|
Name |
Accession |
Description |
Interval |
E-value |
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
63-522 |
0e+00 |
|
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: 826.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 63 ASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSC-EGKFNWR 141
Cdd:TIGR01421 1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNdENTFNWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 142 VIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPkpTIEVSGKKYTAPHILIATGGMPSTPheSQIPGASLGITS 221
Cdd:TIGR01421 81 ELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDG--TVEVNGRDYTAPHILIATGGKPSFP--ENIPGAELGTDS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 222 DGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKT 301
Cdd:TIGR01421 157 DGFFALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 302 LSGLEVSMVTAVpgrlpvmTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKAL 381
Cdd:TIGR01421 237 VEGKLVIHFEDG-------KSIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 382 LTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKC 461
Cdd:TIGR01421 310 LTPVAIAAGRKLSERLFNGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSEKQKC 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50301238 462 VMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 522
Cdd:TIGR01421 390 RMKLVCAGKEEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
65-522 |
0e+00 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 672.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHA-DYGFPSCEGKFNWRVI 143
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYApGYGFDVTENKFDWAKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 144 KEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTsDPKpTIEVSGKKYTAPHILIATGGMPSTPhesQIPGASLGITSDG 223
Cdd:PRK06116 85 IANRDAYIDRLHGSYRNGLENNGVDLIEGFARFV-DAH-TVEVNGERYTADHILIATGGRPSIP---DIPGAEYGITSDG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 224 FFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLS 303
Cdd:PRK06116 160 FFALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 304 G-LEVSMVTavpGRlpvmtmIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALL 382
Cdd:PRK06116 240 GsLTLTLED---GE------TLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVEL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 383 TPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKCV 462
Cdd:PRK06116 311 TPVAIAAGRRLSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 463 MKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 522
Cdd:PRK06116 391 MKLVVVGKEEKVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
65-522 |
1.64e-161 |
|
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: 466.49 E-value: 1.64e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIK 144
Cdd:COG1249 4 YDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAPSVDWAALM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 145 EKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTsDPKpTIEVSGKK-YTAPHILIATGGMPSTPhesQIPGAS--LGITS 221
Cdd:COG1249 84 ARKDKVVDRLRGGVEELLKKNGVDVIRGRARFV-DPH-TVEVTGGEtLTADHIVIATGSRPRVP---PIPGLDevRVLTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 222 DGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKT 301
Cdd:COG1249 159 DEALELEELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 302 LSGLEVsmVTAVPGRLPVMTmipdVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKAL 381
Cdd:COG1249 239 GDGVTV--TLEDGGGEEAVE----ADKVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 382 LTPVAIAAGRKLAHRLFEyKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYgiENVKTYSTSFTPMYHAVTKRKTKC 461
Cdd:COG1249 313 LAHVASAEGRVAAENILG-KKPRPVDYRAIPSVVFTDPEIASVGLTEEEAREAG--IDVKVGKFPFAANGRALALGETEG 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50301238 462 VMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 522
Cdd:COG1249 390 FVKLIADAETGRILGAHIVGPHAGELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
65-521 |
8.61e-145 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 427.88 E-value: 8.61e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGkFNWRVIK 144
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFDTQFS-FNLPLLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 145 EKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEV---------------------------SGKKYTAPHIL 197
Cdd:PTZ00058 128 ERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIKKvsqvdgeadesdddevtivsagvsqldDGQVIEGKNIL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 198 IATGGMPSTPhesQIPGASLGITSDGFFQLEElPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTN 277
Cdd:PTZ00058 208 IAVGNKPIFP---DVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 278 CTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTavPGRLPVmtmipDVDCLLWAIGRVPNTKDLSLNKLGIQTdDKGHI 357
Cdd:PTZ00058 284 LENDMKKNNINIITHANVEEIEKVKEKNLTIYLS--DGRKYE-----HFDYVIYCVGRSPNTEDLNLKALNIKT-PKGYI 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 358 IVDEFQNTNVKGIYAVGDVCGKAL----------------------------------LTPVAIAAGRKLAHRLFEYKED 403
Cdd:PTZ00058 356 KVDDNQRTSVKHIYAVGDCCMVKKnqeiedlnllklyneepylkkkentsgesyynvqLTPVAINAGRLLADRLFGPFSR 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 404 sKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTK----RKTKCVMKMVCANKEEKVVGIHM 479
Cdd:PTZ00058 436 -TTNYKLIPSVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDmdpaQKEKTYLKLVCVGKEELIKGLHI 514
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 50301238 480 QGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTL 521
Cdd:PTZ00058 515 VGLNADEILQGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
65-522 |
1.14e-136 |
|
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: 402.65 E-value: 1.14e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIK 144
Cdd:TIGR01424 3 YDLFVIGAGSGGVRAARLAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVGKARFDWKKLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 145 EKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTsDPKpTIEV--SGKKYTAPHILIATGGMPSTPhesQIPGASLGITSD 222
Cdd:TIGR01424 83 AAKDQEIARLSGLYRKGLANAGAELLDGRAELV-GPN-TVEVlaSGKTYTAEKILIAVGGRPPKP---ALPGHELGITSN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 223 GFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTL 302
Cdd:TIGR01424 158 EAFHLPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDSITSISKDD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 303 SGlevSMVTAVPGRLPVMTmipdvDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALL 382
Cdd:TIGR01424 238 DG---RLKATLSKHEEIVA-----DVVLFATGRSPNTNGLGLEAAGVRLNDLGAIAVDEYSRTSTPSIYAVGDVTDRINL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 383 TPVAIAAGRKLAHRLFeYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGieNVKTYSTSFTPMYHAVTKRKTKCV 462
Cdd:TIGR01424 310 TPVAIHEATCFAETEF-GNNPTSFDHDLIATAVFSQPPIGTVGLTEEEARRKFG--DIEVYRAEFRPMKATFSGRQEKTL 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 463 MKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 522
Cdd:TIGR01424 387 MKLVVDAKDDKVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
65-521 |
1.61e-117 |
|
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: 355.31 E-value: 1.61e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHK---------LGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCE 135
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTptplgtrwgIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 136 G-KFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSdpKPTIEVSGKK-----YTAPHILIATGGMPSTPhe 209
Cdd:TIGR01438 83 TvKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVD--KHRIKATNKKgkekiYSAERFLIATGERPRYP-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 210 sQIPGAS-LGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRhDKVLRSFDSMISTNCTEELENAGVE 288
Cdd:TIGR01438 159 -GIPGAKeLCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDCANKVGEHMEEHGVK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 289 VLKFSQVKEVKKTLSGLEVSMVTAVPGrlpvmtMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDK-GHIIVDEFQNTNV 367
Cdd:TIGR01438 237 FKRQFVPIKVEQIEAKVLVEFTDSTNG------IEEEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 368 KGIYAVGDVC-GKALLTPVAIAAGRKLAHRLFEyKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTS 446
Cdd:TIGR01438 311 PYIYAVGDILeDKPELTPVAIQAGRLLAQRLFK-GSTVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSY 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50301238 447 FTPMYHAVTKRK--TKCVMKMVCANKE-EKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTL 521
Cdd:TIGR01438 390 FWPLEWTIPSRDnhNKCYAKLVCNKKEnERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTL 467
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
65-522 |
8.50e-114 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 348.02 E-value: 8.50e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVE----------SHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFP-S 133
Cdd:PLN02546 80 FDLFTIGAGSGGVRASRFASNFGASAAVCElpfatissdtLGGVGGTCVLRGCVPKKLLVYASKYSHEFEESRGFGWKyE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 134 CEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTsDPKpTIEVSGKKYTAPHILIATGGMPSTPhesQIP 213
Cdd:PLN02546 160 TEPKHDWNTLIANKNAELQRLTGIYKNILKNAGVTLIEGRGKIV-DPH-TVDVDGKLYTARNILIAVGGRPFIP---DIP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 214 GASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFS 293
Cdd:PLN02546 235 GIEHAIDSDAALDLPSKPEKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 294 QVKEVKKTLSGLeVSMVT---AVPGRLPVMtmipdvdcllWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGI 370
Cdd:PLN02546 315 SPQAIIKSADGS-LSLKTnkgTVEGFSHVM----------FATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSI 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 371 YAVGDVCGKALLTPVAIAAGRKLAHRLFEyKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGieNVKTYSTSFTPM 450
Cdd:PLN02546 384 WAVGDVTDRINLTPVALMEGGALAKTLFG-NEPTKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYG--DVDVFTANFRPL 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50301238 451 YHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 522
Cdd:PLN02546 461 KATLSGLPDRVFMKLIVCAKTNKVLGVHMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMR 532
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
65-522 |
1.00e-113 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 346.03 E-value: 1.00e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVE----------SHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSC 134
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpissesIGGVGGTCVIRGCVPKKILVYGATFGGEFEDAKNYGWEIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 135 EG-KFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTsDPKpTIEV-----SGKKYTAPHILIATGGMPSTPH 208
Cdd:PLN02507 106 EKvDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIV-GPN-EVEVtqldgTKLRYTAKHILIATGSRAQRPN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 209 esqIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVE 288
Cdd:PLN02507 184 ---IPGKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGIN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 289 VLKFSQVKEVKKTLSGLEVsmVTAVPGRLpvmtmipDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVK 368
Cdd:PLN02507 261 LHPRTNLTQLTKTEGGIKV--ITDHGEEF-------VADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 369 GIYAVGDVCGKALLTPVAIAAGRKLAHRLFEyKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIhKYGIENVKTYSTSFT 448
Cdd:PLN02507 332 SIWAIGDVTNRINLTPVALMEGTCFAKTVFG-GQPTKPDYENVACAVFCIPPLSVVGLSEEEAV-EQAKGDILVFTSSFN 409
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50301238 449 PMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTLR 522
Cdd:PLN02507 410 PMKNTISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMR 483
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
64-522 |
2.56e-101 |
|
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: 313.45 E-value: 2.56e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 64 SYDYLVIGGGSGGLASARRAAEL-GARAAVVESHK---------LGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYG--F 131
Cdd:TIGR01423 3 AFDLVVIGAGSGGLEAGWNAATLyKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGweF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 132 PSCEGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSH-IEIIRGHAAF----------TSDPKPTIEvsgKKYTAPHILIAT 200
Cdd:TIGR01423 83 DRSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWGALedknvvlvreSADPKSAVK---ERLQAEHILLAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 201 GGMPSTPhesQIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSA---LGSKTSLMIRHDKVLRSFDSMISTN 277
Cdd:TIGR01423 160 GSWPQML---GIPGIEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMILRGFDSTLRKE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 278 CTEELENAGVEVLKFSQVKEVKKTLSGleVSMVTAVPGRlpvmtmIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHI 357
Cdd:TIGR01423 237 LTKQLRANGINIMTNENPAKVTLNADG--SKHVTFESGK------TLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 358 IVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEdSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYgi 437
Cdd:TIGR01423 309 QVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVFGNKP-RKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 438 ENVKTYSTSFTPMYHAVTKRK-TKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSE 516
Cdd:TIGR01423 386 EKVAVYESSFTPLMHNISGSKyKKFVAKIVTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAE 465
|
....*.
gi 50301238 517 ELVTLR 522
Cdd:TIGR01423 466 ELCSMR 471
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
65-521 |
3.17e-98 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 305.98 E-value: 3.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHK---------LGGTCVNVGCVPKKVMWNTA-VHSEFMHDHADYGFpSC 134
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKpstqgtkwgLGGTCVNVGCVPKKLMHYAAnIGSIFHHDSQMYGW-KT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 135 EGKFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPKPTIEVSGKK--YTAPHILIATGGMPSTPHEsqI 212
Cdd:PTZ00052 85 SSSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDNSQEetITAKYILIATGGRPSIPED--V 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 213 PGA-SLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRhDKVLRSFDSMISTNCTEELENAGVEVLK 291
Cdd:PTZ00052 163 PGAkEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVR-SIPLRGFDRQCSEKVVEYMKEQGTLFLE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 292 FSQVKEVKKTLSGLEVSMVTAVpgrlpvmtmIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEfQNTNVKGIY 371
Cdd:PTZ00052 242 GVVPINIEKMDDKIKVLFSDGT---------TELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN-DCTNIPNIF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 372 AVGDVC-GKALLTPVAIAAGRKLAHRLFEyKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPM 450
Cdd:PTZ00052 312 AVGDVVeGRPELTPVAIKAGILLARRLFK-QSNEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 451 YHAVTKRK---------------TKCVMKMVC-ANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTS 514
Cdd:PTZ00052 391 EIAAVHREkherarkdeydfdvsSNCLAKLVCvKSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTD 470
|
....*..
gi 50301238 515 SEELVTL 521
Cdd:PTZ00052 471 AEVFMNL 477
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
64-521 |
1.32e-94 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 295.19 E-value: 1.32e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 64 SYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEG-KFNWRV 142
Cdd:PRK06370 5 RYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPvSVDFKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 143 IKEKRDAYVSRLNAIYQNNLTK-SHIEIIRGHAAFTSdpKPTIEVSGKKYTAPHILIATGGMPSTPHesqIPG-ASLG-I 219
Cdd:PRK06370 85 VMARKRRIRARSRHGSEQWLRGlEGVDVFRGHARFES--PNTVRVGGETLRAKRIFINTGARAAIPP---IPGlDEVGyL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 220 TSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVK 299
Cdd:PRK06370 160 TNETIFSLDELPEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 300 KTLSGLEVSMVTAvPGRLPVmtmipDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGK 379
Cdd:PRK06370 240 RDGDGIAVGLDCN-GGAPEI-----TGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 380 ALLTPVAIAAGRKLAHRLFEyKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAiHKYGIeNVKTYSTSFTPMYHAVTKRKT 459
Cdd:PRK06370 314 GAFTHTAYNDARIVAANLLD-GGRRKVSDRIVPYATYTDPPLARVGMTEAEA-RKSGR-RVLVGTRPMTRVGRAVEKGET 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50301238 460 KCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEELVTL 521
Cdd:PRK06370 391 QGFMKVVVDADTDRILGATILGVHGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTL 452
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
64-518 |
1.92e-90 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 284.35 E-value: 1.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 64 SYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVI 143
Cdd:PRK06416 4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGIDFKKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 144 KEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSdpKPTIEV----SGKKYTAPHILIATGgmpSTPHEsqIPGASLG- 218
Cdd:PRK06416 84 QEWKNGVVNRLTGGVEGLLKKNKVDIIRGEAKLVD--PNTVRVmtedGEQTYTAKNIILATG---SRPRE--LPGIEIDg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 219 ---ITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQV 295
Cdd:PRK06416 157 rviWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERALKKRGIKIKTGAKA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 296 KEVKKTLSGLEVSMvtAVPGRLPVMtmipDVDCLLWAIGRVPNTKDLSLNKLGIQTdDKGHIIVDEFQNTNVKGIYAVGD 375
Cdd:PRK06416 237 KKVEQTDDGVTVTL--EDGGKEETL----EADYVLVAVGRRPNTENLGLEELGVKT-DRGFIEVDEQLRTNVPNIYAIGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 376 vcgkalltpvaIAAGRKLAHRLF-EYK--------EDSKLDYNNIPTVVFSHPPIGTVGLTEDEAihKYGIENVKTYSTS 446
Cdd:PRK06416 310 -----------IVGGPMLAHKASaEGIiaaeaiagNPHPIDYRGIPAVTYTHPEVASVGLTEAKA--KEEGFDVKVVKFP 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50301238 447 FTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEEL 518
Cdd:PRK06416 377 FAGNGKALALGETDGFVKLIFDKKDGEVLGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEAL 448
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
64-516 |
4.40e-87 |
|
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: 275.68 E-value: 4.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 64 SYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAvhsEFMHD--HA-DYGFPSCEGKFNW 140
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSA---EVYDEikHAkDLGIEVENVSVDW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 141 RVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSdpKPTIEVSGKKY----TAPHILIATGGMPSTPHESQIPGAS 216
Cdd:TIGR01350 78 EKMQKRKNKVVKKLVGGVSGLLKKNKVTVIKGEAKFLD--PGTVSVTGENGeetlEAKNIIIATGSRPRSLPGPFDFDGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 217 LGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVK 296
Cdd:TIGR01350 156 VVITSTGALNLEEVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 297 EVKKTLSGLEVSMVtavpGRLPVMTmipDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDV 376
Cdd:TIGR01350 236 AVEKNDDQVTYENK----GGETETL---TGEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 377 CGKALLTPVAIAAGRKLAHRLFEyKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGieNVKTYSTSFTPMYHAVTK 456
Cdd:TIGR01350 309 IGGPMLAHVASHEGIVAAENIAG-KEPAHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGY--DVKIGKFPFAANGKALAL 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 457 RKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSE 516
Cdd:TIGR01350 386 GETDGFVKIIADKKTGEILGAHIIGPHATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
64-516 |
1.02e-85 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 272.05 E-value: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 64 SYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVI 143
Cdd:PRK06292 3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKIDFKKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 144 KEKRDAYVSRL-NAIYQNNLTKSHIEIIRGHAAFTsDPKpTIEVSGKKYTAPHILIATGGmpSTPhesQIPGASLG---- 218
Cdd:PRK06292 83 MARVRRERDRFvGGVVEGLEKKPKIDKIKGTARFV-DPN-TVEVNGERIEAKNIVIATGS--RVP---PIPGVWLIlgdr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 219 -ITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELE-----NAGVEVLKF 292
Cdd:PRK06292 156 lLTSDDAFELDKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSkefkiKLGAKVTSV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 293 SQVKEVKKTLSGLEVSMVTAVpgrlpvmtmipdVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYA 372
Cdd:PRK06292 236 EKSGDEKVEELEKGGKTETIE------------ADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 373 VGDVCGKALLTPVAIAAGRKLAHRLFEYKEDsKLDYNNIPTVVFSHPPIGTVGLTEDEAIhKYGIE-NVKTYSTSFTPMY 451
Cdd:PRK06292 304 AGDVNGKPPLLHEAADEGRIAAENAAGDVAG-GVRYHPIPSVVFTDPQIASVGLTEEELK-AAGIDyVVGEVPFEAQGRA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50301238 452 HAvtKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSE 516
Cdd:PRK06292 382 RV--MGKNDGFVKVYADKKTGRLLGAHIIGPDAEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSE 444
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
65-518 |
7.03e-84 |
|
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: 267.75 E-value: 7.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWnTAVHSEFMHDHADYGFPSCEGKFNW-RVI 143
Cdd:TIGR02053 1 YDLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTCVNVGCVPSKMLL-RAAEVAHYARKPPFGGLAATVAVDFgELL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 144 KEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDpkPTIEVSGKKYT--APHILIATGGMPSTPHesqIPG-ASLG-I 219
Cdd:TIGR02053 80 EGKREVVEELRHEKYEDVLSSYGVDYLRGRARFKDP--KTVKVDLGREVrgAKRFLIATGARPAIPP---IPGlKEAGyL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 220 TSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVK 299
Cdd:TIGR02053 155 TSEEALALDRIPESLAVIGGGAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 300 KtlSGLEVSMVTAVPGRlpvmTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGK 379
Cdd:TIGR02053 235 V--RGGGKIITVEKPGG----QGEVEADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 380 ALLTPVAIAAGRKLAHRLFEYKEdSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKyGIEnVKTYSTSFTPMYHAVTKRKT 459
Cdd:TIGR02053 309 LQLEYVAAKEGVVAAENALGGAN-AKLDLLVIPRVVFTDPAVASVGLTEAEAQKA-GIE-CDCRTLPLTNVPRARINRDT 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 50301238 460 KCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEEL 518
Cdd:TIGR02053 386 RGFIKLVAEPGTGKVLGVQVVAPEAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGL 444
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
89-432 |
5.04e-64 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 215.20 E-value: 5.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 89 RAAVVESHKLGGTCVNVGCVPKKVMWNTA-VHSEFMHDhADYGFPSCEGKFNWRVIkekRDAYVSRLNAI------YQNN 161
Cdd:PRK07846 24 RIAIVEKGTFGGTCLNVGCIPTKMFVYAAdVARTIREA-ARLGVDAELDGVRWPDI---VSRVFGRIDPIaaggeeYRGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 162 LTkSHIEIIRGHAAFTsDPKpTIEV-SGKKYTAPHILIATGGMPSTPhesQIPGASlGI---TSDGFFQLEELPGRSVIV 237
Cdd:PRK07846 100 DT-PNIDVYRGHARFI-GPK-TLRTgDGEEITADQVVIAAGSRPVIP---PVIADS-GVryhTSDTIMRLPELPESLVIV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 238 GAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEeLENAGVEVLKFSQVKEVKKTLSGLEVsmvtavpgRL 317
Cdd:PRK07846 173 GGGFIAAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTE-LASKRWDVRLGRNVVGVSQDGSGVTL--------RL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 318 PVMTMIpDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRL 397
Cdd:PRK07846 244 DDGSTV-EADVLLVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVVQHNL 322
|
330 340 350
....*....|....*....|....*....|....*
gi 50301238 398 FEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAI 432
Cdd:PRK07846 323 LHPDDLIASDHRFVPAAVFTHPQIASVGLTENEAR 357
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
65-390 |
2.38e-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: 203.70 E-value: 2.38e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVEshkLGGTCVNVGCVPKKVMWNTAvhsefmHDHadygfpscEGKFNWRVIK 144
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAA------EAP--------EIASLWADLY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 145 EKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSdpKPTIEVSGKKYTAPHILIATGGMPSTPHesqIPGASLG------ 218
Cdd:pfam07992 64 KRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVL--EELVDGDGETITYDRLVIATGARPRLPP---IPGVELNvgflvr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 219 -ITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKE 297
Cdd:pfam07992 139 tLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 298 VKKTLSGLEVsmVTAVPGRLpvmtmipDVDCLLWAIGRVPNTKDlsLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDV- 376
Cdd:pfam07992 219 IIGDGDGVEV--ILKDGTEI-------DADLVVVAIGRRPNTEL--LEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCr 287
|
330
....*....|....
gi 50301238 377 CGKALLTPVAIAAG 390
Cdd:pfam07992 288 VGGPELAQNAVAQG 301
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
65-516 |
2.36e-58 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 200.92 E-value: 2.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHK-------LGGTCVNVGCVPKKVMWNTAVHSEFM-HDHADYGFPSCEG 136
Cdd:PRK06327 5 FDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKnpkgkpaLGGTCLNVGCIPSKALLASSEEFENAgHHFADHGIHVDGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 137 KFNWRVIKEKRDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTS--DPKPTIEVSGKKY---TAPHILIATGgmpSTPHEsq 211
Cdd:PRK06327 85 KIDVAKMIARKDKVVKKMTGGIEGLFKKNKITVLKGRGSFVGktDAGYEIKVTGEDEtviTAKHVIIATG---SEPRH-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 212 IPGASLG----ITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGV 287
Cdd:PRK06327 160 LPGVPFDnkiiLDNTGALNFTEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 288 EVLKFSQVKEVKKTLSGLEVSmVTAVPGRLPVMtmipDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNV 367
Cdd:PRK06327 240 DIHLGVKIGEIKTGGKGVSVA-YTDADGEAQTL----EVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 368 KGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEdsKLDYNNIPTVVFSHPPIGTVGLTEDEAIhKYGIEnVKTYSTSF 447
Cdd:PRK06327 315 PNVYAIGDVVRGPMLAHKAEEEGVAVAERIAGQKG--HIDYNTIPWVIYTSPEIAWVGKTEQQLK-AEGVE-YKAGKFPF 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50301238 448 TPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSE 516
Cdd:PRK06327 391 MANGRALAMGEPDGFVKIIADAKTDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSE 459
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
65-518 |
3.13e-54 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 188.80 E-value: 3.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHKL--GGTCVNVGCVPKKVMWNTAVHsefmhdHADYGfpscegkfnwRV 142
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVALVEESKAmyGGTCINIGCIPTKTLLVAAEK------NLSFE----------QV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 143 IKEKrDAYVSRLNAIYQNNLTKSHIEIIRGHAAFTSDPkpTIEVSG----KKYTAPHILIATGGMPSTPhesQIPG--AS 216
Cdd:PRK07251 68 MATK-NTVTSRLRGKNYAMLAGSGVDLYDAEAHFVSNK--VIEVQAgdekIELTAETIVINTGAVSNVL---PIPGlaDS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 217 LGI-TSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQV 295
Cdd:PRK07251 142 KHVyDSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 296 KEVKKtlSGLEVsMVTAVPGRLpvmtmipDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGD 375
Cdd:PRK07251 222 TEVKN--DGDQV-LVVTEDETY-------RFDALLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 376 VCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHavT 455
Cdd:PRK07251 292 VNGGPQFTYISLDDFRIVFGYLTGDGSYTLEDRGNVPTTMFITPPLSQVGLTEKEAKEAGLPYAVKELLVAAMPRAH--V 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50301238 456 KRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEEL 518
Cdd:PRK07251 370 NNDLRGAFKVVVNTETKEILGATLFGEGSQEIINLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
69-496 |
1.21e-52 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 187.28 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 69 VIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHA-DYGFPSCEGKFNWRVIKEKR 147
Cdd:PRK13748 103 VIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPfDGGIAATVPTIDRSRLLAQQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 148 DAYVSRL-NAIYQNNL-TKSHIEIIRGHAAFTSDPKPTIEV---SGKKYTAPHILIATGGMPSTPhesQIPG--ASLGIT 220
Cdd:PRK13748 183 QARVDELrHAKYEGILdGNPAITVLHGEARFKDDQTLIVRLndgGERVVAFDRCLIATGASPAVP---PIPGlkETPYWT 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 221 SDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSfDSMISTNCTEELENAGVEVLKFSQVKEVkk 300
Cdd:PRK13748 260 STEALVSDTIPERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFRE-DPAIGEAVTAAFRAEGIEVLEHTQASQV-- 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 301 TLSGLEVSMVTAvPGRLpvmtmipDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKA 380
Cdd:PRK13748 337 AHVDGEFVLTTG-HGEL-------RADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 381 LLTPVAIAAGRKLAHRLfeYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAiHKYGIENV-KTYSTSFTPmyHAVTKRKT 459
Cdd:PRK13748 409 QFVYVAAAAGTRAAINM--TGGDAALDLTAMPAVVFTDPQVATVGYSEAEA-HHDGIETDsRTLTLDNVP--RALANFDT 483
|
410 420 430
....*....|....*....|....*....|....*..
gi 50301238 460 KCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVK 496
Cdd:PRK13748 484 RGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAALAIR 520
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
83-431 |
1.66e-49 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 176.50 E-value: 1.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 83 AAELGARAAVVESHK-LGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYgfpscegkfnwRVIKEKRDAYVSRLNA----- 156
Cdd:PRK05249 24 AAKLGKRVAVIERYRnVGGGCTHTGTIPSKALREAVLRLIGFNQNPLY-----------SSYRVKLRITFADLLAradhv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 157 ------IYQNNLTKSHIEIIRGHAAFTsDPKpTIEVSG-----KKYTAPHILIATGGMPSTPHESQIPGASLgITSDGFF 225
Cdd:PRK05249 93 inkqveVRRGQYERNRVDLIQGRARFV-DPH-TVEVECpdgevETLTADKIVIATGSRPYRPPDVDFDHPRI-YDSDSIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 226 QLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLrSF-DSMISTNCTEELENAGVEVLKFSQVKEVKKTLSG 304
Cdd:PRK05249 170 SLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLL-SFlDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 305 leVSMVTAVPGRLPVmtmipdvDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDE-FQnTNVKGIYAVGDVCGKALLT 383
Cdd:PRK05249 249 --VIVHLKSGKKIKA-------DCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNEnYQ-TAVPHIYAVGDVIGFPSLA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 50301238 384 PVAIAAGRKLAHRLFEykEDSKLDYNNIPTVVFSHPPIGTVGLTEDEA 431
Cdd:PRK05249 319 SASMDQGRIAAQHAVG--EATAHLIEDIPTGIYTIPEISSVGKTEQEL 364
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
65-518 |
6.84e-45 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 163.65 E-value: 6.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHK--LGGTCVNVGCVPKKVMwntavhsefMHDHADYGfpscegkfNWRV 142
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQSNamYGGTCINIGCIPTKTL---------VHDAQQHT--------DFVR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 143 IKEKRDAYVSRL-NAIYQNNLTKSHIEIIRGHAAFTSD-------PKPTIEVSGKKytaphILIATGG---MPSTPHESQ 211
Cdd:PRK08010 67 AIQRKNEVVNFLrNKNFHNLADMPNIDVIDGQAEFINNhslrvhrPEGNLEIHGEK-----IFINTGAqtvVPPIPGITT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 212 IPGAslgITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLK 291
Cdd:PRK08010 142 TPGV---YDSTGLLNLKELPGHLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIIL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 292 FSQVKEVKKTLSGLEVSMVTAVPGrlpvmtmipdVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIY 371
Cdd:PRK08010 219 NAHVERISHHENQVQVHSEHAQLA----------VDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIW 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 372 AVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPmy 451
Cdd:PRK08010 289 AMGDVTGGLQFTYISLDDYRIVRDELLGEGKRSTDDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIP-- 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50301238 452 HAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEEL 518
Cdd:PRK08010 367 RARVMNDTRGVLKAIVDNKTQRILGASLLCVDSHEMINIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
411-521 |
3.68e-44 |
|
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: 151.55 E-value: 3.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 411 IPTVVFSHPPIGTVGLTEDEAIHKYGieNVKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQG 490
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGG--EVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQE 78
|
90 100 110
....*....|....*....|....*....|.
gi 50301238 491 FAVAVKMGATKADFDNTVAIHPTSSEELVTL 521
Cdd:pfam02852 79 AALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
65-518 |
4.14e-37 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 145.44 E-value: 4.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 65 YDYLVIGGGSGGLASARRAAELGARAAVVESHK--LGGTCVNVGCVPKK-VMWNTAVHSEFMHDHADYGF---------- 131
Cdd:PTZ00153 117 YDVGIIGCGVGGHAAAINAMERGLKVIIFTGDDdsIGGTCVNVGCIPSKaLLYATGKYRELKNLAKLYTYgiytnafkng 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 132 ------------------PSCEGKFNWRVIKEKRDAYVSRLnAIYQNNLTKSHIEII--RGHAAFtsdpKPTI--EVSGK 189
Cdd:PTZ00153 197 kndpvernqlvadtvqidITKLKEYTQSVIDKLRGGIENGL-KSKKFCKNSEHVQVIyeRGHIVD----KNTIksEKSGK 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 190 KYTAPHILIATGGMPSTPHESQIPGASLgITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRS 269
Cdd:PTZ00153 272 EFKVKNIIIATGSTPNIPDNIEVDQKSV-FTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 270 FDSMIStNCTEELenagvevlkFSQVKEVKKTLSgLEVSMVTAVPGRLPV------------------MTMIPD--VDCL 329
Cdd:PTZ00153 351 LDADVA-KYFERV---------FLKSKPVRVHLN-TLIEYVRAGKGNQPViighserqtgesdgpkknMNDIKEtyVDSC 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 330 LWAIGRVPNTKDLSLNKLGIQTDdKGHIIVDEF------QNTNVKGIYAVGDVCGKALLTPVA----------IAAGRKL 393
Cdd:PTZ00153 420 LVATGRKPNTNNLGLDKLKIQMK-RGFVSVDEHlrvlreDQEVYDNIFCIGDANGKQMLAHTAshqalkvvdwIEGKGKE 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 394 AHRLFEYKEDSK-LDYNNIPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTySTSFtpmYHAVTK---------------- 456
Cdd:PTZ00153 499 NVNINVENWASKpIIYKNIPSVCYTTPELAFIGLTEKEAKELYPPDNVGV-EISF---YKANSKvlcennisfpnnsknn 574
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50301238 457 ----------RKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIHPTSSEEL 518
Cdd:PTZ00153 575 synkgkyntvDNTEGMVKIVYLKDTKEILGMFIVGSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISEVL 646
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
83-430 |
4.12e-35 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 136.91 E-value: 4.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 83 AAELGARAAVVESHKLGGTCVNVGCVPKKVMWNTAVHSEFMHDHADYGFPSCEGKfNWRVIKEKRDAYVSRLnAIYQ--- 159
Cdd:PRK07845 20 AAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFIDDG-EARVDLPAVNARVKAL-AAAQsad 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 160 --NNLTKSHIEIIRGHAAFTS--DPKPTIEVS---GKKYT--APHILIATGgmpSTPHEsqIPGASlgitSDG------- 223
Cdd:PRK07845 98 irARLEREGVRVIAGRGRLIDpgLGPHRVKVTtadGGEETldADVVLIATG---ASPRI--LPTAE----PDGeriltwr 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 224 -FFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSmistNCTEELENA----GVEVLKFSQVKEV 298
Cdd:PRK07845 169 qLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDA----DAAEVLEEVfarrGMTVLKRSRAESV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 299 KKTLSGLEVSMVTavpGRlpvmtMIPDVDCLLwAIGRVPNTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCG 378
Cdd:PRK07845 245 ERTGDGVVVTLTD---GR-----TVEGSHALM-AVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTG 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 50301238 379 KALLTPVAIAAGR-KLAHRLFEykEDSKLDYNNIPTVVFSHPPIGTVGLTEDE 430
Cdd:PRK07845 316 VLPLASVAAMQGRiAMYHALGE--AVSPLRLKTVASNVFTRPEIATVGVSQAA 366
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
83-390 |
3.27e-27 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 111.37 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 83 AAELGARAAVVESHKLGGTCVNVGCVpkkvmwntavhsefmhdhADY-GFP-SCEGKfnwrvikekrdAYVSRLnaiyQN 160
Cdd:COG0492 19 AARAGLKTLVIEGGEPGGQLATTKEI------------------ENYpGFPeGISGP-----------ELAERL----RE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 161 NLTKSHIEIIRGHA---AFTSDPKpTIEV-SGKKYTAPHILIATGGMPSTPhesQIPGA--------SLGITSDGFFqle 228
Cdd:COG0492 66 QAERFGAEILLEEVtsvDKDDGPF-RVTTdDGTEYEAKAVIIATGAGPRKL---GLPGEeefegrgvSYCATCDGFF--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 229 eLPGRSV-IVGAGYIAVEMAGILSALGSKTSLMIRHDKvLRSFDSMIstnctEEL-ENAGVEVLKFSQVKEV--KKTLSG 304
Cdd:COG0492 139 -FRGKDVvVVGGGDSALEEALYLTKFASKVTLIHRRDE-LRASKILV-----ERLrANPKIEVLWNTEVTEIegDGRVEG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 305 LEVSmvTAVPGRLPVMtmipDVDCLLWAIGRVPNTkDLsLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVCGKALLTp 384
Cdd:COG0492 212 VTLK--NVKTGEEKEL----EVDGVFVAIGLKPNT-EL-LKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQ- 282
|
....*.
gi 50301238 385 VAIAAG 390
Cdd:COG0492 283 AATAAG 288
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
162-397 |
6.93e-27 |
|
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: 110.67 E-value: 6.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 162 LTKSHIEIIRGHAAFTSDP-KPTIEV-SGKKYTAPHILIATGGMPSTPhesQIPGASL-GITSDGFFQ--------LEEL 230
Cdd:COG0446 46 FERKGIDVRTGTEVTAIDPeAKTVTLrDGETLSYDKLVLATGARPRPP---PIPGLDLpGVFTLRTLDdadalreaLKEF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 231 PGRS-VIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTlSGLEVsm 309
Cdd:COG0446 123 KGKRaVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAIDGD-DKVAV-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 310 VTAVPGRLPvmtmipdVDCLLWAIGRVPNTkDLsLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVC-------GKALL 382
Cdd:COG0446 200 TLTDGEEIP-------ADLVVVAPGVRPNT-EL-AKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAevphpvtGKTVY 270
|
250
....*....|....*...
gi 50301238 383 TPVAIAA---GRKLAHRL 397
Cdd:COG0446 271 IPLASAAnkqGRVAAENI 288
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
233-307 |
3.74e-20 |
|
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: 84.56 E-value: 3.74e-20
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50301238 233 RSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEV 307
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVV 75
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
166-397 |
3.30e-17 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 83.65 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 166 HIEIIRGHAAFTSDPKP-TIEV-SGKKYTAPHILIATGGMPSTPhesQIPGASLgitsDGFFQL----------EELPG- 232
Cdd:COG1251 70 GIDLRLGTRVTAIDRAArTVTLaDGETLPYDKLVLATGSRPRVP---PIPGADL----PGVFTLrtlddadalrAALAPg 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 233 -RSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVL-RSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTlsglevSMV 310
Cdd:COG1251 143 kRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGD------DRV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 311 TAVpgRLPVMTMIPdVDCLLWAIGRVPNTkDLsLNKLGIQTDDkGhIIVDEFQNTNVKGIYAVGDVC-------GKAL-- 381
Cdd:COG1251 217 TGV--RLADGEELP-ADLVVVAIGVRPNT-EL-ARAAGLAVDR-G-IVVDDYLRTSDPDIYAAGDCAehpgpvyGRRVle 289
|
250
....*....|....*.
gi 50301238 382 LTPVAIAAGRKLAHRL 397
Cdd:COG1251 290 LVAPAYEQARVAAANL 305
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
195-415 |
2.04e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 74.78 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 195 HILIATGgmpSTPHESQIPGA---SLGI-TSDGFFQL-EEL-----------PGRSVIVGAGYIAVEMAGILSAL----- 253
Cdd:COG1252 100 YLVIATG---SVTNFFGIPGLaehALPLkTLEDALALrERLlaaferaerrrLLTIVVVGGGPTGVELAGELAELlrkll 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 254 ------GSKTSLMI--RHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTlsglevSMVTAVPGRLPvmtmipd 325
Cdd:COG1252 177 rypgidPDKVRITLveAGPRILPGLGEKLSEAAEKELEKRGVEVHTGTRVTEVDAD------GVTLEDGEEIP------- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 326 VDCLLWAIGRVPNtkDLsLNKLGIQTDDKGHIIVDEF-QNTNVKGIYAVGDVC-----GKALLTPVAIAA---GRKLAH- 395
Cdd:COG1252 244 ADTVIWAAGVKAP--PL-LADLGLPTDRRGRVLVDPTlQVPGHPNVFAIGDCAavpdpDGKPVPKTAQAAvqqAKVLAKn 320
|
250 260
....*....|....*....|..
gi 50301238 396 --RLFEYKEDSKLDYNNIPTVV 415
Cdd:COG1252 321 iaALLRGKPLKPFRYRDKGCLA 342
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
196-442 |
4.32e-14 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 74.31 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 196 ILIATGGMPSTPhesQIPGaslgITSDGFFQLEELPG--------------RSVIVGAGYIAVEMAGILSALGSKTSLMI 261
Cdd:PRK09564 107 LMIATGARPIIP---PIKN----INLENVYTLKSMEDglalkellkdeeikNIVIIGAGFIGLEAVEAAKHLGKNVRIIQ 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 262 RHDKVL-RSFDSMISTNCTEELENAGVEvLKFSQvkevkktlsglevsMVTAVPGRLPVMTMIPD-----VDCLLWAIGR 335
Cdd:PRK09564 180 LEDRILpDSFDKEITDVMEEELRENGVE-LHLNE--------------FVKSLIGEDKVEGVVTDkgeyeADVVIVATGV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 336 VPNTKDLSlnKLGIQTDDKGHIIVDEFQNTNVKGIYAVGD-------VCGKALLTPVAIAA---GRKLAHRLFEYKEDSK 405
Cdd:PRK09564 245 KPNTEFLE--DTGLKTLKNGAIIVDEYGETSIENIYAAGDcatiyniVSNKNVYVPLATTAnklGRMVGENLAGRHVSFK 322
|
250 260 270
....*....|....*....|....*....|....*..
gi 50301238 406 LDYNNIPTVVFSHpPIGTVGLTEDEAiHKYGIeNVKT 442
Cdd:PRK09564 323 GTLGSACIKVLDL-EAARTGLTEEEA-KKLGI-DYKT 356
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
213-396 |
1.68e-12 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 69.43 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 213 PGAS---LGITSDGFFQLEELPG--------------RSVIVGAGYIAVEMAGILSALGSKTSLMIRHDKVLRSFDSMIS 275
Cdd:PRK13512 113 PGASansLGFESDITFTLRNLEDtdaidqfikanqvdKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMN 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 276 TNCTEELENAGVEvLKFSQvkEVkktlSGLEVSMVTAVPGRlpvmtmIPDVDCLLWAIGRVPNTKdlSLNKLGIQTDDKG 355
Cdd:PRK13512 193 QPILDELDKREIP-YRLNE--EI----DAINGNEVTFKSGK------VEHYDMIIEGVGTHPNSK--FIESSNIKLDDKG 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 50301238 356 HIIVDEFQNTNVKGIYAVGDVCGKA-----LLTPVAIAAGrklAHR 396
Cdd:PRK13512 258 FIPVNDKFETNVPNIYAIGDIITSHyrhvdLPASVPLAWG---AHR 300
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
189-400 |
1.66e-11 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 65.78 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 189 KKYTAphILIATGGMpsTPHESQIPGASL-GITSD------------GFFQLEELP----GRSVIVGAGYIAVEMAGILS 251
Cdd:PRK12770 117 KKYDA--VLIATGTW--KSRKLGIPGEDLpGVYSAleylfriraaklGYLPWEKVPpvegKKVVVVGAGLTAVDAALEAV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 252 ALGSKTSLMI--RHDKVLRSFDSMIstnctEELENAGVEVLKFSQVKEV--KKTLSGLEVSMVTAVPGR---LPVMTMIP 324
Cdd:PRK12770 193 LLGAEKVYLAyrRTINEAPAGKYEI-----ERLIARGVEFLELVTPVRIigEGRVEGVELAKMRLGEPDesgRPRPVPIP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 325 ------DVDCLLWAIGRVPnTKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDVC-GKALLTPvAIAAGRKLAHRL 397
Cdd:PRK12770 268 gsefvlEADTVVFAIGEIP-TPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVtGPSKIGK-AIKSGLRAAQSI 345
|
...
gi 50301238 398 FEY 400
Cdd:PRK12770 346 HEW 348
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
189-395 |
2.25e-11 |
|
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: 65.93 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 189 KKYTAphILIATGGmpSTPHESQIPGASL-GITS--DgF---FQLEELP------GRSVIV-GAGYIAVEMAGILSALGS 255
Cdd:COG0493 205 EEFDA--VFLATGA--GKPRDLGIPGEDLkGVHSamD-FltaVNLGEAPdtilavGKRVVViGGGNTAMDCARTALRLGA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 256 KTSLMIrhdkVLRSFDSMisTNCTEELENA---GVEVLKFSQVKEVKKT----LSGLEVSMVTAVP----GRlPVMTMIP 324
Cdd:COG0493 280 ESVTIV----YRRTREEM--PASKEEVEEAleeGVEFLFLVAPVEIIGDengrVTGLECVRMELGEpdesGR-RRPVPIE 352
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50301238 325 ------DVDCLLWAIGRVPNTKDLsLNKLGIQTDDKGHIIVDEF-QNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAH 395
Cdd:COG0493 353 gseftlPADLVILAIGQTPDPSGL-EEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAAR 429
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
196-400 |
7.70e-11 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 64.04 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 196 ILIATGGmpSTPHESQIPGASLG--------ITS----DGFFQLEElpGRSVIV-GAGYIAVEMAGILSALGSK-TSLMI 261
Cdd:PRK11749 229 VFIGTGA--GLPRFLGIPGENLGgvysavdfLTRvnqaVADYDLPV--GKRVVViGGGNTAMDAARTAKRLGAEsVTIVY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 262 RhdkvlRSFDSMISTNctEELENA---GVEVLKFSQVKEV---KKTLSGLEVSMVTAVPGRLPVMTMIP--------DVD 327
Cdd:PRK11749 305 R-----RGREEMPASE--EEVEHAkeeGVEFEWLAAPVEIlgdEGRVTGVEFVRMELGEPDASGRRRVPiegseftlPAD 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50301238 328 CLLWAIGRVPNTKDLSLNKlGIQTDDKGHIIVDEFQ-NTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEY 400
Cdd:PRK11749 378 LVIKAIGQTPNPLILSTTP-GLELNRWGTIIADDETgRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEY 450
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
183-389 |
4.91e-09 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 58.00 E-value: 4.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 183 TIEVSGKKYTAPHILIATGGMPSTPhesQIPGASLGIT--SDGFFQLEELP----GRSVIVGAGYIAVEMAGILSALGSK 256
Cdd:PRK04965 90 VVKSQGNQWQYDKLVLATGASAFVP---PIPGRELMLTlnSQQEYRAAETQlrdaQRVLVVGGGLIGTELAMDLCRAGKA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 257 TSLMIRHDKVLRSF-DSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVsmvTAVPGRLPvmtmipDVDCLLWAIGR 335
Cdd:PRK04965 167 VTLVDNAASLLASLmPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRA---TLDSGRSI------EVDAVIAAAGL 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50301238 336 VPNTK-----DLSLNKlGIQTDDKghiivdefQNTNVKGIYAVGDvC----GKAL--LTPVAIAA 389
Cdd:PRK04965 238 RPNTAlarraGLAVNR-GIVVDSY--------LQTSAPDIYALGD-CaeinGQVLpfLQPIQLSA 292
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
196-400 |
9.62e-08 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 54.75 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 196 ILIATG-GMPSTPHesqIPGASL-GITS-----------DGFFQLEELP---GRSV-IVGAGYIAVEMAGILSALGSKTS 258
Cdd:PRK12778 521 IFIASGaGLPNFMN---IPGENSnGVMSsneyltrvnlmDAASPDSDTPikfGKKVaVVGGGNTAMDSARTAKRLGAERV 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 259 LMIRHdkvlRSFDSMISTncTEELENA---GVEVLKFSQVKEVKKTLSGLEVSMVTAV-------------PGRLPVMTM 322
Cdd:PRK12778 598 TIVYR----RSEEEMPAR--LEEVKHAkeeGIEFLTLHNPIEYLADEKGWVKQVVLQKmelgepdasgrrrPVAIPGSTF 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 323 IPDVDCLLWAIGRVPN------TKDLSLNKlgiqtddKGHIIVDEFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHR 396
Cdd:PRK12778 672 TVDVDLVIVSVGVSPNplvpssIPGLELNR-------KGTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAA 744
|
....
gi 50301238 397 LFEY 400
Cdd:PRK12778 745 IDEY 748
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
183-374 |
1.78e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 49.91 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 183 TIEVSGKKYTAPHILIATGGMpSTPHESQIPGasLGITSDGFFQLEELPG-RSVIVGAGYIAVEMAGILSALGSKTSLMI 261
Cdd:pfam13738 109 VVTTSKGTYQARYVIIATGEF-DFPNKLGVPE--LPKHYSYVKDFHPYAGqKVVVIGGYNSAVDAALELVRKGARVTVLY 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 262 RHDKVLRS---FDSMISTNCTEELE----NAGVEVLKFSQVKEVKKTLSGLEVSM----VTAVPGRlPVMtmipdvdcll 330
Cdd:pfam13738 186 RGSEWEDRdsdPSYSLSPDTLNRLEelvkNGKIKAHFNAEVKEITEVDVSYKVHTedgrKVTSNDD-PIL---------- 254
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 50301238 331 wAIGRVPNTKDLSlnKLGIQTDDKGHIIVDEF-QNTNVKGIYAVG 374
Cdd:pfam13738 255 -ATGYHPDLSFLK--KGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
233-400 |
2.95e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 46.55 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 233 RSVIVGAGYIAVEMAGILSALGSKTSLMIRhdkvlRSFDSMisTNCTEELENA---GVEVLKFSQVKEV----KKTLSGL 305
Cdd:PRK12831 283 KVAVVGGGNVAMDAARTALRLGAEVHIVYR-----RSEEEL--PARVEEVHHAkeeGVIFDLLTNPVEIlgdeNGWVKGM 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 306 E-VSMVTAVPG----RLPV----MTMIPDVDCLLWAIGRVPNTKDLSLNKlGIQTDDKGHIIVDEFQN-TNVKGIYAVGD 375
Cdd:PRK12831 356 KcIKMELGEPDasgrRRPVeiegSEFVLEVDTVIMSLGTSPNPLISSTTK-GLKINKRGCIVADEETGlTSKEGVFAGGD 434
|
170 180
....*....|....*....|....*.
gi 50301238 376 -VCGKALLTpVAIAAGRKLAHRLFEY 400
Cdd:PRK12831 435 aVTGAATVI-LAMGAGKKAAKAIDEY 459
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
235-405 |
3.00e-05 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 46.30 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 235 VIVGAGYIAVEMAGILSALGSKTSLMIRHD--------------KVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKK 300
Cdd:PTZ00318 177 VVVGGGPTGVEFAAELADFFRDDVRNLNPElveeckvtvleagsEVLGSFDQALRKYGQRRLRRLGVDIRTKTAVKEVLD 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 301 TlsglevSMVTAVPGRLPVMTMIpdvdcllWA--IGRVPNTKDLSLNKlgiqtDDKGHIIVDE-FQNTNVKGIYAVGDVC 377
Cdd:PTZ00318 257 K------EVVLKDGEVIPTGLVV-------WStgVGPGPLTKQLKVDK-----TSRGRISVDDhLRVKPIPNVFALGDCA 318
|
170 180 190
....*....|....*....|....*....|....*.
gi 50301238 378 G---KALLTPVAIAA--GRKLAHR---LFEYKEDSK 405
Cdd:PTZ00318 319 AneeRPLPTLAQVASqqGVYLAKEfnnELKGKPMSK 354
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
183-405 |
6.25e-05 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 45.70 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 183 TIEVSGKKYTAPHIL-------IATGGMPSTPHESQIPGASLG--ITSDGF-----------FQLEELP---GRSVIV-G 238
Cdd:PRK12775 499 TNKVIGKTFTVPQLMndkgfdaVFLGVGAGAPTFLGIPGEFAGqvYSANEFltrvnlmggdkFPFLDTPislGKSVVViG 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 239 AGYIAVEMAGILSALGSKTslmIRHdkVLRSFDSMISTNcTEELENA---GVEVLKFSQVKEVKKTLSG------LEvSM 309
Cdd:PRK12775 579 AGNTAMDCLRVAKRLGAPT---VRC--VYRRSEAEAPAR-IEEIRHAkeeGIDFFFLHSPVEIYVDAEGsvrgmkVE-EM 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 310 VTAVPG----RLPVMT-MIPDVDC--LLWAIGRVPN------TKDLSLNKLG-IQTDDKGhiiVDEFQNTNVKGIYAVGD 375
Cdd:PRK12775 652 ELGEPDekgrRKPMPTgEFKDLECdtVIYALGTKANpiitqsTPGLALNKWGnIAADDGK---LESTQSTNLPGVFAGGD 728
|
250 260 270
....*....|....*....|....*....|
gi 50301238 376 VCGKALLTPVAIAAGRKLAHRLFEYKEDSK 405
Cdd:PRK12775 729 IVTGGATVILAMGAGRRAARSIATYLRLGK 758
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
302-395 |
1.17e-04 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 44.77 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 302 LSGLEVSMVTAVPGRlpvMTMIP------DVDCLLWAIGRVPNTKDLsLNKLGIQTDDKGHIIVDE--FQnTNVKGIYAV 373
Cdd:PRK12810 362 VTGVKVVRTELGEGD---FEPVEgsefvlPADLVLLAMGFTGPEAGL-LAQFGVELDERGRVAAPDnaYQ-TSNPKVFAA 436
|
90 100
....*....|....*....|..
gi 50301238 374 GDVCGKALLTPVAIAAGRKLAH 395
Cdd:PRK12810 437 GDMRRGQSLVVWAIAEGRQAAR 458
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
333-376 |
1.27e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 44.76 E-value: 1.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 50301238 333 IGRVPNTKDLslnKLGIQTDDKGHIIVDEFQNTNVKGIYAVGDV 376
Cdd:PRK15317 445 IGLVPNTEWL---KGTVELNRRGEIIVDARGATSVPGVFAAGDC 485
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
231-377 |
4.39e-04 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 42.60 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 231 PGRSV-IVGAGYIAVEMAGILSALGSKTSLMIRHDKVL-RSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTlSGLEVS 308
Cdd:PRK09754 143 PERSVvIVGAGTIGLELAASATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDG-EKVELT 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50301238 309 MVTAvpgrlpvMTMIPDVdcLLWAIGrvPNTKDLSLNKLGIQTDdkGHIIVDEFQNTNVKGIYAVGDVC 377
Cdd:PRK09754 222 LQSG-------ETLQADV--VIYGIG--ISANDQLAREANLDTA--NGIVIDEACRTCDPAIFAGGDVA 277
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
190-376 |
1.55e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 40.82 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 190 KYTAPHILIATG------GMPSTpHESQIPGASLGITSDGFFQLEElpgRSVIVGAGYIAVEMAGILSALGSKTSLMIRH 263
Cdd:PRK10262 103 EYTCDALIIATGasarylGLPSE-EAFKGRGVSACATCDGFFYRNQ---KVAVIGGGNTAVEEALYLSNIASEVHLIHRR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 264 DKvLRSfDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVTAVPGRLPVMTMipDVDCLLWAIGRVPNTK--- 340
Cdd:PRK10262 179 DG-FRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIESL--DVAGLFVAIGHSPNTAife 254
|
170 180 190
....*....|....*....|....*....|....*....
gi 50301238 341 ---DLSLNKLGIQTDDKGHIivdefQNTNVKGIYAVGDV 376
Cdd:PRK10262 255 gqlELENGYIKVQSGIHGNA-----TQTSIPGVFAAGDV 288
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
164-375 |
6.36e-03 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 39.33 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 164 KSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPH--ILIATGGMPSTPhesQIPGASlgiTSDGFF--QLEELPG------- 232
Cdd:PRK14989 71 KHGIKVLVGERAITINRQEKVIHSSAGRTVFYdkLIMATGSYPWIP---PIKGSE---TQDCFVyrTIEDLNAieacarr 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50301238 233 --RSVIVGAGYIAVEMAGILSALGSKTSLmIRHDKVL--RSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVS 308
Cdd:PRK14989 145 skRGAVVGGGLLGLEAAGALKNLGVETHV-IEFAPMLmaEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKT 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50301238 309 MVTAVPGRLpvmtmipDVDCLLWAIGRVPntKDLSLNKLGIQTDDKGHIIVDEFQNTNVKGIYAVGD 375
Cdd:PRK14989 224 MRFADGSEL-------EVDFIVFSTGIRP--QDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| |
