDVIRGRARFVDPHTV--EVTGGETL--TADHIVIATGSRPRVPPIPGLDEVRVLTSDEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 183 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGq 261
Cdd:COG1249 163 ELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVeRGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 262 LQVTWEDSttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPTA 341
Cdd:COG1249 242 VTVTLEDG--GGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDERGG-IKVDEYLRTSVPGIYAIGDVT-GGPQLAHVA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 342 IMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDAsQCYVKMV 421
Cdd:COG1249 318 SAEGRVAAENILGKKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAGID--VKVGKFPFAANGRALALGET-EGFVKLI 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 13486927 422 CLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVV 475
Cdd:COG1249 395 ADAE-TGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALK 447
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
23-478 |
2.19e-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: 363.01 E-value: 2.19e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 23 ACAKEAAQLGRKVAVVDYVEpspqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 102
Cdd:TIGR01421 16 ASARRAAEHGAKALLVEAKK---------LGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNDENTFNWPELKEKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 103 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTvcgVAKGGKEIllSADHIIIATGGRPRYPTHIEGAlEYGITSDDIF 182
Cdd:TIGR01421 87 DAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGT---VEVNGRDY--TAPHILIATGGKPSFPENIPGA-ELGTDSDGFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 183 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQ 261
Cdd:TIGR01421 161 ALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRhERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 262 LQVTWEDSTTgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVeGRPELTPTA 341
Cdd:TIGR01421 241 LVIHFEDGKS----IDDVDELIWAIGRKPNTKGLGLENVGIKLN-EKGQIIVDEYQNTNVPGIYALGDVV-GKVELTPVA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 342 IMAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVaGRDASQCYVKM 420
Cdd:TIGR01421 315 IAAGRKLSERLFNGKTDDkLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAM-TSEKQKCRMKL 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 13486927 421 VCLrEPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 478
Cdd:TIGR01421 394 VCA-GKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
9-478 |
4.13e-111 |
|
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, e.g., for maintaining the cellular thiol/disulfide status and for protecting against reactive oxygen species such as hydrogen peroxide. Glutathione-disulfide reductase regenerates reduced glutathione from oxidized glutathione (glutathione disulfide) + NADPH. This model represents one of two closely related subfamilies of glutathione-disulfide reductase. Both are closely related to trypanothione reductase, and separate models are built so each of the three can describe proteins with conserved function. This model describes glutathione-disulfide reductases of plants and some bacteria, including cyanobacteria. [Energy metabolism, Electron transport]
Pssm-ID: 213618 [Multi-domain] Cd Length: 446 Bit Score: 336.40 E-value: 4.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 9 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDyvEPSpqgtrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 88
Cdd:TIGR01424 2 DYDLFVIGAGSGGVRAARLAAALGAKVAIAE--EFR-------VGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 89 QpVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKeilLSADHIIIATGGRPRYPThI 168
Cdd:TIGR01424 73 K-ARFDWKKLLAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVLASGKT---YTAEKILIAVGGRPPKPA-L 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 169 EGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMASHGTRFLR 247
Cdd:TIGR01424 148 PGH-ELGITSNEAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRgKEILRGFDDDMRRGLAAALEERGIRILP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 248 GCAPSRVRRLPDGQLQVtwedsTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAI 327
Cdd:TIGR01424 227 EDSITSISKDDDGRLKA-----TLSKHEEIVADVVLFATGRSPNTNGLGLEAAGVRLN-DLGAIAVDEYSRTSTPSIYAV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 328 GDVVEgRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFT 407
Cdd:TIGR01424 301 GDVTD-RINLTPVAIHEATCFAETEFGNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRPMKAT 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13486927 408 VAGRDaSQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 478
Cdd:TIGR01424 378 FSGRQ-EKTLMKLV-VDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
2-482 |
1.35e-94 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 295.57 E-value: 1.35e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 2 EDQAGQRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDY-VEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDA 80
Cdd:PLN02507 18 EANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICELpFHPISSESIGGVGGTCVIRGCVPKKILVYGATFGGEFEDA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 81 PNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGG 160
Cdd:PLN02507 98 KNYGWEINEKVDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVTQLDGTKLRYTAKHILIATGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 161 RPRYPThIEGAlEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPLRGFDQQMSSMVIEHMA 239
Cdd:PLN02507 178 RAQRPN-IPGK-ELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRkELPLRGFDDEMRAVVARNLE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 240 SHGTRFLRGCAPSRVRRLPDGqLQVTwedSTTGKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREAT 319
Cdd:PLN02507 256 GRGINLHPRTNLTQLTKTEGG-IKVI---TDHGEEFVA--DVVLFATGRAPNTKRLNLEAVGVELD-KAGAVKVDEYSRT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 320 SVPHIYAIGDVVEgRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEhVEVYHA 399
Cdd:PLN02507 329 NIPSIWAIGDVTN-RINLTPVALMEGTCFAKTVFGGQPTKPDYENVACAVFCIPPLSVVGLSEEEAVEQAKGD-ILVFTS 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 400 HYKPLEFTVAGRDaSQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRI 479
Cdd:PLN02507 407 SFNPMKNTISGRQ-EKTVMKLIVDAETDK-VLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMRS 484
|
...
gi 13486927 480 SKR 482
Cdd:PLN02507 485 VTR 487
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
51-482 |
2.01e-83 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 268.28 E-value: 2.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 51 GLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKAS 130
Cdd:PLN02546 122 GVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKYETEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGK 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 131 FVDEHTVcgvAKGGKeiLLSADHIIIATGGRPRYPtHIEGaLEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGI 210
Cdd:PLN02546 202 IVDPHTV---DVDGK--LYTARNILIAVGGRPFIP-DIPG-IEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 211 GLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTwedstTGKEDTGTFDTVLWAIGRV 289
Cdd:PLN02546 275 KSDVHVFIRQKKvLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLK-----TNKGTVEGFSHVMFATGRK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 290 PDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEgRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTV 369
Cdd:PLN02546 350 PNTKNLGLEEVGVKMD-KNGAIEVDEYSRTSVPSIWAVGDVTD-RINLTPVALMEGGALAKTLFGNEPTKPDYRAVPSAV 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 370 FTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREppQLVLGLHFLGPNAGEVTQGFAL 449
Cdd:PLN02546 428 FSQPPIGQVGLTEEQAIEEYGD--VDVFTANFRPLKATLSGLPDRVFMKLIVCAKT--NKVLGVHMCGEDAPEIIQGFAV 503
|
410 420 430
....*....|....*....|....*....|...
gi 13486927 450 GIKCGASYAQVMRTVGIHPTCSEEVVKLRISKR 482
Cdd:PLN02546 504 AVKAGLTKADFDATVGIHPTAAEEFVTMRTPTR 536
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
9-477 |
1.05e-82 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 266.48 E-value: 1.05e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 9 DYDLLVVGGGSGGLACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVA 88
Cdd:PTZ00058 48 VYDLIVIGGGSGGMAAARRAARNKAKVALVE---------KDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 89 QPVphDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVC--GVAKGGKEI------------------- 147
Cdd:PTZ00058 119 FSF--NLPLLVERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLikKVSQVDGEAdesdddevtivsagvsqld 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 148 ---LLSADHIIIATGGRPRYPtHIEGaLEYGITSDDIFWLKEsPGKTLVVGASYVALECAGFLTGIGLDTTIMMR-SIPL 223
Cdd:PTZ00058 197 dgqVIEGKNILIAVGNKPIFP-DVKG-KEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARgNRLL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 224 RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSttGKEDtgTFDTVLWAIGRVPDTRSLNLEKAGVD 303
Cdd:PTZ00058 274 RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDG--RKYE--HFDYVIYCVGRSPNTEDLNLKALNIK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 304 TSPDTqkILVDSREATSVPHIYAIGDVVEGRP---------------------------------ELTPTAIMAGRLLVQ 350
Cdd:PTZ00058 350 TPKGY--IKVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvQLTPVAINAGRLLAD 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 351 RLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDASQ---CYVKMVCLrEPP 427
Cdd:PTZ00058 428 RLFGPFSRTTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDMDPAQkekTYLKLVCV-GKE 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 13486927 428 QLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 477
Cdd:PTZ00058 507 ELIKGLHIVGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
28-478 |
1.78e-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: 253.36 E-value: 1.78e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 28 AAQL-GRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEV-AQPVPHDWRKMAEAVQNH 105
Cdd:TIGR01423 22 AATLyKKRVAVVDVQTHHGPPFYAALGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGWEFdRSSVKANWKALIAAKNKA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 106 VKSLNWGHRVQLQDRK-VKYFNIKASFVDEHTVCgVAKGG------KEiLLSADHIIIATGGRPRYPThIEGaLEYGITS 178
Cdd:TIGR01423 102 VLDINKSYEGMFADTEgLTFFLGWGALEDKNVVL-VRESAdpksavKE-RLQAEHILLATGSWPQMLG-IPG-IEHCISS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 179 DDIFWLKESPGKTLVVGASYVALECAGFLTG---IGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRV 254
Cdd:TIGR01423 178 NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMiLRGFDSTLRKELTKQLRANGINIMTNENPAKV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 255 RRLPDGQLQVTWEdstTGKedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTqKILVDSREATSVPHIYAIGDVVeGR 334
Cdd:TIGR01423 258 TLNADGSKHVTFE---SGK--TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKG-AIQVDEFSRTNVPNIYAIGDVT-DR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 335 PELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHgqEHVEVYHAHYKPLEFTVAGRDAS 414
Cdd:TIGR01423 331 VMLTPVAINEGAAFVDTVFGNKPRKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYK 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13486927 415 QCYVKMVClREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLR 478
Cdd:TIGR01423 409 KFVAKIVT-NHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMR 471
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
24-472 |
1.49e-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: 247.56 E-value: 1.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 24 CAKEAAQLGRKVAVVDYVEpspqgtrwgLGGTCVNVGCIPKK-LMHQAALLGGlIQDAPNYGWEVAQpVPHDWRKMAEAV 102
Cdd:TIGR01350 16 AAIRAAQLGLKVALVEKEY---------LGGTCLNVGCIPTKaLLHSAEVYDE-IKHAKDLGIEVEN-VSVDWEKMQKRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 103 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRY-PTHIEGALEYGITSDDI 181
Cdd:TIGR01350 85 NKVVKKLVGGVSGLLKKNKVTVIKGEAKFLDPGTV-SVTGENGEETLEAKNIIIATGSRPRSlPGPFDFDGKVVITSTGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 182 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPD 259
Cdd:TIGR01350 164 LNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVieMLDRI-LPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKNDD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 260 gqlQVTWEDSTtGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVVEGrPELTP 339
Cdd:TIGR01350 243 ---QVTYENKG-GETETLTGEKVLVAVGRKPNTEGLGLEKLGVELDER-GRIVVDEYMRTNVPGIYAIGDVIGG-PMLAH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 340 TAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGqehvevyhaHYKPLEFTVA--GR----DA 413
Cdd:TIGR01350 317 VASHEGIVAAENIAGKEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGY---------DVKIGKFPFAanGKalalGE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 13486927 414 SQCYVKMVCLREpPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 472
Cdd:TIGR01350 388 TDGFVKIIADKK-TGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
23-477 |
1.57e-71 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 234.33 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 23 ACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRK----M 98
Cdd:PRK06370 19 PLAARAAGLGMKVALIE---------RGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPVSVDFKAvmarK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 99 AEAVQN-HVKSLNWghrvqLQDRK-VKYFNIKASFVDEHTVCgVAkggkEILLSADHIIIATGGRPRYPtHIEGALEYG- 175
Cdd:PRK06370 90 RRIRARsRHGSEQW-----LRGLEgVDVFRGHARFESPNTVR-VG----GETLRAKRIFINTGARAAIP-PIPGLDEVGy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 176 ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiP--LRGFDQQMSSMVIEHMASHGTRFLRGCAPSR 253
Cdd:PRK06370 159 LTNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERG-PrlLPREDEDVAAAVREILEREGIDVRLNAECIR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 254 VRRLPDGqlqVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDvVEG 333
Cdd:PRK06370 238 VERDGDG---IAVGLDCNGGAPEITGSHILVAVGRVPNTDDLGLEAAGVETDARGY-IKVDDQLRTTNPGIYAAGD-CNG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 334 RPELTPTAIMAGRLLVQRLFGGS----SDLmdydNVPTTVFTPLEYGCVGLSEEEAVARhGQEhVEVYHahykpLEFTVA 409
Cdd:PRK06370 313 RGAFTHTAYNDARIVAANLLDGGrrkvSDR----IVPYATYTDPPLARVGMTEAEARKS-GRR-VLVGT-----RPMTRV 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13486927 410 GR----DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 477
Cdd:PRK06370 382 GRavekGETQGFMKVV-VDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
8-472 |
3.67e-71 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 233.50 E-value: 3.67e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 8 RDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEv 87
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVE---------KEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIK- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 88 AQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYPTH 167
Cdd:PRK06416 73 AENVGIDFKKVQEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVDPNTV-RVMTEDGEQTYTAKNIILATGSRPRELPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 168 IEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHGTRF 245
Cdd:PRK06416 152 IEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIveALPRI-LPGEDKEISKLAERALKKRGIKI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 246 LRGcapSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTspDTQKILVDSREATSVPHIY 325
Cdd:PRK06416 231 KTG---AKAKKVEQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPNTENLGLEELGVKT--DRGFIEVDEQLRTNVPNIY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 326 AIGDVVEGrPELTPTAIMAGRLLVQRLFGGSSDlMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYhahykplE 405
Cdd:PRK06416 306 AIGDIVGG-PMLAHKASAEGIIAAEAIAGNPHP-IDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVV-------K 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13486927 406 FTVAGR------DASQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 472
Cdd:PRK06416 375 FPFAGNgkalalGETDGFVKLI-FDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
23-476 |
2.09e-68 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 226.21 E-value: 2.09e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 23 ACAKEAAQLGRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPhDWRKMAEAV 102
Cdd:PRK06292 17 VAARRAAKLGKKVALIE------KGP---LGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKI-DFKKVMARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 103 QNHVKSLNWGH-RVQLQDRKVKYFNIKASFVDEHTVcgvAKGGKEIllSADHIIIATGGR-PRYPThIEGALEYGI-TSD 179
Cdd:PRK06292 87 RRERDRFVGGVvEGLEKKPKIDKIKGTARFVDPNTV---EVNGERI--EAKNIVIATGSRvPPIPG-VWLILGDRLlTSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 180 DIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIpLRGFDQQMSSMVIEHMASHgTRFLRGCAPSRVRRL 257
Cdd:PRK06292 161 DAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVfeRGDRI-LPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 258 PDGQLQVTWEDsttGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVeGRPEL 337
Cdd:PRK06292 239 GDEKVEELEKG---GKTETIEADYVLVATGRRPNTDGLGLENTGIELD-ERGRPVVDEHTQTSVPGIYAAGDVN-GKPPL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 338 TPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARhGQEHVEvyhAHYkplEFTVAGR----DA 413
Cdd:PRK06292 314 LHEAADEGRIAAENAAGDVAGGVRYHPIPSVVFTDPQIASVGLTEEELKAA-GIDYVV---GEV---PFEAQGRarvmGK 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13486927 414 SQCYVKMVCLREPpQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTcSEEVVK 476
Cdd:PRK06292 387 NDGFVKVYADKKT-GRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPT-LSEGLR 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
23-494 |
4.27e-65 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 217.68 E-value: 4.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 23 ACAKEAAQLGRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPnYGWEVAQPVPhDWRKMAEAV 102
Cdd:TIGR02053 14 AAAIKAAELGASVAMVE------RGP---LGGTCVNVGCVPSKMLLRAAEVAHYARKPP-FGGLAATVAV-DFGELLEGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 103 QNHVKSLnwghrvqlqdRKVKYFNI-----------KASFVDEHTVcgVAKGGKEIlLSADHIIIATGGRPRYPtHIEGA 171
Cdd:TIGR02053 83 REVVEEL----------RHEKYEDVlssygvdylrgRARFKDPKTV--KVDLGREV-RGAKRFLIATGARPAIP-PIPGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 172 LEYG-ITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGC 249
Cdd:TIGR02053 149 KEAGyLTSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSdRLLPREEPEISAAVEEALAEEGIEVVTSA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 250 APSRVRRLPDGQLQVTwedSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGD 329
Cdd:TIGR02053 229 QVKAVSVRGGGKIITV---EKPGGQGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGG-ILVDETLRTSNPGIYAAGD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 330 VVeGRPELTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAvarhgQEHVEVYHAHYKPLEFTVA 409
Cdd:TIGR02053 305 VT-GGLQLEYVAAKEGVVAAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEA-----QKAGIECDCRTLPLTNVPR 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 410 GR--DASQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEevvKLRISKRSGL-D 486
Cdd:TIGR02053 379 ARinRDTRGFIKLVAEPGTGK-VLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAE---GLKLAAQTFYrD 454
|
....*...
gi 13486927 487 PTVTGCUG 494
Cdd:TIGR02053 455 VSKLSCCA 462
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
23-345 |
1.84e-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: 1.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 23 ACAKEAAQLGRKVAVVdyvepspqgtrwGLGGTCVNVGCIPKKLMHQAAllggliqdapnygwEVAQPVPHdWRKMAEAV 102
Cdd:pfam07992 14 AAALTLAQLGGKVTLI------------EDEGTCPYGGCVLSKALLGAA--------------EAPEIASL-WADLYKRK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 103 QNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGvakggKEILLSADHIIIATGGRPRYPThIEGALEYG------I 176
Cdd:pfam07992 67 EEVVKKLNNGIEVLLGTEVVSIDPGAKKVVLEELVDG-----DGETITYDRLVIATGARPRLPP-IPGVELNVgflvrtL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 177 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVR 255
Cdd:pfam07992 141 DSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIeALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEII 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 256 RLPDGQLQVTwedsttGKEDTGTFDTVLWAIGRVPDTRslNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVEGRP 335
Cdd:pfam07992 221 GDGDGVEVIL------KDGTEIDADLVVVAIGRRPNTE--LLEAAGLELDERGG-IVVDEYLRTSVPGIYAAGDCRVGGP 291
|
330
....*....|
gi 13486927 336 ELTPTAIMAG 345
Cdd:pfam07992 292 ELAQNAVAQG 301
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
25-442 |
4.10e-54 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 188.44 E-value: 4.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 25 AKEAAQLGRKVAVVDyvepspqgTRWGLGGTCVNVGCIPKKLMHQAAL-LGGLIQDA--PNYGwEVAQPVPHDWRKMAEA 101
Cdd:PRK05249 21 AMQAAKLGKRVAVIE--------RYRNVGGGCTHTGTIPSKALREAVLrLIGFNQNPlySSYR-VKLRITFADLLARADH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 102 VQNHVKSLnwgHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDI 181
Cdd:PRK05249 92 VINKQVEV---RRGQYERNRVDLIQGRARFVDPHTVEVECPDGEVETLTADKIVIATGSRPYRPPDVDFDHPRIYDSDSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 182 FWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDG 260
Cdd:PRK05249 169 LSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTlINTRDRLLSFLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 261 QLqVTWEDsttGKEDTGtfDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYAIGDVVeGRPELTPT 340
Cdd:PRK05249 249 VI-VHLKS---GKKIKA--DCLLYANGRTGNTDGLNLENAGLEADSRGQ-LKVNENYQTAVPHIYAVGDVI-GFPSLASA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 341 AIMAGRLLVQRLFGGSSDLMdYDNVPTTVFTPLEYGCVGLSEEEAVARHGqeHVEVYHAHYKPLeftvA-GRDASQCY-- 417
Cdd:PRK05249 321 SMDQGRIAAQHAVGEATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKV--PYEVGRARFKEL----ArAQIAGDNVgm 393
|
410 420
....*....|....*....|....*
gi 13486927 418 VKMVCLREPPQLvLGLHFLGPNAGE 442
Cdd:PRK05249 394 LKILFHRETLEI-LGVHCFGERATE 417
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
32-474 |
3.94e-44 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 161.28 E-value: 3.94e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 32 GRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVQNHVKSLN 110
Cdd:PRK07846 22 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAADVARTIREAARLG--VDAELDGvRWPDIVSRVFGRIDPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 111 WG---HRVQLQDrKVKYFNIKASFVDEHTVCgVAKGGkeiLLSADHIIIATGGRPRYPTHI-EGALEYGiTSDDIFWLKE 186
Cdd:PRK07846 91 AGgeeYRGRDTP-NIDVYRGHARFIGPKTLR-TGDGE---EITADQVVIAAGSRPVIPPVIaDSGVRYH-TSDTIMRLPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 187 SPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMashGTRF-LR-GCAPSRVRRLPDGqLQ 263
Cdd:PRK07846 165 LPESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSgRLLRHLDDDISERFTELA---SKRWdVRlGRNVVGVSQDGSG-VT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 264 VTWEDSTtgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVveGRP-ELTPTAI 342
Cdd:PRK07846 241 LRLDDGS-----TVEADVLLVATGRVPNGDLLDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV--SSPyQLKHVAN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 343 MAGRLLVQRLFGGSSDL-MDYDNVPTTVFTPLEYGCVGLSEEEAVARhGQEHVeVYHAHYKPLEFTVAGRDASQCyVKMV 421
Cdd:PRK07846 313 HEARVVQHNLLHPDDLIaSDHRFVPAAVFTHPQIASVGLTENEARAA-GLDIT-VKVQNYGDVAYGWAMEDTTGF-VKLI 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 13486927 422 CLREPPQLvLGLHFLGPNAGEVTQGF----ALGIKcgasyAQVM--RTVGIHPTCSEEV 474
Cdd:PRK07846 390 ADRDTGRL-LGAHIIGPQASTLIQPLiqamSFGLD-----AREMarGQYWIHPALPEVV 442
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
7-483 |
2.79e-43 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 159.32 E-value: 2.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 7 QRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEpSPQGTRwGLGGTCVNVGCIPKK-LMHQAALLGGLIQDAPNYGW 85
Cdd:PRK06327 2 SKQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWK-NPKGKP-ALGGTCLNVGCIPSKaLLASSEEFENAGHHFADHGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 86 EVAQpVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFV---DEHTVCGVAKGGKEIlLSADHIIIATGGRP 162
Cdd:PRK06327 80 HVDG-VKIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVgktDAGYEIKVTGEDETV-ITAKHVIIATGSEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 163 RyptHIEGAL---EYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM--MRSIpLRGFDQQMSSMVIEH 237
Cdd:PRK06327 158 R---HLPGVPfdnKIILDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILeaLPAF-LAAADEQVAKEAAKA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 238 MASHGTRFLRGCAPSRVRRLPDGqLQVTWEDStTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSRE 317
Cdd:PRK06327 234 FTKQGLDIHLGVKIGEIKTGGKG-VSVAYTDA-DGEAQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLD-ERGFIPVDDHC 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 318 ATSVPHIYAIGDVVEGrPELTPTAIMAGrLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVArhgqEHVEvY 397
Cdd:PRK06327 311 RTNVPNVYAIGDVVRG-PMLAHKAEEEG-VAVAERIAGQKGHIDYNTIPWVIYTSPEIAWVGKTEQQLKA----EGVE-Y 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 398 HAHYKPleFTVAGR----DASQCYVKMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSeE 473
Cdd:PRK06327 384 KAGKFP--FMANGRalamGEPDGFVKIIADAKTDE-ILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLS-E 459
|
490
....*....|...
gi 13486927 474 VVK---LRISKRS 483
Cdd:PRK06327 460 VWHeaaLAVDKRP 472
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
23-452 |
5.14e-42 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 157.62 E-value: 5.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 23 ACAKEAAQLGRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAV 102
Cdd:PRK13748 112 AAALKAVEQGARVTLIE------RGT---IGGTCVNVGCVPSKIMIRAAHIAHLRRESPFDGGIAATVPTIDRSRLLAQQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 103 QNHVKSLnwghrvqlqdRKVKYFNI------------KASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPThIEG 170
Cdd:PRK13748 183 QARVDEL----------RHAKYEGIldgnpaitvlhgEARFKDDQTLIVRLNDGGERVVAFDRCLIATGASPAVPP-IPG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 171 ALE--YGiTSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRG 248
Cdd:PRK13748 252 LKEtpYW-TSTEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAVTAAFRAEGIEVLEH 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 249 CAPSRVRRLpDGQLQVtwedsTTGKedtGTF--DTVLWAIGRVPDTRSLNLEKAGVDTSPDTQkILVDSREATSVPHIYA 326
Cdd:PRK13748 331 TQASQVAHV-DGEFVL-----TTGH---GELraDKLLVATGRAPNTRSLALDAAGVTVNAQGA-IVIDQGMRTSVPHIYA 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 327 IGDVVEgRPELTPTAIMAGRLLVQRLFGGSSDLmDYDNVPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEF 406
Cdd:PRK13748 401 AGDCTD-QPQFVYVAAAAGTRAAINMTGGDAAL-DLTAMPAVVFTDPQVATVGYSEAE--AHHDGIETDSRTLTLDNVPR 476
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 13486927 407 TVAGRDaSQCYVKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIK 452
Cdd:PRK13748 477 ALANFD-TRGFIKLV-IEEGSGRLIGVQAVAPEAGELIQTAALAIR 520
|
|
| mycothione_red |
TIGR03452 |
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and ... |
32-474 |
6.87e-41 |
|
mycothione reductase; Mycothiol, a glutathione analog in Mycobacterium tuberculosis and related species, can form a disulfide-linked dimer called mycothione. This enzyme can reduce mycothione to regenerate two mycothiol molecules. The enzyme shows some sequence similarity to glutathione-disulfide reductase, trypanothione-disulfide reductase, and dihydrolipoamide dehydrogenase. The characterized protein from M. tuberculosis, a homodimer, has FAD as a cofactor, one per monomer, and uses NADPH as a substrate.
Pssm-ID: 132493 [Multi-domain] Cd Length: 452 Bit Score: 152.60 E-value: 6.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 32 GRKVAVVDyvepspQGTrwgLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGweVAQPVPH-DWRKMAEAVqnhvksln 110
Cdd:TIGR03452 23 DKRIAIVE------KGT---FGGTCLNVGCIPTKMFVYAAEVAQSIGESARLG--IDAEIDSvRWPDIVSRV-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 111 WGHRVQL------------QDRKVKYFNIKASFVDEHTVcgVAKGGKEIllSADHIIIATGGRPRYPTHI-EGALEYgIT 177
Cdd:TIGR03452 84 FGDRIDPiaaggedyrrgdETPNIDVYDGHARFVGPRTL--RTGDGEEI--TGDQIVIAAGSRPYIPPAIaDSGVRY-HT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 178 SDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEhMASHGTRFLRGCAPSRVRR 256
Cdd:TIGR03452 159 NEDIMRLPELPESLVIVGGGYIAAEFAHVFSALGTRVTIVNRSTKlLRHLDEDISDRFTE-IAKKKWDIRLGRNVTAVEQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 257 LPDGqLQVTWEDSTtgkedTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVveGRP- 335
Cdd:TIGR03452 238 DGDG-VTLTLDDGS-----TVTADVLLVATGRVPNGDLLDAEAAGVEVDED-GRIKVDEYGRTSARGVWALGDV--SSPy 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 336 ELTPTAIMAGRLLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVyhAHYKPLEFTVAGRDaS 414
Cdd:TIGR03452 309 QLKHVANAEARVVKHNLLHPNDlRKMPHDFVPSAVFTHPQIATVGLTEQEAREAGHDITVKI--QNYGDVAYGWAMED-T 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13486927 415 QCYVKMVCLREPPQLvLGLHFLGPNAGEVTQGFALGIKCGASYAQVMR-TVGIHPTCSEEV 474
Cdd:TIGR03452 386 TGFCKLIADRDTGKL-LGAHIIGPQASSLIQPLITAMAFGLDAREMARkQYWIHPALPEVV 445
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
25-472 |
9.39e-37 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 140.65 E-value: 9.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 25 AKEAAQLGRKVAVVdyvEPSPQGtrwgLGGTCVNVGCIPKKLMHQAAllggliqdapNYGWEVAQPVPHdwrkmAEAVQN 104
Cdd:PRK07251 19 AAKLASAGKKVALV---EESKAM----YGGTCINIGCIPTKTLLVAA----------EKNLSFEQVMAT-----KNTVTS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 105 HVKSLNWGhrvQLQDRKVKYFNIKASFVDEHTVCGVAkGGKEILLSADHIIIATGGRPRYPThIEGALE--YGITSDDIF 182
Cdd:PRK07251 77 RLRGKNYA---MLAGSGVDLYDAEAHFVSNKVIEVQA-GDEKIELTAETIVINTGAVSNVLP-IPGLADskHVYDSTGIQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 183 WLKESPGKTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQ 261
Cdd:PRK07251 152 SLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLdAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEVKN-DGDQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 262 LQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDvVEGRPELTPTA 341
Cdd:PRK07251 231 VLVVTEDETY------RFDALLYATGRKPNTEPLGLENTDIELT-ERGAIKVDDYCQTSVPGVFAVGD-VNGGPQFTYIS 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 342 IMAGRLLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQehvevyhahYKPLEFTVAG--RDASQCYV 418
Cdd:PRK07251 303 LDDFRIVFGYLTGDGSyTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLP---------YAVKELLVAAmpRAHVNNDL 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 13486927 419 K---MVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 472
Cdd:PRK07251 374 RgafKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAE 430
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
365-477 |
2.94e-36 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 129.98 E-value: 2.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 365 VPTTVFTPLEYGCVGLSEEEAVARHGQehVEVYHAHYKPLEFTVAGRDASqCYVKMVCLREPpQLVLGLHFLGPNAGEVT 444
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTD-GFVKLVADRET-GKILGAHIVGPNAGELI 76
|
90 100 110
....*....|....*....|....*....|...
gi 13486927 445 QGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 477
Cdd:pfam02852 77 QEAALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| chlor_oxi_RclA |
NF040477 |
reactive chlorine resistance oxidoreductase RclA; |
25-472 |
1.17e-30 |
|
reactive chlorine resistance oxidoreductase RclA;
Pssm-ID: 439704 [Multi-domain] Cd Length: 441 Bit Score: 123.74 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 25 AKEAAQLGRKVAVVdyvEPSPQGtrwgLGGTCVNVGCIPKKLmhqaallggLIQDApnygwEVAQPVPHDWRKMAEAVqN 104
Cdd:NF040477 19 AATLAKAGWRVAII---EQSAQM----YGGTCINIGCIPTKT---------LVHDA-----EQHQDFSTAMQRKSSVV-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 105 HVKSLNWGHRVQLQDrkVKYFNIKASFVDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSD 179
Cdd:NF040477 77 FLRDKNYHNLADLDN--VDVINGRAEFIDNHTL-RVFQADGEQELRGEKIFINTGAQSVLPpipglTTTPGVYD----ST 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 180 DIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRS-IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLp 258
Cdd:NF040477 150 GLLNLTQLPARLGILGGGYIGVEFASMFARFGSKVTIFEAAeLFLPREDRDIAQAIATILQDQGVELILNAQVQRVSSH- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 259 DGQLQVTWEDSTTgkedtgTFDTVLWAIGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGrPELT 338
Cdd:NF040477 229 EGEVQLETAEGVL------TVDALLVASGRKPATAGLQLQNAGVAVN-ERGAIVVDKYLRTTADNIWAMGDVTGG-LQFT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 339 PTAIMAGRLLVQRLFG-GSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVagrDASQCY 417
Cdd:NF040477 301 YISLDDFRIVRDSLLGeGKRSTDDRQNVPYSVFMTPPLSRIGMTEEQARASGADIQVVTLPVAAIPRARVM---NDTRGV 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 13486927 418 VKMVcLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 472
Cdd:NF040477 378 LKAV-VDNKTQRILGVSLLCVDSHEMINIVKTVMDAGLPYTVLRDQIFTHPTMSE 431
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
133-379 |
3.93e-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: 119.53 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 133 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITS----DDIFWLKE-----SPGKTLVVGASYVALEC 203
Cdd:COG0446 65 EAKTV--TLRDGETL--SYDKLVLATGARPRPP-PIPGLDLPGVFTlrtlDDADALREalkefKGKRAVVIGGGPIGLEL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 204 AGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGQLQVTWEDsttgkEDTGTFDTV 282
Cdd:COG0446 140 AEALRKRGLKVTLVeRAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAID--GDDKVAVTLTD-----GEEIPADLV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 283 LWAIGRVPDTrSLnLEKAGVDTSPdTQKILVDSREATSVPHIYAIGDVVE------GRPELTP---TAIMAGRLLVQRLF 353
Cdd:COG0446 213 VVAPGVRPNT-EL-AKDAGLALGE-RGWIKVDETLQTSDPDVYAAGDCAEvphpvtGKTVYIPlasAANKQGRVAAENIL 289
|
250 260
....*....|....*....|....*...
gi 13486927 354 GGSsdlMDYDNVPTTVFT--PLEYGCVG 379
Cdd:COG0446 290 GGP---APFPGLGTFISKvfDLCIASTG 314
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
23-472 |
1.93e-25 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 110.00 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 23 ACAKEAAQLGRKVAVVDYVEPSpqgtrwgLGGTCVNVGCIPKKLMHQAA------------LLGGLIQDAPNYGWE---- 86
Cdd:PTZ00153 130 AAAINAMERGLKVIIFTGDDDS-------IGGTCVNVGCIPSKALLYATgkyrelknlaklYTYGIYTNAFKNGKNdpve 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 87 ----VAQPVPHDWRKMAEAVQNHVKSLNWG-------HRVQLQDRKVKYFNIKASFVDEHTVcGVAKGGKEilLSADHII 155
Cdd:PTZ00153 203 rnqlVADTVQIDITKLKEYTQSVIDKLRGGienglksKKFCKNSEHVQVIYERGHIVDKNTI-KSEKSGKE--FKVKNII 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 156 IATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSiplrgfdQQMSSMVI 235
Cdd:PTZ00153 280 IATGSTPNIPDNIEVDQKSVFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYS-------PQLLPLLD 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 236 EHMASHGTRFLRGCAPSRVR--------RLPDGQLQVT--WEDSTTGKEDTGTF----------DTVLWAIGRVPDTRSL 295
Cdd:PTZ00153 353 ADVAKYFERVFLKSKPVRVHlntlieyvRAGKGNQPVIigHSERQTGESDGPKKnmndiketyvDSCLVATGRKPNTNNL 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 296 NLEKAGVDTS----PDTQKILVDSREATSVPHIYAIGDvVEGRPELTPTA----------IMA--GRLLVQRLFGGSSDL 359
Cdd:PTZ00153 433 GLDKLKIQMKrgfvSVDEHLRVLREDQEVYDNIFCIGD-ANGKQMLAHTAshqalkvvdwIEGkgKENVNINVENWASKP 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 360 MDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKP-------LEFTVAGRDASQCY--------------V 418
Cdd:PTZ00153 512 IIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGVEISFYKAnskvlceNNISFPNNSKNNSYnkgkyntvdntegmV 591
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 13486927 419 KMVCLREPPQlVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSE 472
Cdd:PTZ00153 592 KIVYLKDTKE-ILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISE 644
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
28-471 |
2.62e-24 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 105.33 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 28 AAQLGRKVAVVDyvepspqgtRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHdwRKMAEAVQNHVK 107
Cdd:PRK07845 20 AAQLGADVTVIE---------RDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDGEA--RVDLPAVNARVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 108 SLNWGH----RVQLQDRKVKYFNIKASFVDE----HTVCGVAKGGKEILLSADHIIIATGGRPRYpthIEGALEYG---I 176
Cdd:PRK07845 89 ALAAAQsadiRARLEREGVRVIAGRGRLIDPglgpHRVKVTTADGGEETLDADVVLIATGASPRI---LPTAEPDGeriL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 177 TSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTT-IMMRSIPLRGFDQQmSSMVIEH-MASHGTRFLRGCAPSRV 254
Cdd:PRK07845 166 TWRQLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTlVSSRDRVLPGEDAD-AAEVLEEvFARRGMTVLKRSRAESV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 255 RRLPDGQLqVTWEDsttGKEDTGTFdtVLWAIGRVPDTRSLNLEKAGVDTSPdTQKILVD--SReaTSVPHIYAIGDVVE 332
Cdd:PRK07845 245 ERTGDGVV-VTLTD---GRTVEGSH--ALMAVGSVPNTAGLGLEEAGVELTP-SGHITVDrvSR--TSVPGIYAAGDCTG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 333 GRPeLTPTAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSeeEAVARHGQEHVEVY------HAHYKPLEF 406
Cdd:PRK07845 316 VLP-LASVAAMQGRIAMYHALGEAVSPLRLKTVASNVFTRPEIATVGVS--QAAIDSGEVPARTVmlplatNPRAKMSGL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13486927 407 tvagRDAsqcYVKMVClREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCS 471
Cdd:PRK07845 393 ----RDG---FVKLFC-RPGTGVVIGGVVVAPRASELILPIALAVQNRLTVDDLAQTFTVYPSLS 449
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
53-477 |
3.01e-23 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 102.01 E-value: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 53 GGTCVNVGCIPKKLmhqaallggLIQDAPNYG-WEVAQPvphdwRKmaEAVQNHVKSLNWGHRVQLQDrkVKYFNIKASF 131
Cdd:PRK08010 40 GGTCINIGCIPTKT---------LVHDAQQHTdFVRAIQ-----RK--NEVVNFLRNKNFHNLADMPN--IDVIDGQAEF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 132 VDEHTVcGVAKGGKEILLSADHIIIATGGRPRYP-----THIEGALEygitSDDIFWLKESPGKTLVVGASYVALECAGF 206
Cdd:PRK08010 102 INNHSL-RVHRPEGNLEIHGEKIFINTGAQTVVPpipgiTTTPGVYD----STGLLNLKELPGHLGILGGGYIGVEFASM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 207 LTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDSTTgkedtgTFDTVLWA 285
Cdd:PRK08010 177 FANFGSKVTILeAASLFLPREDRDIADNIATILRDQGVDIILNAHVERISH-HENQVQVHSEHAQL------AVDALLIA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 286 IGRVPDTRSLNLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEGRpELTPTAIMAGRLLVQRLFG-GSSDLMDYDN 364
Cdd:PRK08010 250 SGRQPATASLHPENAGIAVN-ERGAIVVDKYLHTTADNIWAMGDVTGGL-QFTYISLDDYRIVRDELLGeGKRSTDDRKN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 365 VPTTVFTPLEYGCVGLSEEEavARHGQEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREppQLVLGLHFLGPNAGEVT 444
Cdd:PRK08010 328 VPYSVFMTPPLSRVGMTEEQ--ARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKT--QRILGASLLCVDSHEMI 403
|
410 420 430
....*....|....*....|....*....|...
gi 13486927 445 QGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 477
Cdd:PRK08010 404 NIVKMVMDAGLPYSILRDQIFTHPSMSESLNDL 436
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
133-389 |
1.96e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 99.06 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 133 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPThIEGALEYGITS----DDIFWLKE--SPGKTLVV-GASYVALECAG 205
Cdd:COG1251 85 AARTV--TLADGETL--PYDKLVLATGSRPRVPP-IPGADLPGVFTlrtlDDADALRAalAPGKRVVViGGGLIGLEAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 206 FLTGIGLDTT-IMMRSIPL-RGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRlPDGQLQVTWEDsttgkedtGTF---D 280
Cdd:COG1251 160 ALRKRGLEVTvVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG-DDRVTGVRLAD--------GEElpaD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 281 TVLWAIGRVPDTrSLnLEKAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE------GRP--ELTPTAIMAGRLLVQRL 352
Cdd:COG1251 231 LVVVAIGVRPNT-EL-ARAAGLAVD---RGIVVDDYLRTSDPDIYAAGDCAEhpgpvyGRRvlELVAPAYEQARVAAANL 305
|
250 260 270
....*....|....*....|....*....|....*....
gi 13486927 353 FGGSSDLMDYDNVPTTVFTPLEYGCVGLSE--EEAVARH 389
Cdd:COG1251 306 AGGPAAYEGSVPSTKLKVFGVDVASAGDAEgdEEVVVRG 344
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
27-347 |
3.13e-17 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 82.09 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 27 EAAQLGRKVAVVDYVEPSPQGTRWglggTCV-NVGCIPKKLMhQAALLGGLIQDAPNYGwevaqpvphdwrkmAEAVQNH 105
Cdd:COG0492 18 YAARAGLKTLVIEGGEPGGQLATT----KEIeNYPGFPEGIS-GPELAERLREQAERFG--------------AEILLEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 106 VKSLnwghrvqlqDRKVKYFNIKASfvdehtvcgvakGGKEIllSADHIIIATGGRPRYPThIEGALE-------YGITS 178
Cdd:COG0492 79 VTSV---------DKDDGPFRVTTD------------DGTEY--EAKAVIIATGAGPRKLG-LPGEEEfegrgvsYCATC 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 179 DDIFWlkesPGKT-LVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGfdqqmSSMVIEHMASH-GTRFLRGCAPSRVrr 256
Cdd:COG0492 135 DGFFF----RGKDvVVVGGGDSALEEALYLTKFASKVTLIHRRDELRA-----SKILVERLRANpKIEVLWNTEVTEI-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 257 LPDGQLQ-VTWEDSTTGKEDTGTFDTVLWAIGRVPDTrSLnLEKAGVDTSPDtQKILVDSREATSVPHIYAIGDVVEGRP 335
Cdd:COG0492 204 EGDGRVEgVTLKNVKTGEEKELEVDGVFVAIGLKPNT-EL-LKGLGLELDED-GYIVVDEDMETSVPGVFAAGDVRDYKY 280
|
330
....*....|..
gi 13486927 336 ELTPTAIMAGRL 347
Cdd:COG0492 281 RQAATAAGEGAI 292
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
108-421 |
5.43e-17 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 83.17 E-value: 5.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 108 SLNWGHRVQLQDRKVKYFNIKAsfvdehtvcgvAKGGKEILLSADHIIIATGGRPRYPTHIEGALE--YGITS-DDIFWL 184
Cdd:PRK09564 72 DVKTEHEVVKVDAKNKTITVKN-----------LKTGSIFNDTYDKLMIATGARPIIPPIKNINLEnvYTLKSmEDGLAL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 185 KESPGKT-----LVVGASYVALECAGFLTGIGLDTTIMMRS--IPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrl 257
Cdd:PRK09564 141 KELLKDEeikniVIIGAGFIGLEAVEAAKHLGKNVRIIQLEdrILPDSFDKEITDVMEEELRENGVELHLNEFVKSL--- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 258 pDGQLQVTWEDSTTGKEDTgtfDTVLWAIGRVPDTRSLnlEKAGVDTSpDTQKILVDSREATSVPHIYAIGD------VV 331
Cdd:PRK09564 218 -IGEDKVEGVVTDKGEYEA---DVVIVATGVKPNTEFL--EDTGLKTL-KNGAIIVDEYGETSIENIYAAGDcatiynIV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 332 EGRPELTPTAIMA---GRLLVQRLFG---------GSSDLMDYDnvpttvftpLEYGCVGLSEEEAVArHGQEHVEVY-- 397
Cdd:PRK09564 291 SNKNVYVPLATTAnklGRMVGENLAGrhvsfkgtlGSACIKVLD---------LEAARTGLTEEEAKK-LGIDYKTVFik 360
|
330 340
....*....|....*....|....*..
gi 13486927 398 ---HAHYKPleftvagrDASQCYVKMV 421
Cdd:PRK09564 361 dknHTNYYP--------GQEDLYVKLI 379
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
190-265 |
1.31e-14 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 68.77 E-value: 1.31e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13486927 190 KTLVVGASYVALECAGFLTGIGLDTTIM-MRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVT 265
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVeRRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
145-352 |
7.83e-11 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 63.47 E-value: 7.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 145 KEILLSADHIIIATGG-RPRYPThIEG--------ALEY---------GITSddifWLKESP---GKTLVVGASYVALEC 203
Cdd:PRK12770 113 EELVKKYDAVLIATGTwKSRKLG-IPGedlpgvysALEYlfriraaklGYLP----WEKVPPvegKKVVVVGAGLTAVDA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 204 A--GFLTGIGLDTTIMMRSIPlrgfDQQMSSMVIEHMASHGTRFLRGCAP------SRVRRLPDGQLQVTWEDST----- 270
Cdd:PRK12770 188 AleAVLLGAEKVYLAYRRTIN----EAPAGKYEIERLIARGVEFLELVTPvriigeGRVEGVELAKMRLGEPDESgrprp 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 271 ---TGKEDTGTFDTVLWAIGRVPdTRSLNLEKAGVDTSPDTqKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGRL 347
Cdd:PRK12770 264 vpiPGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNRKG-EIVVDEKHMTSREGVFAAGDVVTG-PSKIGKAIKSGLR 340
|
....*
gi 13486927 348 LVQRL 352
Cdd:PRK12770 341 AAQSI 345
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
133-387 |
1.07e-10 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 63.23 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 133 DEHTVcgVAKGGKEIllSADHIIIATGGRPRYPtHIEGALEYGITSDDI-----FW----------LKESPGKTLVVGAS 197
Cdd:COG1252 84 EARTV--TLADGRTL--SYDYLVIATGSVTNFF-GIPGLAEHALPLKTLedalaLRerllaaferaERRRLLTIVVVGGG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 198 Y----VALECAGFLTGIGLDTTIMMRSI----------PLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRrlPDGqlq 263
Cdd:COG1252 159 PtgveLAGELAELLRKLLRYPGIDPDKVritlveagprILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVD--ADG--- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 264 VTWEDSTTGKedtgtFDTVLWAIG-RVPDTrslnLEKAGVDTSPDTQkILVDSR-EATSVPHIYAIGDVV-----EGRPe 336
Cdd:COG1252 234 VTLEDGEEIP-----ADTVIWAAGvKAPPL----LADLGLPTDRRGR-VLVDPTlQVPGHPNVFAIGDCAavpdpDGKP- 302
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 13486927 337 LTPTAIMA-------GRLLVQRLFGGssdlmdydnvPTTVFTPLEYGC-VGLSEEEAVA 387
Cdd:COG1252 303 VPKTAQAAvqqakvlAKNIAALLRGK----------PLKPFRYRDKGClASLGRGAAVA 351
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
190-403 |
1.42e-09 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 60.18 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 190 KTLVVGASYVALECAGFLTGIGLDTTIMMRSIP-LRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVrrlpDGQLqVTWEd 268
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKiNKLMDADMNQPILDELDKREIPYRLNEEIDAI----NGNE-VTFK- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 269 stTGKEDtgTFDTVLWAIGRVPDTRSlnLEKAGVDTSpDTQKILVDSREATSVPHIYAIGDVVEG------RPELTPTAI 342
Cdd:PRK13512 224 --SGKVE--HYDMIIEGVGTHPNSKF--IESSNIKLD-DKGFIPVNDKFETNVPNIYAIGDIITShyrhvdLPASVPLAW 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13486927 343 MAGR---LLVQRLFGGSS-DLMDYDNVPTTVFTPLEYGCVGLSEEEaVARHGQEHVEV---YHAHYKP 403
Cdd:PRK13512 297 GAHRaasIVAEQIAGNDTiEFKGFLGNNIVKFFDYTFASVGVKPNE-LKQFDYKMVEVtqgAHANYYP 363
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
152-346 |
2.66e-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: 52.83 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 152 DHIIIATG-GRPRyPTHIEG--------ALEY--GITSDDIFWLKESPGKTLVV-GASYVALECAGflTGIGL---DTTI 216
Cdd:COG0493 208 DAVFLATGaGKPR-DLGIPGedlkgvhsAMDFltAVNLGEAPDTILAVGKRVVViGGGNTAMDCAR--TALRLgaeSVTI 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 217 MMRsiplRGFDQqMSSMV--IEHMASHGTRFLRGCAPSRVRRLPDGQL------QVTW-EDSTTGK----EDTGTF---- 279
Cdd:COG0493 285 VYR----RTREE-MPASKeeVEEALEEGVEFLFLVAPVEIIGDENGRVtglecvRMELgEPDESGRrrpvPIEGSEftlp 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13486927 280 -DTVLWAIGRVPDTRSLnLEKAGVDTSPDTqKILVDSRE-ATSVPHIYAIGDVVEGrPELTPTAIMAGR 346
Cdd:COG0493 360 aDLVILAIGQTPDPSGL-EEELGLELDKRG-TIVVDEETyQTSLPGVFAGGDAVRG-PSLVVWAIAEGR 425
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
152-346 |
7.20e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 48.25 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 152 DHIIIATG-GRPRyPTHIEG--------ALEYGITSDDIFWLKESP-GKTLVV-GASYVALECAGflTGIGL---DTTIM 217
Cdd:PRK11749 227 DAVFIGTGaGLPR-FLGIPGenlggvysAVDFLTRVNQAVADYDLPvGKRVVViGGGNTAMDAAR--TAKRLgaeSVTIV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 218 MRsiplRGFDQqMSSMV--IEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWE--------DSTTGKE----DTGTF--DT 281
Cdd:PRK11749 304 YR----RGREE-MPASEeeVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVrmelgepdASGRRRVpiegSEFTLpaDL 378
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13486927 282 VLWAIGRVPDTRSLNLEKaGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGR 346
Cdd:PRK11749 379 VIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETGRTSLPGVFAGGDIVTG-AATVVWAVGDGK 441
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
113-332 |
1.12e-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: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 113 HRVQLqdrkvkYFNIKASFVDEHTVCGVAKGGKeiLLSADHIIIATGGRPRYPThIEGALEYGITS-------DDIFWLK 185
Cdd:TIGR02374 67 HGITL------YTGETVIQIDTDQKQVITDAGR--TLSYDKLILATGSYPFILP-IPGADKKGVYVfrtiedlDAIMAMA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 186 ESPGKTLVVGASYVALECAGFLTGIGLDTTI--MMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGcapsrvrrlpdgqlQ 263
Cdd:TIGR02374 138 QRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVihHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLE--------------K 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13486927 264 VTWEDSTTGKEDTGTF--------DTVLWAIGRVPDTRsLNLEkAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE 332
Cdd:TIGR02374 204 DTVEIVGATKADRIRFkdgssleaDLIVMAAGIRPNDE-LAVS-AGIKVN---RGIIVNDSMQTSDPDIYAVGECAE 275
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
192-359 |
2.93e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 46.06 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 192 LVVGASYVALECAGFLTGIGLDTTIMMRSiplrgfDQQMSSMV-------IEH-MASHGTRFLRGCAPSRVRRLPDGqLQ 263
Cdd:PRK04965 145 LVVGGGLIGTELAMDLCRAGKAVTLVDNA------ASLLASLMppevssrLQHrLTEMGVHLLLKSQLQGLEKTDSG-IR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13486927 264 VTWEDSttgkeDTGTFDTVLWAIGRVPDTrSLNLEkAGVDTSpdtQKILVDSREATSVPHIYAIGDVVE--GR--PELTP 339
Cdd:PRK04965 218 ATLDSG-----RSIEVDAVIAAAGLRPNT-ALARR-AGLAVN---RGIVVDSYLQTSAPDIYALGDCAEinGQvlPFLQP 287
|
170 180
....*....|....*....|
gi 13486927 340 tAIMAGRLLVQRLFGGSSDL 359
Cdd:PRK04965 288 -IQLSAMALAKNLLGQNTPL 306
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
259-330 |
3.59e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 42.84 E-value: 3.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13486927 259 DGQlQVT---WEDSTTGKEDTGTFDTVLWAIGRVPDTRSLnleKAGVDTSPDTQkILVDSREATSVPHIYAIGDV 330
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 ... |
94-160 |
1.65e-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: 1.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13486927 94 DWRKMAEAVQNHVKSLNW--GHRVQLQDRKVKYFniKASFVDEHTvcgVAKGGKEILLSADHIIIATGG 160
Cdd:cd08704 6 DWSKSAEEIHNLIRALNPwpGAYTTLNGKRLKIL--KAEVLEESG---EAAPGTILAVDKKGLLVACGD 69
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
280-346 |
4.14e-03 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 39.76 E-value: 4.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13486927 280 DTVLWAIGRVPDTRSLnLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGrPELTPTAIMAGR 346
Cdd:PRK12810 390 DLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDNAYQTSNPKVFAAGDMRRG-QSLVVWAIAEGR 454
|
|
| |
