|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
1-442 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 634.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 1 QDFAEIYARFSDERANEQANRCSQCGVPFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDRLCE 80
Cdd:PRK11749 21 QNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQERLCE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 81 GNCVIEQStHGAVTIGSVEKYINDTAWDQGWVKPrTPSRELGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGGL 160
Cdd:PRK11749 101 GACVRGKK-GEPVAIGRLERYITDWAMETGWVLF-KRAPKTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 161 LVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIVAALDYL 240
Cdd:PRK11749 179 LRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPRFLGIPGENLGGVYSAVDFL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 241 TTSNKVSLGDTVEayengslnaAGKHVVVLGGGDTAMDCVRTAIRQGATSVKCLYRRDRKNMPGSQREVAHAEEEGVEFI 320
Cdd:PRK11749 259 TRVNQAVADYDLP---------VGKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPASEEEVEHAKEEGVEFE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 321 WQAAPEGFTGD-TVVTGVRAVRIHLGVADATGRQtPQVIEGSEFTVQADLVIKALGFEPEdLPNAFDEPELKVTRWGTLL 399
Cdd:PRK11749 330 WLAAPVEILGDeGRVTGVEFVRMELGEPDASGRR-RVPIEGSEFTLPADLVIKAIGQTPN-PLILSTTPGLELNRWGTII 407
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 165761230 400 VDHRTKMTNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:PRK11749 408 ADDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEY 450
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
1-442 |
0e+00 |
|
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: 581.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 1 QDFAEIYARFSDERANEQANRCSQCGVPFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPqdRLCE 80
Cdd:COG0493 3 KDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--APCE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 81 GNCVIEQStHGAVTIGSVEKYINDTAWDQGWVKPRTPSRELGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGGL 160
Cdd:COG0493 81 GACVRGIV-DEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 161 LVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIVAALDYL 240
Cdd:COG0493 160 LRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDFL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 241 TTSNKVSLGDTveayengsLNAAGKHVVVLGGGDTAMDCVRTAIRQGATSVKCLYRRDRKNMPGSQREVAHAEEEGVEFI 320
Cdd:COG0493 240 TAVNLGEAPDT--------ILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 321 WQAAPEGFTGDT--VVTGVRAVRIHLGVADATGRQTPQVIEGSEFTVQADLVIKALGFEPeDLPNAFDEPELKVTRWGTL 398
Cdd:COG0493 312 FLVAPVEIIGDEngRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTP-DPSGLEEELGLELDKRGTI 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 165761230 399 LVDHRTKMTNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:COG0493 391 VVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
1-442 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 563.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 1 QDFAEIYARFSDERANEQANRCSQCGVPFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDrlCE 80
Cdd:PRK12810 25 KDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAP--CE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 81 GNCVIEQStHGAVTIGSVEKYINDTAWDQGWVKPRTPSRELGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGGL 160
Cdd:PRK12810 103 GACTLNIN-FGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGGL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 161 LVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIVAALDYL 240
Cdd:PRK12810 182 LRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAYKPRDLGIPGRDLDGVHFAMDFL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 241 TTSNKVSLGDTVEAYengsLNAAGKHVVVLGGGDTAMDCVRTAIRQGATSVKclyRRDRKNMPGSQR------------- 307
Cdd:PRK12810 262 IQNTRRVLGDETEPF----ISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVT---QRDIMPMPPSRRnknnpwpywpmkl 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 308 EVAHAEEEGVEFIWQAAPEGFTG-DTVVTGVRAVRIHLGVADatgrqtPQVIEGSEFTVQADLVIKALGFEPEDlPNAFD 386
Cdd:PRK12810 335 EVSNAHEEGVEREFNVQTKEFEGeNGKVTGVKVVRTELGEGD------FEPVEGSEFVLPADLVLLAMGFTGPE-AGLLA 407
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 165761230 387 EPELKVTRWGTLLVDHRTKMTNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:PRK12810 408 QFGVELDERGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAY 463
|
|
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
2-439 |
2.94e-154 |
|
glutamate synthase small subunit family protein, proteobacterial; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit and homologs. TIGR01317 describes the small subunit (or equivalent region from longer forms) in eukaryotes, Gram-positive bacteria, and some other lineages, both NADH and NADPH-dependent. TIGR01316 describes a protein of similar length, from Archaea and a number of bacterial lineages, that forms glutamate synthase homotetramers without a large subunit. This model describes both glutatate synthase small subunit and closely related paralogs of unknown function from a number of gamma and alpha subdivision Proteobacteria, including E. coli.
Pssm-ID: 273553 [Multi-domain] Cd Length: 467 Bit Score: 445.79 E-value: 2.94e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 2 DFAEIYARFSDERANEQANRCSQCGVPFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDRLCEG 81
Cdd:TIGR01318 22 DFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSHQTNTLPEICGRVCPQDRLCEG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 82 NCVIEQsTHGAVTIGSVEKYINDTAWDQGW------VKPRtpsrelGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYD 155
Cdd:TIGR01318 102 ACTLND-EGGAVTIGNLERYITDTALAMGWrpdlshVQPT------GKRVAVIGAGPAGLACADILARAGVQVVVFDRHP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 156 RMGGLLVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIVA 235
Cdd:TIGR01318 175 EIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRSMRGGLPGEDAPGVLP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 236 ALDYLTTSNKVSLGDTvEAYENGSLNAAGKHVVVLGGGDTAMDCVRTAIRQGATSVKCLYRRDRKNMPGSQREVAHAEEE 315
Cdd:TIGR01318 255 ALPFLIANTRQLMGLP-EEPEEPLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANMPGSRREVANAREE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 316 GVEFIWQAAPEGFTGDTV--VTGVRAVRIHLGVADATGRQTPQVIEGSEFTVQADLVIKALGFEPEDLPnAFDEPELKVT 393
Cdd:TIGR01318 334 GVEFLFNVQPVSIESDEDgqVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHLMP-WLAAHGITLD 412
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 165761230 394 RWG---TLLVDHRTKMTNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGI 439
Cdd:TIGR01318 413 SWGriiTALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGI 461
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
3-442 |
4.78e-132 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 395.65 E-value: 4.78e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 3 FAEIYARFSDERANEQANRCSQCGV-PFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDRLCEG 81
Cdd:PRK12769 208 FDEIYLPFRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLPEITGRVCPQDRLCEG 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 82 NCVIEQStHGAVTIGSVEKYINDTAWDQGWVKPRTPSRELGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGGLL 161
Cdd:PRK12769 288 ACTLRDE-YGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 162 VYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYkaRDIKApgsGLGN-----IVAA 236
Cdd:PRK12769 367 TFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTY--RSMKA---GLPNedapgVYDA 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 237 LDYLTTSNKVSLGDTVEAYENgSLNAAGKHVVVLGGGDTAMDCVRTAIRQGATSVKCLYRRDRKNMPGSQREVAHAEEEG 316
Cdd:PRK12769 442 LPFLIANTKQVMGLEELPEEP-FINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEG 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 317 VEFIWQAAPEGFTGDT--VVTGVRAVRIHLGVADATGRQTPQVIEGSEFTVQADLVIKALGFEPEDLPnAFDEPELKVTR 394
Cdd:PRK12769 521 ANFEFNVQPVALELNEqgHVCGIRFLRTRLGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGFNPHGMP-WLESHGVTVDK 599
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 165761230 395 WGTLLVDHRTKM---TNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:PRK12769 600 WGRIIADVESQYryqTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDW 650
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
1-442 |
1.93e-123 |
|
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate.
Pssm-ID: 162300 [Multi-domain] Cd Length: 485 Bit Score: 368.00 E-value: 1.93e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 1 QDFAEIYARFSDERANEQANRCSQCGVPFCQVH--CPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDrl 78
Cdd:TIGR01317 23 KDWKEFTNPFDKESAKYQAARCMDCGTPFCHNDsgCPLNNLIPEFNDLVFRGRWKEALDRLHATNNFPEFTGRVCPAP-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 79 CEGNCVIEQStHGAVTIGSVEKYINDTAWDQGWVKPRTPSRELGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMG 158
Cdd:TIGR01317 101 CEGACTLGIS-EDPVGIKSIERIIIDKGFQEGWVQPRPPSKRTGKKVAVVGSGPAGLAAADQLNRAGHTVTVFEREDRCG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 159 GLLVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIVAALD 238
Cdd:TIGR01317 180 GLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATKPRDLPIPGRELKGIHYAME 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 239 YLTTSNKVSLGDTVEayENGSLNAAGKHVVVLGGGDTAMDCVRTAIRQGATSV-------KCLYRRDRKNM----PGSQR 307
Cdd:TIGR01317 260 FLPSATKALLGKDFK--DIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVhqfeimpKPPEARAKDNPwpewPRVYR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 308 -EVAHAEEEGV------EFIWQAapEGFTGDTV--VTGVRAVRIHLgVADATGRQTPQVIEGSEFTVQADLVIKALGFEP 378
Cdd:TIGR01317 338 vDYAHEEAAAHygrdprEYSILT--KEFIGDDEgkVTALRTVRVEW-KKSQDGKWQFVEIPGSEEVFEADLVLLAMGFVG 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 165761230 379 EDLPNaFDEPELKVTRWGTLLVDHRTKMTNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:TIGR01317 415 PEQIL-LDDFGVKKTRRGNISAGYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVDRY 477
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
1-436 |
1.01e-118 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 360.88 E-value: 1.01e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 1 QDFAEIYARFSDERANEQANRCSQCG-VPFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDRLC 79
Cdd:PRK12809 189 THFGEIYCGLDPQQATYESDRCVYCAeKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDRLC 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 80 EGNCVIEQSThGAVTIGSVEKYINDTAWDQGW---VKPRTPSRElglSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDR 156
Cdd:PRK12809 269 EGACTLKDHS-GAVSIGNLERYITDTALAMGWrpdVSKVVPRSE---KVAVIGAGPAGLGCADILARAGVQVDVFDRHPE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 157 MGGLLVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIVAA 236
Cdd:PRK12809 345 IGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQA 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 237 LDYLTTSNKVSLGdTVEAYENGSLNAAGKHVVVLGGGDTAMDCVRTAIRQGATSVKCLYRRDRKNMPGSQREVAHAEEEG 316
Cdd:PRK12809 425 LPFLTAHTRQLMG-LPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 317 VEFIWQAAPEGFTGDT--VVTGVRAVRIHLGVADATGRQTPQVIEGSEFTVQADLVIKALGFEPEDLPnAFDEPELKVTR 394
Cdd:PRK12809 504 VEFQFNVQPQYIACDEdgRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAHAMP-WLQGSGIKLDK 582
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 165761230 395 WGTLL---VDHRTKMTNMDGVFAAGDIVRGASLVVWAIRDGRDAA 436
Cdd:PRK12809 583 WGLIQtgdVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAA 627
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
2-442 |
8.09e-113 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 340.07 E-value: 8.09e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 2 DFAEIYARFSDERANEQANRCSQCGVPFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDRLCEG 81
Cdd:PRK12831 22 NFEEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPQESQCEG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 82 NCVIEQSTHgAVTIGSVEKYINDTAWDQGwVKPRTPSRELGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGGLL 161
Cdd:PRK12831 102 KCVLGIKGE-PVAIGKLERFVADWARENG-IDLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 162 VYGIPGFKLEKS-VVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHV--AVLVATGVYKARDIKAPGSGLGNIVAALD 238
Cdd:PRK12831 180 VYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEEGfdAVFIGSGAGLPKFMGIPGENLNGVFSANE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 239 YLTTSNkvslgdTVEAYENGSLN--AAGKHVVVLGGGDTAMDCVRTAIRQGAtSVKCLYRRDRKNMPGSQREVAHAEEEG 316
Cdd:PRK12831 260 FLTRVN------LMKAYKPEYDTpiKVGKKVAVVGGGNVAMDAARTALRLGA-EVHIVYRRSEEELPARVEEVHHAKEEG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 317 VEFIWQAAPEGFTGDT--VVTGVRAVRIHLGVADATGRQTPQVIEGSEFTVQADLVIKALGFEPEDLPNAfDEPELKVTR 394
Cdd:PRK12831 333 VIFDLLTNPVEILGDEngWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISS-TTKGLKINK 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 165761230 395 WGTLLVDHRTKMTNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:PRK12831 412 RGCIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEY 459
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
3-444 |
4.19e-105 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 329.01 E-value: 4.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 3 FAEIYARFSDERANEQANRCSQCGVPFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDRLCEGN 82
Cdd:PRK12778 312 FEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPQEKQCESK 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 83 CVIEQSTHGAVTIGSVEKYINDtaWDQGWVKPRTPS--RELGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGGL 160
Cdd:PRK12778 392 CIHGKMGEEAVAIGYLERFVAD--YERESGNISVPEvaEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGV 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 161 LVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHV-AVLVATGVYKARDIKAPGSGLGNIVAALDY 239
Cdd:PRK12778 470 LKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEGFkGIFIASGAGLPNFMNIPGENSNGVMSSNEY 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 240 LTTSNkvslgdTVEAYENGSLN--AAGKHVVVLGGGDTAMDCVRTAIRQGATSVKCLYRRDRKNMPGSQREVAHAEEEGV 317
Cdd:PRK12778 550 LTRVN------LMDAASPDSDTpiKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARLEEVKHAKEEGI 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 318 EFIWQAAPEGFTGDTV--VTGVRAVRIHLGVADATGRQTPQVIEGSEFTVQADLVIKALGFEPEDL-PNAFdePELKVTR 394
Cdd:PRK12778 624 EFLTLHNPIEYLADEKgwVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLvPSSI--PGLELNR 701
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 165761230 395 WGTLLVDHRTkMTNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGIHAYAK 444
Cdd:PRK12778 702 KGTIVVDEEM-QSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLS 750
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
1-442 |
1.44e-100 |
|
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 130383 [Multi-domain] Cd Length: 449 Bit Score: 307.95 E-value: 1.44e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 1 QDFAEIYARFSDERANEQANRCSQCGVPF--CQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDRL 78
Cdd:TIGR01316 7 KLFQEAALGYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVCPQERQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 79 CEGNCVIEQSTHG---AVTIGSVEKYINDTAWDQGWVKPRTPSRELGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYD 155
Cdd:TIGR01316 87 CEGQCTVGKMFKDvgkPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVTVFEALH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 156 RMGGLLVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIVA 235
Cdd:TIGR01316 167 KPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEELCGVYS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 236 ALDYLTTSNKVSLGDTVEAyenGSLNAAGKHVVVLGGGDTAMDCVRTAIRQGAtSVKCLYRRDRKNMPGSQREVAHAEEE 315
Cdd:TIGR01316 247 ANDFLTRANLMKAYEFPHA---DTPVYAGKSVVVIGGGNTAVDSARTALRLGA-EVHCLYRRTREDMTARVEEIAHAEEE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 316 GVEFIWQAAPEGFTGDTV--VTGVRAVRIHLGVADATGRQTPQVIEGSEFTVQADLVIKALGFEPEdlPNAFDEPELKVT 393
Cdd:TIGR01316 323 GVKFHFLCQPVEIIGDEEgnVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSN--PIMAETTRLKTS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 165761230 394 RWGTLLVDHRtKMTNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:TIGR01316 401 ERGTIVVDED-QRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEY 448
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
28-442 |
1.08e-92 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 291.39 E-value: 1.08e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 28 PFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDrlCEGNC---VIEQsthgAVTIGSVEKYIND 104
Cdd:PRK12771 47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCnrgQVDD----AVGINAVERFLGD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 105 TAWDQGWvKPRTPSRELGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGGLLVYGIPGFKLEKSVVERRVKLLAD 184
Cdd:PRK12771 121 YAIANGW-KFPAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILD 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 185 AGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIVAALDYLttsnkvslgdtvEAYENGSLNAAG 264
Cdd:PRK12771 200 LGVEVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFL------------RAVGEGEPPFLG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 265 KHVVVLGGGDTAMDCVRTAIRQGATSVKCLYRRDRKNMPGSQREVAHAEEEGVEFIWQAAPEGFTGDT-VVTGVRAVRIH 343
Cdd:PRK12771 268 KRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDEnGATGLRVITVE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 344 LGVADATGRqtPQVIEGSEFTVQADLVIKALG----FEP-EDLPNAfdepelkVTRWGTLLVDHRTKMTNMDGVFAAGDI 418
Cdd:PRK12771 348 KMELDEDGR--PSPVTGEEETLEADLVVLAIGqdidSAGlESVPGV-------EVGRGVVQVDPNFMMTGRPGVFAGGDM 418
|
410 420
....*....|....*....|....
gi 165761230 419 VRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:PRK12771 419 VPGPRTVTTAIGHGKKAARNIDAF 442
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
2-442 |
1.97e-81 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 271.04 E-value: 1.97e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 2 DFAEIYARFSDERANEQANRCSQCGVPFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDRLCEG 81
Cdd:PRK12775 313 NFKEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCPQETQCEA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 82 NCVIEQStHGAVTIGSVEKYINDTAWDQGwVKPRTPSRELGlSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGGLL 161
Cdd:PRK12775 393 QCIIAKK-HESVGIGRLERFVGDNARAKP-VKPPRFSKKLG-KVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 162 VYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPEL--RRKHVAVLVATGVYKARDIKAPGSGLGNIVAALDY 239
Cdd:PRK12775 470 QYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLmnDKGFDAVFLGVGAGAPTFLGIPGEFAGQVYSANEF 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 240 LTTSNkvSLGDTVEAYENGSLnAAGKHVVVLGGGDTAMDCVRTAIRQGATSVKCLYRRDRKNMPGSQREVAHAEEEGVEF 319
Cdd:PRK12775 550 LTRVN--LMGGDKFPFLDTPI-SLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGIDF 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 320 IWQAAPEGF--TGDTVVTGVRAVRIHLGVADATGRQTPqvIEGSEFT-VQADLVIKALGFEPEDLPNAfDEPELKVTRWG 396
Cdd:PRK12775 627 FFLHSPVEIyvDAEGSVRGMKVEEMELGEPDEKGRRKP--MPTGEFKdLECDTVIYALGTKANPIITQ-STPGLALNKWG 703
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 165761230 397 TLLVD----HRTKMTNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:PRK12775 704 NIAADdgklESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARSIATY 753
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
2-442 |
5.96e-81 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 263.13 E-value: 5.96e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 2 DFAEIYA--RFSDERANEQanRCSQCGVPfCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDrlC 79
Cdd:PRK12814 77 ENAELHAmrRQSLERLIEQ--HCGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--C 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 80 EGNCvieqSTHGA---VTIGSVEKYI--NDTAWDQGWVKPRTPSRelGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRY 154
Cdd:PRK12814 152 EEAC----RRHGVdepVSICALKRYAadRDMESAERYIPERAPKS--GKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDAN 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 155 DRMGGLLVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIV 234
Cdd:PRK12814 226 EQAGGMMRYGIPRFRLPESVIDADIAPLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 235 AALDYLttsNKVSLGDTVeayengslnAAGKHVVVLGGGDTAMDCVRTAIRQGATSVKCLYRRDRKNMPGSQREVAHAEE 314
Cdd:PRK12814 306 SGIDFL---RNVALGTAL---------HPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 315 EGVEFIWQAAPEGFTGDTVVTGVRAVRIHLGVADATGRQTPQVIEGSEFTVQADLVIKALGFEPEdlPNAFDEPELKVTR 394
Cdd:PRK12814 374 EGVSLRELAAPVSIERSEGGLELTAIKMQQGEPDESGRRRPVPVEGSEFTLQADTVISAIGQQVD--PPIAEAAGIGTSR 451
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 165761230 395 WGTLLVDHRTKMTNMDGVFAAGDIVRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:PRK12814 452 NGTVKVDPETLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLF 499
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
115-442 |
4.87e-75 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 239.12 E-value: 4.87e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 115 RTPSRELGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGGLLVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFE 194
Cdd:PRK12770 11 KEKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 195 V---------------GRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIVAALDYL--TTSNKVSLGDTVEAYEn 257
Cdd:PRK12770 91 VccgeplheeegdefvERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLfrIRAAKLGYLPWEKVPP- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 258 gslnAAGKHVVVLGGGDTAMDCVRTAIRQGATSVKCLYRRDRKNMPGSQREVAHAEEEGVEFIWQAAPEGFTGDTVVTGV 337
Cdd:PRK12770 170 ----VEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIGEGRVEGV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 338 RAVRIHLGVADATGRQTPQVIEGSEFTVQADLVIKALGFEPEDlPNAFDEPELKVTRWGTLLVDHRtKMTNMDGVFAAGD 417
Cdd:PRK12770 246 ELAKMRLGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTP-PFAKECLGIELNRKGEIVVDEK-HMTSREGVFAAGD 323
|
330 340
....*....|....*....|....*
gi 165761230 418 IVRGASLVVWAIRDGRDAAEGIHAY 442
Cdd:PRK12770 324 VVTGPSKIGKAIKSGLRAAQSIHEW 348
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
34-439 |
6.50e-64 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 222.01 E-value: 6.50e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 34 CPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDRLCEGNCvieqsTHGA--VTIGSVEKYINDTawdQGW 111
Cdd:PRK12779 214 CPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVC-----THTKrpIEIGQLEWYLPQH---EKL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 112 VKPRTPSRELGL----------SVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGGLLVYGIPGFKLEKSVVERRVKL 181
Cdd:PRK12779 286 VNPNANERFAGRispwaaavkpPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEK 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 182 LADAGVIYHPNFEVGRDASLPELRRKHVA-VLVATGVYKARDIKAPGSGLGNIVAALDYLTTSNKVSLGDtvEAYENGSL 260
Cdd:PRK12779 366 IKLLGGRFVKNFVVGKTATLEDLKAAGFWkIFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRVNLMRGLD--DDYETPLP 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 261 NAAGKHVVVLGGGDTAMDCVRTAIRQGAtSVKCLYRRDRKNMPGSQREVAHAEEEGVEFIWQAAPEGFTGDT---VVTGV 337
Cdd:PRK12779 444 EVKGKEVFVIGGGNTAMDAARTAKRLGG-NVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGDDhthFVTHA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 338 RAVRIHLGVADATGRQTPQVIeGSEFTVQADLVIKALGFEPEdlPNAFD-EPELKVTRWGTLLVDHRTKMTNMDGVFAAG 416
Cdd:PRK12779 523 LLDVNELGEPDKSGRRSPKPT-GEIERVPVDLVIMALGNTAN--PIMKDaEPGLKTNKWGTIEVEKGSQRTSIKGVYSGG 599
|
410 420
....*....|....*....|...
gi 165761230 417 DIVRGASLVVWAIRDGRDAAEGI 439
Cdd:PRK12779 600 DAARGGSTAIRAAGDGQAAAKEI 622
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
3-444 |
6.52e-60 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 206.16 E-value: 6.52e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 3 FAEIYARFSDERANEQANRCSQCGVpfCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDrlCEGN 82
Cdd:PRK13984 168 FIEIVKGYSKEQAMQEAARCVECGI--CTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVCTHK--CETV 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 83 CVIEQSTHgAVTIGSVEKYINDTAWDQGW---VKPRTPSRelGLSVGVIGAGPAGLAAAEELRAKGYEVHVYDRYDRMGG 159
Cdd:PRK13984 244 CSIGHRGE-PIAIRWLKRYIVDNVPVEKYseiLDDEPEKK--NKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 160 LLVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARDIKAPGSGLGNIVAALDY 239
Cdd:PRK13984 321 VMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGTDHPDVIQALPL 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 240 LTTSNKVSLGDTVEAYengslnaAGKHVVVLGGGDTAMDCVRTAIR-----QGATSVKCL-YRRDRKNMPGSQREVAHAE 313
Cdd:PRK13984 401 LREIRDYLRGEGPKPK-------IPRSLVVIGGGNVAMDIARSMARlqkmeYGEVNVKVTsLERTFEEMPADMEEIEEGL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 314 EEGVEFIWQAAP-EGFTGDTVVTGVRAVRIhLGVADATGRQTPQVIEGSEFTVQADLVIKALGFEP--EDLPNAFDEpEL 390
Cdd:PRK13984 474 EEGVVIYPGWGPmEVVIENDKVKGVKFKKC-VEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQAPdySYLPEELKS-KL 551
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 165761230 391 KVTRwGTLLVDHRTKmTNMDGVFAAGDIVRGASlVVWAIRDGRDAAEGIHAYAK 444
Cdd:PRK13984 552 EFVR-GRILTNEYGQ-TSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYLR 602
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
1-111 |
1.33e-54 |
|
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.
Pssm-ID: 434132 [Multi-domain] Cd Length: 113 Bit Score: 177.73 E-value: 1.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 1 QDFAEIYARFSDERANEQANRCSQCGVPFCQVHCPVSNNIPDWLKLTSEGRLEEAYEVSQATNNFPEICGRICPQDRLCE 80
Cdd:pfam14691 3 KNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQCE 82
|
90 100 110
....*....|....*....|....*....|.
gi 165761230 81 GNCVIEQSTHGAVTIGSVEKYINDTAWDQGW 111
Cdd:pfam14691 83 GACVLGKKGFEPVAIGRLERFAADWARENGI 113
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
210-442 |
3.37e-20 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 90.56 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 210 AVLVATGVYkARDIKAPG----SGLGnivaaldylttsnkVSLGDTVEAYEngslnAAGKHVVVLGGGDTAMDcvrTAI- 284
Cdd:COG0492 103 AVIIATGAG-PRKLGLPGeeefEGRG--------------VSYCATCDGFF-----FRGKDVVVVGGGDSALE---EALy 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 285 -RQGATSVKCLYRRDrkNMPGSQREVAHAEE-EGVEFIWQAAPEGFTGDTVVTGVRavrihlgVADatgrqtpqVIEGSE 362
Cdd:COG0492 160 lTKFASKVTLIHRRD--ELRASKILVERLRAnPKIEVLWNTEVTEIEGDGRVEGVT-------LKN--------VKTGEE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 363 FTVQADLVIKALGFEPE-DLpnaFDEPELKVTRWGTLLVDHRTKmTNMDGVFAAGDIVRGAS-LVVWAIRDGRDAAEGIH 440
Cdd:COG0492 223 KELEVDGVFVAIGLKPNtEL---LKGLGLELDEDGYIVVDEDME-TSVPGVFAAGDVRDYKYrQAATAAGEGAIAALSAA 298
|
..
gi 165761230 441 AY 442
Cdd:COG0492 299 RY 300
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
134-432 |
2.64e-13 |
|
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: 70.42 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 134 GLAAAEELRAKGYEVHVYDRydrmGGLLVYG--------------IPGFKLEKSVVERR----------VKLLADAGVIy 189
Cdd:pfam07992 12 GLAAALTLAQLGGKVTLIED----EGTCPYGgcvlskallgaaeaPEIASLWADLYKRKeevvkklnngIEVLLGTEVV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 190 hpnfEVGRDAS---LPELRRKHV------AVLVATGVyKARDIKAPGSGLGNIvaaldylttsnkvSLGDTVEAYENGSL 260
Cdd:pfam07992 87 ----SIDPGAKkvvLEELVDGDGetitydRLVIATGA-RPRLPPIPGVELNVG-------------FLVRTLDSAEALRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 261 NAAGKHVVVLGGGDTAMDCVRTAIRQGAtSVKCLYRRDR----KNMPGSQREVAHAEEEGVEFIWQAAPEGFTGDTVVTg 336
Cdd:pfam07992 149 KLLPKRVVVVGGGYIGVELAAALAKLGK-EVTLIEALDRllraFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGV- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 337 vravrihlgvadatgrqtpQVIEGSEFTVQADLVIKALGFEPEdlPNAFDEPELKVTRWGTLLVDHRTKmTNMDGVFAAG 416
Cdd:pfam07992 227 -------------------EVILKDGTEIDADLVVVAIGRRPN--TELLEAAGLELDERGGIVVDEYLR-TSVPGIYAAG 284
|
330
....*....|....*..
gi 165761230 417 DI-VRGASLVVWAIRDG 432
Cdd:pfam07992 285 DCrVGGPELAQNAVAQG 301
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
144-285 |
4.84e-10 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 61.25 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 144 KGYEVHVYDRYDRMGGLLVYGI-PGFKLEKSVVERRVKLLADAGVIYHPNFEVGRDASLPELRRKHVAVLVATGVYKARD 222
Cdd:PLN02852 50 DGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVTLGRDVSLSELRDLYHVVVLAYGAESDRR 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 165761230 223 IKAPGSGLGNIVAALDYLTTSNkvslGDTVEAYENGSLNaAGKHVVVLGGGDTAMDCVRTAIR 285
Cdd:PLN02852 130 LGIPGEDLPGVLSAREFVWWYN----GHPDCVHLPPDLK-SSDTAVVLGQGNVALDCARILLR 187
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
203-437 |
6.57e-06 |
|
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: 48.16 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 203 ELRRKHVavLVATGvykARDIKAPGSGLGNivaalDYLTTSNkvslgdtvEAYEngsLNAAGKHVVVLGGGdtamdcvrt 282
Cdd:COG1249 128 TLTADHI--VIATG---SRPRVPPIPGLDE-----VRVLTSD--------EALE---LEELPKSLVVIGGG--------- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 283 AI---------RQGAtSVKCLYRRDRKnMPGSQREVAHA-----EEEGVEFIwqaapegfTGdTVVTGVRA----VRIHL 344
Cdd:COG1249 178 YIglefaqifaRLGS-EVTLVERGDRL-LPGEDPEISEAlekalEKEGIDIL--------TG-AKVTSVEKtgdgVTVTL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 345 GVADAtgrqtpqviegsEFTVQADLVIKALGFEP--EDLpnAFDEPELKVTRWGTLLVDHRTKmTNMDGVFAAGDIVRGA 422
Cdd:COG1249 247 EDGGG------------EEAVEADKVLVATGRRPntDGL--GLEAAGVELDERGGIKVDEYLR-TSVPGIYAIGDVTGGP 311
|
250
....*....|....*
gi 165761230 423 SLVVWAIRDGRDAAE 437
Cdd:COG1249 312 QLAHVASAEGRVAAE 326
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
147-420 |
1.09e-05 |
|
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: 47.11 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 147 EVHVYDR-----YDRMGGLLVYGIPGFKLEKSVVeRRVKLLADAGVIYHPNFEV-GRDASlpelrRKHVAV--------- 211
Cdd:COG0446 7 EITVIEKgphhsYQPCGLPYYVGGGIKDPEDLLV-RTPESFERKGIDVRTGTEVtAIDPE-----AKTVTLrdgetlsyd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 212 --LVATGvykARDIKA--PGSGLGNIvaaldyltTSNKvSLGDTVEAYENgSLNAAGKHVVVLGGGDTAMDCVRTAIRQG 287
Cdd:COG0446 81 klVLATG---ARPRPPpiPGLDLPGV--------FTLR-TLDDADALREA-LKEFKGKRAVVIGGGPIGLELAEALRKRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 288 AtSVKCLYRRDRKnMPGSQREVA-----HAEEEGVEFIWQAAPEGFTGDTVVTgvravrihlgvadatgrqtpqVIEGSE 362
Cdd:COG0446 148 L-KVTLVERAPRL-LGVLDPEMAalleeELREHGVELRLGETVVAIDGDDKVA---------------------VTLTDG 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 165761230 363 FTVQADLVIKALGFEPE-DLpnaFDEPELKVTRWGTLLVDHRTKmTNMDGVFAAGDIVR 420
Cdd:COG0446 205 EEIPADLVVVAPGVRPNtEL---AKDAGLALGERGWIKVDETLQ-TSDPDVYAAGDCAE 259
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
266-338 |
4.56e-05 |
|
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: 41.81 E-value: 4.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 165761230 266 HVVVLGGGDTAMDCVrTAIRQGATSVKCLYRRDRKnMPGSQREVA-----HAEEEGVEFIWQAAPEGFTGDTVVTGVR 338
Cdd:pfam00070 1 RVVVVGGGYIGLELA-GALARLGSKVTVVERRDRL-LPGFDPEIAkilqeKLEKNGIEFLLNTTVEAIEGNGDGVVVV 76
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
265-417 |
8.54e-05 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 44.65 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 265 KHVVVLGGGDTAMDCVRTAIRQGaTSVKCLYRRDRKnMPGS-QRE-VAHAEEE----GVEFIWQAAPEGFTGDTVVTGVR 338
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLG-KNVRIIQLEDRI-LPDSfDKEiTDVMEEElrenGVELHLNEFVKSLIGEDKVEGVV 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 165761230 339 AvrihlgvadatgrqtpqviegSEFTVQADLVIKALGFEPEDlpNAFDEPELKVTRWGTLLVDhRTKMTNMDGVFAAGD 417
Cdd:PRK09564 228 T---------------------DKGEYEADVVIVATGVKPNT--EFLEDTGLKTLKNGAIIVD-EYGETSIENIYAAGD 282
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
139-420 |
1.82e-04 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 43.59 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 139 EELRAKGYEVHV-------YDRYDRMggLLVYGIPGFKLEKSVVERRVKLLADAGVIYHPNFEVGR-DASlpelrRKHV- 209
Cdd:COG1251 18 EELRKLDPDGEItvigaepHPPYNRP--PLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTAiDRA-----ARTVt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 210 ----------AVLVATGVYkARDIKAPGSGLGNIVaaldYLTTsnkvsLGDtVEAYENGSlnAAGKHVVVLGGGDTAMDC 279
Cdd:COG1251 91 ladgetlpydKLVLATGSR-PRVPPIPGADLPGVF----TLRT-----LDD-ADALRAAL--APGKRVVVIGGGLIGLEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 280 VRTAIRQGAtSVKCLYRRDRKnMP------GSQREVAHAEEEGVEFIWQAAPEGFTGDTVVTGVRavrihlgvaDATGRq 353
Cdd:COG1251 158 AAALRKRGL-EVTVVERAPRL-LPrqldeeAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVR---------LADGE- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 165761230 354 tpqviegsefTVQADLVIKALGFEPED--LPNAfdepELKVTRwGtLLVDHRTKmTNMDGVFAAGDIVR 420
Cdd:COG1251 226 ----------ELPADLVVVAIGVRPNTelARAA----GLAVDR-G-IVVDDYLR-TSDPDIYAAGDCAE 277
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
359-444 |
8.10e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 41.70 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 359 EGSEFTVQADLVIKALGFEP--EDLpnAFDEPELKVTRWGTLLVDHRTkMTNMDGVFAAGDIVRGASLVVWAIRDGRDAA 436
Cdd:PRK06292 249 GGKTETIEADYVLVATGRRPntDGL--GLENTGIELDERGRPVVDEHT-QTSVPGIYAAGDVNGKPPLLHEAADEGRIAA 325
|
....*...
gi 165761230 437 EGIHAYAK 444
Cdd:PRK06292 326 ENAAGDVA 333
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
266-441 |
3.64e-03 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 39.35 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 266 HVVVLGGGDT------AMD------CVRTAIRQGATSVKCLYRRDR--KNMPGSQREVAHA--EEEGVEFIWQAAPEGFT 329
Cdd:COG1252 151 TIVVVGGGPTgvelagELAellrklLRYPGIDPDKVRITLVEAGPRilPGLGEKLSEAAEKelEKRGVEVHTGTRVTEVD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165761230 330 GDTVVTgvravrihlgvadATGRqtpqviegsefTVQADLVIKALGFEPedlPNAFDEPELKVTRWGTLLVDHRTKMTNM 409
Cdd:COG1252 231 ADGVTL-------------EDGE-----------EIPADTVIWAAGVKA---PPLLADLGLPTDRRGRVLVDPTLQVPGH 283
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 165761230 410 DGVFAAGDIvrgASLV-----------VWAIRDGRDAAEGIHA 441
Cdd:COG1252 284 PNVFAIGDC---AAVPdpdgkpvpktaQAAVQQAKVLAKNIAA 323
|
|
| |
