|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
1-450 |
0e+00 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 898.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 1 MTKHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQIREAIHMYGPDYGFDTTINHFD 80
Cdd:PRK06116 1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDVTENKFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 81 WDKLIASRTAYIDRIHTSYDNVLGKNNVDVIHGFARFVDAKTIEVNGETITADHILIATGGRPSHPNIPGVEYGIDSDGF 160
Cdd:PRK06116 81 WAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSDGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 161 FELPALPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADG 240
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 241 SLTLELEDGRSQTVDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRR 320
Cdd:PRK06116 241 SLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 321 LSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPDE 400
Cdd:PRK06116 321 LSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1418711633 401 KIVGIHGIGFGMDEILQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:PRK06116 401 KVVGLHGIGFGADEMIQGFAVAIKMGATKADFDNTVAIHPTAAEEFVTMR 450
|
|
| gluta_reduc_1 |
TIGR01421 |
glutathione-disulfide reductase, animal/bacterial; The tripeptide glutathione is an important ... |
3-450 |
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: 661.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 3 KHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQIREAIHmYGPDYGFDTTI-NHFDW 81
Cdd:TIGR01421 1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMH-DAADYGFYQNDeNTFNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 82 DKLIASRTAYIDRIHTSYDNVLGKNNVDVIHGFARFVDAKTIEVNGETITADHILIATGGRPSHP-NIPGVEYGIDSDGF 160
Cdd:TIGR01421 80 PELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTAPHILIATGGKPSFPeNIPGAELGTDSDGF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 161 FELPALPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADG 240
Cdd:TIGR01421 160 FALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 241 SLTLELEDGR-SQTVDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGR 319
Cdd:TIGR01421 240 KLVIHFEDGKsIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVELTPVAIAAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 320 RLSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPD 399
Cdd:TIGR01421 320 KLSERLFNGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSEKQKCRMKLVCAGKE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1418711633 400 EKIVGIHGIGFGMDEILQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:TIGR01421 400 EKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
22-450 |
4.94e-174 |
|
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: 495.38 E-value: 4.94e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQIREAIHmYGPDYGFDTTINHFDWDKLIASRTAYIDRIHTSYDN 101
Cdd:COG1249 21 RAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEAR-HAAEFGISAGAPSVDWAALMARKDKVVDRLRGGVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 102 VLGKNNVDVIHGFARFVDAKTIEVNG-ETITADHILIATGGRPSHPNIPGV--EYGIDSDGFFELPALPKRVAVVGAGYI 178
Cdd:COG1249 100 LLKKNGVDVIRGRARFVDPHTVEVTGgETLTADHIVIATGSRPRVPPIPGLdeVRVLTSDEALELEELPKSLVVIGGGYI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 179 AVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGsLTLELEDGRSQT---VD 255
Cdd:COG1249 180 GLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG-VTVTLEDGGGEEaveAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 256 CLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPdEHLD 335
Cdd:COG1249 259 KVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENILGKKP-RPVD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 336 YSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPDEKIVGIHGIGFGMDEI 415
Cdd:COG1249 338 YRAIPSVVFTDPEIASVGLTEEEAREAGID--VKVGKFPFAANGRALALGETEGFVKLIADAETGRILGAHIVGPHAGEL 415
|
410 420 430
....*....|....*....|....*....|....*
gi 1418711633 416 LQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:COG1249 416 IHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
5-449 |
9.76e-149 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 434.81 E-value: 9.76e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 5 YDYIAIGGGSGGIASINRAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQIREAIHMYGpDYGFDTTINhFDWDKL 84
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSR-HYGFDTQFS-FNLPLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 85 IASRTAYIDRIHTSYDNVLGKNNVDVIHGFARFV----------------------DAKTI-------EVNGETITADHI 135
Cdd:PTZ00058 127 VERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLsenqvlikkvsqvdgeadesddDEVTIvsagvsqLDDGQVIEGKNI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 136 LIATGGRPSHPNIPGVEYGIDSDGFFELPAlPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLV 215
Cdd:PTZ00058 207 LIAVGNKPIFPDVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 216 EVMNTEGPTLHTNAVPKAVVKNADGSLTLELEDGRSQ-TVDCLIWAIGREPANDNFNLGVTGVKTdEKGYIVVDKFQNTS 294
Cdd:PTZ00058 286 NDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKYeHFDYVIYCVGRSPNTEDLNLKALNIKT-PKGYIKVDDNQRTS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 295 VPGIYAVGDNTGA----------------------------------VELTPVAVAAGRRLSERLFNNKPDEHlDYSNIP 340
Cdd:PTZ00058 365 VKHIYAVGDCCMVkknqeiedlnllklyneepylkkkentsgesyynVQLTPVAINAGRLLADRLFGPFSRTT-NYKLIP 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 341 TVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSAFTAMYTAV----TSHRQPCRMKLVCVGPDEKIVGIHGIGFGMDEIL 416
Cdd:PTZ00058 444 SVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVydmdPAQKEKTYLKLVCVGKEELIKGLHIVGLNADEIL 523
|
490 500 510
....*....|....*....|....*....|...
gi 1418711633 417 QGFAVALKMGATKKDFDNTVAIHPTAAEEFVTM 449
Cdd:PTZ00058 524 QGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
23-450 |
4.38e-141 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 415.43 E-value: 4.38e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 23 AAMYGQKCALIE----------AKALGGTCVNVGCVPKKVMWHAAQIReaiHMYGPDYGF----DTTINHfDWDKLIASR 88
Cdd:PLN02546 98 ASNFGASAAVCElpfatissdtLGGVGGTCVLRGCVPKKLLVYASKYS---HEFEESRGFgwkyETEPKH-DWNTLIANK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 89 TAYIDRIHTSYDNVLGKNNVDVIHGFARFVDAKTIEVNGETITADHILIATGGRPSHPNIPGVEYGIDSDGFFELPALPK 168
Cdd:PLN02546 174 NAELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGKLYTARNILIAVGGRPFIPDIPGIEHAIDSDAALDLPSKPE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 169 RVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGSLTLELED 248
Cdd:PLN02546 254 KIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 249 GRSQTVDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNN 328
Cdd:PLN02546 334 GTVEGFSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGN 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 329 KPDEHlDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPDEKIVGIHGI 408
Cdd:PLN02546 414 EPTKP-DYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD--VDVFTANFRPLKATLSGLPDRVFMKLIVCAKTNKVLGVHMC 490
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1418711633 409 GFGMDEILQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:PLN02546 491 GEDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMR 532
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
22-450 |
1.89e-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: 399.57 E-value: 1.89e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQIREAIHMyGPDYGFDTTINHFDWDKLIASRTAYIDRIHTSYDN 101
Cdd:TIGR01424 20 LAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFED-AAGYGWTVGKARFDWKKLLAAKDQEIARLSGLYRK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 102 VLGKNNVDVIHGFARFVDAKTIEV--NGETITADHILIATGGRPSHPNIPGVEYGIDSDGFFELPALPKRVAVVGAGYIA 179
Cdd:TIGR01424 99 GLANAGAELLDGRAELVGPNTVEVlaSGKTYTAEKILIAVGGRPPKPALPGHELGITSNEAFHLPTLPKSILIAGGGYIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 180 VELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGSLTLELEDGRSQTVDCLIW 259
Cdd:TIGR01424 179 VEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDSITSISKDDDGRLKATLSKHEEIVADVVLF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 260 AIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEhLDYSNI 339
Cdd:TIGR01424 259 ATGRSPNTNGLGLEAAGVRLNDLGAIAVDEYSRTSTPSIYAVGDVTDRINLTPVAIHEATCFAETEFGNNPTS-FDHDLI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 340 PTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPDEKIVGIHGIGFGMDEILQGF 419
Cdd:TIGR01424 338 ATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRPMKATFSGRQEKTLMKLVVDAKDDKVLGAHMVGPDAAEIIQGL 415
|
410 420 430
....*....|....*....|....*....|.
gi 1418711633 420 AVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:TIGR01424 416 AIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
22-449 |
3.06e-114 |
|
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: 344.14 E-value: 3.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEAK---------ALGGTCVNVGCVPKKVMWHAAQIREAIH---MYGpdYGFDTTINHfDWDKLIASRT 89
Cdd:TIGR01438 20 EAAAYGAKVMLLDFVtptplgtrwGIGGTCVNVGCIPKKLMHQAALLGQALKdsrNYG--WKVEETVKH-DWKRLVEAVQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 90 AYIDRIHTSYDNVLGKNNVDVIHGFARFVDAKTIEVNG-----ETITADHILIATGGRPSHPNIPGV-EYGIDSDGFFEL 163
Cdd:TIGR01438 97 NHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNkkgkeKIYSAERFLIATGERPRYPGIPGAkELCITSDDLFSL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 164 PALPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKhAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGSLT 243
Cdd:TIGR01438 177 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 244 --LELEDGRSQTVDCLIWAIGREPANDNFNLGVTGVKTDEK-GYIVVDKFQNTSVPGIYAVGD-NTGAVELTPVAVAAGR 319
Cdd:TIGR01438 256 efTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPYIYAVGDiLEDKPELTPVAIQAGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 320 RLSERLFNNKpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSAFTAM-YTAVtsHRQP---CRMKLVC 395
Cdd:TIGR01438 336 LLAQRLFKGS-TVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLeWTIP--SRDNhnkCYAKLVC 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1418711633 396 -VGPDEKIVGIHGIGFGMDEILQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTM 449
Cdd:TIGR01438 413 nKKENERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTL 467
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
23-450 |
2.32e-112 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 339.87 E-value: 2.32e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 23 AAMYGQKCALIE----------AKALGGTCVNVGCVPKKVMWHAAQIREAIHMyGPDYGFDttINH---FDWDKLIASRT 89
Cdd:PLN02507 44 SANFGAKVGICElpfhpissesIGGVGGTCVIRGCVPKKILVYGATFGGEFED-AKNYGWE--INEkvdFNWKKLLQKKT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 90 AYIDRIHTSYDNVLGKNNVDVIHGFARFVDAKTIEV---NGETI--TADHILIATGGRPSHPNIPGVEYGIDSDGFFELP 164
Cdd:PLN02507 121 DEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqlDGTKLryTAKHILIATGSRAQRPNIPGKELAITSDEALSLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 165 ALPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGsLTL 244
Cdd:PLN02507 201 ELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-IKV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 245 ELEDGRSQTVDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSER 324
Cdd:PLN02507 280 ITDHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDVTNRINLTPVALMEGTCFAKT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 325 LFNNKPDEHlDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDqVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPDEKIVG 404
Cdd:PLN02507 360 VFGGQPTKP-DYENVACAVFCIPPLSVVGLSEEEAVEQAKGD-ILVFTSSFNPMKNTISGRQEKTVMKLIVDAETDKVLG 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1418711633 405 IHGIGFGMDEILQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:PLN02507 438 ASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMR 483
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
21-450 |
4.04e-106 |
|
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: 323.46 E-value: 4.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 21 NRAAMYGQKCALIEAK---------ALGGTCVNVGCVPKKVMWHAAQ----IREAIhmyGPDYGFDTTINHFDWDKLIAS 87
Cdd:TIGR01423 21 NAATLYKKRVAVVDVQthhgppfyaALGGTCVNVGCVPKKLMVTGAQymdtLRESA---GFGWEFDRSSVKANWKALIAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 88 RTAYIDRIHTSYDNVLGKNN-VDVIHGFARFVDAKTIEVNG---------ETITADHILIATGGRPSHPNIPGVEYGIDS 157
Cdd:TIGR01423 98 KNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVREsadpksavkERLQAEHILLATGSWPQMLGIPGIEHCISS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 158 DGFFELPALPKRVAVVGAGYIAVELAGVING---LGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAV 234
Cdd:TIGR01423 178 NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 235 VKNADGSLTLELEDGRSQTVDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVA 314
Cdd:TIGR01423 258 TLNADGSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTDRVMLTPVA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 315 VAAGRRLSERLFNNKPdEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYgdDQVKVYKSAFTA-MYTAVTSHRQPCRMKL 393
Cdd:TIGR01423 338 INEGAAFVDTVFGNKP-RKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPlMHNISGSKYKKFVAKI 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1418711633 394 VCVGPDEKIVGIHGIGFGMDEILQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:TIGR01423 415 VTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMR 471
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
5-446 |
5.62e-105 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 320.62 E-value: 5.62e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 5 YDYIAIGGGSGGIASINRAAMYGQKCALIE---------AKALGGTCVNVGCVPKKVMWHAAQIREAIHMYGPDYGFDTT 75
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGTCVNVGCVPKKLMHYAANIGSIFHHDSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 76 iNHFDWDKLIASRTAYIDRIHTSYDNVLGKNNVDVIHGFARFVDAKTIEVNG----ETITADHILIATGGRPSHP-NIPG 150
Cdd:PTZ00052 86 -SSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDnsqeETITAKYILIATGGRPSIPeDVPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 151 -VEYGIDSDGFFELPALPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKhAPLRSFDPLIVDTLVEVMNTEGPTLHTNA 229
Cdd:PTZ00052 165 aKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRS-IPLRGFDRQCSEKVVEYMKEQGTLFLEGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 230 VPKAVVKnADGSLTLELEDGRSQTVDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKfQNTSVPGIYAVGD-NTGAV 308
Cdd:PTZ00052 244 VPINIEK-MDDKIKVLFSDGTTELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN-DCTNIPNIFAVGDvVEGRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 309 ELTPVAVAAGRRLSERLFNNKpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSAFTAMYTAvTSHRQP 388
Cdd:PTZ00052 322 ELTPVAIKAGILLARRLFKQS-NEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIA-AVHREK 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418711633 389 ----------------CRMKLVCV-GPDEKIVGIHGIGFGMDEILQGFAVALKMGATKKDFDNTVAIHPTAAEEF 446
Cdd:PTZ00052 400 herarkdeydfdvssnCLAKLVCVkSEDNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVF 474
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
22-444 |
6.07e-96 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 296.32 E-value: 6.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQIREAIHMyGPDYGFDTTINHFDWDKLIASRTAYIDRIHTS-YD 100
Cdd:PRK06292 21 RAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKH-AEEFGIHADGPKIDFKKVMARVRRERDRFVGGvVE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 101 NVLGKNNVDVIHGFARFVDAKTIEVNGETITADHILIATGGRPshPNIPGVEYG-----IDSDGFFELPALPKRVAVVGA 175
Cdd:PRK06292 100 GLEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGSRV--PPIPGVWLIlgdrlLTSDDAFELDKLPKSLAVIGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 176 GYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPtLHTNAVPKAVVKNADGSLTLELEDGRSQT-- 253
Cdd:PRK06292 178 GVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKEFK-IKLGAKVTSVEKSGDEKVEELEKGGKTETie 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 254 VDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDeH 333
Cdd:PRK06292 257 ADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGDVAG-G 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 334 LDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPDEKIVGIHGIGFGMD 413
Cdd:PRK06292 336 VRYHPIPSVVFTDPQIASVGLTEEELKAAGID--YVVGEVPFEAQGRARVMGKNDGFVKVYADKKTGRLLGAHIIGPDAE 413
|
410 420 430
....*....|....*....|....*....|.
gi 1418711633 414 EILQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06292 414 HLIHLLAWAMQQGLTVEDLLRMPFYHPTLSE 444
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
22-444 |
2.70e-94 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 292.05 E-value: 2.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQI-REAIHMygPDYGFDTTINHFDWDKLIASRTAYIDRIHTSYD 100
Cdd:PRK06416 22 RAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERaDEARHS--EDFGIKAENVGIDFKKVQEWKNGVVNRLTGGVE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 101 NVLGKNNVDVIHGFARFVDAKTIEVN----GETITADHILIATGGRPShpNIPGVEYG----IDSDGFFELPALPKRVAV 172
Cdd:PRK06416 100 GLLKKNKVDIIRGEAKLVDPNTVRVMtedgEQTYTAKNIILATGSRPR--ELPGIEIDgrviWTSDEALNLDEVPKSLVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 173 VGAGYIAVELAGVINGLGAEA-------HLfvrkhapLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGsLTLE 245
Cdd:PRK06416 178 IGGGYIGVEFASAYASLGAEVtivealpRI-------LPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQTDDG-VTVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 246 LEDG---RSQTVDCLIWAIGREPANDNFNLGVTGVKTDeKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLS 322
Cdd:PRK06416 250 LEDGgkeETLEADYVLVAVGRRPNTENLGLEELGVKTD-RGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKASAEGIIAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 323 ERLFNNkpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPDEKI 402
Cdd:PRK06416 329 EAIAGN--PHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVVKFPFAGNGKALALGETDGFVKLIFDKKDGEV 404
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1418711633 403 VGIHGIGFGMDEILQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06416 405 LGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
22-444 |
2.86e-93 |
|
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: 289.16 E-value: 2.86e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQI-REAIHmyGPDYGFDTTINHFDWDKLIASRTAYIDRIHTSYD 100
Cdd:TIGR01350 19 RAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVyDEIKH--AKDLGIEVENVSVDWEKMQKRKNKVVKKLVGGVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 101 NVLGKNNVDVIHGFARFVDAKTIEVNGE----TITADHILIATGGRPSHPNIP---GVEYGIDSDGFFELPALPKRVAVV 173
Cdd:TIGR01350 97 GLLKKNKVTVIKGEAKFLDPGTVSVTGEngeeTLEAKNIIIATGSRPRSLPGPfdfDGKVVITSTGALNLEEVPESLVII 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 174 GAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNaDGSLTLELEDGRSQT 253
Cdd:TIGR01350 177 GGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKN-DDQVTYENKGGETET 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 254 V--DCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFnNKPD 331
Cdd:TIGR01350 256 LtgEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVASHEGIVAAENIA-GKEP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 332 EHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPDEKIVGIHGIGFG 411
Cdd:TIGR01350 335 AHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYD--VKIGKFPFAANGKALALGETDGFVKIIADKKTGEILGAHIIGPH 412
|
410 420 430
....*....|....*....|....*....|...
gi 1418711633 412 MDEILQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:TIGR01350 413 ATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
22-444 |
3.79e-89 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 278.62 E-value: 3.79e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQireAIHM--YGPDYGFDTTIN-HFDWDKLIASRTAYIDRIHTS 98
Cdd:PRK06370 23 RAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASAR---AAHLarRAAEYGVSVGGPvSVDFKAVMARKRRIRARSRHG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 99 YDNVL-GKNNVDVIHGFARFVDAKTIEVNGETITADHILIATGGRPSHPNIPGVE---YgIDSDGFFELPALPKRVAVVG 174
Cdd:PRK06370 100 SEQWLrGLEGVDVFRGHARFESPNTVRVGGETLRAKRIFINTGARAAIPPIPGLDevgY-LTNETIFSLDELPEHLVIIG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 175 AGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADG-SLTLELEDGRSQ- 252
Cdd:PRK06370 179 GGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGDGiAVGLDCNGGAPEi 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 253 TVDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPdE 332
Cdd:PRK06370 259 TGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAYNDARIVAANLLDGGR-R 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 333 HLDYSNIPTVVFSHPPIGTVGLTEPQAReQYGDDqVKVYKSAFTAMYTAVTSHRQPCRMKLVcVGPDEK------IVGIH 406
Cdd:PRK06370 338 KVSDRIVPYATYTDPPLARVGMTEAEAR-KSGRR-VLVGTRPMTRVGRAVEKGETQGFMKVV-VDADTDrilgatILGVH 414
|
410 420 430
....*....|....*....|....*....|....*...
gi 1418711633 407 GigfgmDEILQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06370 415 G-----DEMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
22-444 |
7.77e-85 |
|
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: 7.77e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQIREAIHmyGPDYGFDTTINHFDWDKLIASRTAYIDRI-HTSYD 100
Cdd:TIGR02053 18 KAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYAR--KPPFGGLAATVAVDFGELLEGKREVVEELrHEKYE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 101 NVLGKNNVDVIHGFARFVDAKTIEVNGETIT--ADHILIATGGRPSHPNIPG---VEYgIDSDGFFELPALPKRVAVVGA 175
Cdd:TIGR02053 96 DVLSSYGVDYLRGRARFKDPKTVKVDLGREVrgAKRFLIATGARPAIPPIPGlkeAGY-LTSEEALALDRIPESLAVIGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 176 GYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGSL-TLELEDGRSQT- 253
Cdd:TIGR02053 175 GAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIiTVEKPGGQGEVe 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 254 VDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNkPDEH 333
Cdd:TIGR02053 255 ADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEYVAAKEGVVAAENALGG-ANAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 334 LDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKsaFTAMYTAVTSHRQPCRMKLVCVGPDEKIVGIHGIGFGMD 413
Cdd:TIGR02053 334 LDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLP--LTNVPRARINRDTRGFIKLVAEPGTGKVLGVQVVAPEAA 411
|
410 420 430
....*....|....*....|....*....|.
gi 1418711633 414 EILQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:TIGR02053 412 EVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
27-444 |
4.76e-74 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 239.47 E-value: 4.76e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 27 GQKCALIEAKALGGTCVNVGCVPKKVMWHAAQIREAIHmYGPDYGFDTTINHFDWDKlIASRT-AYIDRIHTS---YdNV 102
Cdd:PRK07846 22 DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIR-EAARLGVDAELDGVRWPD-IVSRVfGRIDPIAAGgeeY-RG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 103 LGKNNVDVIHGFARFVDAKTIEV-NGETITADHILIATGGRPSHPNIP---GVEYGIdSDGFFELPALPKRVAVVGAGYI 178
Cdd:PRK07846 99 RDTPNIDVYRGHARFIGPKTLRTgDGEEITADQVVIAAGSRPVIPPVIadsGVRYHT-SDTIMRLPELPESLVIVGGGFI 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 179 AVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPT-LHTNAVPkavVKNADGSLTLELEDGRSQTVDCL 257
Cdd:PRK07846 178 AAEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKRWDVrLGRNVVG---VSQDGSGVTLRLDDGSTVEADVL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 258 IWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYS 337
Cdd:PRK07846 255 LVATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVVQHNLLHPDDLIASDHR 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 338 NIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSAFTAMYTAVTSHRQPCrmKLVCVGPDEKIVGIHGIGFGMDEILQ 417
Cdd:PRK07846 335 FVPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAMEDTTGFV--KLIADRDTGRLLGAHIIGPQASTLIQ 412
|
410 420
....*....|....*....|....*...
gi 1418711633 418 GFAVALKMGATKKDF-DNTVAIHPTAAE 444
Cdd:PRK07846 413 PLIQAMSFGLDAREMaRGQYWIHPALPE 440
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
22-318 |
1.92e-71 |
|
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: 227.59 E-value: 1.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEakaLGGTCVNVGCVPKKVMWHAAQIREAIHmygpdygfdttinhfDWDKLIASRTAYIDRIHTSYDN 101
Cdd:pfam07992 18 TLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIAS---------------LWADLYKRKEEVVKKLNNGIEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 102 VLGKNNVDVIHGFARFVDAKTIEVNGETITADHILIATGGRPSHPNIPGVEYG-------IDSDGFFELPALPKRVAVVG 174
Cdd:pfam07992 80 LLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNvgflvrtLDSAEALRLKLLPKRVVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 175 AGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGsLTLELEDGRSQTV 254
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDG-VEVILKDGTEIDA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418711633 255 DCLIWAIGREPANDnfNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNT-GAVELTPVAVAAG 318
Cdd:pfam07992 239 DLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRvGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
22-362 |
1.88e-67 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 225.03 E-value: 1.88e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQI----REAihmygP-DYGFDTTINHFDWDKLIASRTAYIDRI- 95
Cdd:PRK13748 116 KAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIahlrRES-----PfDGGIAATVPTIDRSRLLAQQQARVDELr 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 96 HTSYDNVLGKN-NVDVIHGFARFVDAKTIEV----NGE-TITADHILIATGGRPSHPNIPGVE---YGIDSDGFFElPAL 166
Cdd:PRK13748 191 HAKYEGILDGNpAITVLHGEARFKDDQTLIVrlndGGErVVAFDRCLIATGASPAVPPIPGLKetpYWTSTEALVS-DTI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 167 PKRVAVVGAGYIAVELAGVINGLGAEAHLFVRkHAPLRSFDPLIVDTLVEVMNTEGPTL--HTNAvpkAVVKNADGSLTL 244
Cdd:PRK13748 270 PERLAVIGSSVVALELAQAFARLGSKVTILAR-STLFFREDPAIGEAVTAAFRAEGIEVleHTQA---SQVAHVDGEFVL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 245 ELEDGrSQTVDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSER 324
Cdd:PRK13748 346 TTGHG-ELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAIN 424
|
330 340 350
....*....|....*....|....*....|....*...
gi 1418711633 325 LFNNkpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQ 362
Cdd:PRK13748 425 MTGG--DAALDLTAMPAVVFTDPQVATVGYSEAEAHHD 460
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
22-444 |
3.11e-67 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 222.11 E-value: 3.11e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAMYGQKCALIEA-------KALGGTCVNVGCVPKKVMWHAAQIREAIHMYGPDYGFDTTINHFDWDKLIASRTAYIDR 94
Cdd:PRK06327 22 RAAQLGLKVACIEAwknpkgkPALGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIHVDGVKIDVAKMIARKDKVVKK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 95 IHTSYDNVLGKNNVDVIHGFARFVDAKT----IEVNGE---TITADHILIATGGRPSHpnIPGVEYG----IDSDGFFEL 163
Cdd:PRK06327 102 MTGGIEGLFKKNKITVLKGRGSFVGKTDagyeIKVTGEdetVITAKHVIIATGSEPRH--LPGVPFDnkiiLDNTGALNF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 164 PALPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADG-SL 242
Cdd:PRK06327 180 TEVPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGvSV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 243 TLELEDGRSQT--VDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRR 320
Cdd:PRK06327 260 AYTDADGEAQTleVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGPMLAHKAEEEGVA 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 321 LSERLFNNKPdeHLDYSNIPTVVFSHPPIGTVGLTEPQAREQygDDQVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPDE 400
Cdd:PRK06327 340 VAERIAGQKG--HIDYNTIPWVIYTSPEIAWVGKTEQQLKAE--GVEYKAGKFPFMANGRALAMGEPDGFVKIIADAKTD 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1418711633 401 KIVGIHGIGFGMDEILQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06327 416 EILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSE 459
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
22-444 |
1.58e-63 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 211.94 E-value: 1.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 22 RAAM----YGQKCALIEAK-ALGGTCVNVGCVPKKVMWHAA----QIREAiHMYGpDYGFdttINHFDWDKLIASRTAYI 92
Cdd:PRK05249 19 GAAMqaakLGKRVAVIERYrNVGGGCTHTGTIPSKALREAVlrliGFNQN-PLYS-SYRV---KLRITFADLLARADHVI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 93 DR---IHTSYdnvLGKNNVDVIHGFARFVDAKTIEVNG-----ETITADHILIATGGRPSHPniPGVEYG----IDSDGF 160
Cdd:PRK05249 94 NKqveVRRGQ---YERNRVDLIQGRARFVDPHTVEVECpdgevETLTADKIVIATGSRPYRP--PDVDFDhpriYDSDSI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 161 FELPALPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLrSF-DPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNAD 239
Cdd:PRK05249 169 LSLDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLL-SFlDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 240 GSLTlELEDGRSQTVDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDK-FQnTSVPGIYAVGDNTGAVELTPVAVAAG 318
Cdd:PRK05249 248 GVIV-HLKSGKKIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNEnYQ-TAVPHIYAVGDVIGFPSLASASMDQG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 319 RRLSERLFNNkPDEHLdYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGP 398
Cdd:PRK05249 326 RIAAQHAVGE-ATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKVP--YEVGRARFKELARAQIAGDNVGMLKILFHRE 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1418711633 399 DEKIVGIHGIGFGMDEILQ-GFAVaLKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK05249 402 TLEILGVHCFGERATEIIHiGQAI-MEQKGTIEYFVNTTFNYPTMAE 447
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
27-446 |
1.82e-63 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 211.15 E-value: 1.82e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 27 GQKCALIEAKAL--GGTCVNVGCVPKKVMWHAAQireaihmygpdygfdttiNHFDWDKLIASRTAYIDRIHTSYDNVLG 104
Cdd:PRK07251 26 GKKVALVEESKAmyGGTCINIGCIPTKTLLVAAE------------------KNLSFEQVMATKNTVTSRLRGKNYAMLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 105 KNNVDVIHGFARFVDAKTIEVNG----ETITADHILIATGGRPSHPNIPGV---EYGIDSDGFFELPALPKRVAVVGAGY 177
Cdd:PRK07251 88 GSGVDLYDAEAHFVSNKVIEVQAgdekIELTAETIVINTGAVSNVLPIPGLadsKHVYDSTGIQSLETLPERLGIIGGGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 178 IAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVvKNADGSLTLELEDGrSQTVDCL 257
Cdd:PRK07251 168 IGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEV-KNDGDQVLVVTEDE-TYRFDAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 258 IWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYS 337
Cdd:PRK07251 246 LYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISLDDFRIVFGYLTGDGSYTLEDRG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 338 NIPTVVFSHPPIGTVGLTEPQAREQYGddQVKVYKSAFTAMYTAVTSHRQPCRMKLVcVGPDEK-IVGIHGIGFGMDEIL 416
Cdd:PRK07251 326 NVPTTMFITPPLSQVGLTEKEAKEAGL--PYAVKELLVAAMPRAHVNNDLRGAFKVV-VNTETKeILGATLFGEGSQEII 402
|
410 420 430
....*....|....*....|....*....|
gi 1418711633 417 QGFAVALKMGATKKDFDNTVAIHPTAAEEF 446
Cdd:PRK07251 403 NLITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
24-444 |
4.22e-48 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 170.58 E-value: 4.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 24 AMYGQKCALIEAKA--LGGTCVNVGCVPKKVMWHAAQireaihmygpdygfdttiNHFDWDKLIASRTAYIDRIHT-SYD 100
Cdd:PRK08010 23 AKAGWRVALIEQSNamYGGTCINIGCIPTKTLVHDAQ------------------QHTDFVRAIQRKNEVVNFLRNkNFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 101 NVLGKNNVDVIHGFARFVDAKTIEV---NGE-TITADHILIATGGRPSHPNIPGVEY--GI-DSDGFFELPALPKRVAVV 173
Cdd:PRK08010 85 NLADMPNIDVIDGQAEFINNHSLRVhrpEGNlEIHGEKIFINTGAQTVVPPIPGITTtpGVyDSTGLLNLKELPGHLGIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 174 GAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVvKNADGSLTLELEDGrSQT 253
Cdd:PRK08010 165 GGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERI-SHHENQVQVHSEHA-QLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 254 VDCLIWAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEH 333
Cdd:PRK08010 243 VDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGKRST 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 334 LDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSAftAMYTAVTSHRQPCRMKLVCVGPDEKIVGIHGIGFGMD 413
Cdd:PRK08010 323 DDRKNVPYSVFMTPPLSRVGMTEEQARESGADIQVVTLPVA--AIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDSH 400
|
410 420 430
....*....|....*....|....*....|.
gi 1418711633 414 EILQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK08010 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSE 431
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
339-449 |
1.73e-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: 150.78 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 339 IPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSAFTAMYTAVTSHRQPCRMKLVCVGPDEKIVGIHGIGFGMDEILQG 418
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQE 78
|
90 100 110
....*....|....*....|....*....|.
gi 1418711633 419 FAVALKMGATKKDFDNTVAIHPTAAEEFVTM 449
Cdd:pfam02852 79 AALAIKMGATVEDLANTIHIHPTLSEALVEA 109
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
119-330 |
1.07e-33 |
|
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: 128.78 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 119 DAKTIEV-NGETITADHILIATGGRPSHPNIPGveygIDSDGFF------ELPAL--------PKRVAVVGAGYIAVELA 183
Cdd:COG0446 65 EAKTVTLrDGETLSYDKLVLATGARPRPPPIPG----LDLPGVFtlrtldDADALrealkefkGKRAVVIGGGPIGLELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 184 GVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVvkNADGSLTLELEDGRSQTVDCLIWAIGR 263
Cdd:COG0446 141 EALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAI--DGDDKVAVTLTDGEEIPADLVVVAPGV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418711633 264 EPandNFNLGV-TGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGA----------VELTPVAVAAGRRLSERLFNNKP 330
Cdd:COG0446 219 RP---NTELAKdAGLALGERGWIKVDETLQTSDPDVYAAGDCAEVphpvtgktvyIPLASAANKQGRVAAENILGGPA 293
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
23-361 |
2.22e-33 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 130.75 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 23 AAMYGQKCALIEAKALGGTCVNVGCVPKKVMWHAAQIREAIHmYGPDYGfdttINHFDWDKLIASrtayIDRIHT----- 97
Cdd:PRK07845 20 AAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELR-RAAELG----IRFIDDGEARVD----LPAVNArvkal 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 98 ----SYD--NVLGKNNVDVIHGFARFVDAK----TIEVNG-----ETITADHILIATGGRPShpNIPGVEygidSDG--- 159
Cdd:PRK07845 91 aaaqSADirARLEREGVRVIAGRGRLIDPGlgphRVKVTTadggeETLDADVVLIATGASPR--ILPTAE----PDGeri 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 160 -----FFELPALPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAV 234
Cdd:PRK07845 165 ltwrqLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 235 VKNADGsLTLELEDGRsqTVD---CLIwAIGREPANDNFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELT 311
Cdd:PRK07845 245 ERTGDG-VVVTLTDGR--TVEgshALM-AVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGVLPLA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1418711633 312 PVAVAAGR-----RLSERLfnnKPdehLDYSNIPTVVFSHPPIGTVGLTEPQARE 361
Cdd:PRK07845 321 SVAAMQGRiamyhALGEAV---SP---LRLKTVASNVFTRPEIATVGVSQAAIDS 369
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
37-444 |
5.65e-29 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 120.02 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 37 ALGGTCVNVGCVPKKVMWHAA----QIREAIHMYGpdYGFDTTIN------------------HFDWDKLIASRTAYIDR 94
Cdd:PTZ00153 151 SIGGTCVNVGCIPSKALLYATgkyrELKNLAKLYT--YGIYTNAFkngkndpvernqlvadtvQIDITKLKEYTQSVIDK 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 95 IHTSYDNVLGKN-------NVDVIHGFARFVDAKTI--EVNGETITADHILIATGgrpSHPNIP-GVEygID------SD 158
Cdd:PTZ00153 229 LRGGIENGLKSKkfcknseHVQVIYERGHIVDKNTIksEKSGKEFKVKNIIIATG---STPNIPdNIE--VDqksvftSD 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 159 GFFELPALPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPT-LHTNAVPKAV--- 234
Cdd:PTZ00153 304 TAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLDADVAKYFERVFLKSKPVrVHLNTLIEYVrag 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 235 --------------VKNADGSLTLELEDGRSQTVDCLIwAIGREPANDNFNLGVTGVKTDeKGYIVVD------KFQNTS 294
Cdd:PTZ00153 384 kgnqpviighserqTGESDGPKKNMNDIKETYVDSCLV-ATGRKPNTNNLGLDKLKIQMK-RGFVSVDehlrvlREDQEV 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 295 VPGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEH-----------LDYSNIPTVVFSHPPIGTVGLTEPQAREQY 363
Cdd:PTZ00153 462 YDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKENVninvenwaskpIIYKNIPSVCYTTPELAFIGLTEKEAKELY 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 364 GDDQVKVYKSAFTAMYTAVTSHRQPCR----------------------MKLVCVGPDEKIVGIHGIGFGMDEILQGFAV 421
Cdd:PTZ00153 542 PPDNVGVEISFYKANSKVLCENNISFPnnsknnsynkgkyntvdntegmVKIVYLKDTKEILGMFIVGSYASILIHEGVL 621
|
490 500
....*....|....*....|...
gi 1418711633 422 ALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PTZ00153 622 AINLKLSVKDLAHMVHSHPTISE 644
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
23-318 |
1.55e-26 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 108.67 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 23 AAMYGQKCALIEAKALGG-----TCV-NVGCVPKKV--MWHAAQIREAIHMYGPDYgFDTTINHFDwdkliasRTAYIDR 94
Cdd:COG0492 19 AARAGLKTLVIEGGEPGGqlattKEIeNYPGFPEGIsgPELAERLREQAERFGAEI-LLEEVTSVD-------KDDGPFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 95 IHTSydnvlgknnvdvihgfarfvdaktievNGETITADHILIATGGRPSHPNIP--------GVEYGIDSDGFFelpaL 166
Cdd:COG0492 91 VTTD---------------------------DGTEYEAKAVIIATGAGPRKLGLPgeeefegrGVSYCATCDGFF----F 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 167 P-KRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHApLRSfDPLIVDtlvEVMNTEGPTLHTNAVPKAVvkNADGSLT-L 244
Cdd:COG0492 140 RgKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDE-LRA-SKILVE---RLRANPKIEVLWNTEVTEI--EGDGRVEgV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 245 ELEDGRSQT-----VDCLIWAIGREPANDNFNlgVTGVKTDEKGYIVVDKFQNTSVPGIYAVGD-NTGAVELtpVAVAAG 318
Cdd:COG0492 213 TLKNVKTGEekeleVDGVFVAIGLKPNTELLK--GLGLELDEDGYIVVDEDMETSVPGVFAAGDvRDYKYRQ--AATAAG 288
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
93-343 |
5.14e-26 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 108.68 E-value: 5.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 93 DRIHTSYDNVLGKNNVDVIHGFARFVD--AKTIEV-NGETITADHILIATGGRPSHPNIPGVE---YGIDS--------- 157
Cdd:COG1252 56 DDIAIPLRELLRRAGVRFIQGEVTGIDpeARTVTLaDGRTLSYDYLVIATGSVTNFFGIPGLAehaLPLKTledalalre 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 158 --DGFFELPALPK--RVAVVGAGYIAVELAGvinglgaEAHLFVRKHAPLRSFDPLIVD-TLVEVMNTEGPTLHTNAVPK 232
Cdd:COG1252 136 rlLAAFERAERRRllTIVVVGGGPTGVELAG-------ELAELLRKLLRYPGIDPDKVRiTLVEAGPRILPGLGEKLSEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 233 AV---------------VKNADGSlTLELEDGRSQTVDCLIWAIGREPANDnfnLGVTGVKTDEKGYIVVDKF-QNTSVP 296
Cdd:COG1252 209 AEkelekrgvevhtgtrVTEVDAD-GVTLEDGEEIPADTVIWAAGVKAPPL---LADLGLPTDRRGRVLVDPTlQVPGHP 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1418711633 297 GIYAVGDnTGAVE------LTPVAVAA---GRRLSE---RLFNNKPDEHLDYSNIPTVV 343
Cdd:COG1252 285 NVFAIGD-CAAVPdpdgkpVPKTAQAAvqqAKVLAKniaALLRGKPLKPFRYRDKGCLA 342
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
105-372 |
1.57e-25 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 107.53 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 105 KNNVDVIHGfARFV----DAKTIEV-NGETITADHILIATGGRPSHPNIPGVE----YGI----DSDGFFELPALPKRVA 171
Cdd:COG1251 68 ENGIDLRLG-TRVTaidrAARTVTLaDGETLPYDKLVLATGSRPRVPPIPGADlpgvFTLrtldDADALRAALAPGKRVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 172 VVGAGYIAVELAGVINGLGAEAHLFVRKHAPL-RSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNaDGSLTLELEDGR 250
Cdd:COG1251 147 VIGGGLIGLEAAAALRKRGLEVTVVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGD-DRVTGVRLADGE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 251 SQTVDCLIWAIGREPaNDNFnLGVTGVKTDeKGyIVVDKFQNTSVPGIYAVGD---------NTGAVELTPVAVAAGRRL 321
Cdd:COG1251 226 ELPADLVVVAIGVRP-NTEL-ARAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDcaehpgpvyGRRVLELVAPAYEQARVA 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1418711633 322 SERLfNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQARE-QYGDDQVKVYK 372
Cdd:COG1251 302 AANL-AGGPAAYEGSVPSTKLKVFGVDVASAGDAEGDEEVvVRGDPARGVYK 352
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
122-320 |
7.64e-20 |
|
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: 91.35 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 122 TIEVN---GETITA-------DHILIATG-GRPSHPNIPG-----VEYGID-------SDGFFELPALPKRVAVVGAGYI 178
Cdd:COG0493 187 EFRTNvevGKDITLdelleefDAVFLATGaGKPRDLGIPGedlkgVHSAMDfltavnlGEAPDTILAVGKRVVVIGGGNT 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 179 AVELAGVINGLGAE-AHLFVR---KHAPLRSFdplivdtlvEVMN--TEGPTLHTNAVPKAVVKNADGSLT------LEL 246
Cdd:COG0493 267 AMDCARTALRLGAEsVTIVYRrtrEEMPASKE---------EVEEalEEGVEFLFLVAPVEIIGDENGRVTglecvrMEL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 247 ----EDGRSQTV-----------DCLIWAIGREPaNDNFNLGVTGVKTDEKGYIVVDKF-QNTSVPGIYAVGDN-TGA-- 307
Cdd:COG0493 338 gepdESGRRRPVpiegseftlpaDLVILAIGQTP-DPSGLEEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAvRGPsl 416
|
250
....*....|....
gi 1418711633 308 -VEltpvAVAAGRR 320
Cdd:COG0493 417 vVW----AIAEGRK 426
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
119-325 |
1.28e-19 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 90.87 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 119 DAKTIEV----NGETITA--DHILIATGGRPSHPNIPGveygIDSDGFFELPALP--------------KRVAVVGAGYI 178
Cdd:PRK09564 85 KNKTITVknlkTGSIFNDtyDKLMIATGARPIIPPIKN----INLENVYTLKSMEdglalkellkdeeiKNIVIIGAGFI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 179 AVELAGVINGLGAEAHLFVR-KHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVknADGSLTLELEDGRSQTVDCL 257
Cdd:PRK09564 161 GLEAVEAAKHLGKNVRIIQLeDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLI--GEDKVEGVVTDKGEYEADVV 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418711633 258 IWAIGREPANDNFNlgVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDN-------TGAVELTPVAVAA---GRRLSERL 325
Cdd:PRK09564 239 IVATGVKPNTEFLE--DTGLKTLKNGAIIVDEYGETSIENIYAAGDCatiynivSNKNVYVPLATTAnklGRMVGENL 314
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
169-249 |
2.61e-18 |
|
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: 79.17 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 169 RVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGSlTLELED 248
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV-VVVLTD 79
|
.
gi 1418711633 249 G 249
Cdd:pfam00070 80 G 80
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
122-302 |
3.75e-15 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 75.72 E-value: 3.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 122 TIEVNGETITADHILIATgGRPSHPNIPGV-EYGIDSdGFFELPALP--KRVAVVGAGYIAVELAGVINGLGAEAHLFVR 198
Cdd:pfam13738 109 VVTTSKGTYQARYVIIAT-GEFDFPNKLGVpELPKHY-SYVKDFHPYagQKVVVIGGYNSAVDAALELVRKGARVTVLYR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 199 KHA-------PLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAvVKNADGSLTLELEDGRSQTVDC-LIWAIGREPandNF 270
Cdd:pfam13738 187 GSEwedrdsdPSYSLSPDTLNRLEELVKNGKIKAHFNAEVKE-ITEVDVSYKVHTEDGRKVTSNDdPILATGYHP---DL 262
|
170 180 190
....*....|....*....|....*....|....
gi 1418711633 271 N-LGVTGVKTDEKGYIVVDKF-QNTSVPGIYAVG 302
Cdd:pfam13738 263 SfLKKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
118-303 |
2.47e-14 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 74.18 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 118 VDAKTIEVNGETITADHILIATGGRPSHPNIPGVEYGIDSDGFFELPA------LPKRVAVVGAGYIAVELAGVINGLGA 191
Cdd:PRK04965 86 AEAQVVKSQGNQWQYDKLVLATGASAFVPPIPGRELMLTLNSQQEYRAaetqlrDAQRVLVVGGGLIGTELAMDLCRAGK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 192 EAHLFVRKHAPLRSFDPLIVDT-LVEVMNTEGPTLHTNAVPKAVVKNADGsLTLELEDGRSQTVDCLIWAIGREPandnf 270
Cdd:PRK04965 166 AVTLVDNAASLLASLMPPEVSSrLQHRLTEMGVHLLLKSQLQGLEKTDSG-IRATLDSGRSIEVDAVIAAAGLRP----- 239
|
170 180 190
....*....|....*....|....*....|....*.
gi 1418711633 271 NLGV---TGVKTdEKGyIVVDKFQNTSVPGIYAVGD 303
Cdd:PRK04965 240 NTALarrAGLAV-NRG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
122-320 |
7.87e-14 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 72.90 E-value: 7.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 122 TIEVN---GETITA-------DHILIATG-GRPSHPNIPG-----VEYGID-------SDGFFELPAlPKRVAVVGAGYI 178
Cdd:PRK11749 206 EIRTNtevGRDITLdelragyDAVFIGTGaGLPRFLGIPGenlggVYSAVDfltrvnqAVADYDLPV-GKRVVVIGGGNT 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 179 AVELAGVINGLGAE-AHLFVRkhaplRSFDPLIVdTLVEVMN--TEGPTLHTNAVPKAVVKNADGSLTLELE-------- 247
Cdd:PRK11749 285 AMDAARTAKRLGAEsVTIVYR-----RGREEMPA-SEEEVEHakEEGVEFEWLAAPVEILGDEGRVTGVEFVrmelgepd 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 248 -DGRSQT----------VDCLIWAIGREPaNDNFNLGVTGVKTDEKGYIVVD--KFQnTSVPGIYAVGDNTGAVELTPVA 314
Cdd:PRK11749 359 aSGRRRVpiegseftlpADLVIKAIGQTP-NPLILSTTPGLELNRWGTIIADdeTGR-TSLPGVFAGGDIVTGAATVVWA 436
|
....*.
gi 1418711633 315 VAAGRR 320
Cdd:PRK11749 437 VGDGKD 442
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
133-325 |
2.09e-13 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 71.17 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 133 DHILIATGG-RPSHPNIPG------------------VEYG-IDSDGFFelPALPKRVAVVGAGYIAVELAGVINGLGAE 192
Cdd:PRK12770 120 DAVLIATGTwKSRKLGIPGedlpgvysaleylfriraAKLGyLPWEKVP--PVEGKKVVVVGAGLTAVDAALEAVLLGAE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 193 AHLFV----RKHAPLRSFDpliVDTLVEvmntEGPTLHTNAVPKAV--------VKNADGSLTLELEDGRSQTV------ 254
Cdd:PRK12770 198 KVYLAyrrtINEAPAGKYE---IERLIA----RGVEFLELVTPVRIigegrvegVELAKMRLGEPDESGRPRPVpipgse 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418711633 255 -----DCLIWAIGREPANDnFNLGVTGVKTDEKGYIVVDKFQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSERL 325
Cdd:PRK12770 271 fvleaDTVVFAIGEIPTPP-FAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSI 345
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
72-303 |
8.79e-12 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 67.16 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 72 FDTTI----NHFDWDKLIASrtAYIDRIHTSYDNVLGKNNVDVIHGFARFVDAKTIEVN----------GETITADHILI 137
Cdd:TIGR02374 25 FEITIfgeePHPNYNRILLS--SVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQIDtdqkqvitdaGRTLSYDKLIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 138 ATGGRPSHPNIPGVE----YGI----DSDGFFELPALPKRVAVVGAGYIAVELAGVINGLGAEAHlfVRKHAPL---RSF 206
Cdd:TIGR02374 103 ATGSYPFILPIPGADkkgvYVFrtieDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVS--VIHHAPGlmaKQL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 207 DPLIVDTLVEVMNTEGPTLHTNAVPKAVVKnADGSLTLELEDGRSQTVDCLIWAIGREPandNFNLGV-TGVKTDekGYI 285
Cdd:TIGR02374 181 DQTAGRLLQRELEQKGLTFLLEKDTVEIVG-ATKADRIRFKDGSSLEADLIVMAAGIRP---NDELAVsAGIKVN--RGI 254
|
250
....*....|....*...
gi 1418711633 286 VVDKFQNTSVPGIYAVGD 303
Cdd:TIGR02374 255 IVNDSMQTSDPDIYAVGE 272
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
28-303 |
4.48e-11 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 64.42 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 28 QKCALIEAKALGGTCvnvgcvpkkvmwhAAQIREAihmygpDYGFDTTINHFDWDKLIAS--RTAYIDRIHTSYDNVLG- 104
Cdd:PRK13512 2 PKIIVVGAVAGGATC-------------ASQIRRL------DKESDIIIFEKDRDMSFANcaLPYYIGEVVEDRKYALAy 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 105 -------KNNVDV--IHGFARFVDA-KTIEV----NGETITA--DHILIATGGRPSHPNIpgveygiDSDGFFELPALP- 167
Cdd:PRK13512 63 tpekfydRKQITVktYHEVIAINDErQTVTVlnrkTNEQFEEsyDKLILSPGASANSLGF-------ESDITFTLRNLEd 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 168 -------------KRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAV 234
Cdd:PRK13512 136 tdaidqfikanqvDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAI 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 235 VKNadgslTLELEDGRSQTVDCLIWAIGREPaNDNFnLGVTGVKTDEKGYIVV-DKFQnTSVPGIYAVGD 303
Cdd:PRK13512 216 NGN-----EVTFKSGKVEHYDMIIEGVGTHP-NSKF-IESSNIKLDDKGFIPVnDKFE-TNVPNIYAIGD 277
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
118-320 |
2.21e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 62.34 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 118 VDAKTIEVNGETITADHIL---------IATG-GRPSHPNIPGveygIDSDGFF-------------------ELP-ALP 167
Cdd:PRK12831 206 VKIETNVVVGKTVTIDELLeeegfdavfIGSGaGLPKFMGIPG----ENLNGVFsanefltrvnlmkaykpeyDTPiKVG 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 168 KRVAVVGAGYIAVELAGVINGLGAEAHLFVR---KHAPLRSFDplivdtlVEVMNTEGPTLHTNAVPKAVVKNADGSLT- 243
Cdd:PRK12831 282 KKVAVVGGGNVAMDAARTALRLGAEVHIVYRrseEELPARVEE-------VHHAKEEGVIFDLLTNPVEILGDENGWVKg 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 244 -----LELED----GRSQTV-----------DCLIWAIGREPaNDNFNLGVTGVKTDEKGYIVVDKFQN-TSVPGIYAVG 302
Cdd:PRK12831 355 mkcikMELGEpdasGRRRPVeiegsefvlevDTVIMSLGTSP-NPLISSTTKGLKINKRGCIVADEETGlTSKEGVFAGG 433
|
250
....*....|....*....
gi 1418711633 303 DN-TGAVELTpVAVAAGRR 320
Cdd:PRK12831 434 DAvTGAATVI-LAMGAGKK 451
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
88-303 |
7.94e-10 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 61.29 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 88 RTAYiDRIH-TSY-------------DNVLGKNNVDVIHGFARFV---DAKTIEVN-GETITADHILIATGGRPSHPNIP 149
Cdd:PRK14989 41 RIAY-DRVHlSSYfshhtaeelslvrEGFYEKHGIKVLVGERAITinrQEKVIHSSaGRTVFYDKLIMATGSYPWIPPIK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 150 GVEygiDSDGFF-----ELPAL------PKRVAVVGAGYIAVELAGVINGLGAEAHlfVRKHAPL---RSFDPLIVDTLV 215
Cdd:PRK14989 120 GSE---TQDCFVyrtieDLNAIeacarrSKRGAVVGGGLLGLEAAGALKNLGVETH--VIEFAPMlmaEQLDQMGGEQLR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 216 EVMNTEGPTLHTNAVPKAVVKNA-DGSLTLELEDGRSQTVDCLIWAIGREPANdnfNLGV-TGVKTDEKGYIVVDKFQNT 293
Cdd:PRK14989 195 RKIESMGVRVHTSKNTLEIVQEGvEARKTMRFADGSELEVDFIVFSTGIRPQD---KLATqCGLAVAPRGGIVINDSCQT 271
|
250
....*....|
gi 1418711633 294 SVPGIYAVGD 303
Cdd:PRK14989 272 SDPDIYAIGE 281
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
119-305 |
3.33e-09 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 58.63 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 119 DAKTIEV-NGETITADHILIATGGRPSHPNIP--------GVEYGIDSDG-FFElpalPKRVAVVGAGYIAVE----LAG 184
Cdd:PRK15317 297 GLIEVELaNGAVLKAKTVILATGARWRNMNVPgedeyrnkGVAYCPHCDGpLFK----GKRVAVIGGGNSGVEaaidLAG 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 185 VInglgaeAHLFVRKHAP-LRSfDPLIVDTLVEVMNTegpTLHTNAVPKAVVKNADGSLTLELED---GRSQTVDC--LI 258
Cdd:PRK15317 373 IV------KHVTVLEFAPeLKA-DQVLQDKLRSLPNV---TIITNAQTTEVTGDGDKVTGLTYKDrttGEEHHLELegVF 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1418711633 259 WAIGREPaNDNFNLGVtgVKTDEKGYIVVDKFQNTSVPGIYAVGDNT 305
Cdd:PRK15317 443 VQIGLVP-NTEWLKGT--VELNRRGEIIVDARGATSVPGVFAAGDCT 486
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
133-330 |
8.57e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 57.82 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 133 DHILIATGG-RPSHPNIPG-----VEYGID-----SDGffELPALPKRVAVVGAGYIAVELAGVINGLGAEAH--LFVRK 199
Cdd:PRK12814 280 DAVLLAVGAqKASKMGIPGeelpgVISGIDflrnvALG--TALHPGKKVVVIGGGNTAIDAARTALRLGAESVtiLYRRT 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 200 HAPLRSFDPLIVDTLvevmnTEGPTLHTNAVPKAVVKNADGsltLEL-----------EDGRSQTV-----------DCL 257
Cdd:PRK12814 358 REEMPANRAEIEEAL-----AEGVSLRELAAPVSIERSEGG---LELtaikmqqgepdESGRRRPVpvegseftlqaDTV 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 258 IWAIGRE---PANDNfnlgvTGVKTDEKGYIVVDK-FQNTSVPGIYAVGDNTGAVELTPVAVAAGRRLSE---RLFNNKP 330
Cdd:PRK12814 430 ISAIGQQvdpPIAEA-----AGIGTSRNGTVKVDPeTLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHaidLFLNGKP 504
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
131-303 |
1.45e-08 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 56.22 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 131 TADHILIATGGRPSHPNIP--------GVEYGIDSDGFFelpALPKRVAVVGAGYIAVELAGVINGLGAEAHLFVRKHAp 202
Cdd:PRK10262 105 TCDALIIATGASARYLGLPseeafkgrGVSACATCDGFF---YRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 203 LRSfDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGSLTLELEDGRS----QTVDC--LIWAIGREPANDNFNlgvtG 276
Cdd:PRK10262 181 FRA-EKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNsdniESLDVagLFVAIGHSPNTAIFE----G 255
|
170 180 190
....*....|....*....|....*....|..
gi 1418711633 277 VKTDEKGYIVVD-----KFQNTSVPGIYAVGD 303
Cdd:PRK10262 256 QLELENGYIKVQsgihgNATQTSIPGVFAAGD 287
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
107-306 |
1.49e-08 |
|
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: 56.41 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 107 NVDVIHgfARFVDAK---TIEV-NGETITADHILIATGG--RPSHPNIPGVE-YGIDS------DGFFELPalPKRVAVV 173
Cdd:COG2072 102 GTEVTS--ARWDEADgrwTVTTdDGETLTARFVVVATGPlsRPKIPDIPGLEdFAGEQlhsadwRNPVDLA--GKRVLVV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 174 GAGY----IAVELAGVinglGAEAHLFVRKH---APLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVVKNADGSL---- 242
Cdd:COG2072 178 GTGAsavqIAPELARV----AAHVTVFQRTPpwvLPRPNYDPERGRPANYLGLEAPPALNRRDARAWLRRLLRAQVkdpe 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 243 -------------------------------------------TLELEDGRSQTVDCLIWAIGREPANDNFNL------- 272
Cdd:COG2072 254 lglltpdyppgckrpllstdyyealrrgnvelvtggieritedGVVFADGTEHEVDVIVWATGFRADLPWLAPldvrgrd 333
|
250 260 270
....*....|....*....|....*....|....
gi 1418711633 273 GVTGVKTdEKGYIVVDkfqntsVPGIYAVGDNTG 306
Cdd:COG2072 334 GRSGPRA-YLGVVVPG------FPNLFFLGPNSP 360
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
126-303 |
4.68e-08 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 54.93 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 126 NGETITADHILIATGGRPSH--------PNIPGVEYGIDSDGFFELPALPKRVAVVGAGYIAVELAGVINGLGA------ 191
Cdd:PRK09754 95 NGESWHWDQLFIATGAAARPlplldalgERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCkvtvie 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 192 EAHLFVRKHAPlrsfdPLIVDTLVEVMNTEGPTLHTNavpKAVVKNADGS-LTLELEDGRSQTVDCLIWAIGREpANDNF 270
Cdd:PRK09754 175 LAATVMGRNAP-----PPVQRYLLQRHQQAGVRILLN---NAIEHVVDGEkVELTLQSGETLQADVVIYGIGIS-ANDQL 245
|
170 180 190
....*....|....*....|....*....|...
gi 1418711633 271 NLGvTGVKTDekGYIVVDKFQNTSVPGIYAVGD 303
Cdd:PRK09754 246 ARE-ANLDTA--NGIVIDEACRTCDPAIFAGGD 275
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
162-334 |
4.71e-08 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 55.27 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 162 ELPALPKRVAVVGAGYIAVELAGVINGLGAE----AHLFVRKHAPLRSFDpliVDTLVEvmntEGPTLHTNAVPKAVVKN 237
Cdd:PRK12771 262 EPPFLGKRVVVIGGGNTAMDAARTARRLGAEevtiVYRRTREDMPAHDEE---IEEALR----EGVEINWLRTPVEIEGD 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 238 ADGSLTLEL---------EDGRSQTV---------DCLIWAIGREpANDNFNLGVTGVkTDEKGYIVVDK-FQNTSVPGI 298
Cdd:PRK12771 335 ENGATGLRVitvekmeldEDGRPSPVtgeeetleaDLVVLAIGQD-IDSAGLESVPGV-EVGRGVVQVDPnFMMTGRPGV 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1418711633 299 YAVGDNTGAVELTPVAVAAGRR--------LSERLFNNKPDEHL 334
Cdd:PRK12771 413 FAGGDMVPGPRTVTTAIGHGKKaarnidafLGGEPYEHRPKREI 456
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
103-320 |
1.71e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 53.59 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 103 LGKNNVDV-IHGFARF-VDAKTIEVNGETITADH--------ILIATG-GRPSHPNIPGVEY-GIDS-----------DG 159
Cdd:PRK12778 479 LPKKIVDVeIENLKKLgVKFETDVIVGKTITIEEleeegfkgIFIASGaGLPNFMNIPGENSnGVMSsneyltrvnlmDA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 160 FFELPALP----KRVAVVGAGYIAVELAGVINGLGAEAHLFV----RKHAPLRsfdplivdtLVEVMNT--EGPTLHTNA 229
Cdd:PRK12778 559 ASPDSDTPikfgKKVAVVGGGNTAMDSARTAKRLGAERVTIVyrrsEEEMPAR---------LEEVKHAkeEGIEFLTLH 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 230 VPKAVVKNADGSLT------LELED-------------GRSQTVDC--LIWAIGREPaNDNFNLGVTGVKTDEKGYIVVD 288
Cdd:PRK12778 630 NPIEYLADEKGWVKqvvlqkMELGEpdasgrrrpvaipGSTFTVDVdlVIVSVGVSP-NPLVPSSIPGLELNRKGTIVVD 708
|
250 260 270
....*....|....*....|....*....|...
gi 1418711633 289 KFQNTSVPGIYAVGDN-TGAVELTpVAVAAGRR 320
Cdd:PRK12778 709 EEMQSSIPGIYAGGDIvRGGATVI-LAMGDGKR 740
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
118-320 |
2.39e-06 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 49.94 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 118 VDAKTIEVNGETITADHILIATG----------GRPSHPNIPGvEY-----------------GIDSDGFFELP-ALPKR 169
Cdd:PRK12775 495 VKIETNKVIGKTFTVPQLMNDKGfdavflgvgaGAPTFLGIPG-EFagqvysanefltrvnlmGGDKFPFLDTPiSLGKS 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 170 VAVVGAGYIAVELAGVINGLGA----------EAHLFVR----KHAPLRSFDPLIVDTLVEVMNTEGPTLHTNAVPKAVV 235
Cdd:PRK12775 574 VVVIGAGNTAMDCLRVAKRLGAptvrcvyrrsEAEAPARieeiRHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKVEEMEL 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418711633 236 KNADgsltlelEDGRSQTV----------DCLIWAIGREPaNDNFNLGVTGVKTDEKGYIVVDKF-----QNTSVPGIYA 300
Cdd:PRK12775 654 GEPD-------EKGRRKPMptgefkdlecDTVIYALGTKA-NPIITQSTPGLALNKWGNIAADDGklestQSTNLPGVFA 725
|
250 260
....*....|....*....|
gi 1418711633 301 VGDNTGAVELTPVAVAAGRR 320
Cdd:PRK12775 726 GGDIVTGGATVILAMGAGRR 745
|
|
| |
