|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
19-467 |
0e+00 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 637.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 19 KEFDYLVIGGGSGGIASARRAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHA-DYGFDVTLNKFDWK 97
Cdd:PRK06116 3 KDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYApGYGFDVTENKFDWA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 98 VIKKSRDEYIKRLNGLYESGLKGSSVEYIRGRATFAEDGTVEVNGAKYRGKNTLIAVGGKPTIPNIKGAEHGIDSDGFFD 177
Cdd:PRK06116 83 KLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSDGFFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 178 LEDLPSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMdeETNPLHLHKNTQVTEVIKGDDG 257
Cdd:PRK06116 163 LEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEM--EKKGIRLHTNAVPKAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 258 LLTIKTTTGVIEKVQTLIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRR 337
Cdd:PRK06116 241 SLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 338 LSHRLFNGETDNKLTYENIATVVFSHPLIGTVGLTEAEAVEKYGKDEVTLYKSRFNPMLFAVTKHKEKAAMKLVCVGKDE 417
Cdd:PRK06116 321 LSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 71983419 418 KVVGVHVFGVGSDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEELVTMR 467
Cdd:PRK06116 401 KVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
19-467 |
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: 581.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 19 KEFDYLVIGGGSGGIASARRAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDVT-LNKFDWK 97
Cdd:TIGR01421 1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMHDAADYGFYQNdENTFNWP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 98 VIKKSRDEYIKRLNGLYESGLKGSSVEYIRGRATFAEDGTVEVNGAKYRGKNTLIAVGGKPTIP-NIKGAEHGIDSDGFF 176
Cdd:TIGR01421 81 ELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTAPHILIATGGKPSFPeNIPGAELGTDSDGFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 177 DLEDLPSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEETnpLHLHKNTQVTEVIKGDD 256
Cdd:TIGR01421 161 ALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEG--INVHKLSKPVKVEKTVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 257 GLLTIKTTTGV-IEKVQTLIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAG 335
Cdd:TIGR01421 239 GKLVIHFEDGKsIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVELTPVAIAAG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 336 RRLSHRLFNGETDNKLTYENIATVVFSHPLIGTVGLTEAEAVEKYGKDEVTLYKSRFNPMLFAVTKHKEKAAMKLVCVGK 415
Cdd:TIGR01421 319 RKLSERLFNGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSEKQKCRMKLVCAGK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 71983419 416 DEKVVGVHVFGVGSDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEELVTMR 467
Cdd:TIGR01421 399 EEKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
37-470 |
3.42e-137 |
|
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: 402.54 E-value: 3.42e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 37 RRAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDVTLNKFDWKVIKKSRDEYIKRLNGLYES 116
Cdd:COG1249 20 IRAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEARHAAEFGISAGAPSVDWAALMARKDKVVDRLRGGVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 117 GLKGSSVEYIRGRATFAEDGTVEVNGAK-YRGKNTLIAVGGKPTIPNIKGA--EHGIDSDGFFDLEDLPSRTVVVGAGYI 193
Cdd:COG1249 100 LLKKNGVDVIRGRARFVDPHTVEVTGGEtLTADHIVIATGSRPRVPPIPGLdeVRVLTSDEALELEELPKSLVVIGGGYI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 194 AVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEETnpLHLHKNTQVTEVIKGDDGlLTIKTTTGVIEKVQT 273
Cdd:COG1249 180 GLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEG--IDILTGAKVTSVEKTGDG-VTVTLEDGGGEEAVE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 274 ---LIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFnGETDNK 350
Cdd:COG1249 257 adkVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENIL-GKKPRP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 351 LTYENIATVVFSHPLIGTVGLTEAEAVEKygKDEVTLYKSRFNPMLFAVTKHKEKAAMKLVCVGKDEKVVGVHVFGVGSD 430
Cdd:COG1249 336 VDYRAIPSVVFTDPEIASVGLTEEEAREA--GIDVKVGKFPFAANGRALALGETEGFVKLIADAETGRILGAHIVGPHAG 413
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 71983419 431 EMLQGFAVAVTMGATKKQFDQTVAIHPTSAEELVTMRGGV 470
Cdd:COG1249 414 ELIHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAALAL 453
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
21-466 |
7.82e-134 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 397.83 E-value: 7.82e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 21 FDYLVIGGGSGGIASARRAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDvTLNKFDWKVIK 100
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSRHYGFD-TQFSFNLPLLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 101 KSRDEYIKRLNGLYESGLKGSSVEYIRGRAT-----------------------------FAEDGTVEVNGAKYRGKNTL 151
Cdd:PTZ00058 128 ERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSllsenqvlikkvsqvdgeadesdddevtiVSAGVSQLDDGQVIEGKNIL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 152 IAVGGKPTIPNIKGAEHGIDSDGFFDLEDlPSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTA 231
Cdd:PTZ00058 208 IAVGNKPIFPDVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELEN 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 232 DMDEETNPLHLHKNTQVTEVIKgDDGLLTIKTTTGVIEKVQTLIWAIGRDPLTKELNLERVGVKTDKsGHIIVDEYQNTS 311
Cdd:PTZ00058 287 DMKKNNINIITHANVEEIEKVK-EKNLTIYLSDGRKYEHFDYVIYCVGRSPNTEDLNLKALNIKTPK-GYIKVDDNQRTS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 312 APGILSVGDDTG----------------------------------KFLLTPVAIAAGRRLSHRLFnGETDNKLTYENIA 357
Cdd:PTZ00058 365 VKHIYAVGDCCMvkknqeiedlnllklyneepylkkkentsgesyyNVQLTPVAINAGRLLADRLF-GPFSRTTNYKLIP 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 358 TVVFSHPLIGTVGLTEAEAVEKYGKDEVTLYKSRFNPMLFAVTK----HKEKAAMKLVCVGKDEKVVGVHVFGVGSDEML 433
Cdd:PTZ00058 444 SVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVYDmdpaQKEKTYLKLVCVGKEELIKGLHIVGLNADEIL 523
|
490 500 510
....*....|....*....|....*....|...
gi 71983419 434 QGFAVAVTMGATKKQFDQTVAIHPTSAEELVTM 466
Cdd:PTZ00058 524 QGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
20-467 |
6.94e-125 |
|
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: 370.68 E-value: 6.94e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 20 EFDYLVIGGGSGGIASARRAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDVTLNKFDWKVI 99
Cdd:TIGR01424 2 DYDLFVIGAGSGGVRAARLAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFEDAAGYGWTVGKARFDWKKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 100 KKSRDEYIKRLNGLYESGLKGSSVEYIRGRATFAEDGTVEV--NGAKYRGKNTLIAVGGKPTIPNIKGAEHGIDSDGFFD 177
Cdd:TIGR01424 82 LAAKDQEIARLSGLYRKGLANAGAELLDGRAELVGPNTVEVlaSGKTYTAEKILIAVGGRPPKPALPGHELGITSNEAFH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 178 LEDLPSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEETnpLHLHKNTQVTEVIKGDDG 257
Cdd:TIGR01424 162 LPTLPKSILIAGGGYIAVEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERG--IRILPEDSITSISKDDDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 258 LLTIKTTTGVIEKVQTLIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRR 337
Cdd:TIGR01424 240 RLKATLSKHEEIVADVVLFATGRSPNTNGLGLEAAGVRLNDLGAIAVDEYSRTSTPSIYAVGDVTDRINLTPVAIHEATC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 338 LSHRLFNGETdNKLTYENIATVVFSHPLIGTVGLTEAEAVEKYGKDEVtlYKSRFNPMLFAVTKHKEKAAMKLVCVGKDE 417
Cdd:TIGR01424 320 FAETEFGNNP-TSFDHDLIATAVFSQPPIGTVGLTEEEARRKFGDIEV--YRAEFRPMKATFSGRQEKTLMKLVVDAKDD 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 71983419 418 KVVGVHVFGVGSDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEELVTMR 467
Cdd:TIGR01424 397 KVLGAHMVGPDAAEIIQGLAIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
37-467 |
1.57e-119 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 361.12 E-value: 1.57e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 37 RRAREFGVSVGLIE----------SGRLGGTCVNVGCVPKKVMYNCSLHA-EFIRDHadyGFDVTLN---KFDWKVIKKS 102
Cdd:PLN02546 96 RFASNFGASAAVCElpfatissdtLGGVGGTCVLRGCVPKKLLVYASKYShEFEESR---GFGWKYEtepKHDWNTLIAN 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 103 RDEYIKRLNGLYESGLKGSSVEYIRGRATFAEDGTVEVNGAKYRGKNTLIAVGGKPTIPNIKGAEHGIDSDGFFDLEDLP 182
Cdd:PLN02546 173 KNAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGKLYTARNILIAVGGRPFIPDIPGIEHAIDSDAALDLPSKP 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 183 SRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEETNPLHLHKNTQVteVIKGDDGLLTIK 262
Cdd:PLN02546 253 EKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQA--IIKSADGSLSLK 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 263 TTTGVIEKVQTLIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRL 342
Cdd:PLN02546 331 TNKGTVEGFSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTL 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 343 FNGETdNKLTYENIATVVFSHPLIGTVGLTEAEAVEKYGkdEVTLYKSRFNPMLFAVTKHKEKAAMKLVCVGKDEKVVGV 422
Cdd:PLN02546 411 FGNEP-TKPDYRAVPSAVFSQPPIGQVGLTEEQAIEEYG--DVDVFTANFRPLKATLSGLPDRVFMKLIVCAKTNKVLGV 487
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 71983419 423 HVFGVGSDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEELVTMR 467
Cdd:PLN02546 488 HMCGEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMR 532
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
20-467 |
3.18e-109 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 332.55 E-value: 3.18e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 20 EFDYLVIGGGSGGIASARRAREFGVSVGLIE----------SGRLGGTCVNVGCVPKKVM-YNCSLHAEFiRDHADYGFD 88
Cdd:PLN02507 25 DFDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpissesIGGVGGTCVIRGCVPKKILvYGATFGGEF-EDAKNYGWE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 89 VTLN-KFDWKVIKKSRDEYIKRLNGLYESGLKGSSVEYIRGRATFAEDGTVEV---NGAK--YRGKNTLIAVGGKPTIPN 162
Cdd:PLN02507 104 INEKvDFNWKKLLQKKTDEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqlDGTKlrYTAKHILIATGSRAQRPN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 163 IKGAEHGIDSDGFFDLEDLPSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDkmlsDELTADM--DEETNPL 240
Cdd:PLN02507 184 IPGKELAITSDEALSLEELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFD----DEMRAVVarNLEGRGI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 241 HLHKNTQVTEVIKGDDGlltIKTTTGVIEKVQT--LIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSV 318
Cdd:PLN02507 260 NLHPRTNLTQLTKTEGG---IKVITDHGEEFVAdvVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 319 GDDTGKFLLTPVAIAAGRRLSHRLFNGETdNKLTYENIATVVFSHPLIGTVGLTEAEAVEKyGKDEVTLYKSRFNPMLFA 398
Cdd:PLN02507 337 GDVTNRINLTPVALMEGTCFAKTVFGGQP-TKPDYENVACAVFCIPPLSVVGLSEEEAVEQ-AKGDILVFTSSFNPMKNT 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983419 399 VTKHKEKAAMKLVCVGKDEKVVGVHVFGVGSDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEELVTMR 467
Cdd:PLN02507 415 ISGRQEKTVMKLIVDAETDKVLGASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMR 483
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
20-466 |
4.52e-103 |
|
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: 316.41 E-value: 4.52e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 20 EFDYLVIGGGSGGIASARRAREFGVSVGLIE---------SGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYG--FD 88
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplgtRWGIGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGwkVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 89 VTLnKFDWKVIKKSRDEYIKRLNGLYESGLKGSSVEYIRGRATFAEDGTVEV---NGAK--YRGKNTLIAVGGKPTIPNI 163
Cdd:TIGR01438 82 ETV-KHDWKRLVEAVQNHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKAtnkKGKEkiYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 164 KGA-EHGIDSDGFFDLEDLPSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRyDKVLRTFDKMLSDELTADMdeETNPLHL 242
Cdd:TIGR01438 161 PGAkELCITSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVR-SILLRGFDQDCANKVGEHM--EEHGVKF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 243 HKNTQVTEVIKGDDGLLTIKT--TTGVIEKVQTLIWAIGRDPLTKELNLERVGVKTDK-SGHIIVDEYQNTSAPGILSVG 319
Cdd:TIGR01438 238 KRQFVPIKVEQIEAKVLVEFTdsTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKkTGKIPADEEEQTNVPYIYAVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 320 DDT-GKFLLTPVAIAAGRRLSHRLFNGeTDNKLTYENIATVVFSHPLIGTVGLTEAEAVEKYGKDEVTLYKSRFNPMLFA 398
Cdd:TIGR01438 318 DILeDKPELTPVAIQAGRLLAQRLFKG-STVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLEWT 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71983419 399 VTKHKE--KAAMKLVCVGKD-EKVVGVHVFGVGSDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEELVTM 466
Cdd:TIGR01438 397 IPSRDNhnKCYAKLVCNKKEnERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTL 467
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
54-469 |
1.21e-83 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 266.69 E-value: 1.21e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 54 LGGTCVNVGCVPKKVM-YNCSLHAEFIRDHADYGFDVTlNKFDWKVIKKSRDEYIKRLNGLYESGLKGSSVEYIRGRATF 132
Cdd:PTZ00052 48 LGGTCVNVGCVPKKLMhYAANIGSIFHHDSQMYGWKTS-SSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 133 AEDGTVEVNG----AKYRGKNTLIAVGGKPTIP-NIKGA-EHGIDSDGFFDLEDLPSRTVVVGAGYIAVEIAGVLANLGS 206
Cdd:PTZ00052 127 KDEHTVSYGDnsqeETITAKYILIATGGRPSIPeDVPGAkEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 207 DTHLLIRyDKVLRTFDKMLSDELTADMdEETNPLHLHKNTQVtEVIKGDDGLLtIKTTTGVIEKVQTLIWAIGRDPLTKE 286
Cdd:PTZ00052 207 DVTVAVR-SIPLRGFDRQCSEKVVEYM-KEQGTLFLEGVVPI-NIEKMDDKIK-VLFSDGTTELFDTVLYATGRKPDIKG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 287 LNLERVGVKTDKSGHIIVDEyQNTSAPGILSVGD-DTGKFLLTPVAIAAGRRLSHRLFNGeTDNKLTYENIATVVFSHPL 365
Cdd:PTZ00052 283 LNLNAIGVHVNKSNKIIAPN-DCTNIPNIFAVGDvVEGRPELTPVAIKAGILLARRLFKQ-SNEFIDYTFIPTTIFTPIE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 366 IGTVGLTEAEAVEKYGKDEVTLYKSRFNPMLFAVTkHKEK----------------AAMKLVCV-GKDEKVVGVHVFGVG 428
Cdd:PTZ00052 361 YGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIAAV-HREKherarkdeydfdvssnCLAKLVCVkSEDNKVVGFHFVGPN 439
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 71983419 429 SDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEEL----VTMRGG 469
Cdd:PTZ00052 440 AGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVFmnlsVTRRSG 484
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
37-461 |
4.64e-81 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 258.57 E-value: 4.64e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 37 RRAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDVTLNKFDWK-VIKKSRDEYIKRLNGLYE 115
Cdd:PRK06292 20 RRAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKHAEEFGIHADGPKIDFKkVMARVRRERDRFVGGVVE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 116 SGLKGSSVEYIRGRATFAEDGTVEVNGAKYRGKNTLIAVGGKptIPNIKGAEHG-----IDSDGFFDLEDLPSRTVVVGA 190
Cdd:PRK06292 100 GLEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGSR--VPPIPGVWLIlgdrlLTSDDAFELDKLPKSLAVIGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 191 GYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEEtnpLHLHKNTQVTEVIKGDDGLLTIKTTTGVIEK 270
Cdd:PRK06292 178 GVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKE---FKIKLGAKVTSVEKSGDEKVEELEKGGKTET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 271 VQT--LIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFNGETD 348
Cdd:PRK06292 255 IEAdyVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGDVAG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 349 nKLTYENIATVVFSHPLIGTVGLTEAEAVEKYGKDEVTLYKSRFNPMlfAVTKHKEKAAMKLVCVGKDEKVVGVHVFGVG 428
Cdd:PRK06292 335 -GVRYHPIPSVVFTDPQIASVGLTEEELKAAGIDYVVGEVPFEAQGR--ARVMGKNDGFVKVYADKKTGRLLGAHIIGPD 411
|
410 420 430
....*....|....*....|....*....|...
gi 71983419 429 SDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAE 461
Cdd:PRK06292 412 AEHLIHLLAWAMQQGLTVEDLLRMPFYHPTLSE 444
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
54-467 |
4.73e-77 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 249.12 E-value: 4.73e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 54 LGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYG--FDVTLNKFDWKVIKKSRDEYIKRLNGLYESGLKGSS-VEYIRGRA 130
Cdd:TIGR01423 47 LGGTCVNVGCVPKKLMVTGAQYMDTLRESAGFGweFDRSSVKANWKALIAAKNKAVLDINKSYEGMFADTEgLTFFLGWG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 131 TFAEDGTVEVNGA---------KYRGKNTLIAVGGKPTIPNIKGAEHGIDSDGFFDLEDLPSRTVVVGAGYIAVEIAGVL 201
Cdd:TIGR01423 127 ALEDKNVVLVRESadpksavkeRLQAEHILLATGSWPQMLGIPGIEHCISSNEAFYLDEPPRRVLTVGGGFISVEFAGIF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 202 ---ANLGSDTHLLIRYDKVLRTFDKMLSDELTADMdeETNPLHLHKNTQVTEVIKGDDGLLTIKTTTGVIEKVQTLIWAI 278
Cdd:TIGR01423 207 nayKPRGGKVTLCYRNNMILRGFDSTLRKELTKQL--RANGINIMTNENPAKVTLNADGSKHVTFESGKTLDVDVVMMAI 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 279 GRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFnGETDNKLTYENIAT 358
Cdd:TIGR01423 285 GRVPRTQTLQLDKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTVF-GNKPRKTDHTRVAS 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 359 VVFSHPLIGTVGLTEAEAVEKYgkDEVTLYKSRFNPMLFAVTKHKEKAAM-KLVCVGKDEKVVGVHVFGVGSDEMLQGFA 437
Cdd:TIGR01423 364 AVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPLMHNISGSKYKKFVaKIVTNHADGTVLGVHLLGDSSPEIIQAVG 441
|
410 420 430
....*....|....*....|....*....|
gi 71983419 438 VAVTMGATKKQFDQTVAIHPTSAEELVTMR 467
Cdd:TIGR01423 442 ICLKLNAKISDFYNTIGVHPTSAEELCSMR 471
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
38-463 |
1.57e-74 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 241.59 E-value: 1.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 38 RAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDVTLNKFDWKVIKKSRDEYIKRLNGLYESG 117
Cdd:PRK06416 22 RAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERADEARHSEDFGIKAENVGIDFKKVQEWKNGVVNRLTGGVEGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 118 LKGSSVEYIRGRATFAEDGTVEVNGAK----YRGKNTLIAVGGKP-TIPNIK-GAEHGIDSDGFFDLEDLPSRTVVVGAG 191
Cdd:PRK06416 102 LKKNKVDIIRGEAKLVDPNTVRVMTEDgeqtYTAKNIILATGSRPrELPGIEiDGRVIWTSDEALNLDEVPKSLVVIGGG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 192 YIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMdeETNPLHLHKNTQVTEVIKGDDGlltIKTTTGVIEKV 271
Cdd:PRK06416 182 YIGVEFASAYASLGAEVTIVEALPRILPGEDKEISKLAERAL--KKRGIKIKTGAKAKKVEQTDDG---VTVTLEDGGKE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 272 QT-----LIWAIGRDPLTKELNLERVGVKTDKsGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVA-----IAAGRRLSHr 341
Cdd:PRK06416 257 ETleadyVLVAVGRRPNTENLGLEELGVKTDR-GFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKAsaegiIAAEAIAGN- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 342 lfngetDNKLTYENIATVVFSHPLIGTVGLTEAEAVEKYgkDEVTLYKSRF--NPMlfAVTKHKEKAAMKLVCVGKDEKV 419
Cdd:PRK06416 335 ------PHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEG--FDVKVVKFPFagNGK--ALALGETDGFVKLIFDKKDGEV 404
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 71983419 420 VGVHVFGVGSDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEEL 463
Cdd:PRK06416 405 LGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSEAL 448
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
38-463 |
1.58e-73 |
|
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: 239.25 E-value: 1.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 38 RAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDhADYGFDVTLNKFDWKVIKKSRDEYIKRL-NGLYES 116
Cdd:TIGR02053 18 KAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYARK-PPFGGLAATVAVDFGELLEGKREVVEELrHEKYED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 117 GLKGSSVEYIRGRATFAEDGTVEVNGAKY-RG-KNTLIAVGGKPTIPNIKG-AEHG-IDSDGFFDLEDLPSRTVVVGAGY 192
Cdd:TIGR02053 97 VLSSYGVDYLRGRARFKDPKTVKVDLGREvRGaKRFLIATGARPAIPPIPGlKEAGyLTSEEALALDRIPESLAVIGGGA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 193 IAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEETnpLHLHKNTQVTEVIKGDDGLLTIKTTTGVIEKVQ 272
Cdd:TIGR02053 177 IGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEG--IEVVTSAQVKAVSVRGGGKIITVEKPGGQGEVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 273 T--LIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFNGeTDNK 350
Cdd:TIGR02053 255 AdeLLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEYVAAKEGVVAAENALGG-ANAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 351 LTYENIATVVFSHPLIGTVGLTEAEAVEKYGKdevtlYKSRFNPMLF---AVTKHKEKAAMKLVCVGKDEKVVGVHVFGV 427
Cdd:TIGR02053 334 LDLLVIPRVVFTDPAVASVGLTEAEAQKAGIE-----CDCRTLPLTNvprARINRDTRGFIKLVAEPGTGKVLGVQVVAP 408
|
410 420 430
....*....|....*....|....*....|....*.
gi 71983419 428 GSDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEEL 463
Cdd:TIGR02053 409 EAAEVINEAALAIRAGMTVDDLIDTLHPFPTMAEGL 444
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
37-472 |
2.28e-73 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 238.56 E-value: 2.28e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 37 RRAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDVTLN-KFDWKVIKKSRDEYIKRLNGLYE 115
Cdd:PRK06370 22 ARAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASARAAHLARRAAEYGVSVGGPvSVDFKAVMARKRRIRARSRHGSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 116 SGLKG-SSVEYIRGRATFAEDGTVEVNGAKYRGKNTLIAVGGKPTIPNIKG-AEHG-IDSDGFFDLEDLPSRTVVVGAGY 192
Cdd:PRK06370 102 QWLRGlEGVDVFRGHARFESPNTVRVGGETLRAKRIFINTGARAAIPPIPGlDEVGyLTNETIFSLDELPEHLVIIGGGY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 193 IAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEETNPLHLhkNTQVTEVIKGDDGLLTIKTTTGVIEKVQ 272
Cdd:PRK06370 182 IGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRL--NAECIRVERDGDGIAVGLDCNGGAPEIT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 273 T--LIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFNGEtDNK 350
Cdd:PRK06370 260 GshILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAYNDARIVAANLLDGG-RRK 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 351 LTYENIATVVFSHPLIGTVGLTEAEAvEKYGKDevtlYKSRFNPML---FAVTKHKEKAAMKLVCVGKDEKVVGVHVFGV 427
Cdd:PRK06370 339 VSDRIVPYATYTDPPLARVGMTEAEA-RKSGRR----VLVGTRPMTrvgRAVEKGETQGFMKVVVDADTDRILGATILGV 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 71983419 428 GSDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAEELVTMRGGVKP 472
Cdd:PRK06370 414 HGDEMIHEILDAMYAGAPYTTLSRAIHIHPTVSELIPTLAQALRR 458
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
38-461 |
2.10e-70 |
|
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: 230.61 E-value: 2.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 38 RAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDVTLNKFDWKVIKKSRDEYIKRLNGLYESG 117
Cdd:TIGR01350 19 RAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVYDEIKHAKDLGIEVENVSVDWEKMQKRKNKVVKKLVGGVSGL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 118 LKGSSVEYIRGRATFAEDGTVEVNGAKYRG----KNTLIAVGGKPTIPNIKGAEHG---IDSDGFFDLEDLPSRTVVVGA 190
Cdd:TIGR01350 99 LKKNKVTVIKGEAKFLDPGTVSVTGENGEEtleaKNIIIATGSRPRSLPGPFDFDGkvvITSTGALNLEEVPESLVIIGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 191 GYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMdeETNPLHLHKNTQVTEVIKGDDGL--LTIKTTTGVI 268
Cdd:TIGR01350 179 GVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKAL--KKKGVKILTNTKVTAVEKNDDQVtyENKGGETETL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 269 EKVQTLIwAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFnGETD 348
Cdd:TIGR01350 257 TGEKVLV-AVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVASHEGIVAAENIA-GKEP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 349 NKLTYENIATVVFSHPLIGTVGLTEAEAVEKYGKDEVTLYKSRFNPMlfAVTKHKEKAAMKLVCVGKDEKVVGVHVFGVG 428
Cdd:TIGR01350 335 AHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYDVKIGKFPFAANGK--ALALGETDGFVKIIADKKTGEILGAHIIGPH 412
|
410 420 430
....*....|....*....|....*....|...
gi 71983419 429 SDEMLQGFAVAVTMGATKKQFDQTVAIHPTSAE 461
Cdd:TIGR01350 413 ATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
45-379 |
1.64e-61 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 207.11 E-value: 1.64e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 45 SVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDVTLNKFDWKVIkksRDEYIKRLNGLYESGLKG---- 120
Cdd:PRK07846 24 RIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIREAARLGVDAELDGVRWPDI---VSRVFGRIDPIAAGGEEYrgrd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 121 -SSVEYIRGRATFAEDGTVEV-NGAKYRGKNTLIAVGGKPTIPNIKgAEHGID---SDGFFDLEDLPSRTVVVGAGYIAV 195
Cdd:PRK07846 101 tPNIDVYRGHARFIGPKTLRTgDGEEITADQVVIAAGSRPVIPPVI-ADSGVRyhtSDTIMRLPELPESLVIVGGGFIAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 196 EIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEetnPLHLHKNTQVTEVIKGDDGLlTIKTTTGVIEKVQTLI 275
Cdd:PRK07846 180 EFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASK---RWDVRLGRNVVGVSQDGSGV-TLRLDDGSTVEADVLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 276 WAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFNGETDNKLTYEN 355
Cdd:PRK07846 256 VATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVVQHNLLHPDDLIASDHRF 335
|
330 340
....*....|....*....|....
gi 71983419 356 IATVVFSHPLIGTVGLTEAEAVEK 379
Cdd:PRK07846 336 VPAAVFTHPQIASVGLTENEARAA 359
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
37-335 |
1.44e-58 |
|
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: 194.84 E-value: 1.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 37 RRAREFGVSVGLIEsgrLGGTCVNVGCVPKKVMyncsLHAEFIRDHAdygfdvtlnkFDWKVIKKSRDEYIKRLNGLYES 116
Cdd:pfam07992 17 LTLAQLGGKVTLIE---DEGTCPYGGCVLSKAL----LGAAEAPEIA----------SLWADLYKRKEEVVKKLNNGIEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 117 GLKGSSVEYIRGRATFAEDGTVEVNGAKYRGKNTLIAVGGKPTIPNIKGAEHG-------IDSDGFFDLEDLPSRTVVVG 189
Cdd:pfam07992 80 LLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNvgflvrtLDSAEALRLKLLPKRVVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 190 AGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMdeETNPLHLHKNTQVTEVIkGDDGLLTIKTTTGVIE 269
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKAL--EKNGVEVRLGTSVKEII-GDGDGVEVILKDGTEI 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71983419 270 KVQTLIWAIGRDPLTKelNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGD-DTGKFLLTPVAIAAG 335
Cdd:pfam07992 237 DADLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDcRVGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
38-376 |
7.96e-48 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 173.03 E-value: 7.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 38 RAREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHA-DYGFDVTLNKFDWKVIKKSRDEYIKRL-NGLYE 115
Cdd:PRK13748 116 KAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIAHLRRESPfDGGIAATVPTIDRSRLLAQQQARVDELrHAKYE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 116 SGLKGS-SVEYIRGRATFAEDGT--VEVNGAKYR---GKNTLIAVGGKPTIPNI---KGAEHGIDSDGFFDlEDLPSRTV 186
Cdd:PRK13748 196 GILDGNpAITVLHGEARFKDDQTliVRLNDGGERvvaFDRCLIATGASPAVPPIpglKETPYWTSTEALVS-DTIPERLA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 187 VVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTfDKMLSDELTADMDEETnpLHLHKNTQVTEVIKgDDGLLTIKTTTG 266
Cdd:PRK13748 275 VIGSSVVALELAQAFARLGSKVTILARSTLFFRE-DPAIGEAVTAAFRAEG--IEVLEHTQASQVAH-VDGEFVLTTGHG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 267 VIEKVQTLIwAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFNGE 346
Cdd:PRK13748 351 ELRADKLLV-ATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAINMTGGD 429
|
330 340 350
....*....|....*....|....*....|
gi 71983419 347 TdnKLTYENIATVVFSHPLIGTVGLTEAEA 376
Cdd:PRK13748 430 A--ALDLTAMPAVVFTDPQVATVGYSEAEA 457
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
38-376 |
1.36e-42 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 157.01 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 38 RAREFGVSVGLIES-------GRLGGTCVNVGCVPKKVMYNCSLHAEFIRDH-ADYGFDVTLNKFDWKVIKKSRDEYIKR 109
Cdd:PRK06327 22 RAAQLGLKVACIEAwknpkgkPALGGTCLNVGCIPSKALLASSEEFENAGHHfADHGIHVDGVKIDVAKMIARKDKVVKK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 110 LNGLYESGLKGSSVEYIRGRATF---AEDGT-VEVNGAKY---RGKNTLIAVGGKP-TIPNIKGAEHGI-DSDGFFDLED 180
Cdd:PRK06327 102 MTGGIEGLFKKNKITVLKGRGSFvgkTDAGYeIKVTGEDEtviTAKHVIIATGSEPrHLPGVPFDNKIIlDNTGALNFTE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 181 LPSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEETnpLHLHKNTQVTEVIKGDDGLlT 260
Cdd:PRK06327 182 VPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQG--LDIHLGVKIGEIKTGGKGV-S 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 261 IKTTTG----VIEKVQTLIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVA----I 332
Cdd:PRK06327 259 VAYTDAdgeaQTLEVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGPMLAHKAeeegV 338
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 71983419 333 AAGRRLSHRlfNGETDnkltYENIATVVFSHPLIGTVGLTEAEA 376
Cdd:PRK06327 339 AVAERIAGQ--KGHID----YNTIPWVIYTSPEIAWVGKTEQQL 376
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
43-379 |
4.70e-39 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 146.82 E-value: 4.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 43 GVSVGLIESGRL--GGTCVNVGCVPKKVMyncsLHAEfirdHADYGFDVTLNKfdwkvikksRDEYIKRLNGLYESGLKG 120
Cdd:PRK07251 26 GKKVALVEESKAmyGGTCINIGCIPTKTL----LVAA----EKNLSFEQVMAT---------KNTVTSRLRGKNYAMLAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 121 SSVEYIRGRATFAEDGTVEVNGAKYR----GKNTLI---AVGGKPTIPNIKGAEHGIDSDGFFDLEDLPSRTVVVGAGYI 193
Cdd:PRK07251 89 SGVDLYDAEAHFVSNKVIEVQAGDEKieltAETIVIntgAVSNVLPIPGLADSKHVYDSTGIQSLETLPERLGIIGGGNI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 194 AVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSdELTADMDEETNpLHLHKNTQVTEVIKGDDGLLTikTTTGVIEKVQT 273
Cdd:PRK07251 169 GLEFAGLYNKLGSKVTVLDAASTILPREEPSVA-ALAKQYMEEDG-ITFLLNAHTTEVKNDGDQVLV--VTEDETYRFDA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 274 LIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFNGETDNKLTY 353
Cdd:PRK07251 245 LLYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISLDDFRIVFGYLTGDGSYTLEDR 324
|
330 340
....*....|....*....|....*.
gi 71983419 354 ENIATVVFSHPLIGTVGLTEAEAVEK 379
Cdd:PRK07251 325 GNVPTTMFITPPLSQVGLTEKEAKEA 350
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
43-385 |
1.01e-37 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 143.37 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 43 GVSVGLIESGR-LGGTCVNVGCVPKK-----VMY------NcSLHAEfIRDHADYGFDVTLNKFDwKVIKKSRDeyikrl 110
Cdd:PRK05249 28 GKRVAVIERYRnVGGGCTHTGTIPSKalreaVLRligfnqN-PLYSS-YRVKLRITFADLLARAD-HVINKQVE------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 111 ngLYESGLKGSSVEYIRGRATFAEDGTVEVNGA-----KYRGKNTLIAVGGKPTIP---NIKGaEHGIDSDGFFDLEDLP 182
Cdd:PRK05249 99 --VRRGQYERNRVDLIQGRARFVDPHTVEVECPdgeveTLTADKIVIATGSRPYRPpdvDFDH-PRIYDSDSILSLDHLP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 183 SRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEetNPLHLHKNTQVTEVIKGDDG-LLTI 261
Cdd:PRK05249 176 RSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSFLDDEISDALSYHLRD--SGVTIRHNEEVEKVEGGDDGvIVHL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 262 KTttGVIEKVQTLIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHR 341
Cdd:PRK05249 254 KS--GKKIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIGFPSLASASMDQGRIAAQH 331
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 71983419 342 LFnGETDNKLTyENIATVVFSHPLIGTVGLTEAEAVEKYGKDEV 385
Cdd:PRK05249 332 AV-GEATAHLI-EDIPTGIYTIPEISSVGKTEQELTAAKVPYEV 373
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
43-463 |
6.67e-34 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 132.44 E-value: 6.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 43 GVSVGLIE--SGRLGGTCVNVGCVPKKVM-YNCSLHAEFIRDHADYGfdvtlnkfdwKVIKKSRDEYIKRLNGLyesglk 119
Cdd:PRK08010 26 GWRVALIEqsNAMYGGTCINIGCIPTKTLvHDAQQHTDFVRAIQRKN----------EVVNFLRNKNFHNLADM------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 120 gSSVEYIRGRATFAEDGTVEVNGA----KYRGKNTLIAVGGKPTIPNIKG--AEHGI-DSDGFFDLEDLPSRTVVVGAGY 192
Cdd:PRK08010 90 -PNIDVIDGQAEFINNHSLRVHRPegnlEIHGEKIFINTGAQTVVPPIPGitTTPGVyDSTGLLNLKELPGHLGILGGGY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 193 IAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEETNPLHLHKNTQvteVIKGDDGLLTIKTTTGVIeKVQ 272
Cdd:PRK08010 169 IGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVE---RISHHENQVQVHSEHAQL-AVD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 273 TLIWAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVAIAAGRRLSHRLFNGETDNKLT 352
Cdd:PRK08010 245 ALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGKRSTDD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 353 YENIATVVFSHPLIGTVGLTEAEAVEKYGKDEVTLYKSRFNPMlfAVTKHKEKAAMKLVCVGKDEKVVGVHVFGVGSDEM 432
Cdd:PRK08010 325 RKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVAAIPR--ARVMNDTRGVLKAIVDNKTQRILGASLLCVDSHEM 402
|
410 420 430
....*....|....*....|....*....|.
gi 71983419 433 LQGFAVAVTMGATKKQFDQTVAIHPTSAEEL 463
Cdd:PRK08010 403 INIVKMVMDAGLPYSILRDQIFTHPSMSESL 433
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
39-387 |
1.65e-33 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 131.52 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 39 AREFGVSVGLIESGRLGGTCVNVGCVPKKVMYNCSLHAEFIRDHADYGFDVTlnkfDWKVIKKSRDEYIKRLNGL----- 113
Cdd:PRK07845 20 AAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELRRAAELGIRFI----DDGEARVDLPAVNARVKALaaaqs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 114 --YESGLKGSSVEYIRGRATFAEDG----TVEVNGA-----KYRGKNTLIAVGGKPTIpnIKGAEhgidSDG-------- 174
Cdd:PRK07845 96 adIRARLEREGVRVIAGRGRLIDPGlgphRVKVTTAdggeeTLDADVVLIATGASPRI--LPTAE----PDGeriltwrq 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 175 FFDLEDLPSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTfdkmlSDELTADMDEET---NPLHLHKNTQVTEV 251
Cdd:PRK07845 170 LYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPG-----EDADAAEVLEEVfarRGMTVLKRSRAESV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 252 IKGDDGLLTIKTTTGVIEKVQTLIwAIGRDPLTKELNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTPVA 331
Cdd:PRK07845 245 ERTGDGVVVTLTDGRTVEGSHALM-AVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGVLPLASVA 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 71983419 332 IAAGR-RLSHRLfnGETDNKLTYENIATVVFSHPLIGTVGLTEAEAVE-KYGKDEVTL 387
Cdd:PRK07845 324 AMQGRiAMYHAL--GEAVSPLRLKTVASNVFTRPEIATVGVSQAAIDSgEVPARTVML 379
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
356-466 |
3.11e-31 |
|
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: 116.11 E-value: 3.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 356 IATVVFSHPLIGTVGLTEAEAVEKYGkdEVTLYKSRFNPMLFAVTKHKEKAAMKLVCVGKDEKVVGVHVFGVGSDEMLQG 435
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGG--EVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQE 78
|
90 100 110
....*....|....*....|....*....|.
gi 71983419 436 FAVAVTMGATKKQFDQTVAIHPTSAEELVTM 466
Cdd:pfam02852 79 AALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
39-385 |
2.26e-25 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 109.62 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 39 AREFGVSVGLIESGR--LGGTCVNVGCVPKK-VMYNCSLHAEFIRDHADYGFDVTLNKF--------------------D 95
Cdd:PTZ00153 135 AMERGLKVIIFTGDDdsIGGTCVNVGCIPSKaLLYATGKYRELKNLAKLYTYGIYTNAFkngkndpvernqlvadtvqiD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 96 WKVIKKSRDEYIKRLNGLYESGLKGSS---------VEYIRGRATFAEDGTVEVNGAKYRGKNTLIAVGGKPTIP-NIKG 165
Cdd:PTZ00153 215 ITKLKEYTQSVIDKLRGGIENGLKSKKfcknsehvqVIYERGHIVDKNTIKSEKSGKEFKVKNIIIATGSTPNIPdNIEV 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 166 AEHGI-DSDGFFDLEDLPSRTVVVGAGYIAVEIAGVLANLGSD-------THLLIRYDK-VLRTFDKMLSDEltadmdee 236
Cdd:PTZ00153 295 DQKSVfTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEvvsfeysPQLLPLLDAdVAKYFERVFLKS-------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 237 tNPLHLHKNTQVTEV-----------------IKGDDGllTIKTTTGVIE-KVQTLIWAIGRDPLTKELNLERVGVKTdK 298
Cdd:PTZ00153 367 -KPVRVHLNTLIEYVragkgnqpviighserqTGESDG--PKKNMNDIKEtYVDSCLVATGRKPNTNNLGLDKLKIQM-K 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 299 SGHIIVDEY------QNTSAPGILSVGDDTGKFLLTPVA----------IAAGRRLSHRLFNGETDNK-LTYENIATVVF 361
Cdd:PTZ00153 443 RGFVSVDEHlrvlreDQEVYDNIFCIGDANGKQMLAHTAshqalkvvdwIEGKGKENVNINVENWASKpIIYKNIPSVCY 522
|
410 420
....*....|....*....|....
gi 71983419 362 SHPLIGTVGLTEAEAVEKYGKDEV 385
Cdd:PTZ00153 523 TTPELAFIGLTEKEAKELYPPDNV 546
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
151-347 |
3.88e-23 |
|
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: 99.50 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 151 LIAVGGKPTIPNIKGaehgIDSDGFF---DLEDL-----------PSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDK 216
Cdd:COG0446 83 VLATGARPRPPPIPG----LDLPGVFtlrTLDDAdalrealkefkGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 217 VLRTFDKMLSDELTADMDEetNPLHLHKNTQVTEvIKGDDGlLTIKTTTGVIEKVQTLIWAIGRDPLTkELnLERVGVKT 296
Cdd:COG0446 159 LLGVLDPEMAALLEEELRE--HGVELRLGETVVA-IDGDDK-VAVTLTDGEEIPADLVVVAPGVRPNT-EL-AKDAGLAL 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71983419 297 DKSGHIIVDEYQNTSAPGILSVGD-------DTGKFLLTPVAIAA---GRRLSHRLFNGET 347
Cdd:COG0446 233 GERGWIKVDETLQTSDPDVYAAGDcaevphpVTGKTVYIPLASAAnkqGRVAAENILGGPA 293
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
151-376 |
1.57e-20 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 93.57 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 151 LIAVGGKPTIPNIKGaehgIDSDGFFDLEDLP--------------SRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDK 216
Cdd:PRK09564 108 MIATGARPIIPPIKN----INLENVYTLKSMEdglalkellkdeeiKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDR 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 217 VL-RTFDKmlsdELTADMDEE--TNPLHLHKNTQVTEVIkGDDGLLTIKTTTGVIEkVQTLIWAIGRDPLTkELnLERVG 293
Cdd:PRK09564 184 ILpDSFDK----EITDVMEEElrENGVELHLNEFVKSLI-GEDKVEGVVTDKGEYE-ADVVIVATGVKPNT-EF-LEDTG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 294 VKTDKSGHIIVDEYQNTSAPGILSVGDD-------TGKFLLTPVAIAA---GRRLSHRLFNGETDNKLTYENIATVVFSH 363
Cdd:PRK09564 256 LKTLKNGAIIVDEYGETSIENIYAAGDCatiynivSNKNVYVPLATTAnklGRMVGENLAGRHVSFKGTLGSACIKVLDL 335
|
250
....*....|...
gi 71983419 364 PLiGTVGLTEAEA 376
Cdd:PRK09564 336 EA-ARTGLTEEEA 347
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
123-335 |
1.67e-19 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 88.64 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 123 VEYIRGRAT--FAEDGTVEV---NGAKYRGKNTLIAVGGKPTIPNIKGAE----HGI----DSDGFFdLEDLpsRTVVVG 189
Cdd:COG0492 72 AEILLEEVTsvDKDDGPFRVttdDGTEYEAKAVIIATGAGPRKLGLPGEEefegRGVsycaTCDGFF-FRGK--DVVVVG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 190 AGYIAVEIAGVLANLGSDTHLLIRYDKvLRtfdkmlSDELTADMDEETNPLHLHKNTQVTEvIKGDDGL--LTIK-TTTG 266
Cdd:COG0492 149 GGDSALEEALYLTKFASKVTLIHRRDE-LR------ASKILVERLRANPKIEVLWNTEVTE-IEGDGRVegVTLKnVKTG 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71983419 267 VIE--KVQTLIWAIGRDPLTkELnLERVGVKTDKSGHIIVDEYQNTSAPGILSVGDDTGKFLLTpVAIAAG 335
Cdd:COG0492 221 EEKelEVDGVFVAIGLKPNT-EL-LKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQ-AATAAG 288
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
151-320 |
2.13e-19 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 89.82 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 151 LIAVGGKPTIPNIKGAehgiDSDGFF---DLEDL---------PSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVL 218
Cdd:COG1251 103 VLATGSRPRVPPIPGA----DLPGVFtlrTLDDAdalraalapGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 219 -RTFDKMLSDELTADMdeETNPLHLHKNTQVTEvIKGDDGLLTIKTTTG-VIEkVQTLIWAIGRDPLTkELnLERVGVKT 296
Cdd:COG1251 179 pRQLDEEAGALLQRLL--EALGVEVRLGTGVTE-IEGDDRVTGVRLADGeELP-ADLVVVAIGVRPNT-EL-ARAAGLAV 252
|
170 180
....*....|....*....|....
gi 71983419 297 DKsGhIIVDEYQNTSAPGILSVGD 320
Cdd:COG1251 253 DR-G-IVVDDYLRTSDPDIYAAGD 274
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
184-261 |
1.20e-15 |
|
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: 71.85 E-value: 1.20e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71983419 184 RTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMdeETNPLHLHKNTQVTEVIKGDDGLLTI 261
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKL--EKNGIEFLLNTTVEAIEGNGDGVVVV 76
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
118-360 |
1.96e-12 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 68.62 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 118 LKGSSVEYIRGRATF--AEDGTVEVNGAKyrgknTL------IAVGGKPTIPNIKGAE---HGIDS--------DGFFDL 178
Cdd:COG1252 66 LRRAGVRFIQGEVTGidPEARTVTLADGR-----TLsydylvIATGSVTNFFGIPGLAehaLPLKTledalalrERLLAA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 179 EDLPSRT-----VVVGAGYIAVEIAGVLANLGSDT-------------HLLIRYDKVLRTFDKMLSDELTADMDEetnpL 240
Cdd:COG1252 141 FERAERRrlltiVVVGGGPTGVELAGELAELLRKLlrypgidpdkvriTLVEAGPRILPGLGEKLSEAAEKELEK----R 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 241 H--LHKNTQVTEVikgDDGllTIKTTTGVIEKVQTLIWAIG-R-DPLTKELNLErvgvkTDKSGHIIVDEY-QNTSAPGI 315
Cdd:COG1252 217 GveVHTGTRVTEV---DAD--GVTLEDGEEIPADTVIWAAGvKaPPLLADLGLP-----TDRRGRVLVDPTlQVPGHPNV 286
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 71983419 316 LSVGD------DTGKFL--LTPVAIAAGRRLSH---RLFNGETDNKLTYENIATVV 360
Cdd:COG1252 287 FAIGDcaavpdPDGKPVpkTAQAAVQQAKVLAKniaALLRGKPLKPFRYRDKGCLA 342
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
184-320 |
4.50e-11 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 64.42 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 184 RTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVLRTFDKMLSDELTADMDEETNPLHLHKntqvtEVIKGDDGLLTIKt 263
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNE-----EIDAINGNEVTFK- 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 71983419 264 tTGVIEKVQTLIWAIGRDPLTKelNLERVGVKTDKSGHIIVDEYQNTSAPGILSVGD 320
Cdd:PRK13512 224 -SGKVEHYDMIIEGVGTHPNSK--FIESSNIKLDDKGFIPVNDKFETNVPNIYAIGD 277
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
149-320 |
4.64e-10 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 62.15 E-value: 4.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 149 NTLI-AVGGKPTIPNIKGAEHGiDSDGFFDLEDLPS---------RTVVVGAGYIAVEIAGVLANLGSDTHlLIRYDKVL 218
Cdd:TIGR02374 98 DKLIlATGSYPFILPIPGADKK-GVYVFRTIEDLDAimamaqrfkKAAVIGGGLLGLEAAVGLQNLGMDVS-VIHHAPGL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 219 --RTFDKMLSDELTADMDEETNPLHLHKNtqvTEVIKGDDGLLTIKTTTGVIEKVQTLIWAIG---RDPLTKELNLervg 293
Cdd:TIGR02374 176 maKQLDQTAGRLLQRELEQKGLTFLLEKD---TVEIVGATKADRIRFKDGSSLEADLIVMAAGirpNDELAVSAGI---- 248
|
170 180
....*....|....*....|....*..
gi 71983419 294 vktDKSGHIIVDEYQNTSAPGILSVGD 320
Cdd:TIGR02374 249 ---KVNRGIIVNDSMQTSDPDIYAVGE 272
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
151-320 |
6.24e-09 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 58.59 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 151 LIAVGGKPTIPNIKGAEHgidSDGFF--DLEDLPS---------RTVVVGAGYIAVEIAGVLANLGSDTHlLIRYDKVL- 218
Cdd:PRK14989 106 IMATGSYPWIPPIKGSET---QDCFVyrTIEDLNAieacarrskRGAVVGGGLLGLEAAGALKNLGVETH-VIEFAPMLm 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 219 -RTFDKMLSDELTADMDEETNPLHLHKNTQvtEVI-KGDDGLLTIKTTTGVIEKVQTLIWAIG---RDPLTKELNLErvg 293
Cdd:PRK14989 182 aEQLDQMGGEQLRRKIESMGVRVHTSKNTL--EIVqEGVEARKTMRFADGSELEVDFIVFSTGirpQDKLATQCGLA--- 256
|
170 180
....*....|....*....|....*..
gi 71983419 294 vkTDKSGHIIVDEYQNTSAPGILSVGD 320
Cdd:PRK14989 257 --VAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
184-355 |
2.04e-08 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 56.09 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 184 RTVVVGAGYIAVEIAGVLANLGSDTHLLIRYDKVL-RTFDKMLSDELTADMDEETNPLHLhkNTQVTEVIKGDDGLLTIK 262
Cdd:PRK09754 146 SVVIVGAGTIGLELAASATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILL--NNAIEHVVDGEKVELTLQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 263 TTTGVIEKVqtLIWAIG---RDPLTKELNLervgvktDKSGHIIVDEYQNTSAPGILSVGDdtgkflltpVAIaagrrls 339
Cdd:PRK09754 224 SGETLQADV--VIYGIGisaNDQLAREANL-------DTANGIVIDEACRTCDPAIFAGGD---------VAI------- 278
|
170
....*....|....*.
gi 71983419 340 HRLFNGETDNKLTYEN 355
Cdd:PRK09754 279 TRLDNGALHRCESWEN 294
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
151-337 |
2.47e-08 |
|
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: 55.91 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 151 LIAVG-GKPTIPNIKGAEH-----GID-------SDGFFDLEDLPSRTVVVGAGYIAVEIAGVLANLG-SDTHLLIRYDK 216
Cdd:COG0493 211 FLATGaGKPRDLGIPGEDLkgvhsAMDfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGaESVTIVYRRTR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 217 vlrtfdkmlsDELTAdMDEETNPLH-----LHKNTQVTEVIKGDDG----LLTIKTTTG-----------------VIEK 270
Cdd:COG0493 291 ----------EEMPA-SKEEVEEALeegveFLFLVAPVEIIGDENGrvtgLECVRMELGepdesgrrrpvpiegseFTLP 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71983419 271 VQTLIWAIGRDPLTKELnLERVGVKTDKSGHIIVDE-YQNTSAPGILSVGDD-TGKFLLTpVAIAAGRR 337
Cdd:COG0493 360 ADLVILAIGQTPDPSGL-EEELGLELDKRGTIVVDEeTYQTSLPGVFAGGDAvRGPSLVV-WAIAEGRK 426
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
137-319 |
5.23e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 51.07 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 137 TVEVNGAKYRGKNTLIAVG--GKPTIPNIKgaEHGIDSDGFFDLEDLP-SRTVVVGAGYIAVEIAGVLANLGSDTHLLIR 213
Cdd:pfam13738 109 VVTTSKGTYQARYVIIATGefDFPNKLGVP--ELPKHYSYVKDFHPYAgQKVVVIGGYNSAVDAALELVRKGARVTVLYR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 214 yDKVLRTFDKMLSDELTADMDEE------TNPLHLHKNTQVTEvIKGDDGLLTIKTTTG-VIEKVQTLIWAIGRDPlTKE 286
Cdd:pfam13738 187 -GSEWEDRDSDPSYSLSPDTLNRleelvkNGKIKAHFNAEVKE-ITEVDVSYKVHTEDGrKVTSNDDPILATGYHP-DLS 263
|
170 180 190
....*....|....*....|....*....|....
gi 71983419 287 LnLERVGVKTDKSGHIIVD-EYQNTSAPGILSVG 319
Cdd:pfam13738 264 F-LKKGLFELDEDGRPVLTeETESTNVPGLFLAG 296
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
151-350 |
3.45e-06 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 49.38 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 151 LIAVGGKPTIPNIKGAEhgidSDGFFDLE------------------DLPS----------RTVVVGAGYIAVEIAGVLA 202
Cdd:PTZ00318 118 VVAHGARPNTFNIPGVE----ERAFFLKEvnhargirkrivqcieraSLPTtsveerkrllHFVVVGGGPTGVEFAAELA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 203 NLGSD-----THLLIRY---------DKVLRTFDKMLSDELTADMDEetNPLHLHKNTQVTEVIkgDDGLLtikTTTGVI 268
Cdd:PTZ00318 194 DFFRDdvrnlNPELVEEckvtvleagSEVLGSFDQALRKYGQRRLRR--LGVDIRTKTAVKEVL--DKEVV---LKDGEV 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 269 EKVQTLIWA--IGRDPLTKELNLERvgvktDKSGHIIVDEY-QNTSAPGILSVGD--DTGKFLLTPVAIAAGRRLSH--R 341
Cdd:PTZ00318 267 IPTGLVVWStgVGPGPLTKQLKVDK-----TSRGRISVDDHlRVKPIPNVFALGDcaANEERPLPTLAQVASQQGVYlaK 341
|
....*....
gi 71983419 342 LFNGETDNK 350
Cdd:PTZ00318 342 EFNNELKGK 350
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
137-320 |
7.00e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 47.99 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 137 TVEVNGAKYRGKNTLIAVGGKPTIPNIKGAEHGI--DSDGFFDLEDLP----SRTVVVGAGYIAVEIAGVLANLGSDTHL 210
Cdd:PRK04965 90 VVKSQGNQWQYDKLVLATGASAFVPPIPGRELMLtlNSQQEYRAAETQlrdaQRVLVVGGGLIGTELAMDLCRAGKAVTL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 211 LIRYDKVLRTfdkMLSDELTAdmdeetnPL---------HLHKNTQVTEVIKGDDGLLtIKTTTGVIEKVQTLIWAIGrd 281
Cdd:PRK04965 170 VDNAASLLAS---LMPPEVSS-------RLqhrltemgvHLLLKSQLQGLEKTDSGIR-ATLDSGRSIEVDAVIAAAG-- 236
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 71983419 282 pLTKELNL-ERVGVKTDKSghIIVDEYQNTSAPGILSVGD 320
Cdd:PRK04965 237 -LRPNTALaRRAGLAVNRG--IVVDSYLQTSAPDIYALGD 273
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
173-320 |
2.78e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 42.74 E-value: 2.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 173 DGFFDLEdlpSRTVVVGAGYIAVEIAGVLANLGSDTHLLIRYD--KVLRTFDKMLSDELtadmdeETNPLHLHKNTQVTE 250
Cdd:PRK10262 140 DGFFYRN---QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDgfRAEKILIKRLMDKV------ENGNIILHTNRTLEE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 251 VIKGDDGL--LTIKTT--TGVIE--KVQTLIWAIGRDPLTK----ELNLERVGVKTDKSGHiivDEYQNTSAPGILSVGD 320
Cdd:PRK10262 211 VTGDQMGVtgVRLRDTqnSDNIEslDVAGLFVAIGHSPNTAifegQLELENGYIKVQSGIH---GNATQTSIPGVFAAGD 287
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
184-322 |
8.30e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 41.68 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 184 RTVVVGAGYIAVEIAGVLANLGSdtHL-LIRYDKVLRTfDKMLSDELtadmdEETNPLHLHKNTQVTEVIkGDD----GL 258
Cdd:PRK15317 353 RVAVIGGGNSGVEAAIDLAGIVK--HVtVLEFAPELKA-DQVLQDKL-----RSLPNVTIITNAQTTEVT-GDGdkvtGL 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71983419 259 LTIKTTTGVIEK-------VQtliwaIGRDPLTKELNlervG-VKTDKSGHIIVDEYQNTSAPGILSVGDDT 322
Cdd:PRK15317 424 TYKDRTTGEEHHlelegvfVQ-----IGLVPNTEWLK----GtVELNRRGEIIVDARGATSVPGVFAAGDCT 486
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
129-213 |
4.61e-03 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 39.08 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71983419 129 RATFAEDG---TVEV-NGAKYRGKNTLIAVGG--KPTIPNIKGAE-------HGIDSDGFFDLEDLpsRTVVVGAGYIAV 195
Cdd:COG2072 107 SARWDEADgrwTVTTdDGETLTARFVVVATGPlsRPKIPDIPGLEdfageqlHSADWRNPVDLAGK--RVLVVGTGASAV 184
|
90
....*....|....*...
gi 71983419 196 EIAGVLANLGSDTHLLIR 213
Cdd:COG2072 185 QIAPELARVAAHVTVFQR 202
|
|
| |
