|
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: 902.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 1 MTKHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHMYGPDYGFDTTINKFN 80
Cdd:PRK06116 1 MTKDYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGTCVNVGCVPKKLMWYGAQIAEAFHDYAPGYGFDVTENKFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 81 WETLIASRTAYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPDIPGVEYGIDSDGF 160
Cdd:PRK06116 81 WAKLIANRDAYIDRLHGSYRNGLENNGVDLIEGFARFVDAHTVEVNGERYTADHILIATGGRPSIPDIPGAEYGITSDGF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 161 FALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADG 240
Cdd:PRK06116 161 FALEELPKRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 241 SLTLELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRR 320
Cdd:PRK06116 241 SLTLTLEDGETLTVDCLIWAIGREPNTDGLGLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVTGRVELTPVAIAAGRR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 321 LSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEE 400
Cdd:PRK06116 321 LSERLFNNKPDEKLDYSNIPTVVFSHPPIGTVGLTEEEAREQYGEDNVKVYRSSFTPMYTALTGHRQPCLMKLVVVGKEE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446082953 401 KIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 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: 672.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 3 KHYDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHmYGPDYGFDTTI-NKFNW 81
Cdd:TIGR01421 1 KHYDYLVIGGGSGGIASARRAAEHGAKALLVEAKKLGGTCVNVGCVPKKVMWYASDLAERMH-DAADYGFYQNDeNTFNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 82 ETLIASRTAYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPD-IPGVEYGIDSDGF 160
Cdd:TIGR01421 80 PELKEKRDAYVDRLNGIYQKNLEKNKVDVIFGHARFTKDGTVEVNGRDYTAPHILIATGGKPSFPEnIPGAELGTDSDGF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 161 FALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADG 240
Cdd:TIGR01421 160 FALEELPKRVVIVGAGYIAVELAGVLHGLGSETHLVIRHERVLRSFDSMISETITEEYEKEGINVHKLSKPVKVEKTVEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 241 SLTLELEDGR-SETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGR 319
Cdd:TIGR01421 240 KLVIHFEDGKsIDDVDELIWAIGRKPNTKGLGLENVGIKLNEKGQIIVDEYQNTNVPGIYALGDVVGKVELTPVAIAAGR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 320 RLSERLFNNKPDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSE 399
Cdd:TIGR01421 320 KLSERLFNGKTDDKLDYNNVPTVVFSHPPIGTIGLTEKEAIEKYGKENIKVYNSSFTPMYYAMTSEKQKCRMKLVCAGKE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446082953 400 EKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:TIGR01421 400 EKVVGLHGIGDGVDEMLQGFAVAIKMGATKADFDNTVAIHPTSSEELVTMR 450
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
22-450 |
4.01e-178 |
|
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: 505.78 E-value: 4.01e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHmYGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYEN 101
Cdd:COG1249 21 RAAQLGLKVALVEKGRLGGTCLNVGCIPSKALLHAAEVAHEAR-HAAEFGISAGAPSVDWAALMARKDKVVDRLRGGVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 102 VLGKNNVDVIKGFARFVDAKTLEVNG-ETITADHILIATGGRPSHPDIPGV--EYGIDSDGFFALPALPERVAVVGAGYI 178
Cdd:COG1249 100 LLKKNGVDVIRGRARFVDPHTVEVTGgETLTADHIVIATGSRPRVPPIPGLdeVRVLTSDEALELEELPKSLVVIGGGYI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 179 AVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADGsLTLELEDGRSET---VD 255
Cdd:COG1249 180 GLEFAQIFARLGSEVTLVERGDRLLPGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDG-VTVTLEDGGGEEaveAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 256 CLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPdEHLD 335
Cdd:COG1249 259 KVLVATGRRPNTDGLGLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENILGKKP-RPVD 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 336 YSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMDEM 415
Cdd:COG1249 338 YRAIPSVVFTDPEIASVGLTEEEAREAGID--VKVGKFPFAANGRALALGETEGFVKLIADAETGRILGAHIVGPHAGEL 415
|
410 420 430
....*....|....*....|....*....|....*
gi 446082953 416 LQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:COG1249 416 IHEAALAMEMGLTVEDLADTIHAHPTLSEALKEAA 450
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
5-449 |
1.07e-148 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 434.81 E-value: 1.07e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 5 YDYIAIGGGSGGIASINRAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHMYGpDYGFDTTINkFNWETL 84
Cdd:PTZ00058 49 YDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVGCVPKKIMFNAASIHDILENSR-HYGFDTQFS-FNLPLL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 85 IASRTAYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEV-----------------------------NGETITADHI 135
Cdd:PTZ00058 127 VERRDKYIRRLNDIYRQNLKKDNVEYFEGKGSLLSENQVLIkkvsqvdgeadesdddevtivsagvsqldDGQVIEGKNI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 136 LIATGGRPSHPDIPGVEYGIDSDGFFALPAlPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLV 215
Cdd:PTZ00058 207 LIAVGNKPIFPDVKGKEFTISSDDFFKIKE-AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLLRKFDETIINELE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 216 EVMNAEGPQLHTNAIPKAVVKNADGSLTLELEDGRS-ETVDCLIWAIGREPANDNINLEAAGVKTnEKGYIVVDKYQNTN 294
Cdd:PTZ00058 286 NDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKyEHFDYVIYCVGRSPNTEDLNLKALNIKT-PKGYIKVDDNQRTS 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 295 IEGIYAVGDNTGA----------------------------------VELTPVAVAAGRRLSERLFNNKPDEHlDYSNIP 340
Cdd:PTZ00058 365 VKHIYAVGDCCMVkknqeiedlnllklyneepylkkkentsgesyynVQLTPVAINAGRLLADRLFGPFSRTT-NYKLIP 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 341 TVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSSFTAMYTAV----TTHRQPCRMKLVCVGSEEKIVGIHGIGFGMDEML 416
Cdd:PTZ00058 444 SVIFSHPPIGTIGLSEQEAIDIYGKENVKIYESRFTNLFFSVydmdPAQKEKTYLKLVCVGKEELIKGLHIVGLNADEIL 523
|
490 500 510
....*....|....*....|....*....|...
gi 446082953 417 QGFAVALKMGATKKDFDNTVAIHPTAAEEFVTM 449
Cdd:PTZ00058 524 QGFAVALKMNATKADFDETIPIHPTAAEEFVTM 556
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
23-450 |
1.73e-139 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 411.19 E-value: 1.73e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 23 AAMYGQKCALIE----------AKELGGTCVNVGCVPKKVMWHAAQIR---EAIHMYGPDYGFDTtinKFNWETLIASRT 89
Cdd:PLN02546 98 ASNFGASAAVCElpfatissdtLGGVGGTCVLRGCVPKKLLVYASKYShefEESRGFGWKYETEP---KHDWNTLIANKN 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 90 AYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPDIPGVEYGIDSDGFFALPALPER 169
Cdd:PLN02546 175 AELQRLTGIYKNILKNAGVTLIEGRGKIVDPHTVDVDGKLYTARNILIAVGGRPFIPDIPGIEHAIDSDAALDLPSKPEK 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 170 VAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADGSLTLELEDG 249
Cdd:PLN02546 255 IAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKTNKG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 250 RSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNK 329
Cdd:PLN02546 335 TVEGFSHVMFATGRKPNTKNLGLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVTDRINLTPVALMEGGALAKTLFGNE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 330 PDEHlDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIG 409
Cdd:PLN02546 415 PTKP-DYRAVPSAVFSQPPIGQVGLTEEQAIEEYGD--VDVFTANFRPLKATLSGLPDRVFMKLIVCAKTNKVLGVHMCG 491
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446082953 410 FGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:PLN02546 492 EDAPEIIQGFAVAVKAGLTKADFDATVGIHPTAAEEFVTMR 532
|
|
| gluta_reduc_2 |
TIGR01424 |
glutathione-disulfide reductase, plant; The tripeptide glutathione is an important reductant, ... |
22-450 |
5.53e-138 |
|
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: 403.42 E-value: 5.53e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHMyGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYEN 101
Cdd:TIGR01424 20 LAAALGAKVAIAEEFRVGGTCVIRGCVPKKLMVYASQFAEHFED-AAGYGWTVGKARFDWKKLLAAKDQEIARLSGLYRK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 102 VLGKNNVDVIKGFARFVDAKTLEV--NGETITADHILIATGGRPSHPDIPGVEYGIDSDGFFALPALPERVAVVGAGYIA 179
Cdd:TIGR01424 99 GLANAGAELLDGRAELVGPNTVEVlaSGKTYTAEKILIAVGGRPPKPALPGHELGITSNEAFHLPTLPKSILIAGGGYIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 180 VELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADGSLTLELEDGRSETVDCLIW 259
Cdd:TIGR01424 179 VEFAGIFRGLGVQTTLIYRGKEILRGFDDDMRRGLAAALEERGIRILPEDSITSISKDDDGRLKATLSKHEEIVADVVLF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 260 AIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEhLDYSNI 339
Cdd:TIGR01424 259 ATGRSPNTNGLGLEAAGVRLNDLGAIAVDEYSRTSTPSIYAVGDVTDRINLTPVAIHEATCFAETEFGNNPTS-FDHDLI 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 340 PTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMDEMLQGF 419
Cdd:TIGR01424 338 ATAVFSQPPIGTVGLTEEEARRKFGD--IEVYRAEFRPMKATFSGRQEKTLMKLVVDAKDDKVLGAHMVGPDAAEIIQGL 415
|
410 420 430
....*....|....*....|....*....|.
gi 446082953 420 AVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:TIGR01424 416 AIALKMGATKDDFDSTVAVHPTSAEELVTMR 446
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
23-450 |
9.06e-113 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 340.64 E-value: 9.06e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 23 AAMYGQKCALIE----------AKELGGTCVNVGCVPKKVMWHAAQIREAIHMyGPDYGFDttINK---FNWETLIASRT 89
Cdd:PLN02507 44 SANFGAKVGICElpfhpissesIGGVGGTCVIRGCVPKKILVYGATFGGEFED-AKNYGWE--INEkvdFNWKKLLQKKT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 90 AYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEV---NGETI--TADHILIATGGRPSHPDIPGVEYGIDSDGFFALP 164
Cdd:PLN02507 121 DEILRLNGIYKRLLANAGVKLYEGEGKIVGPNEVEVtqlDGTKLryTAKHILIATGSRAQRPNIPGKELAITSDEALSLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 165 ALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADGsLTL 244
Cdd:PLN02507 201 ELPKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPLRGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGG-IKV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 245 ELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSER 324
Cdd:PLN02507 280 ITDHGEEFVADVVLFATGRAPNTKRLNLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDVTNRINLTPVALMEGTCFAKT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 325 LFNNKPDEHlDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVG 404
Cdd:PLN02507 360 VFGGQPTKP-DYENVACAVFCIPPLSVVGLSEEEAVEQAKGD-ILVFTSSFNPMKNTISGRQEKTVMKLIVDAETDKVLG 437
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446082953 405 IHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:PLN02507 438 ASMCGPDAPEIMQGIAVALKCGATKAQFDSTVGIHPSAAEEFVTMR 483
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
22-449 |
1.36e-112 |
|
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: 339.91 E-value: 1.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEAKE---------LGGTCVNVGCVPKKVMWHAAQIREAIH---MYGpdYGFDTTInKFNWETLIASRT 89
Cdd:TIGR01438 20 EAAAYGAKVMLLDFVTptplgtrwgIGGTCVNVGCIPKKLMHQAALLGQALKdsrNYG--WKVEETV-KHDWKRLVEAVQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 90 AYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEVNG-----ETITADHILIATGGRPSHPDIPGV-EYGIDSDGFFAL 163
Cdd:TIGR01438 97 NHIGSLNWGYRVALREKKVKYENAYAEFVDKHRIKATNkkgkeKIYSAERFLIATGERPRYPGIPGAkELCITSDDLFSL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 164 PALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKhAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADGSLT 243
Cdd:TIGR01438 177 PYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRS-ILLRGFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQIEAKVLV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 244 --LELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEK-GYIVVDKYQNTNIEGIYAVGD-NTGAVELTPVAVAAGR 319
Cdd:TIGR01438 256 efTDSTNGIEEEYDTVLLAIGRDACTRKLNLENVGVKINKKtGKIPADEEEQTNVPYIYAVGDiLEDKPELTPVAIQAGR 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 320 RLSERLFNNKpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSSFTAM-YTAVttHRQP---CRMKLVC 395
Cdd:TIGR01438 336 LLAQRLFKGS-TVICDYENVPTTVFTPLEYGACGLSEEKAVEKFGEENVEVFHSYFWPLeWTIP--SRDNhnkCYAKLVC 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446082953 396 VGSE-EKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTM 449
Cdd:TIGR01438 413 NKKEnERVVGFHVVGPNAGEVTQGFAAALRCGLTKKDLDNTIGIHPVCAEVFTTL 467
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
21-450 |
1.46e-108 |
|
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: 329.63 E-value: 1.46e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 21 NRAAMYGQKCALIEAKE---------LGGTCVNVGCVPKKVMWHAAQ----IREAIhmyGPDYGFDTTINKFNWETLIAS 87
Cdd:TIGR01423 21 NAATLYKKRVAVVDVQThhgppfyaaLGGTCVNVGCVPKKLMVTGAQymdtLRESA---GFGWEFDRSSVKANWKALIAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 88 RTAYIDRIHTSYENVLGKNN-VDVIKGFARFVDAKTLEVNG---------ETITADHILIATGGRPSHPDIPGVEYGIDS 157
Cdd:TIGR01423 98 KNKAVLDINKSYEGMFADTEgLTFFLGWGALEDKNVVLVREsadpksavkERLQAEHILLATGSWPQMLGIPGIEHCISS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 158 DGFFALPALPERVAVVGAGYIAVELAGVING---LGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAV 234
Cdd:TIGR01423 178 NEAFYLDEPPRRVLTVGGGFISVEFAGIFNAykpRGGKVTLCYRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 235 VKNADGSLTLELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVA 314
Cdd:TIGR01423 258 TLNADGSKHVTFESGKTLDVDVVMMAIGRVPRTQTLQLDKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTDRVMLTPVA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 315 VAAGRRLSERLFNNKPdEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYgdDQVKVYKSSFTA-MYTAVTTHRQPCRMKL 393
Cdd:TIGR01423 338 INEGAAFVDTVFGNKP-RKTDHTRVASAVFSIPPIGTCGLVEEDAAKKF--EKVAVYESSFTPlMHNISGSKYKKFVAKI 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 446082953 394 VCVGSEEKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEFVTMR 450
Cdd:TIGR01423 415 VTNHADGTVLGVHLLGDSSPEIIQAVGICLKLNAKISDFYNTIGVHPTSAEELCSMR 471
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
5-446 |
2.31e-108 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 329.48 E-value: 2.31e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 5 YDYIAIGGGSGGIASINRAAMYGQKCALIEAKE---------LGGTCVNVGCVPKKVMWHAAQIREAIHMYGPDYGFDTT 75
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKpstqgtkwgLGGTCVNVGCVPKKLMHYAANIGSIFHHDSQMYGWKTS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 76 iNKFNWETLIASRTAYIDRIHTSYENVLGKNNVDVIKGFARFVDAKTLEVNG----ETITADHILIATGGRPSHP-DIPG 150
Cdd:PTZ00052 86 -SSFNWGKLVTTVQNHIRSLNFSYRTGLRSSKVEYINGLAKLKDEHTVSYGDnsqeETITAKYILIATGGRPSIPeDVPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 151 -VEYGIDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKhAPLRSFDPMISETLVEVMNAEGPQLHTNA 229
Cdd:PTZ00052 165 aKEYSITSDDIFSLSKDPGKTLIVGASYIGLETAGFLNELGFDVTVAVRS-IPLRGFDRQCSEKVVEYMKEQGTLFLEGV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 230 IPKAVVKnADGSLTLELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKyQNTNIEGIYAVGD-NTGAV 308
Cdd:PTZ00052 244 VPINIEK-MDDKIKVLFSDGTTELFDTVLYATGRKPDIKGLNLNAIGVHVNKSNKIIAPN-DCTNIPNIFAVGDvVEGRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 309 ELTPVAVAAGRRLSERLFNNKpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSSFTAMYTAvTTHRQP 388
Cdd:PTZ00052 322 ELTPVAIKAGILLARRLFKQS-NEFIDYTFIPTTIFTPIEYGACGYSSEAAIAKYGEDDIEEYLQEFNTLEIA-AVHREK 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446082953 389 ----------------CRMKLVCVGSE-EKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAEEF 446
Cdd:PTZ00052 400 herarkdeydfdvssnCLAKLVCVKSEdNKVVGFHFVGPNAGEITQGFSLALKLGAKKSDFDSMIGIHPTDAEVF 474
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
22-444 |
9.21e-98 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 300.94 E-value: 9.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHMyGPDYGFDTTINKFNWETLIASRTAYIDRIHTS-YE 100
Cdd:PRK06292 21 RAAKLGKKVALIEKGPLGGTCLNVGCIPSKALIAAAEAFHEAKH-AEEFGIHADGPKIDFKKVMARVRRERDRFVGGvVE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 101 NVLGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPshPDIPGVEYG-----IDSDGFFALPALPERVAVVGA 175
Cdd:PRK06292 100 GLEKKPKIDKIKGTARFVDPNTVEVNGERIEAKNIVIATGSRV--PPIPGVWLIlgdrlLTSDDAFELDKLPKSLAVIGG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 176 GYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPqLHTNAIPKAVVKNADGSLTLELEDG--RSET 253
Cdd:PRK06292 178 GVIGLELGQALSRLGVKVTVFERGDRILPLEDPEVSKQAQKILSKEFK-IKLGAKVTSVEKSGDEKVEELEKGGktETIE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 254 VDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDeH 333
Cdd:PRK06292 257 ADYVLVATGRRPNTDGLGLENTGIELDERGRPVVDEHTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAGDVAG-G 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 334 LDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMD 413
Cdd:PRK06292 336 VRYHPIPSVVFTDPQIASVGLTEEELKAAGID--YVVGEVPFEAQGRARVMGKNDGFVKVYADKKTGRLLGAHIIGPDAE 413
|
410 420 430
....*....|....*....|....*....|.
gi 446082953 414 EMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06292 414 HLIHLLAWAMQQGLTVEDLLRMPFYHPTLSE 444
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
22-444 |
2.91e-97 |
|
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: 299.56 E-value: 2.91e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQI-REAIHmyGPDYGFDTTINKFNWETLIASRTAYIDRIHTSYE 100
Cdd:TIGR01350 19 RAAQLGLKVALVEKEYLGGTCLNVGCIPTKALLHSAEVyDEIKH--AKDLGIEVENVSVDWEKMQKRKNKVVKKLVGGVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 101 NVLGKNNVDVIKGFARFVDAKTLEVNGE----TITADHILIATGGRPSHPDIP---GVEYGIDSDGFFALPALPERVAVV 173
Cdd:TIGR01350 97 GLLKKNKVTVIKGEAKFLDPGTVSVTGEngeeTLEAKNIIIATGSRPRSLPGPfdfDGKVVITSTGALNLEEVPESLVII 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 174 GAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNaDGSLTLELEDGRSET 253
Cdd:TIGR01350 177 GGGVIGIEFASIFASLGSKVTVIEMLDRILPGEDAEVSKVLQKALKKKGVKILTNTKVTAVEKN-DDQVTYENKGGETET 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 254 V--DCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFnNKPD 331
Cdd:TIGR01350 256 LtgEKVLVAVGRKPNTEGLGLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDVIGGPMLAHVASHEGIVAAENIA-GKEP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 332 EHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFG 411
Cdd:TIGR01350 335 AHIDYDAVPSVIYTDPEVASVGLTEEQAKEAGYD--VKIGKFPFAANGKALALGETDGFVKIIADKKTGEILGAHIIGPH 412
|
410 420 430
....*....|....*....|....*....|...
gi 446082953 412 MDEMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:TIGR01350 413 ATELISEAALAMELEGTVEELARTIHPHPTLSE 445
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
22-444 |
1.95e-95 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 295.13 E-value: 1.95e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQI-REAIHMygPDYGFDTTINKFNWETLIASRTAYIDRIHTSYE 100
Cdd:PRK06416 22 RAAQLGLKVAIVEKEKLGGTCLNRGCIPSKALLHAAERaDEARHS--EDFGIKAENVGIDFKKVQEWKNGVVNRLTGGVE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 101 NVLGKNNVDVIKGFARFVDAKTLEVN----GETITADHILIATGGRPShpDIPGVEYG----IDSDGFFALPALPERVAV 172
Cdd:PRK06416 100 GLLKKNKVDIIRGEAKLVDPNTVRVMtedgEQTYTAKNIILATGSRPR--ELPGIEIDgrviWTSDEALNLDEVPKSLVV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 173 VGAGYIAVELAGVINGLGAKT-------HLfvrkhapLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADGsLTLE 245
Cdd:PRK06416 178 IGGGYIGVEFASAYASLGAEVtivealpRI-------LPGEDKEISKLAERALKKRGIKIKTGAKAKKVEQTDDG-VTVT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 246 LEDGRSE---TVDCLIWAIGREPANDNINLEAAGVKTnEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLS 322
Cdd:PRK06416 250 LEDGGKEetlEADYVLVAVGRRPNTENLGLEELGVKT-DRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKASAEGIIAA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 323 ERLFNNkpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKI 402
Cdd:PRK06416 329 EAIAGN--PHPIDYRGIPAVTYTHPEVASVGLTEAKAKEEGFD--VKVVKFPFAGNGKALALGETDGFVKLIFDKKDGEV 404
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446082953 403 VGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06416 405 LGAHMVGARASELIQEAQLAINWEATPEDLALTIHPHPTLSE 446
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
22-444 |
2.53e-95 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 294.80 E-value: 2.53e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQireAIHM--YGPDYGFDTTIN-KFNWETLIASRTAYIDRIHTS 98
Cdd:PRK06370 23 RAAGLGMKVALIERGLLGGTCVNTGCVPTKTLIASAR---AAHLarRAAEYGVSVGGPvSVDFKAVMARKRRIRARSRHG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 99 YENVL-GKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPDIPGVE---YgIDSDGFFALPALPERVAVVG 174
Cdd:PRK06370 100 SEQWLrGLEGVDVFRGHARFESPNTVRVGGETLRAKRIFINTGARAAIPPIPGLDevgY-LTNETIFSLDELPEHLVIIG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 175 AGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADG-SLTLELEDGRSE- 252
Cdd:PRK06370 179 GGYIGLEFAQMFRRFGSEVTVIERGPRLLPREDEDVAAAVREILEREGIDVRLNAECIRVERDGDGiAVGLDCNGGAPEi 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 253 TVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPdE 332
Cdd:PRK06370 259 TGSHILVAVGRVPNTDDLGLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCNGRGAFTHTAYNDARIVAANLLDGGR-R 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 333 HLDYSNIPTVVFSHPPIGTVGLTEPQAReQYGDDqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGM 412
Cdd:PRK06370 338 KVSDRIVPYATYTDPPLARVGMTEAEAR-KSGRR-VLVGTRPMTRVGRAVEKGETQGFMKVVVDADTDRILGATILGVHG 415
|
410 420 430
....*....|....*....|....*....|..
gi 446082953 413 DEMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06370 416 DEMIHEILDAMYAGAPYTTLSRAIHIHPTVSE 447
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
22-444 |
5.73e-87 |
|
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: 273.14 E-value: 5.73e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHmyGPDYGFDTTINKFNWETLIASRTAYIDRI-HTSYE 100
Cdd:TIGR02053 18 KAAELGASVAMVERGPLGGTCVNVGCVPSKMLLRAAEVAHYAR--KPPFGGLAATVAVDFGELLEGKREVVEELrHEKYE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 101 NVLGKNNVDVIKGFARFVDAKTLEVNGETIT--ADHILIATGGRPSHPDIPG---VEYgIDSDGFFALPALPERVAVVGA 175
Cdd:TIGR02053 96 DVLSSYGVDYLRGRARFKDPKTVKVDLGREVrgAKRFLIATGARPAIPPIPGlkeAGY-LTSEEALALDRIPESLAVIGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 176 GYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADGSL-TLELEDGRSET- 253
Cdd:TIGR02053 175 GAIGVELAQAFARLGSEVTILQRSDRLLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIiTVEKPGGQGEVe 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 254 VDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNkPDEH 333
Cdd:TIGR02053 255 ADELLVATGRRPNTDGLGLEKAGVKLDERGGILVDETLRTSNPGIYAAGDVTGGLQLEYVAAKEGVVAAENALGG-ANAK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 334 LDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSSFTAmytAVTTHRQPCRM-KLVCVGSEEKIVGIHGIGFGM 412
Cdd:TIGR02053 334 LDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVP---RARINRDTRGFiKLVAEPGTGKVLGVQVVAPEA 410
|
410 420 430
....*....|....*....|....*....|..
gi 446082953 413 DEMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:TIGR02053 411 AEVINEAALAIRAGMTVDDLIDTLHPFPTMAE 442
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
27-444 |
4.59e-78 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 249.87 E-value: 4.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 27 GQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHmYGPDYGFDTTINKFNWETlIASRT-AYIDRIHTSYEN--VL 103
Cdd:PRK07846 22 DKRIAIVEKGTFGGTCLNVGCIPTKMFVYAADVARTIR-EAARLGVDAELDGVRWPD-IVSRVfGRIDPIAAGGEEyrGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 104 GKNNVDVIKGFARFVDAKTLEV-NGETITADHILIATGGRPSHPDIP---GVEYGIdSDGFFALPALPERVAVVGAGYIA 179
Cdd:PRK07846 100 DTPNIDVYRGHARFIGPKTLRTgDGEEITADQVVIAAGSRPVIPPVIadsGVRYHT-SDTIMRLPELPESLVIVGGGFIA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 180 VELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAE-GPQLHTNAIPkavVKNADGSLTLELEDGRSETVDCLI 258
Cdd:PRK07846 179 AEFAHVFSALGVRVTVVNRSGRLLRHLDDDISERFTELASKRwDVRLGRNVVG---VSQDGSGVTLRLDDGSTVEADVLL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 259 WAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYSN 338
Cdd:PRK07846 256 VATGRVPNGDLLDAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQLKHVANHEARVVQHNLLHPDDLIASDHRF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 339 IPTVVFSHPPIGTVGLTEPQAREQYGDDQVKVYKSSFTAMYTAV--TTHrqpcRMKLVCVGSEEKIVGIHGIGFGMDEML 416
Cdd:PRK07846 336 VPAAVFTHPQIASVGLTENEARAAGLDITVKVQNYGDVAYGWAMedTTG----FVKLIADRDTGRLLGAHIIGPQASTLI 411
|
410 420
....*....|....*....|....*....
gi 446082953 417 QGFAVALKMGATKKDF-DNTVAIHPTAAE 444
Cdd:PRK07846 412 QPLIQAMSFGLDAREMaRGQYWIHPALPE 440
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
22-318 |
5.10e-76 |
|
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: 239.53 E-value: 5.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEakeLGGTCVNVGCVPKKVMWHAAQIREAIHmygpdygfdttinkfNWETLIASRTAYIDRIHTSYEN 101
Cdd:pfam07992 18 TLAQLGGKVTLIE---DEGTCPYGGCVLSKALLGAAEAPEIAS---------------LWADLYKRKEEVVKKLNNGIEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 102 VLGKNNVDVIKGFARFVDAKTLEVNGETITADHILIATGGRPSHPDIPGVEYG-------IDSDGFFALPALPERVAVVG 174
Cdd:pfam07992 80 LLGTEVVSIDPGAKKVVLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNvgflvrtLDSAEALRLKLLPKRVVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 175 AGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADGsLTLELEDGRSETV 254
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIEALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDG-VEVILKDGTEIDA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446082953 255 DCLIWAIGREPANDniNLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNT-GAVELTPVAVAAG 318
Cdd:pfam07992 239 DLVVVAIGRRPNTE--LLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRvGGPELAQNAVAQG 301
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
22-362 |
1.94e-71 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 235.43 E-value: 1.94e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQI----REAihmygP-DYGFDTTINKFNWETLIASRTAYIDRI- 95
Cdd:PRK13748 116 KAVEQGARVTLIERGTIGGTCVNVGCVPSKIMIRAAHIahlrRES-----PfDGGIAATVPTIDRSRLLAQQQARVDELr 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 96 HTSYENVLGKN-NVDVIKGFARFVDAKTLEV----NGE-TITADHILIATGGRPSHPDIPGVE---YGIDSDGFFAlPAL 166
Cdd:PRK13748 191 HAKYEGILDGNpAITVLHGEARFKDDQTLIVrlndGGErVVAFDRCLIATGASPAVPPIPGLKetpYWTSTEALVS-DTI 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 167 PERVAVVGAGYIAVELAGVINGLGAKTHLFVRkHAPLRSFDPMISETLVEVMNAEGPQL--HTNAipkAVVKNADGSLTL 244
Cdd:PRK13748 270 PERLAVIGSSVVALELAQAFARLGSKVTILAR-STLFFREDPAIGEAVTAAFRAEGIEVleHTQA---SQVAHVDGEFVL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 245 ELEDGrSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSER 324
Cdd:PRK13748 346 TTGHG-ELRADKLLVATGRAPNTRSLALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAAIN 424
|
330 340 350
....*....|....*....|....*....|....*...
gi 446082953 325 LFNNkpDEHLDYSNIPTVVFSHPPIGTVGLTEPQAREQ 362
Cdd:PRK13748 425 MTGG--DAALDLTAMPAVVFTDPQVATVGYSEAEAHHD 460
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
22-444 |
1.63e-67 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 222.88 E-value: 1.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAMYGQKCALIEA-------KELGGTCVNVGCVPKKVMWHAAQIREAIHMYGPDYGFDTTINKFNWETLIASRTAYIDR 94
Cdd:PRK06327 22 RAAQLGLKVACIEAwknpkgkPALGGTCLNVGCIPSKALLASSEEFENAGHHFADHGIHVDGVKIDVAKMIARKDKVVKK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 95 IHTSYENVLGKNNVDVIKGFARFVDAKT----LEVNGE---TITADHILIATGGRPSHpdIPGVEYG----IDSDGFFAL 163
Cdd:PRK06327 102 MTGGIEGLFKKNKITVLKGRGSFVGKTDagyeIKVTGEdetVITAKHVIIATGSEPRH--LPGVPFDnkiiLDNTGALNF 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 164 PALPERVAVVGAGYIAVELAGVINGLGAktHLFVRKHAP--LRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADG- 240
Cdd:PRK06327 180 TEVPKKLAVIGAGVIGLELGSVWRRLGA--EVTILEALPafLAAADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGv 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 241 SLTLELEDGRSET--VDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAG 318
Cdd:PRK06327 258 SVAYTDADGEAQTleVDKLIVSIGRVPNTDGLGLEAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGPMLAHKAEEEG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 319 RRLSERLFNNKPdeHLDYSNIPTVVFSHPPIGTVGLTEPQAREQygDDQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGS 398
Cdd:PRK06327 338 VAVAERIAGQKG--HIDYNTIPWVIYTSPEIAWVGKTEQQLKAE--GVEYKAGKFPFMANGRALAMGEPDGFVKIIADAK 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446082953 399 EEKIVGIHGIGFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK06327 414 TDEILGVHVIGPNASELIAEAVVAMEFKASSEDIARICHAHPTLSE 459
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
22-444 |
1.00e-62 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 210.01 E-value: 1.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 22 RAAM----YGQKCALIEAKE-LGGTCVNVGCVPKKVMWHAA----QIREAiHMYGpDYGFdttINKFNWETLIASRTAYI 92
Cdd:PRK05249 19 GAAMqaakLGKRVAVIERYRnVGGGCTHTGTIPSKALREAVlrliGFNQN-PLYS-SYRV---KLRITFADLLARADHVI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 93 DRIHTSYENVLGKNNVDVIKGFARFVDAKTLEVNG-----ETITADHILIATGGRPSHPdiPGVEYG----IDSDGFFAL 163
Cdd:PRK05249 94 NKQVEVRRGQYERNRVDLIQGRARFVDPHTVEVECpdgevETLTADKIVIATGSRPYRP--PDVDFDhpriYDSDSILSL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 164 PALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLrSF-DPMISETLVEVMNAEGPQLHTNAIPKAVVKNADGSL 242
Cdd:PRK05249 172 DHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLL-SFlDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDGVI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 243 TlELEDGRSETVDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLS 322
Cdd:PRK05249 251 V-HLKSGKKIKADCLLYANGRTGNTDGLNLENAGLEADSRGQLKVNENYQTAVPHIYAVGDVIGFPSLASASMDQGRIAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 323 ERLFNNkPDEHLdYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKI 402
Cdd:PRK05249 330 QHAVGE-ATAHL-IEDIPTGIYTIPEISSVGKTEQELTAAKVP--YEVGRARFKELARAQIAGDNVGMLKILFHRETLEI 405
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 446082953 403 VGIHGIGFGMDEMLQ-GFAVaLKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK05249 406 LGVHCFGERATEIIHiGQAI-MEQKGTIEYFVNTTFNYPTMAE 447
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
27-446 |
2.57e-62 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 208.45 E-value: 2.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 27 GQKCALIEAKEL--GGTCVNVGCVPKKVMWHAAQireaihmygpdygfdttiNKFNWETLIASRTAYIDRIHTSYENVLG 104
Cdd:PRK07251 26 GKKVALVEESKAmyGGTCINIGCIPTKTLLVAAE------------------KNLSFEQVMATKNTVTSRLRGKNYAMLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 105 KNNVDVIKGFARFVDAKTLEVNG----ETITADHILIATGGRPSHPDIPGV---EYGIDSDGFFALPALPERVAVVGAGY 177
Cdd:PRK07251 88 GSGVDLYDAEAHFVSNKVIEVQAgdekIELTAETIVINTGAVSNVLPIPGLadsKHVYDSTGIQSLETLPERLGIIGGGN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 178 IAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVvKNADGSLTLELEDGrSETVDCL 257
Cdd:PRK07251 168 IGLEFAGLYNKLGSKVTVLDAASTILPREEPSVAALAKQYMEEDGITFLLNAHTTEV-KNDGDQVLVVTEDE-TYRFDAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 258 IWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEHLDYS 337
Cdd:PRK07251 246 LYATGRKPNTEPLGLENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGPQFTYISLDDFRIVFGYLTGDGSYTLEDRG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 338 NIPTVVFSHPPIGTVGLTEPQAREQYGddQVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMDEMLQ 417
Cdd:PRK07251 326 NVPTTMFITPPLSQVGLTEKEAKEAGL--PYAVKELLVAAMPRAHVNNDLRGAFKVVVNTETKEILGATLFGEGSQEIIN 403
|
410 420
....*....|....*....|....*....
gi 446082953 418 GFAVALKMGATKKDFDNTVAIHPTAAEEF 446
Cdd:PRK07251 404 LITMAMDNKIPYTYFKKQIFTHPTMAENL 432
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
24-444 |
5.46e-52 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 180.98 E-value: 5.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 24 AMYGQKCALIE--AKELGGTCVNVGCVPKKVMWHAAQiREAihmygpdygfdttinkfNWETLIASRTAYIDRIHT-SYE 100
Cdd:PRK08010 23 AKAGWRVALIEqsNAMYGGTCINIGCIPTKTLVHDAQ-QHT-----------------DFVRAIQRKNEVVNFLRNkNFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 101 NVLGKNNVDVIKGFARFVDAKTLEV---NGE-TITADHILIATGGRPSHPDIPGVEY--GI-DSDGFFALPALPERVAVV 173
Cdd:PRK08010 85 NLADMPNIDVIDGQAEFINNHSLRVhrpEGNlEIHGEKIFINTGAQTVVPPIPGITTtpGVyDSTGLLNLKELPGHLGIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 174 GAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVvKNADGSLTLELEDGrSET 253
Cdd:PRK08010 165 GGGYIGVEFASMFANFGSKVTILEAASLFLPREDRDIADNIATILRDQGVDIILNAHVERI-SHHENQVQVHSEHA-QLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 254 VDCLIWAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEH 333
Cdd:PRK08010 243 VDALLIASGRQPATASLHPENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQFTYISLDDYRIVRDELLGEGKRST 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 334 LDYSNIPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMD 413
Cdd:PRK08010 323 DDRKNVPYSVFMTPPLSRVGMTEEQARESGAD--IQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASLLCVDSH 400
|
410 420 430
....*....|....*....|....*....|.
gi 446082953 414 EMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PRK08010 401 EMINIVKMVMDAGLPYSILRDQIFTHPSMSE 431
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
339-449 |
1.72e-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: 1.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 339 IPTVVFSHPPIGTVGLTEPQAREQYGDdqVKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMDEMLQG 418
Cdd:pfam02852 1 IPSVVFTDPEIASVGLTEEEAKEKGGE--VKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVGPNAGELIQE 78
|
90 100 110
....*....|....*....|....*....|.
gi 446082953 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 |
1.66e-35 |
|
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: 133.78 E-value: 1.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 119 DAKTLEV-NGETITADHILIATGGRPSHPDIPGveygIDSDGFFAL------PAL--------PERVAVVGAGYIAVELA 183
Cdd:COG0446 65 EAKTVTLrDGETLSYDKLVLATGARPRPPPIPG----LDLPGVFTLrtlddaDALrealkefkGKRAVVIGGGPIGLELA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 184 GVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVvkNADGSLTLELEDGRSETVDCLIWAIGR 263
Cdd:COG0446 141 EALRKRGLKVTLVERAPRLLGVLDPEMAALLEEELREHGVELRLGETVVAI--DGDDKVAVTLTDGEEIPADLVVVAPGV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446082953 264 EPandNINL-EAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGA----------VELTPVAVAAGRRLSERLFNNKP 330
Cdd:COG0446 219 RP---NTELaKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEVphpvtgktvyIPLASAANKQGRVAAENILGGPA 293
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
23-361 |
4.69e-32 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 127.28 E-value: 4.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 23 AAMYGQKCALIEAKELGGTCVNVGCVPKKVMWHAAQIREAIHmYGPDYGfdttINKFNWETLIASRTAYIDR-------- 94
Cdd:PRK07845 20 AAQLGADVTVIERDGLGGAAVLTDCVPSKTLIATAEVRTELR-RAAELG----IRFIDDGEARVDLPAVNARvkalaaaq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 95 ---IHTSyenvLGKNNVDVIKGFARFVDAK----TLEVNG-----ETITADHILIATGGRPShpDIPGVEygidSDG--- 159
Cdd:PRK07845 95 sadIRAR----LEREGVRVIAGRGRLIDPGlgphRVKVTTadggeETLDADVVLIATGASPR--ILPTAE----PDGeri 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 160 -----FFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAV 234
Cdd:PRK07845 165 ltwrqLYDLDELPEHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGEDADAAEVLEEVFARRGMTVLKRSRAESV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 235 VKNADGsLTLELEDGRseTVD---CLIwAIGREPANDNINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELT 311
Cdd:PRK07845 245 ERTGDG-VVVTLTDGR--TVEgshALM-AVGSVPNTAGLGLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDCTGVLPLA 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 446082953 312 PVAVAAGR-----RLSERLfnnKPdehLDYSNIPTVVFSHPPIGTVGLTEPQARE 361
Cdd:PRK07845 321 SVAAMQGRiamyhALGEAV---SP---LRLKTVASNVFTRPEIATVGVSQAAIDS 369
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
23-444 |
1.63e-30 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 124.64 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 23 AAMYGQKCALIEAKE--LGGTCVNVGCVPKKVMWHAA----QIREAIHMYGpdYGFDTTINKFNWETLIASRT------- 89
Cdd:PTZ00153 135 AMERGLKVIIFTGDDdsIGGTCVNVGCIPSKALLYATgkyrELKNLAKLYT--YGIYTNAFKNGKNDPVERNQlvadtvq 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 90 -----------AYIDRIHTSYENVLGKN-------NVDVIKGFARFVDAKTL--EVNGETITADHILIATGGRPSHPDip 149
Cdd:PTZ00153 213 iditklkeytqSVIDKLRGGIENGLKSKkfcknseHVQVIYERGHIVDKNTIksEKSGKEFKVKNIIIATGSTPNIPD-- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 150 GVEYG----IDSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGP-Q 224
Cdd:PTZ00153 291 NIEVDqksvFTSDTAVKLEGLQNYMGIVGMGIIGLEFMDIYTALGSEVVSFEYSPQLLPLLDADVAKYFERVFLKSKPvR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 225 LHTNAIPKAV-----------------VKNADGSLTLELEDGRSETVDCLIwAIGREPANDNINLEAAGVKTNeKGYIVV 287
Cdd:PTZ00153 371 VHLNTLIEYVragkgnqpviighserqTGESDGPKKNMNDIKETYVDSCLV-ATGRKPNTNNLGLDKLKIQMK-RGFVSV 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 288 D------KYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERLFNNKPDEH-----------LDYSNIPTVVFSHPPIG 350
Cdd:PTZ00153 449 DehlrvlREDQEVYDNIFCIGDANGKQMLAHTASHQALKVVDWIEGKGKENVninvenwaskpIIYKNIPSVCYTTPELA 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 351 TVGLTEPQAREQYGDDQVKVYKSSFTAMYTAVTTHRQPCR----------------------MKLVCVGSEEKIVGIHGI 408
Cdd:PTZ00153 529 FIGLTEKEAKELYPPDNVGVEISFYKANSKVLCENNISFPnnsknnsynkgkyntvdntegmVKIVYLKDTKEILGMFIV 608
|
490 500 510
....*....|....*....|....*....|....*.
gi 446082953 409 GFGMDEMLQGFAVALKMGATKKDFDNTVAIHPTAAE 444
Cdd:PTZ00153 609 GSYASILIHEGVLAINLKLSVKDLAHMVHSHPTISE 644
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
56-372 |
8.80e-30 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 119.86 E-value: 8.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 56 AAQIREAihmygpdyGFDTTInkfnweTLIA--SRTAYiDRIHTSY---------------ENVLGKNNVDVIKGfARFV 118
Cdd:COG1251 17 AEELRKL--------DPDGEI------TVIGaePHPPY-NRPPLSKvlagetdeedlllrpADFYEENGIDLRLG-TRVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 119 ----DAKTLEV-NGETITADHILIATGGRPSHPDIPGVeygiDSDGFFAL----------PALPE--RVAVVGAGYIAVE 181
Cdd:COG1251 81 aidrAARTVTLaDGETLPYDKLVLATGSRPRVPPIPGA----DLPGVFTLrtlddadalrAALAPgkRVVVIGGGLIGLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 182 LAGVINGLGAKTHLFVRKHAPL-RSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNaDGSLTLELEDGRSETVDCLIWA 260
Cdd:COG1251 157 AAAALRKRGLEVTVVERAPRLLpRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGD-DRVTGVRLADGEELPADLVVVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 261 IGREPandNINL-EAAGVKTNeKGyIVVDKYQNTNIEGIYAVGD---------NTGAVELTPVAVAAGRRLSERLfNNKP 330
Cdd:COG1251 236 IGVRP---NTELaRAAGLAVD-RG-IVVDDYLRTSDPDIYAAGDcaehpgpvyGRRVLELVAPAYEQARVAAANL-AGGP 309
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446082953 331 DEHLDYSNIPTVVFSHPPIGTVGLTEPQARE-QYGDDQVKVYK 372
Cdd:COG1251 310 AAYEGSVPSTKLKVFGVDVASAGDAEGDEEVvVRGDPARGVYK 352
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
23-318 |
4.75e-27 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 110.21 E-value: 4.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 23 AAMYGQKCALIEAKELGG-----TCV-NVGCVPKKVMwhaaqireaihmyGPDYG---------FDTTInkfnwetlias 87
Cdd:COG0492 19 AARAGLKTLVIEGGEPGGqlattKEIeNYPGFPEGIS-------------GPELAerlreqaerFGAEI----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 88 rtayidrihtSYENVLGknnVDVIKgfarfvDAKTLEV-NGETITADHILIATGGRPSHPDIP--------GVEYGIDSD 158
Cdd:COG0492 75 ----------LLEEVTS---VDKDD------GPFRVTTdDGTEYEAKAVIIATGAGPRKLGLPgeeefegrGVSYCATCD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 159 GFFalpaLP-ERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHaplrsfDPMISETLVE-VMNAEGPQLHTNAIPKAVvk 236
Cdd:COG0492 136 GFF----FRgKDVVVVGGGDSALEEALYLTKFASKVTLIHRRD------ELRASKILVErLRANPKIEVLWNTEVTEI-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 237 NADGSLT-LELEDGRSET-----VDCLIWAIGREPANDNinLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGD-NTGAVE 309
Cdd:COG0492 204 EGDGRVEgVTLKNVKTGEekeleVDGVFVAIGLKPNTEL--LKGLGLELDEDGYIVVDEDMETSVPGVFAAGDvRDYKYR 281
|
....*....
gi 446082953 310 LtpVAVAAG 318
Cdd:COG0492 282 Q--AATAAG 288
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
93-343 |
6.30e-25 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 105.60 E-value: 6.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 93 DRIHTSYENVLGKNNVDVIKGFARFVD--AKTLEV-NGETITADHILIATGGRPSHPDIPGVE---YGIDS--------- 157
Cdd:COG1252 56 DDIAIPLRELLRRAGVRFIQGEVTGIDpeARTVTLaDGRTLSYDYLVIATGSVTNFFGIPGLAehaLPLKTledalalre 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 158 --DGFFALPALPE--RVAVVGAGYIAVELAGVINGLGAKTHLFVRKHA-------------PLRSFDPMISETLVEVMNA 220
Cdd:COG1252 136 rlLAAFERAERRRllTIVVVGGGPTGVELAGELAELLRKLLRYPGIDPdkvritlveagprILPGLGEKLSEAAEKELEK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 221 EGPQLHTNAIPKAVVKNadgslTLELEDGRSETVDCLIWAIGREPANDninLEAAGVKTNEKGYIVVDKY-QNTNIEGIY 299
Cdd:COG1252 216 RGVEVHTGTRVTEVDAD-----GVTLEDGEEIPADTVIWAAGVKAPPL---LADLGLPTDRRGRVLVDPTlQVPGHPNVF 287
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446082953 300 AVGDnTGAVE------LTPVAVAA---GRRLSE---RLFNNKPDEHLDYSNIPTVV 343
Cdd:COG1252 288 AIGD-CAAVPdpdgkpVPKTAQAAvqqAKVLAKniaALLRGKPLKPFRYRDKGCLA 342
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
127-320 |
1.69e-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: 93.28 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 127 GETITA-------DHILIATG-GRPSHPDIPG-----VEYGID-------SDGFFALPALPERVAVVGAGYIAVELAGVI 186
Cdd:COG0493 195 GKDITLdelleefDAVFLATGaGKPRDLGIPGedlkgVHSAMDfltavnlGEAPDTILAVGKRVVVIGGGNTAMDCARTA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 187 NGLGAKT-HLFVRkhaplRSFDPMiSETLVEVMNA--EGPQLHTNAIPKAVVKNADGSLT------LEL----EDGR--- 250
Cdd:COG0493 275 LRLGAESvTIVYR-----RTREEM-PASKEEVEEAleEGVEFLFLVAPVEIIGDENGRVTglecvrMELgepdESGRrrp 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 251 -----SETV---DCLIWAIGREPaNDNINLEAAGVKTNEKGYIVVDK-YQNTNIEGIYAVGDN-TGA---VEltpvAVAA 317
Cdd:COG0493 349 vpiegSEFTlpaDLVILAIGQTP-DPSGLEEELGLELDKRGTIVVDEeTYQTSLPGVFAGGDAvRGPslvVW----AIAE 423
|
...
gi 446082953 318 GRR 320
Cdd:COG0493 424 GRK 426
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
131-304 |
4.24e-20 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 92.03 E-value: 4.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 131 TADHILIATGGRPSHPDIPGveygIDSDGFFALPALPE--------------RVAVVGAGYIAVELAGVINGLGAKTHLF 196
Cdd:PRK09564 103 TYDKLMIATGARPIIPPIKN----INLENVYTLKSMEDglalkellkdeeikNIVIIGAGFIGLEAVEAAKHLGKNVRII 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 197 VR-KHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNaDGSLTLELEDGRSETvDCLIWAIGREPANDNinLEAA 275
Cdd:PRK09564 179 QLeDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGE-DKVEGVVTDKGEYEA-DVVIVATGVKPNTEF--LEDT 254
|
170 180
....*....|....*....|....*....
gi 446082953 276 GVKTNEKGYIVVDKYQNTNIEGIYAVGDN 304
Cdd:PRK09564 255 GLKTLKNGAIIVDEYGETSIENIYAAGDC 283
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
169-249 |
1.09e-19 |
|
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: 83.02 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 169 RVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNADGSlTLELED 248
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV-VVVLTD 79
|
.
gi 446082953 249 G 249
Cdd:pfam00070 80 G 80
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
118-303 |
1.00e-15 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 78.42 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 118 VDAKTLEVNGETITADHILIATGGRPSHPDIPGVEYGIdsdgffALPALPE------------RVAVVGAGYIAVELAGV 185
Cdd:PRK04965 86 AEAQVVKSQGNQWQYDKLVLATGASAFVPPIPGRELML------TLNSQQEyraaetqlrdaqRVLVVGGGLIGTELAMD 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 186 INGLGAKTHLFVRKHAPLRSFDP-MISETLVEVMNAEGPQLHTNAIPKAVVKNADGsLTLELEDGRSETVDCLIWAIGRE 264
Cdd:PRK04965 160 LCRAGKAVTLVDNAASLLASLMPpEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG-IRATLDSGRSIEVDAVIAAAGLR 238
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446082953 265 PandNINL-EAAGVKTNeKGyIVVDKYQNTNIEGIYAVGD 303
Cdd:PRK04965 239 P---NTALaRRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
127-320 |
2.26e-15 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 77.91 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 127 GETITA-------DHILIATG-GRPSHPDIPG-----VEYGID-------SDGFFALPAlPERVAVVGAGYIAVELAGVI 186
Cdd:PRK11749 214 GRDITLdelragyDAVFIGTGaGLPRFLGIPGenlggVYSAVDfltrvnqAVADYDLPV-GKRVVVIGGGNTAMDAARTA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 187 NGLGAK-THLFVRkhaplRSFDPMiSETLVEVMNA--EGPQLHTNAIPKAVVKNADGSLTLELE---------DGR---- 250
Cdd:PRK11749 293 KRLGAEsVTIVYR-----RGREEM-PASEEEVEHAkeEGVEFEWLAAPVEILGDEGRVTGVEFVrmelgepdaSGRrrvp 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446082953 251 ---SE---TVDCLIWAIGREPaNDNINLEAAGVKTNEKGYIVVD-KYQNTNIEGIYAVGDNTGAVELTPVAVAAGRR 320
Cdd:PRK11749 367 iegSEftlPADLVIKAIGQTP-NPLILSTTPGLELNRWGTIIADdETGRTSLPGVFAGGDIVTGAATVVWAVGDGKD 442
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
99-302 |
3.20e-14 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 73.03 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 99 YENVLGKNNVDV-----IKGFARFVDAKTLEVNGETITADHILIATG--GRPSHPDIP--GVEYGIDSDG--FFAlpalp 167
Cdd:pfam13738 81 LRRVADHFELPInlfeeVTSVKKEDDGFVVTTSKGTYQARYVIIATGefDFPNKLGVPelPKHYSYVKDFhpYAG----- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 168 ERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHA-------PLRSFDPMISETLVEVMNAEGPQLHTNAIPKAvVKNADG 240
Cdd:pfam13738 156 QKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEwedrdsdPSYSLSPDTLNRLEELVKNGKIKAHFNAEVKE-ITEVDV 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446082953 241 SLTLELEDGRSETVDC-LIWAIGREPandNIN-LEAAGVKTNEKGYIVVDK-YQNTNIEGIYAVG 302
Cdd:pfam13738 235 SYKVHTEDGRKVTSNDdPILATGYHP---DLSfLKKGLFELDEDGRPVLTEeTESTNVPGLFLAG 296
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
127-303 |
2.51e-12 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 69.09 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 127 GETITADHILIATGGRPSHPDIPGVE----YGI----DSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHlfVR 198
Cdd:TIGR02374 92 GRTLSYDKLILATGSYPFILPIPGADkkgvYVFrtieDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVS--VI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 199 KHAPL---RSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKnADGSLTLELEDGRSETVDCLIWAIGREPandNINL-EA 274
Cdd:TIGR02374 170 HHAPGlmaKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVG-ATKADRIRFKDGSSLEADLIVMAAGIRP---NDELaVS 245
|
170 180
....*....|....*....|....*....
gi 446082953 275 AGVKTNekGYIVVDKYQNTNIEGIYAVGD 303
Cdd:TIGR02374 246 AGIKVN--RGIIVNDSMQTSDPDIYAVGE 272
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
168-303 |
8.72e-12 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 66.73 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 168 ERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPKAVVKNadgslTLELE 247
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEIDAINGN-----EVTFK 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446082953 248 DGRSETVDCLIWAIGREPANDNInlEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGD 303
Cdd:PRK13512 224 SGKVEHYDMIIEGVGTHPNSKFI--ESSNIKLDDKGFIPVNDKFETNVPNIYAIGD 277
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
133-325 |
1.14e-11 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 65.78 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 133 DHILIATGG-RPSHPDIPG------------------VEYG-IDSDGFFalPALPERVAVVGAGYIAVELAGVINGLGAK 192
Cdd:PRK12770 120 DAVLIATGTwKSRKLGIPGedlpgvysaleylfriraAKLGyLPWEKVP--PVEGKKVVVVGAGLTAVDAALEAVLLGAE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 193 --THLFVR--KHAPLRSFDpmisetlVEVMNAEGPQLHTNAIPKAV--------VKNADGSLTLELEDGRSETV------ 254
Cdd:PRK12770 198 kvYLAYRRtiNEAPAGKYE-------IERLIARGVEFLELVTPVRIigegrvegVELAKMRLGEPDESGRPRPVpipgse 270
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446082953 255 -----DCLIWAIGREPANDnINLEAAGVKTNEKGYIVVDKYQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSERL 325
Cdd:PRK12770 271 fvleaDTVVFAIGEIPTPP-FAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSI 345
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
118-320 |
1.32e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 63.11 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 118 VDAKTLEVNGETITADHIL---------IATG-GRPSHPDIPGveygIDSDGFFA--------------LP------ALP 167
Cdd:PRK12831 206 VKIETNVVVGKTVTIDELLeeegfdavfIGSGaGLPKFMGIPG----ENLNGVFSanefltrvnlmkayKPeydtpiKVG 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 168 ERVAVVGAGYIAVELAGVINGLGAKTHLFVRkhaplRSFDPMISEtLVEVMNA--EGPQLHTNAIPKAVVKNADGSLT-- 243
Cdd:PRK12831 282 KKVAVVGGGNVAMDAARTALRLGAEVHIVYR-----RSEEELPAR-VEEVHHAkeEGVIFDLLTNPVEILGDENGWVKgm 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 244 ----LELED----GR--------SE---TVDCLIWAIGREPaNDNINLEAAGVKTNEKGYIVVDKYQN-TNIEGIYAVGD 303
Cdd:PRK12831 356 kcikMELGEpdasGRrrpveiegSEfvlEVDTVIMSLGTSP-NPLISSTTKGLKINKRGCIVADEETGlTSKEGVFAGGD 434
|
250
....*....|....*...
gi 446082953 304 N-TGAVELTpVAVAAGRR 320
Cdd:PRK12831 435 AvTGAATVI-LAMGAGKK 451
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
88-303 |
3.07e-10 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 62.44 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 88 RTAYiDRIH-TSY-------------ENVLGKNNVDVIKGFARFV---DAKTLEVN-GETITADHILIATGGRPSHPDIP 149
Cdd:PRK14989 41 RIAY-DRVHlSSYfshhtaeelslvrEGFYEKHGIKVLVGERAITinrQEKVIHSSaGRTVFYDKLIMATGSYPWIPPIK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 150 GVE------YGI--DSDGFFALPALPERVAVVGAGYIAVELAGVINGLGAKTHlfVRKHAPL---RSFDPMISETLVEVM 218
Cdd:PRK14989 120 GSEtqdcfvYRTieDLNAIEACARRSKRGAVVGGGLLGLEAAGALKNLGVETH--VIEFAPMlmaEQLDQMGGEQLRRKI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 219 NAEGPQLHTNAIPKAVVKNA-DGSLTLELEDGRSETVDCLIWAIGREPaNDNINLEaAGVKTNEKGYIVVDKYQNTNIEG 297
Cdd:PRK14989 198 ESMGVRVHTSKNTLEIVQEGvEARKTMRFADGSELEVDFIVFSTGIRP-QDKLATQ-CGLAVAPRGGIVINDSCQTSDPD 275
|
....*.
gi 446082953 298 IYAVGD 303
Cdd:PRK14989 276 IYAIGE 281
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
147-330 |
8.16e-10 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 60.90 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 147 DIPGVEYGID-----SDGffALPALPERVAVVGAGYIAVELAGVINGLGAK--THLFVRKHAPLRSFDPMISETLvevmn 219
Cdd:PRK12814 300 ELPGVISGIDflrnvALG--TALHPGKKVVVIGGGNTAIDAARTALRLGAEsvTILYRRTREEMPANRAEIEEAL----- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 220 AEGPQLHTNAIPKAVVKNADGsltLEL-----------EDGRSETV-----------DCLIWAIGREPanDNINLEAAGV 277
Cdd:PRK12814 373 AEGVSLRELAAPVSIERSEGG---LELtaikmqqgepdESGRRRPVpvegseftlqaDTVISAIGQQV--DPPIAEAAGI 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446082953 278 KTNEKGYIVVDK-YQNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSE---RLFNNKP 330
Cdd:PRK12814 448 GTSRNGTVKVDPeTLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHaidLFLNGKP 504
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
126-262 |
6.76e-09 |
|
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: 57.57 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 126 NGETITADHILIATGG--RPSHPDIPGveygIDSdgfFALPAL-------PE-----RVAVVGAGY----IAVELAGVin 187
Cdd:COG2072 123 DGETLTARFVVVATGPlsRPKIPDIPG----LED---FAGEQLhsadwrnPVdlagkRVLVVGTGAsavqIAPELARV-- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 188 glGAKTHLFVRKH---APLRSFD-----------------------------------------------------PMIS 211
Cdd:COG2072 194 --AAHVTVFQRTPpwvLPRPNYDpergrpanylgleappalnrrdarawlrrllraqvkdpelglltpdyppgckrPLLS 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446082953 212 ETLVEVMNAEGPQLHTNAI----PKAVVknadgsltleLEDGRSETVDCLIWAIG 262
Cdd:COG2072 272 TDYYEALRRGNVELVTGGIeritEDGVV----------FADGTEHEVDVIVWATG 316
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
163-334 |
1.22e-07 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 54.11 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 163 LPALPERVAVVGAGYIAVELAGVINGLGAK----THLFVRKHAPLRSFdpmisetlvEVMNA--EGPQLHTNAIPKAVVK 236
Cdd:PRK12771 263 PPFLGKRVVVIGGGNTAMDAARTARRLGAEevtiVYRRTREDMPAHDE---------EIEEAlrEGVEINWLRTPVEIEG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 237 NADGSLTLEL---------EDGR-------SETVDC--LIWAIGRepANDNINLEAAGVKTNEKGYIVVDK-YQNTNIEG 297
Cdd:PRK12771 334 DENGATGLRVitvekmeldEDGRpspvtgeEETLEAdlVVLAIGQ--DIDSAGLESVPGVEVGRGVVQVDPnFMMTGRPG 411
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446082953 298 IYAVGDNTGAVELTPVAVAAGRR--------LSERLFNNKPDEHL 334
Cdd:PRK12771 412 VFAGGDMVPGPRTVTTAIGHGKKaarnidafLGGEPYEHRPKREI 456
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
103-320 |
2.57e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 53.21 E-value: 2.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 103 LGKNNVDV-IKGFARF-VDAKTLEVNGETITADH--------ILIATG-GRPSHPDIPGVEY-GIDS-----------DG 159
Cdd:PRK12778 479 LPKKIVDVeIENLKKLgVKFETDVIVGKTITIEEleeegfkgIFIASGaGLPNFMNIPGENSnGVMSsneyltrvnlmDA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 160 FFALPALP----ERVAVVGAGYIAVELAGVINGLGAKTHLFVRKhaplRSFDPMISEtLVEVMNA--EGPQLHTNAIPKA 233
Cdd:PRK12778 559 ASPDSDTPikfgKKVAVVGGGNTAMDSARTAKRLGAERVTIVYR----RSEEEMPAR-LEEVKHAkeEGIEFLTLHNPIE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 234 VVKNADGSLT------LELED-------------GRSETVDC--LIWAIGREPaNDNINLEAAGVKTNEKGYIVVDKYQN 292
Cdd:PRK12778 634 YLADEKGWVKqvvlqkMELGEpdasgrrrpvaipGSTFTVDVdlVIVSVGVSP-NPLVPSSIPGLELNRKGTIVVDEEMQ 712
|
250 260
....*....|....*....|....*....
gi 446082953 293 TNIEGIYAVGDN-TGAVELTpVAVAAGRR 320
Cdd:PRK12778 713 SSIPGIYAGGDIvRGGATVI-LAMGDGKR 740
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
126-303 |
1.43e-06 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 50.31 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 126 NGETITADHILIATGGRPSHPDIpgveygIDSDG--FFALPALPE------------RVAVVGAGYIAVELAGVINGLGA 191
Cdd:PRK09754 95 NGESWHWDQLFIATGAAARPLPL------LDALGerCFTLRHAGDaarlrevlqperSVVIVGAGTIGLELAASATQRRC 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 192 KTHLFVRKHAPL-RSFDPMISETLVEVMNAEGPQLHTNaipKAVVKNADGS-LTLELEDGRSETVDCLIWAIGREpANDN 269
Cdd:PRK09754 169 KVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLN---NAIEHVVDGEkVELTLQSGETLQADVVIYGIGIS-ANDQ 244
|
170 180 190
....*....|....*....|....*....|....
gi 446082953 270 INLEAAGVKTNEkgyIVVDKYQNTNIEGIYAVGD 303
Cdd:PRK09754 245 LAREANLDTANG---IVIDEACRTCDPAIFAGGD 275
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
131-303 |
1.44e-05 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 46.98 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 131 TADHILIATGGRPSHPDIP--------GVEYGIDSDGFFALPalpERVAVVGAGYIAVELAGVINGLGAKTHLFVRKHAp 202
Cdd:PRK10262 105 TCDALIIATGASARYLGLPseeafkgrGVSACATCDGFFYRN---QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDG- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 203 LRSFDPMISETLVEVMNAEgPQLHTNAIPKAVVKNADGSLTLELEDGRS----ETVDC--LIWAIGREPaNDNInleAAG 276
Cdd:PRK10262 181 FRAEKILIKRLMDKVENGN-IILHTNRTLEEVTGDQMGVTGVRLRDTQNsdniESLDVagLFVAIGHSP-NTAI---FEG 255
|
170 180 190
....*....|....*....|....*....|..
gi 446082953 277 VKTNEKGYIVVD-----KYQNTNIEGIYAVGD 303
Cdd:PRK10262 256 QLELENGYIKVQsgihgNATQTSIPGVFAAGD 287
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
122-305 |
1.33e-04 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 44.38 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 122 TLEvNGETITADHILIATGGRPSHPDIP--------GVEYGIDSDG-FFAlpalPERVAVVGAGYIAVE----LAGVINg 188
Cdd:PRK15317 302 ELA-NGAVLKAKTVILATGARWRNMNVPgedeyrnkGVAYCPHCDGpLFK----GKRVAVIGGGNSGVEaaidLAGIVK- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 189 lgaktHLFVRKHAP-LRSfDPMISETLVEVMNAEgpqLHTNAIPKAVVKNADGSLTLELED---GRSETVDC--LIWAIG 262
Cdd:PRK15317 376 -----HVTVLEFAPeLKA-DQVLQDKLRSLPNVT---IITNAQTTEVTGDGDKVTGLTYKDrttGEEHHLELegVFVQIG 446
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446082953 263 REPandniNLEAAG--VKTNEKGYIVVDKYQNTNIEGIYAVGDNT 305
Cdd:PRK15317 447 LVP-----NTEWLKgtVELNRRGEIIVDARGATSVPGVFAAGDCT 486
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
118-320 |
1.44e-04 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 44.55 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 118 VDAKTLEVNGETITADHILIATG----------GRPSHPDIPGvEY-----------------GIDSDGFFALP-ALPER 169
Cdd:PRK12775 495 VKIETNKVIGKTFTVPQLMNDKGfdavflgvgaGAPTFLGIPG-EFagqvysanefltrvnlmGGDKFPFLDTPiSLGKS 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 170 VAVVGAGYIAVELAGVINGLGAKThlfVR-----------------KHAPLRSFDPMISETLVEVMNAEGPQLHTNAIPK 232
Cdd:PRK12775 574 VVVIGAGNTAMDCLRVAKRLGAPT---VRcvyrrseaeaparieeiRHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKVEE 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 233 AVVKNADgsltlelEDGRSETV----------DCLIWAIGREPaNDNINLEAAGVKTNEKGYIVVDKY-----QNTNIEG 297
Cdd:PRK12775 651 MELGEPD-------EKGRRKPMptgefkdlecDTVIYALGTKA-NPIITQSTPGLALNKWGNIAADDGklestQSTNLPG 722
|
250 260
....*....|....*....|...
gi 446082953 298 IYAVGDNTGAVELTPVAVAAGRR 320
Cdd:PRK12775 723 VFAGGDIVTGGATVILAMGAGRR 745
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
216-329 |
8.67e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 41.55 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 216 EVMNA--EGPQLHTNAIPKAVVKNADGSLTL----------ELEDGR--------SE---TVDCLIWAIGREPaNDNINL 272
Cdd:PRK12809 495 EVVNAreEGVEFQFNVQPQYIACDEDGRLTAvglirtamgePGPDGRrrprpvagSEfelPADVLIMAFGFQA-HAMPWL 573
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446082953 273 EAAGVK--------TNEKGYIVVdkyqNTNIEGIYAVGDNTGAVELTPVAVAAGRRLSER---LFNNK 329
Cdd:PRK12809 574 QGSGIKldkwgliqTGDVGYLPT----QTHLKKVFAGGDAVHGADLVVTAMAAGRQAARDmltLFDTK 637
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
126-176 |
3.64e-03 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 39.55 E-value: 3.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446082953 126 NGETITADHILIATGGRPSHPDiPGVEYGidSDGFF-------ALPALP--ERVAVVGAG 176
Cdd:COG4529 145 DGETLRADAVVLATGHPPPAPP-PGLAAG--SPRYIadpwppgALARIPpdARVLIIGTG 201
|
|
| |
