|
Name |
Accession |
Description |
Interval |
E-value |
| gltD_gamma_fam |
TIGR01318 |
glutamate synthase small subunit family protein, proteobacterial; This model represents one of ... |
6-472 |
0e+00 |
|
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: 948.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 6 YQFIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAAELSH 85
Cdd:TIGR01318 1 FQFIDLPRQDPDKIPVEERKTDFREIYGPFDKGQAQYQADRCLDCGNPYCEWKCPVHNAIPQWLQLVQEGRIDEAAELSH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 86 QTNTLPEVCGRVCPQDRLCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADVL 165
Cdd:TIGR01318 81 QTNTLPEICGRVCPQDRLCEGACTLNDEGGAVTIGNLERYITDTALAMGWRPDLSHVQPTGKRVAVIGAGPAGLACADIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 166 TRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSM 245
Cdd:TIGR01318 161 ARAGVQVVVFDRHPEIGGLLTFGIPSFKLDKAVLSRRREIFTAMGIEFRLNCEVGRDISLDDLLEDYDAVFLGVGTYRSM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 246 RGGLENEDADGVYAALPFLIANTKQLMGFGETRDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEENM 325
Cdd:TIGR01318 241 RGGLPGEDAPGVLPALPFLIANTRQLMGLPEEPEEPLIDVEGKRVVVLGGGDTAMDCVRTAIRLGATKVTCAYRRDEANM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 326 PGSRREVKNAREEGVEFKFNVQPLGIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPHN 405
Cdd:TIGR01318 321 PGSRREVANAREEGVEFLFNVQPVSIESDEDGQVIGVTVVRTKLGEPDANGRRRPVPVAGSEFVLPADVVIMAFGFSPHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131103 406 MEWLAKHSVELDSQGRIIAPEGSDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWLEV 472
Cdd:TIGR01318 401 MPWLAAHGITLDSWGRIITALSSGLTYQTTNPKIFAGGDAVRGADLVVTAVAEGRDAAQGILDWLGV 467
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
13-472 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 850.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 13 RVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGN-PYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTLP 91
Cdd:PRK12769 193 RGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLP 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 92 EVCGRVCPQDRLCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADVLTRNGVK 171
Cdd:PRK12769 273 EITGRVCPQDRLCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNGVA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 172 AVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSMRGGLEN 251
Cdd:PRK12769 353 VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLPN 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 252 EDADGVYAALPFLIANTKQLMGFGETRDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEENMPGSRRE 331
Cdd:PRK12769 433 EDAPGVYDALPFLIANTKQVMGLEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKE 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 332 VKNAREEGVEFKFNVQPLGIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPHNMEWLAK 411
Cdd:PRK12769 513 VKNAREEGANFEFNVQPVALELNEQGHVCGIRFLRTRLGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGFNPHGMPWLES 592
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131103 412 HSVELDSQGRIIAPEGSDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWLEV 472
Cdd:PRK12769 593 HGVTVDKWGRIIADVESQYRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWLGV 653
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
2-472 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 804.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 2 SQNVYQFIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAA 81
Cdd:PRK12810 1 MGKPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 82 ELSHQTNTLPEVCGRVCPQDrlCEGSCTLNDEFGAVTIGNIERYINDKAFEMGW-RPDmSGVKQTGKKVAIIGAGPAGLA 160
Cdd:PRK12810 81 ERLHQTNNFPEFTGRVCPAP--CEGACTLNINFGPVTIKNIERYIIDKAFEEGWvKPD-PPVKRTGKKVAVVGSGPAGLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 161 CADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVG 240
Cdd:PRK12810 158 AADQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 241 TYQSMRGGLENEDADGVYAALPFLIANTKQLMGFGetrDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKHVTcayRR 320
Cdd:PRK12810 238 AYKPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDE---TEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVT---QR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 321 DEENMPGSRR-------------EVKNAREEGVEFKFNVQPLGIeVNGNGKVSGVKMVRTEMGEPDakgrrrAEIVAGSE 387
Cdd:PRK12810 312 DIMPMPPSRRnknnpwpywpmklEVSNAHEEGVEREFNVQTKEF-EGENGKVTGVKVVRTELGEGD------FEPVEGSE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 388 HIVPADAVIMAFGFRPHNMEWLAKHSVELDSQGRIIAPegsDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIM 467
Cdd:PRK12810 385 FVLPADLVLLAMGFTGPEAGLLAQFGVELDERGRVAAP---DNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAID 461
|
....*
gi 16131103 468 NWLEV 472
Cdd:PRK12810 462 AYLMG 466
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
24-466 |
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: 665.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 24 RKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTLPEVCGRVCPqdRL 103
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCP--AP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 104 CEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGG 183
Cdd:COG0493 79 CEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 184 LLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSMRGGLENEDADGVYAALPF 263
Cdd:COG0493 159 LLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 264 LIANTKQlmgfgetRDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEENMPGSRREVKNAREEGVEFK 343
Cdd:COG0493 239 LTAVNLG-------EAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 344 FNVQPLGIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPHNMEWLAKHSVELDSQGRII 423
Cdd:COG0493 312 FLVAPVEIIGDENGRVTGLECVRMELGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIV 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 16131103 424 APEGSdnaFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGI 466
Cdd:COG0493 392 VDEET---YQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAI 431
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
10-463 |
0e+00 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 636.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 10 DLQRVDPPKKPLKI----RKIEFVEIYEPFSEGQAKAQADRCLSCGN-PYCEWKCPVHNYIPNWLKLANEGRIFEAAELS 84
Cdd:PRK12809 169 ALLPVNSRKGADKIsaseRKTHFGEIYCGLDPQQATYESDRCVYCAEkANCNWHCPLHNAIPDYIRLVQEGKIIEAAELC 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 85 HQTNTLPEVCGRVCPQDRLCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADV 164
Cdd:PRK12809 249 HQTSSLPEICGRVCPQDRLCEGACTLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADI 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 165 LTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQS 244
Cdd:PRK12809 329 LARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGM 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 245 MRGGLENEDADGVYAALPFLIANTKQLMGFGETRDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEEN 324
Cdd:PRK12809 409 MRADLPHEDAPGVIQALPFLTAHTRQLMGLPESEEYPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 325 MPGSRREVKNAREEGVEFKFNVQPLGIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPH 404
Cdd:PRK12809 489 MPGSRKEVVNAREEGVEFQFNVQPQYIACDEDGRLTAVGLIRTAMGEPGPDGRRRPRPVAGSEFELPADVLIMAFGFQAH 568
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16131103 405 NMEWLAKHSVELDSQGRIIAPEGSDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAA 463
Cdd:PRK12809 569 AMPWLQGSGIKLDKWGLIQTGDVGYLPTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAA 627
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
7-471 |
0e+00 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 585.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 7 QFIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQ 86
Cdd:PRK11749 2 KFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 87 TNTLPEVCGRVCPQDRLCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPDMSGVKqTGKKVAIIGAGPAGLACADVLT 166
Cdd:PRK11749 82 TNPLPAVCGRVCPQERLCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKRAPK-TGKKVAVIGAGPAGLTAAHRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 167 RNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSMR 246
Cdd:PRK11749 161 RKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPRF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 247 GGLENEDADGVYAALPFLiANTKQlmgfGETRDEPFVsmeGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEENMP 326
Cdd:PRK11749 241 LGIPGENLGGVYSAVDFL-TRVNQ----AVADYDLPV---GKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 327 GSRREVKNAREEGVEFKFNVQPLGIEVNGNGkVSGVKMVRTEMGEPDAKGRRRaEIVAGSEHIVPADAVIMAFGFRPHNM 406
Cdd:PRK11749 313 ASEEEVEHAKEEGVEFEWLAAPVEILGDEGR-VTGVEFVRMELGEPDASGRRR-VPIEGSEFTLPADLVIKAIGQTPNPL 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131103 407 EWLAKHSVELDSQGRIIApegSDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWLE 471
Cdd:PRK11749 391 ILSTTPGLELNRWGTIIA---DDETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLE 452
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
11-471 |
2.92e-132 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 390.15 E-value: 2.92e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 11 LQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTL 90
Cdd:PRK12831 6 KKRVPVREQDPEVRATNFEEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 91 PEVCGRVCPQDRLCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPdMSGVKQTGKKVAIIGAGPAGLACADVLTRNGV 170
Cdd:PRK12831 86 PAVCGRVCPQESQCEGKCVLGIKGEPVAIGKLERFVADWARENGIDL-SETEEKKGKKVAVIGSGPAGLTCAGDLAKMGY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 171 KAVVFDRHPEIGGLLTFGIPAFKLEKE-VMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSD--YDAVFLGVGTYQSMRG 247
Cdd:PRK12831 165 DVTIFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFDAVFIGSGAGLPKFM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 248 GLENEDADGVYAALPFLIANtkQLM-GFGETRDEPFVSmeGKRVVVLGGGDTAMDCVRTSVRQGAKhVTCAYRRDEENMP 326
Cdd:PRK12831 245 GIPGENLNGVFSANEFLTRV--NLMkAYKPEYDTPIKV--GKKVAVVGGGNVAMDAARTALRLGAE-VHIVYRRSEEELP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 327 GSRREVKNAREEGVEFKFNVQPLGIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPHNM 406
Cdd:PRK12831 320 ARVEEVHHAKEEGVIFDLLTNPVEILGDENGWVKGMKCIKMELGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPL 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131103 407 EWLAKHSVELDSQGRIIAPEgsdNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWLE 471
Cdd:PRK12831 400 ISSTTKGLKINKRGCIVADE---ETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLS 461
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
8-463 |
2.08e-120 |
|
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: 360.68 E-value: 2.08e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 8 FIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYC--EWKCPVHNYIPNWLKLANEGRIFEAAELSH 85
Cdd:TIGR01317 5 FLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFChnDSGCPLNNLIPEFNDLVFRGRWKEALDRLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 86 QTNTLPEVCGRVCPQDrlCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADVL 165
Cdd:TIGR01317 85 ATNNFPEFTGRVCPAP--CEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPRPPSKRTGKKVAVVGSGPAGLAAADQL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 166 TRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSM 245
Cdd:TIGR01317 163 NRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGATKPR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 246 RGGLENEDADGVYAALPFLIANTKQLMGfGETRDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKHVT-------CAY 318
Cdd:TIGR01317 243 DLPIPGRELKGIHYAMEFLPSATKALLG-KDFKDIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHqfeimpkPPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 319 RRDEENM----PGSRReVKNAREEGVEF------KFNVQPLGIEVNGNGKVSGVKMVRTEMgEPDAKGRRRAEIVAGSEH 388
Cdd:TIGR01317 322 ARAKDNPwpewPRVYR-VDYAHEEAAAHygrdprEYSILTKEFIGDDEGKVTALRTVRVEW-KKSQDGKWQFVEIPGSEE 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131103 389 IVPADAVIMAFGFRPHNMEWLAKHSVELDSQGRIIAPEGSDnafQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAA 463
Cdd:TIGR01317 400 VFEADLVLLAMGFVGPEQILLDDFGVKKTRRGNISAGYDDY---STSIPGVFAAGDCRRGQSLIVWAINEGRKAA 471
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
16-470 |
1.83e-112 |
|
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: 339.15 E-value: 1.83e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 16 PPKKplkiRKIEFVEIYEPFSEGQAKAQADRCLSCGNPY--CEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTLPEV 93
Cdd:TIGR01316 1 PPEE----RSKLFQEAALGYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 94 CGRVCPQDRLCEGSCTLNDEFG----AVTIGNIERYINDKAFEMGWRPDMSGVKQTGKKVAIIGAGPAGLACADVLTRNG 169
Cdd:TIGR01316 77 CGRVCPQERQCEGQCTVGKMFKdvgkPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 170 VKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSMRGGL 249
Cdd:TIGR01316 157 HSVTVFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 250 ENEDADGVYAALPFLIANTkqLMGFGETRDEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAKhVTCAYRRDEENMPGSR 329
Cdd:TIGR01316 237 PGEELCGVYSANDFLTRAN--LMKAYEFPHADTPVYAGKSVVVIGGGNTAVDSARTALRLGAE-VHCLYRRTREDMTARV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 330 REVKNAREEGVEFKFNVQPLGIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPHNMewL 409
Cdd:TIGR01316 314 EEIAHAEEEGVKFHFLCQPVEIIGDEEGNVRAVKFRKMDCQEQIDSGERRFLPCGDAECKLEADAVIVAIGNGSNPI--M 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131103 410 AKHS-VELDSQGRIIApegsDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWL 470
Cdd:TIGR01316 392 AETTrLKTSERGTIVV----DEDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
9-470 |
1.94e-112 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 348.66 E-value: 1.94e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 9 IDLQRVDPPKKPLKIRKI-EFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQT 87
Cdd:PRK12778 292 TAIERVPMPELDPEYRAHnRFEEVNLGLTKEQAMTEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKET 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 88 NTLPEVCGRVCPQDRLCEGSCTL---NDEfgAVTIGNIERYINDKAFEMGwRPDMSGVKQ-TGKKVAIIGAGPAGLACAD 163
Cdd:PRK12778 372 SALPAVCGRVCPQEKQCESKCIHgkmGEE--AVAIGYLERFVADYERESG-NISVPEVAEkNGKKVAVIGSGPAGLSFAG 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 164 VLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLS-DYDAVFLGVGTY 242
Cdd:PRK12778 449 DLAKRGYDVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEeGFKGIFIASGAG 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 243 QSMRGGLENEDADGVYAALPFLianTK-QLM-GFGETRDEPFVSmeGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRR 320
Cdd:PRK12778 529 LPNFMNIPGENSNGVMSSNEYL---TRvNLMdAASPDSDTPIKF--GKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRR 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 321 DEENMPGSRREVKNAREEGVEFKFNVQPLGIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFG 400
Cdd:PRK12778 604 SEEEMPARLEEVKHAKEEGIEFLTLHNPIEYLADEKGWVKQVVLQKMELGEPDASGRRRPVAIPGSTFTVDVDLVIVSVG 683
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 401 FRPHNMEWLAKHSVELDSQGRIIApegsDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWL 470
Cdd:PRK12778 684 VSPNPLVPSSIPGLELNRKGTIVV----DEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYL 749
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
53-470 |
2.31e-107 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 329.91 E-value: 2.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 53 PYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTLPEVCGRVCPQDrlCEGSCTLNDEFGAVTIGNIERYINDKAFE 132
Cdd:PRK12771 47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHP--CESGCNRGQVDDAVGINAVERFLGDYAIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 133 MGWRPDMSGVkQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMtrRREI--FTGMG 210
Cdd:PRK12771 125 NGWKFPAPAP-DTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVL--DAEIqrILDLG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 211 IEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSMRGGLENEDADGVYAALPFLIAntkqlmgFGETRDePFVsmeGKRV 290
Cdd:PRK12771 202 VEVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLRA-------VGEGEP-PFL---GKRV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 291 VVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEENMPGSRREVKNAREEGVEFKFNVQPLGIEVNGNGkVSGVKMVRTEMG 370
Cdd:PRK12771 271 VVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENG-ATGLRVITVEKM 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 371 EPDAKGRRRAeiVAGSEHIVPADAVIMAFGfRPHNMEWLAKHSVELDSQGRIIApegsDNAFQ-TSNPKIFAGGDIVRGS 449
Cdd:PRK12771 350 ELDEDGRPSP--VTGEEETLEADLVVLAIG-QDIDSAGLESVPGVEVGRGVVQV----DPNFMmTGRPGVFAGGDMVPGP 422
|
410 420
....*....|....*....|.
gi 16131103 450 DLVVTAIAEGRKAADGIMNWL 470
Cdd:PRK12771 423 RTVTTAIGHGKKAARNIDAFL 443
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
17-470 |
9.19e-94 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 304.94 E-value: 9.19e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 17 PKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEgRIFEAA-ELSHQTNTLPEVCG 95
Cdd:PRK12775 303 PERDAVERARNFKEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFIRHVVV-RDFDGAlEVIYEASIFPSICG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 96 RVCPQDRLCEGSCTLNDEFGAVTIGNIERYINDKA-FEMGWRPDMSgvKQTGKkVAIIGAGPAGLACADVLTRNGVKAVV 174
Cdd:PRK12775 382 RVCPQETQCEAQCIIAKKHESVGIGRLERFVGDNArAKPVKPPRFS--KKLGK-VAICGSGPAGLAAAADLVKYGVDVTV 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 175 FDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSD--YDAVFLGVGTYQSMRGGLENE 252
Cdd:PRK12775 459 YEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGAGAPTFLGIPGE 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 253 DADGVYAALPFLiaNTKQLMGfGET---RDEPfVSMeGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEENMPGSR 329
Cdd:PRK12775 539 FAGQVYSANEFL--TRVNLMG-GDKfpfLDTP-ISL-GKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARI 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 330 REVKNAREEGVEFKFNVQPLGIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAeIVAGSEHIVPADAVIMAFGFRPHNMEWL 409
Cdd:PRK12775 614 EEIRHAKEEGIDFFFLHSPVEIYVDAEGSVRGMKVEEMELGEPDEKGRRKP-MPTGEFKDLECDTVIYALGTKANPIITQ 692
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131103 410 AKHSVELDSQGRIIAPEGSDNAFQTSN-PKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWL 470
Cdd:PRK12775 693 STPGLALNKWGNIAADDGKLESTQSTNlPGVFAGGDIVTGGATVILAMGAGRRAARSIATYL 754
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
44-470 |
1.38e-93 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 296.64 E-value: 1.38e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 44 ADRCLSCGNPyCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTLPEVCGRVCPQDrlCEGSCTLN--DEfgAVTIGN 121
Cdd:PRK12814 94 EQHCGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAP--CEEACRRHgvDE--PVSICA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 122 IERYINDKAFEMGWR--PDMSgvKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVM 199
Cdd:PRK12814 169 LKRYAADRDMESAERyiPERA--PKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVI 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 200 TRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQSMRGGLENEDADGVYAALPFL--IANTKQLmgfget 277
Cdd:PRK12814 247 DADIAPLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFLrnVALGTAL------ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 278 rdEPfvsmeGKRVVVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEENMPGSRREVKNAREEGVEFKFNVQPLGIE-VNGN 356
Cdd:PRK12814 321 --HP-----GKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIErSEGG 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 357 GKVSGVKMvrtEMGEPDAKGRRRAEIVAGSEHIVPADAVIMAFGfRPHNMEWLAKHSVELDSQGRIIAPEGSdnaFQTSN 436
Cdd:PRK12814 394 LELTAIKM---QQGEPDESGRRRPVPVEGSEFTLQADTVISAIG-QQVDPPIAEAAGIGTSRNGTVKVDPET---LQTSV 466
|
410 420 430
....*....|....*....|....*....|....
gi 16131103 437 PKIFAGGDIVRGSDLVVTAIAEGRKAADGIMNWL 470
Cdd:PRK12814 467 AGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFL 500
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
7-466 |
2.85e-82 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 265.86 E-value: 2.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 7 QFIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGnpYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQ 86
Cdd:PRK13984 147 ELLDLERVEMEEIPPEERVKSFIEIVKGYSKEQAMQEAARCVECG--ICTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 87 TNTLPEVCGRVCPQDrlCEGSCTLNDEFGAVTIGNIERYINDKAFEMGWRP--DMSGVKQtGKKVAIIGAGPAGLACADV 164
Cdd:PRK13984 225 TNPLSMVCGRVCTHK--CETVCSIGHRGEPIAIRWLKRYIVDNVPVEKYSEilDDEPEKK-NKKVAIVGSGPAGLSAAYF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 165 LTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDDLLSDYDAVFLGVGTYQS 244
Cdd:PRK13984 302 LATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLG 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 245 MRGGLENEDADGVYAALPFLIANTKQLMGFGEtrdEPFVSmegKRVVVLGGGDTAMDCVRTSVR----QGAK---HVTCa 317
Cdd:PRK13984 382 RSTRIPGTDHPDVIQALPLLREIRDYLRGEGP---KPKIP---RSLVVIGGGNVAMDIARSMARlqkmEYGEvnvKVTS- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 318 YRRDEENMPGSRREVKNAREEGVEFKFNVQPLGIEVNgNGKVSGVKMVR-TEMGepDAKGRRRAEIVAGSEHIVPADAVI 396
Cdd:PRK13984 455 LERTFEEMPADMEEIEEGLEEGVVIYPGWGPMEVVIE-NDKVKGVKFKKcVEVF--DEEGRFNPKFDESDQIIVEADMVV 531
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16131103 397 MAFGFRPhNMEWLA---KHSVELdSQGRIIapegSDNAFQTSNPKIFAGGDIVRGSDlVVTAIAEGRKAADGI 466
Cdd:PRK13984 532 EAIGQAP-DYSYLPeelKSKLEF-VRGRIL----TNEYGQTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGI 597
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
145-471 |
1.67e-81 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 256.07 E-value: 1.67e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 145 TGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEV----- 219
Cdd:PRK12770 17 TGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTKVccgep 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 220 ----------GRDVQLDDLLSDYDAVFLGVGTYQSMRGGLENEDADGVYAALPFLIAntKQLMGFGETRDEPFVSMEGKR 289
Cdd:PRK12770 97 lheeegdefvERIVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFR--IRAAKLGYLPWEKVPPVEGKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 290 VVVLGGGDTAMDCVRTSVRQGAKHVTCAYRRDEENMPGSRREVKNAREEGVEFKFNVQPlgIEVNGNGKVSGVKMVRTEM 369
Cdd:PRK12770 175 VVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTP--VRIIGEGRVEGVELAKMRL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 370 GEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPHNMEWLAKHSVELDSQGRIIApegsDNAFQTSNPKIFAGGDIVRGS 449
Cdd:PRK12770 253 GEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVV----DEKHMTSREGVFAAGDVVTGP 328
|
330 340
....*....|....*....|..
gi 16131103 450 DLVVTAIAEGRKAADGIMNWLE 471
Cdd:PRK12770 329 SKIGKAIKSGLRAAQSIHEWLD 350
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
59-466 |
3.04e-60 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 212.38 E-value: 3.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 59 CPVHNYIPNWLKLANEGRIFEAAELSHQTNTLPEVCGRVCPQDRLCEGSCTLNDEfgAVTIGNIERY-----------IN 127
Cdd:PRK12779 214 CPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTKR--PIEIGQLEWYlpqheklvnpnAN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 128 DKaFEMGWRPDMSGVKqtgKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGIPAFKLEKEVMTRRREIFT 207
Cdd:PRK12779 292 ER-FAGRISPWAAAVK---PPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 208 GMGIEFKLNTEVGRDVQLDDLLSD-YDAVFLGVG----TYQSMRGglenEDADGVYAALPFLianTK-QLM-GFGETRDE 280
Cdd:PRK12779 368 LLGGRFVKNFVVGKTATLEDLKAAgFWKIFVGTGaglpTFMNVPG----EHLLGVMSANEFL---TRvNLMrGLDDDYET 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 281 PFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAkHVTCAYRRDEENMPGSRREVKNAREEGVEFKFNVQPLgiEVNGNGK-- 358
Cdd:PRK12779 441 PLPEVKGKEVFVIGGGNTAMDAARTAKRLGG-NVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPR--EFIGDDHth 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 359 -VSGVKMVRTEMGEPDAKGRRRAEIVAGSEHiVPADAVIMAFGFRPHNMEWLAKHSVELDSQGRIIAPEGSDnafQTSNP 437
Cdd:PRK12779 518 fVTHALLDVNELGEPDKSGRRSPKPTGEIER-VPVDLVIMALGNTANPIMKDAEPGLKTNKWGTIEVEKGSQ---RTSIK 593
|
410 420
....*....|....*....|....*....
gi 16131103 438 KIFAGGDIVRGSDLVVTAIAEGRKAADGI 466
Cdd:PRK12779 594 GVYSGGDAARGGSTAIRAAGDGQAAAKEI 622
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
24-135 |
4.26e-60 |
|
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: 192.37 E-value: 4.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 24 RKIEFVEIYEPFSEGQAKAQADRCLSCGNPYCEWKCPVHNYIPNWLKLANEGRIFEAAELSHQTNTLPEVCGRVCPQDRL 103
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQERQ 80
|
90 100 110
....*....|....*....|....*....|...
gi 16131103 104 CEGSCTLN-DEFGAVTIGNIERYINDKAFEMGW 135
Cdd:pfam14691 81 CEGACVLGkKGFEPVAIGRLERFAADWARENGI 113
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
148-471 |
2.84e-38 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 141.41 E-value: 2.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRhPEIGGLLT--------FGIPAFKLEKEVMTRRREIFTGMGIEFKLnTEV 219
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPEGISGPELAERLREQAERFGAEILL-EEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 220 gRDVQLDD-----LLSDY-----DAVFLGVGTyQSMRGGLENEDA---DGVYAALpfliantkqlmgfgeTRDEPFvsME 286
Cdd:COG0492 80 -TSVDKDDgpfrvTTDDGteyeaKAVIIATGA-GPRKLGLPGEEEfegRGVSYCA---------------TCDGFF--FR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 287 GKRVVVLGGGDTAMDCVRTsVRQGAKHVTCAYRRDEenMPGSRREVKNARE-EGVEFKFNVQPlgIEVNGNGKVSGVKMV 365
Cdd:COG0492 141 GKDVVVVGGGDSALEEALY-LTKFASKVTLIHRRDE--LRASKILVERLRAnPKIEVLWNTEV--TEIEGDGRVEGVTLK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 366 RTEMGEpdakgrrraeivagsEHIVPADAVIMAFGFRPHNmEWLAKHSVELDSQGRIIApegsDNAFQTSNPKIFAGGDI 445
Cdd:COG0492 216 NVKTGE---------------EKELEVDGVFVAIGLKPNT-ELLKGLGLELDEDGYIVV----DEDMETSVPGVFAAGDV 275
|
330 340
....*....|....*....|....*..
gi 16131103 446 VRGS-DLVVTAIAEGRKAADGIMNWLE 471
Cdd:COG0492 276 RDYKyRQAATAAGEGAIAALSAARYLE 302
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
147-459 |
8.95e-28 |
|
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: 112.41 E-value: 8.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKAVVFDR---HPEIGGLLTFGIPA-------FKLEKEVMTRRREIFTGM--GIEFK 214
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDegtCPYGGCVLSKALLGaaeapeiASLWADLYKRKEEVVKKLnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 215 LNTEV------GRDVQLDDLLSD------YDAVFLGVGTyQSMRGGLENEDaDGVYAALPFLiantkqlmgfgETRDEPF 282
Cdd:pfam07992 81 LGTEVvsidpgAKKVVLEELVDGdgetitYDRLVIATGA-RPRLPPIPGVE-LNVGFLVRTL-----------DSAEALR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 283 VSMEGKRVVVLGGGDTAMDCVRTSVRQGaKHVTCAYRRDE----ENMPGSRREVKNAREEGVEFKFNVQPLGIEVNGNGk 358
Cdd:pfam07992 148 LKLLPKRVVVVGGGYIGVELAAALAKLG-KEVTLIEALDRllraFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDG- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 359 vsgvkmvrtemgepdakgrrrAEIVAGSEHIVPADAVIMAFGFRPhNMEWLAKHSVELDSQGRIIApegsDNAFQTSNPK 438
Cdd:pfam07992 226 ---------------------VEVILKDGTEIDADLVVVAIGRRP-NTELLEAAGLELDERGGIVV----DEYLRTSVPG 279
|
330 340
....*....|....*....|..
gi 16131103 439 IFAGGDI-VRGSDLVVTAIAEG 459
Cdd:pfam07992 280 IYAAGDCrVGGPELAQNAVAQG 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
148-470 |
2.48e-24 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 102.71 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGI----PAFK---LEKEVMTRRREIFTGMGIEFKLNtevg 220
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEvenyPGFPegiSGPELMEKMKEQAVKFGAEIIYE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 221 rDVQLDDLLSDYDAVFLGVG-TYQSM-----------RGGLENEDAdgvyaalpfliantkqLMGFG----ETRDEPFvs 284
Cdd:TIGR01292 77 -EVIKVDKSDRPFKVYTGDGkEYTAKaviiatgasarKLGIPGEDE----------------FWGRGvsycATCDGPF-- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 285 MEGKRVVVLGGGDTAMD--CVRTSVrqgAKHVTCAYRRDeenmpGSRRE---VKNARE-EGVEFKFNVQPlgIEVNGNGK 358
Cdd:TIGR01292 138 FKNKEVAVVGGGDSAIEeaLYLTRI---AKKVTLVHRRD-----KFRAEkilLDRLKKnPKIEFLWNSTV--EEIVGDNK 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 359 VSGVKMVRTEMGEpdakgrrraeivagsEHIVPADAVIMAFGFRPHNMewLAKHSVELDSQGRIIAPEGSdnafQTSNPK 438
Cdd:TIGR01292 208 VEGVKIKNTVTGE---------------EEELEVDGVFIAIGHEPNTE--LLKGLLELDENGYIVTDEGM----RTSVPG 266
|
330 340 350
....*....|....*....|....*....|...
gi 16131103 439 IFAGGDIV-RGSDLVVTAIAEGRKAADGIMNWL 470
Cdd:TIGR01292 267 VFAAGDVRdKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
149-468 |
7.99e-17 |
|
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: 82.44 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 149 VAIIGAGPAGLACADVLTRNGVKAVVFDRHPeIGG------------LL-------------TFGIPAFKLE---KEVMT 200
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGR-LGGtclnvgcipskaLLhaaevahearhaaEFGISAGAPSvdwAALMA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 201 RRREIFTGM--GIEFKLNtevGRDVqldDLLSDYdAVFLGVGTYQsmrggLENEDadgVYAALPFLIA-----NTKQLMG 273
Cdd:COG1249 85 RKDKVVDRLrgGVEELLK---KNGV---DVIRGR-ARFVDPHTVE-----VTGGE---TLTADHIVIAtgsrpRVPPIPG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 274 FGETR----DEpFVSME--GKRVVVLGGGDTAMDCVrtSV--RQGAKhVTCAYRR-------DEEnmpgSRREVKNA-RE 337
Cdd:COG1249 150 LDEVRvltsDE-ALELEelPKSLVVIGGGYIGLEFA--QIfaRLGSE-VTLVERGdrllpgeDPE----ISEALEKAlEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 338 EGVEFKFNVQPLGIEVNGNGKVsgvkmVRTEMGepdakgrrraeivaGSEHIVPADAVIMAFGFRPhNMEW--LAKHSVE 415
Cdd:COG1249 222 EGIDILTGAKVTSVEKTGDGVT-----VTLEDG--------------GGEEAVEADKVLVATGRRP-NTDGlgLEAAGVE 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 16131103 416 LDSQGRIIApegsDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMN 468
Cdd:COG1249 282 LDERGGIKV----DEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAENILG 330
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
149-402 |
8.72e-16 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 79.36 E-value: 8.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 149 VAIIGAGPAGLACADVLTR--NGVKAVVFDRHPEIGGLLTFGI-PAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQL 225
Cdd:PLN02852 29 VCVVGSGPAGFYTADKLLKahDGARVDIIERLPTPFGLVRSGVaPDHPETKNVTNQFSRVATDDRVSFFGNVTLGRDVSL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 226 DDLLSDYDAVFLGVGTYQSMRGGLENEDADGVYAALPFLIANTkqlmGFGETRDEPFVSMEGKRVVVLGGGDTAMDCVRT 305
Cdd:PLN02852 109 SELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYN----GHPDCVHLPPDLKSSDTAVVLGQGNVALDCARI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 306 SVR--------------------QGAKHVTCAYRR-----------------------------------DEENMPGSR- 329
Cdd:PLN02852 185 LLRptdelastdiaehalealrgSSVRKVYLVGRRgpvqaactakelrellglknvrvrikeadltlspeDEEELKASRp 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 330 ----RE--VKNAREEG---------VEFKFNVQPLGIEV--NGNGKVSGVKMVRTEMgEPDAKGRRRAEIVAGSEHIVPA 392
Cdd:PLN02852 265 krrvYEllSKAAAAGKcapsggqreLHFVFFRNPTRFLDsgDGNGHVAGVKLERTVL-EGAAGSGKQVAVGTGEFEDLPC 343
|
330
....*....|
gi 16131103 393 DAVIMAFGFR 402
Cdd:PLN02852 344 GLVLKSIGYK 353
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
147-467 |
1.38e-14 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 75.18 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKA--VVF--DRHP---------EIGGLLTfgipafklEKEVMTRRREIFTGMGIEF 213
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDPDGeiTVIgaEPHPpynrpplskVLAGETD--------EEDLLLRPADFYEENGIDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 214 KLNTEV------GRDVQLDDLLS-DYDAVFLGVGTYqSMRGGLENEDADGVYAalpfL--IANTKQLMGFGEtrdepfvs 284
Cdd:COG1251 74 RLGTRVtaidraARTVTLADGETlPYDKLVLATGSR-PRVPPIPGADLPGVFT----LrtLDDADALRAALA-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 285 mEGKRVVVLGGG----DTAMDC----VRTSVRQGAKHVtcaYRR--DEEnmpGSRREVKNAREEGVEFKFNVQPLGIEvn 354
Cdd:COG1251 141 -PGKRVVVIGGGliglEAAAALrkrgLEVTVVERAPRL---LPRqlDEE---AGALLQRLLEALGVEVRLGTGVTEIE-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 355 GNGKVSGVKMvrtemgepdAKGRRraeivagsehiVPADAVIMAFGFRPhNMEWLAKHSVELDsqGRIIApegsDNAFQT 434
Cdd:COG1251 212 GDDRVTGVRL---------ADGEE-----------LPADLVVVAIGVRP-NTELARAAGLAVD--RGIVV----DDYLRT 264
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 16131103 435 SNPKIFAGGDIV---------RGSDLVVTAIAEGRKAADGIM 467
Cdd:COG1251 265 SDPDIYAAGDCAehpgpvygrRVLELVAPAYEQARVAAANLA 306
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
149-468 |
3.56e-12 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 68.28 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 149 VAIIGAGPAGLACADVLTRNGVKAVVFDRHP------------------------EIGGLLTFGIPAFKLE---KEVMTR 201
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPlggtclnvgcipskaliaaaeafhEAKHAEEFGIHADGPKidfKKVMAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 202 RREI---FTGMGIEF--KLNTE-----VGR--D---VQLDDLLSDYDAVFLGVGTYQSMRGGLENEDADGvyaalpfLIA 266
Cdd:PRK06292 86 VRRErdrFVGGVVEGleKKPKIdkikgTARfvDpntVEVNGERIEAKNIVIATGSRVPPIPGVWLILGDR-------LLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 267 NTKQLmgfgETRDEPfvsmegKRVVVLGGG----DTAmdcvrtSV--RQGAKhVTCAYRRDEEnMPGSRREVKN-AR--- 336
Cdd:PRK06292 159 SDDAF----ELDKLP------KSLAVIGGGviglELG------QAlsRLGVK-VTVFERGDRI-LPLEDPEVSKqAQkil 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 337 EEGVEFKFNVQPLGIEVNGNGKVsgvkmvrtemgepdakgrrRAEIVAGSEHIVPADAVIMAFGFRPhNMEWL--AKHSV 414
Cdd:PRK06292 221 SKEFKIKLGAKVTSVEKSGDEKV-------------------EELEKGGKTETIEADYVLVATGRRP-NTDGLglENTGI 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 16131103 415 ELDSQGRIIApegsDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGIMN 468
Cdd:PRK06292 281 ELDERGRPVV----DEHTQTSVPGIYAAGDVNGKPPLLHEAADEGRIAAENAAG 330
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
173-467 |
6.77e-12 |
|
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: 66.37 E-value: 6.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 173 VVFDRHPEIG----GLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEV------GRDVQLDD--LLSdYDAVFLGVG 240
Cdd:COG0446 9 TVIEKGPHHSyqpcGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVtaidpeAKTVTLRDgeTLS-YDKLVLATG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 241 TyQSMRGGLENEDADGVYAALPFLIA-NTKQLMGfgetrdepfvSMEGKRVVVLGGG------DTAMdcvrtsVRQGAKh 313
Cdd:COG0446 88 A-RPRPPPIPGLDLPGVFTLRTLDDAdALREALK----------EFKGKRAVVIGGGpiglelAEAL------RKRGLK- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 314 VTCAYRRDEEnMPGSRREV-----KNAREEGVEFKFNVQPLGIEvnGNGKVSgvkmVRTEMGEpdakgrrraeivagseh 388
Cdd:COG0446 150 VTLVERAPRL-LGVLDPEMaalleEELREHGVELRLGETVVAID--GDDKVA----VTLTDGE----------------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 389 IVPADAVIMAFGFRPhNMEWLAKHSVELDSQGRIIApegsDNAFQTSNPKIFAGGDIVRGSDLVV----------TAIAE 458
Cdd:COG0446 206 EIPADLVVVAPGVRP-NTELAKDAGLALGERGWIKV----DETLQTSDPDVYAAGDCAEVPHPVTgktvyiplasAANKQ 280
|
....*....
gi 16131103 459 GRKAADGIM 467
Cdd:COG0446 281 GRVAAENIL 289
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
147-444 |
6.14e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 61.21 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKA--VVFDRHPEIG----GLLTFGIPAFKLEKEVMTRRREIFTGMGIEFKLNTEVG 220
Cdd:PRK09564 1 MKIIIIGGTAAGMSAAAKAKRLNKELeiTVYEKTDIVSfgacGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHEVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 221 -----------RDVQLDDLLSD-YDAVFLGVGTyQSMRGGLENEDADGVYaalpflianTKQLMGFGETRDEPFVSMEGK 288
Cdd:PRK09564 81 kvdaknktitvKNLKTGSIFNDtYDKLMIATGA-RPIIPPIKNINLENVY---------TLKSMEDGLALKELLKDEEIK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 289 RVVVLGGGDTAMDCVRTSVRQGaKHVTcAYRRDEENMPGS-RREV-----KNAREEGVEFKFNVQPLgiEVNGNGKVSGV 362
Cdd:PRK09564 151 NIVIIGAGFIGLEAVEAAKHLG-KNVR-IIQLEDRILPDSfDKEItdvmeEELRENGVELHLNEFVK--SLIGEDKVEGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 363 kmvRTEMGEPDAkgrrraeivagsehivpaDAVIMAFGFRPhNMEWLAKHSVELDSQGRIIApegsDNAFQTSNPKIFAG 442
Cdd:PRK09564 227 ---VTDKGEYEA------------------DVVIVATGVKP-NTEFLEDTGLKTLKNGAIIV----DEYGETSIENIYAA 280
|
..
gi 16131103 443 GD 444
Cdd:PRK09564 281 GD 282
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
149-320 |
9.38e-10 |
|
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: 60.26 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 149 VAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGL--------LTFGIPAFKL---------EKEVMTRRREIF----- 206
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTwrdnrypgLRLDTPSHLYslpffpnwsDDPDFPTGDEILaylea 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 207 ----TGMGIEFKLNTEVgRDVQLDD-------LLSD-----YDAVFLGVGTYQsmrgglenedaDGVYAALPfliantkq 270
Cdd:COG2072 89 yadkFGLRRPIRFGTEV-TSARWDEadgrwtvTTDDgetltARFVVVATGPLS-----------RPKIPDIP-------- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131103 271 lmgfGETR-----------DEPfVSMEGKRVVVLGGGDTAMDCVRTSVRQgAKHVTCAYRR 320
Cdd:COG2072 149 ----GLEDfageqlhsadwRNP-VDLAGKRVLVVGTGASAVQIAPELARV-AAHVTVFQRT 203
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
148-196 |
8.18e-09 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 57.59 E-value: 8.18e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLL-TFGIPAFKLEK 196
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIER 50
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
147-471 |
2.12e-08 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 55.91 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 147 KKVAIIGAGPAGLACADVLTRN---GVKAVVFDRHPE----------IGGLLTFGipafklekEVMTRRREIFTGMGIEF 213
Cdd:COG1252 2 KRIVIVGGGFAGLEAARRLRKKlggDAEVTLIDPNPYhlfqpllpevAAGTLSPD--------DIAIPLRELLRRAGVRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 214 ------KLNTEvGRDVQLDDLLS-DYDAVFLGVGTYQSMRG--GLEnEDADGVY---AALPFLiantKQLMGFGETRDEP 281
Cdd:COG1252 74 iqgevtGIDPE-ARTVTLADGRTlSYDYLVIATGSVTNFFGipGLA-EHALPLKtleDALALR----ERLLAAFERAERR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 282 fvsmEGKRVVVLGGGDT------AMD------CVRTSVRQGAKHVTCAYRRDE--ENMPG-SRREVKNAREEgvefkfnv 346
Cdd:COG1252 148 ----RLLTIVVVGGGPTgvelagELAellrklLRYPGIDPDKVRITLVEAGPRilPGLGEkLSEAAEKELEK-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 347 qpLGIEVNGNGKVSGVkmvrtemgEPDAkgrrraeIVAGSEHIVPADAVIMAFGFRPHnmEWLAKHSVELDSQGRIIApe 426
Cdd:COG1252 216 --RGVEVHTGTRVTEV--------DADG-------VTLEDGEEIPADTVIWAAGVKAP--PLLADLGLPTDRRGRVLV-- 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 16131103 427 gsDNAFQT-SNPKIFAGGDIVRGSD--------LVVTAIAEGRKAADGIMNWLE 471
Cdd:COG1252 275 --DPTLQVpGHPNVFAIGDCAAVPDpdgkpvpkTAQAAVQQAKVLAKNIAALLR 326
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
147-183 |
3.61e-08 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 54.88 E-value: 3.61e-08
10 20 30
....*....|....*....|....*....|....*..
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGG 183
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
151-445 |
4.14e-08 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 55.21 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 151 IIGAGPAGLACADVLTRNGVKAVVFDRHPeIGG-LLTFG-IP---------AFKLE------------------KEVMTR 201
Cdd:PRK06370 10 VIGAGQAGPPLAARAAGLGMKVALIERGL-LGGtCVNTGcVPtktliasarAAHLArraaeygvsvggpvsvdfKAVMAR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 202 RREI-----------FTGM-GIEFKLNT---EVGRDVQLDDLLSDYDAVFLGVGTyqsmRgglenedadgvyAALPflia 266
Cdd:PRK06370 89 KRRIrarsrhgseqwLRGLeGVDVFRGHarfESPNTVRVGGETLRAKRIFINTGA----R------------AAIP---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 267 ntkQLMGFGETR---DEPFVSMEG--KRVVVLGGGDTAMDCVRTSVRQGAKhVTCAyRRDEENMPGSRREVKNA-----R 336
Cdd:PRK06370 149 ---PIPGLDEVGyltNETIFSLDElpEHLVIIGGGYIGLEFAQMFRRFGSE-VTVI-ERGPRLLPREDEDVAAAvreilE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 337 EEGVEFKFNVQPLGIEVNGNGKVSGVKmvrtemgepdakgrrraeiVAGSEHIVPADAVIMAFGFRPhNMEW--LAKHSV 414
Cdd:PRK06370 224 REGIDVRLNAECIRVERDGDGIAVGLD-------------------CNGGAPEITGSHILVAVGRVP-NTDDlgLEAAGV 283
|
330 340 350
....*....|....*....|....*....|.
gi 16131103 415 ELDSQGRIIApegsDNAFQTSNPKIFAGGDI 445
Cdd:PRK06370 284 ETDARGYIKV----DDQLRTTNPGIYAAGDC 310
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
147-184 |
1.20e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 53.74 E-value: 1.20e-07
10 20 30
....*....|....*....|....*....|....*...
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGL 184
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
147-183 |
1.33e-07 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 53.70 E-value: 1.33e-07
10 20 30
....*....|....*....|....*....|....*..
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGG 183
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
151-183 |
1.43e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 48.30 E-value: 1.43e-07
10 20 30
....*....|....*....|....*....|...
gi 16131103 151 IIGAGPAGLACADVLTRNGVKAVVFDRHPEIGG 183
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGG 33
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
143-257 |
1.57e-07 |
|
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: 52.71 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 143 KQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIgglltfgipAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRD 222
Cdd:pfam07992 149 KLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL---------LRAFDEEISAALEKALEKNGVEVRLGTSVKEI 219
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 16131103 223 VQLDDLLS---------DYDAVFLGVGtyqsMRGGLENEDADGV 257
Cdd:pfam07992 220 IGDGDGVEvilkdgteiDADLVVVAIG----RRPNTELLEAAGL 259
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
147-185 |
1.92e-07 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 53.30 E-value: 1.92e-07
10 20 30
....*....|....*....|....*....|....*....
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLL 185
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
148-227 |
2.83e-07 |
|
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: 47.97 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGlltfgipafKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQLDD 227
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLP---------GFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGD 71
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
156-443 |
7.34e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 50.69 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 156 PAGLACADVLTRNGVKAVV----------FDRHPEIGGLLT-------FGI-----------PAFKLEKEVMTRR----- 202
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDYLilekgnignsFYRYPTHMTFFSpsftsngFGIpdlnaispgtsPAFTFNREHPSGNeyaey 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 203 -REIFTGMGIEFKLNTEVgRDVQLDDLL-------SDYDAVFLGVGTyqsmrgglenedadGVYAalpflIANtkqLMGF 274
Cdd:pfam13738 81 lRRVADHFELPINLFEEV-TSVKKEDDGfvvttskGTYQARYVIIAT--------------GEFD-----FPN---KLGV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 275 GETR-----DEPFVSMEGKRVVVLGGGDTAMDCVRTSVRQGAkHVTCAYRRDEENMPGS----------RREVKNAREEG 339
Cdd:pfam13738 138 PELPkhysyVKDFHPYAGQKVVVIGGYNSAVDAALELVRKGA-RVTVLYRGSEWEDRDSdpsyslspdtLNRLEELVKNG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 340 VefkfnvqplgIEVNGNGKVsgvkmvrTEMGEPDAKGRRRAEivAGSEHIVPaDAVIMAFGFRPhNMEWLAKHSVELDSQ 419
Cdd:pfam13738 217 K----------IKAHFNAEV-------KEITEVDVSYKVHTE--DGRKVTSN-DDPILATGYHP-DLSFLKKGLFELDED 275
|
330 340
....*....|....*....|....
gi 16131103 420 GRiiaPEGSDNAFQTSNPKIFAGG 443
Cdd:pfam13738 276 GR---PVLTEETESTNVPGLFLAG 296
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
143-240 |
9.44e-07 |
|
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: 50.58 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 143 KQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGlltfgipafKLEKEVMTRRREIFTGMGIEFKLNTEV--- 219
Cdd:COG0446 121 EFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLG---------VLDPEMAALLEEELREHGVELRLGETVvai 191
|
90 100
....*....|....*....|....*...
gi 16131103 220 -GRD---VQLDD---LlsDYDAVFLGVG 240
Cdd:COG0446 192 dGDDkvaVTLTDgeeI--PADLVVVAPG 217
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
289-359 |
1.13e-06 |
|
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: 46.04 E-value: 1.13e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131103 289 RVVVLGGGDTAMDCVRTSVRQGaKHVTCAYRRDE----ENMPGSRREVKNAREEGVEFKFNVQPLGIEVNGNGKV 359
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLG-SKVTVVERRDRllpgFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVV 74
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
148-253 |
1.14e-06 |
|
adrenodoxin reductase; Provisional
Pssm-ID: 240308 Cd Length: 506 Bit Score: 51.04 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 148 KVAIIGAGPAGLACADVLTRN-GVKAVVFDRHPEIGGLLTFGI-PAFKLEKEVMTRRREIFTGMGIEFKLNTEVGRDVQL 225
Cdd:PTZ00188 41 KVGIIGAGPSALYCCKHLLKHeRVKVDIFEKLPNPYGLIRYGVaPDHIHVKNTYKTFDPVFLSPNYRFFGNVHVGVDLKM 120
|
90 100
....*....|....*....|....*....
gi 16131103 226 DDLLSDYDAVFLGVGTYQ-SMRGGLENED 253
Cdd:PTZ00188 121 EELRNHYNCVIFCCGASEvSIPIGQQDED 149
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
144-183 |
1.58e-06 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 50.30 E-value: 1.58e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 16131103 144 QTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGG 183
Cdd:COG1231 5 ARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
288-464 |
1.98e-06 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 50.15 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 288 KRVVVLGGGDTAMD--CVRTSVrqGAKhVTCAYRRDE--ENMPGSRRE--VKNAREEGVEFKFNVQPLGIEVNGNGKVSg 361
Cdd:PRK06116 168 KRVAVVGAGYIAVEfaGVLNGL--GSE-THLFVRGDAplRGFDPDIREtlVEEMEKKGIRLHTNAVPKAVEKNADGSLT- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 362 vkmVRTEMGEpdakgrrraeivagsehIVPADAVIMAFGFRP--HNMEwLAKHSVELDSQGRIIApegsDNAFQTSNPKI 439
Cdd:PRK06116 244 ---LTLEDGE-----------------TLTVDCLIWAIGREPntDGLG-LENAGVKLNEKGYIIV----DEYQNTNVPGI 298
|
170 180
....*....|....*....|....*
gi 16131103 440 FAGGDIVRGSDLVVTAIAEGRKAAD 464
Cdd:PRK06116 299 YAVGDVTGRVELTPVAIAAGRRLSE 323
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
148-182 |
3.41e-06 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 48.78 E-value: 3.41e-06
10 20 30
....*....|....*....|....*....|....*
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIG 182
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPR 39
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
148-213 |
4.01e-06 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 48.55 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIG--------GLLTFGI------PAFKLEKEVMTRRREIFTGMGIEF 213
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLrylepsELARLALEALDLWEELEEELGIDC 80
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
150-182 |
5.60e-06 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 48.51 E-value: 5.60e-06
10 20 30
....*....|....*....|....*....|...
gi 16131103 150 AIIGAGPAGLACADVLTRNGVKAVVFDRHPEIG 182
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
145-184 |
7.96e-06 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 48.32 E-value: 7.96e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 16131103 145 TGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGL 184
Cdd:PLN02172 9 NSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGL 48
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
141-177 |
9.31e-06 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 47.80 E-value: 9.31e-06
10 20 30
....*....|....*....|....*....|....*..
gi 16131103 141 GVKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDR 177
Cdd:COG2509 25 GIPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
145-183 |
1.38e-05 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 47.16 E-value: 1.38e-05
10 20 30
....*....|....*....|....*....|....*....
gi 16131103 145 TGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGG 183
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PRK08243 |
PRK08243 |
4-hydroxybenzoate 3-monooxygenase; Validated |
148-177 |
2.48e-05 |
|
4-hydroxybenzoate 3-monooxygenase; Validated
Pssm-ID: 236198 [Multi-domain] Cd Length: 392 Bit Score: 46.33 E-value: 2.48e-05
10 20 30
....*....|....*....|....*....|
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDR 177
Cdd:PRK08243 4 QVAIIGAGPAGLLLGQLLHLAGIDSVVLER 33
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
147-182 |
2.82e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 46.42 E-value: 2.82e-05
10 20 30
....*....|....*....|....*....|....*.
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIG 182
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
279-463 |
3.38e-05 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 46.30 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 279 DEPFvsMEGKRVVVLGGGDT----AMDCVrtsvrqG-AKHVTCAyrrdeENMPGSR---------REVKNareegVEFKF 344
Cdd:PRK15317 345 DGPL--FKGKRVAVIGGGNSgveaAIDLA------GiVKHVTVL-----EFAPELKadqvlqdklRSLPN-----VTIIT 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 345 NVQPlgIEVNGNG-KVSGVKMVRTEMGEpdakgrrraeivagsEHIVPADAVIMAFGFRPhNMEWLaKHSVELDSQGRII 423
Cdd:PRK15317 407 NAQT--TEVTGDGdKVTGLTYKDRTTGE---------------EHHLELEGVFVQIGLVP-NTEWL-KGTVELNRRGEII 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131103 424 ApegsDNAFQTSNPKIFAGGDIvrgSDL----VVTAIAEGRKAA 463
Cdd:PRK15317 468 V----DARGATSVPGVFAAGDC---TTVpykqIIIAMGEGAKAA 504
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
149-180 |
4.61e-05 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 45.70 E-value: 4.61e-05
10 20 30
....*....|....*....|....*....|..
gi 16131103 149 VAIIGAGPAGLACADVLTRNGVKAVVFDRHPE 180
Cdd:PRK09126 6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQPL 37
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
149-188 |
1.04e-04 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 44.52 E-value: 1.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 16131103 149 VAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFG 188
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLTSG 41
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
146-180 |
1.97e-04 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 43.53 E-value: 1.97e-04
10 20 30
....*....|....*....|....*....|....*
gi 16131103 146 GKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPE 180
Cdd:COG0771 4 GKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPA 38
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
3-60 |
2.12e-04 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 43.71 E-value: 2.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131103 3 QNVYQFIDLQRVDPPKKPLKIRKIEFVEIYEPFSEGQAKAQADRCLSCGNPY----CEWKCP 60
Cdd:PRK12771 462 LNLWYFTDAPRAQRPELDADERVGDFDEVLGGLTEEEARQEAARCLSCGNCFecdnCYGACP 523
|
|
| PTDH |
cd12157 |
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ... |
123-179 |
2.25e-04 |
|
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.
Pssm-ID: 240634 [Multi-domain] Cd Length: 318 Bit Score: 43.04 E-value: 2.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131103 123 ERYINDKAFEmGWRPDMSGVKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHP 179
Cdd:cd12157 122 DRFVRSGKFG-GWRPKFYGTGLDGKTVGILGMGALGRAIARRLSGFGATLLYYDPHP 177
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
146-183 |
3.19e-04 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 43.32 E-value: 3.19e-04
10 20 30
....*....|....*....|....*....|....*...
gi 16131103 146 GKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGG 183
Cdd:PLN02976 693 RKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
148-180 |
3.56e-04 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 42.70 E-value: 3.56e-04
10 20 30
....*....|....*....|....*....|...
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHPE 180
Cdd:pfam01494 3 DVLIVGGGPAGLMLALLLARAGVRVVLVERHAT 35
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
149-183 |
4.84e-04 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 41.69 E-value: 4.84e-04
10 20 30
....*....|....*....|....*....|....*.
gi 16131103 149 VAIIGAGPAGLACADVLTRN-GVKAVVFDRHPEIGG 183
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLAKNrGLKVAIIERSVSPGG 55
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
147-182 |
5.32e-04 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 42.25 E-value: 5.32e-04
10 20 30
....*....|....*....|....*....|....*....
gi 16131103 147 KKVAIIGAGPAGLACADVLTRN---GVKAVVFDRHPEIG 182
Cdd:COG4529 6 KRIAIIGGGASGTALAIHLLRRapePLRITLFEPRPELG 44
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
125-219 |
5.47e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 42.09 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 125 YINDKAFEMGWRPdmsgvkqtgKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLltfgipafkLEKEVMTRRRE 204
Cdd:PRK06292 157 LTSDDAFELDKLP---------KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPL---------EDPEVSKQAQK 218
|
90
....*....|....*
gi 16131103 205 IFTGMgIEFKLNTEV 219
Cdd:PRK06292 219 ILSKE-FKIKLGAKV 232
|
|
| PRK06126 |
PRK06126 |
hypothetical protein; Provisional |
148-180 |
6.26e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235704 [Multi-domain] Cd Length: 545 Bit Score: 42.29 E-value: 6.26e-04
10 20 30
....*....|....*....|....*....|...
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHPE 180
Cdd:PRK06126 9 PVLIVGGGPVGLALALDLGRRGVDSILVERKDG 41
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
285-444 |
7.36e-04 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 41.83 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 285 MEGKRVVVLGGG----DTAMDCVRTsvrqgAKHVT---CAYRRDEENMPG--SRREVKNAREEGVEFKFNVQPLGIEVNG 355
Cdd:PRK04965 139 RDAQRVLVVGGGligtELAMDLCRA-----GKAVTlvdNAASLLASLMPPevSSRLQHRLTEMGVHLLLKSQLQGLEKTD 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 356 NGKvsgvkmvrtemgepdakgrrRAEIVAGSEHIVpaDAVIMAFGFRPhNMEwLAKHSvELDSQGRIIApegsDNAFQTS 435
Cdd:PRK04965 214 SGI--------------------RATLDSGRSIEV--DAVIAAAGLRP-NTA-LARRA-GLAVNRGIVV----DSYLQTS 264
|
....*....
gi 16131103 436 NPKIFAGGD 444
Cdd:PRK04965 265 APDIYALGD 273
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
136-182 |
7.39e-04 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 41.78 E-value: 7.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 16131103 136 RPDMSGVKQTGKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIG 182
Cdd:PRK08132 13 HADQDADDPARHPVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLS 59
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
277-466 |
8.22e-04 |
|
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: 41.88 E-value: 8.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 277 TRDEPFVSMEG-KRVVVLGGGDTAMDC--VRTSVRQGAKHVTCAYRRD------EENMpgsRREV-KNAREEGVEFKFNV 346
Cdd:TIGR01423 176 SSNEAFYLDEPpRRVLTVGGGFISVEFagIFNAYKPRGGKVTLCYRNNmilrgfDSTL---RKELtKQLRANGINIMTNE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 347 QPLGIEVNGNGKvsgvKMVRTEMGEPdakgrrraeivagsehiVPADAVIMAFGFRPHNmewlakHSVELDSQGRIIAPE 426
Cdd:TIGR01423 253 NPAKVTLNADGS----KHVTFESGKT-----------------LDVDVVMMAIGRVPRT------QTLQLDKVGVELTKK 305
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16131103 427 GS---DNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGI 466
Cdd:TIGR01423 306 GAiqvDEFSRTNVPNIYAIGDVTDRVMLTPVAINEGAAFVDTV 348
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
147-253 |
8.53e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 41.66 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGlltfgipafKLEKEVMTRRREIFTGMGIEFKLN---TEVGRD- 222
Cdd:PRK07251 158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILP---------REEPSVAALAKQYMEEDGITFLLNahtTEVKNDg 228
|
90 100 110
....*....|....*....|....*....|....*.
gi 16131103 223 ----VQLDDLLSDYDAVFLGVGTYQSMRG-GLENED 253
Cdd:PRK07251 229 dqvlVVTEDETYRFDALLYATGRKPNTEPlGLENTD 264
|
|
| Malic_M |
smart00919 |
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the ... |
139-241 |
9.94e-04 |
|
Malic enzyme, NAD binding domain; Malic enzymes (malate oxidoreductases) catalyse the oxidative decarboxylation of malate to form pyruvate.
Pssm-ID: 214912 Cd Length: 231 Bit Score: 40.48 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 139 MSGVKQTGK-----KVAIIGAGPAGLACADVLTRNGVKA---VVFDRHpeigGLLTFGipafklEKEVMTRRREiftgmg 210
Cdd:smart00919 13 LNALKITGKkledqRIVVNGAGAAGIGIAKLLVAAGVKRkniWLVDSK----GLLTKG------REDNLNPYKK------ 76
|
90 100 110
....*....|....*....|....*....|.
gi 16131103 211 iEFKLNTEVGRDVQLDDLLSDYDaVFLGVGT 241
Cdd:smart00919 77 -PFARKTNERETGTLEEAVKGAD-VLIGVSG 105
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
148-179 |
1.00e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 41.43 E-value: 1.00e-03
10 20 30
....*....|....*....|....*....|..
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHP 179
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERGR 35
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
149-181 |
1.04e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 41.43 E-value: 1.04e-03
10 20 30
....*....|....*....|....*....|...
gi 16131103 149 VAIIGAGPAGLACADVLTRNGVKAVVFDRHPEI 181
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
151-463 |
1.11e-03 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 41.30 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 151 IIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTF-G-IPAFKLEKEVM----TRRREIFTGMGiefklnteVGRDVQ 224
Cdd:PRK05249 10 VIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTHtGtIPSKALREAVLrligFNQNPLYSSYR--------VKLRIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 225 LDDLLSDYDAVflgVGTYQSMRGG---------------------LENEDADG---VYAALPFLIA-NTK----QLMGFG 275
Cdd:PRK05249 82 FADLLARADHV---INKQVEVRRGqyernrvdliqgrarfvdphtVEVECPDGeveTLTADKIVIAtGSRpyrpPDVDFD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 276 ETR----DEpFVSMEG--KRVVVLGGGD---------TAMDCvrtsvrqgakHVTCAYRRDeenmpgsR------REVKN 334
Cdd:PRK05249 159 HPRiydsDS-ILSLDHlpRSLIIYGAGVigceyasifAALGV----------KVTLINTRD-------RllsfldDEISD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 335 A-----REEGVEFKFNVQPLGIEVNGNGKVsgvkmvrTEMgepdAKGRRraeivagsehiVPADAVIMAFGfRPHNMEWL 409
Cdd:PRK05249 221 AlsyhlRDSGVTIRHNEEVEKVEGGDDGVI-------VHL----KSGKK-----------IKADCLLYANG-RTGNTDGL 277
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131103 410 AKHSV--ELDSQGRIIApegsDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAA 463
Cdd:PRK05249 278 NLENAglEADSRGQLKV----NENYQTAVPHIYAVGDVIGFPSLASASMDQGRIAA 329
|
|
| FMO-like |
pfam00743 |
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ... |
146-187 |
1.15e-03 |
|
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases.
Pssm-ID: 395602 [Multi-domain] Cd Length: 531 Bit Score: 41.30 E-value: 1.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 16131103 146 GKKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTF 187
Cdd:pfam00743 1 AKKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRF 42
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
350-466 |
1.22e-03 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 41.28 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 350 GIEVNGNGKVSGVkmvrtemgEPDAKGRRRAEIVAGSEHIVPADAVIMAFGFRPhNME--WLAKHSVELDsQGRIIApeg 427
Cdd:PRK06416 227 GIKIKTGAKAKKV--------EQTDDGVTVTLEDGGKEETLEADYVLVAVGRRP-NTEnlGLEELGVKTD-RGFIEV--- 293
|
90 100 110
....*....|....*....|....*....|....*....
gi 16131103 428 sDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAADGI 466
Cdd:PRK06416 294 -DEQLRTNVPNIYAIGDIVGGPMLAHKASAEGIIAAEAI 331
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
149-418 |
1.32e-03 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 41.12 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 149 VAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGLLTFGipafklekevmtrrreiftGMGIEFKLNTEVGRDvqlddl 228
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATAWS-------------------SGGIDALGNPPQGGI------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 229 lSDYDAVFlgvgtYQSMRGGLENEDADGVYAalpfLIANTKQLMGFGETRDEPFVSMEGKRVVV--LGGgdtamdcvrts 306
Cdd:pfam00890 57 -DSPELHP-----TDTLKGLDELADHPYVEA----FVEAAPEAVDWLEALGVPFSRTEDGHLDLrpLGG----------- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 307 VRQGAKHVTCAYRRDEENMPGSR---REVKNAREEGVEFKFNVQPLGIEVNgNGKVSGVKMVrtemgepDAKGRRRAEIV 383
Cdd:pfam00890 116 LSATWRTPHDAADRRRGLGTGHAllaRLLEGLRKAGVDFQPRTAADDLIVE-DGRVTGAVVE-------NRRNGREVRIR 187
|
250 260 270
....*....|....*....|....*....|....*
gi 16131103 384 AGSehivpadAVIMAFGFRPHNMEWLAKHSVELDS 418
Cdd:pfam00890 188 AIA-------AVLLATGGFGRLAELLLPAAGYADT 215
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
277-459 |
1.70e-03 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 40.95 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 277 TRDEPfVSMEG--KRVVVLGGGDTAMDCVRTSVRQGAkHVTCAYRR-------DEEnmpgsRREV--KNAREEGVefkfN 345
Cdd:PLN02507 192 TSDEA-LSLEElpKRAVVLGGGYIAVEFASIWRGMGA-TVDLFFRKelplrgfDDE-----MRAVvaRNLEGRGI----N 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 346 VQPlGIEVNGNGKVSGVKMVRTEMGEpdakgrrraeivagsEHIvpADAVIMAFGFRPH----NMEWLAkhsVELDSQGR 421
Cdd:PLN02507 261 LHP-RTNLTQLTKTEGGIKVITDHGE---------------EFV--ADVVLFATGRAPNtkrlNLEAVG---VELDKAGA 319
|
170 180 190
....*....|....*....|....*....|....*...
gi 16131103 422 IIAPEGSdnafQTSNPKIFAGGDIVRGSDLVVTAIAEG 459
Cdd:PLN02507 320 VKVDEYS----RTNIPSIWAIGDVTNRINLTPVALMEG 353
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
150-182 |
2.04e-03 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 40.27 E-value: 2.04e-03
10 20 30
....*....|....*....|....*....|...
gi 16131103 150 AIIGAGPAGLACADVLTRNGVKAVVFDRHPEIG 182
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
147-219 |
2.18e-03 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 40.61 E-value: 2.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIGGL---LTFGIPAFKLEKEVMTRR-REIFTGMGIEFKLNTEV 219
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDCPQCILEPLiAEVEANPNITVYTGAEV 217
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
148-181 |
2.24e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 40.06 E-value: 2.24e-03
10 20 30
....*....|....*....|....*....|....
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEI 181
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
|
|
| SfcA |
COG0281 |
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: ... |
139-186 |
2.43e-03 |
|
Malic enzyme [Energy production and conversion]; Malic enzyme is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440050 [Multi-domain] Cd Length: 414 Bit Score: 39.99 E-value: 2.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131103 139 MSGVKQTGK-----KVAIIGAGPAGLACADVLTRNGVKA---VVFDRHpeigGLLT 186
Cdd:COG0281 179 LNALKLVGKkledqKIVINGAGAAGIAIARLLVAAGLSEeniIMVDSK----GLLY 230
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
147-182 |
2.50e-03 |
|
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;
Pssm-ID: 234978 [Multi-domain] Cd Length: 662 Bit Score: 40.21 E-value: 2.50e-03
10 20 30
....*....|....*....|....*....|....*.
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEIG 182
Cdd:PRK01747 261 RDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
|
|
| Tdh |
COG1063 |
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ... |
138-250 |
3.11e-03 |
|
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440683 [Multi-domain] Cd Length: 341 Bit Score: 39.74 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 138 DMSGVKQtGKKVAIIGAGPAGLACADVLTRNGVKAV-VFDRHPEigglltfgipafklekevmtrRREIFTGMGIEFKLN 216
Cdd:COG1063 155 ERAGVKP-GDTVLVIGAGPIGLLAALAARLAGAARViVVDRNPE---------------------RLELARELGADAVVN 212
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 16131103 217 TevgRDVQLDDLLSD------YDAVFLGVGTYQSMRGGLE 250
Cdd:COG1063 213 P---REEDLVEAVREltggrgADVVIEAVGAPAALEQALD 249
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
350-463 |
3.62e-03 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 39.75 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131103 350 GIEVNGNGKVSGVKMVRTEMGEPDAKGRRRAeivagsehivpaDAVIMAFGFRPhNMEWLAKHS--VELDSQGRIIApeg 427
Cdd:PRK13748 324 GIEVLEHTQASQVAHVDGEFVLTTGHGELRA------------DKLLVATGRAP-NTRSLALDAagVTVNAQGAIVI--- 387
|
90 100 110
....*....|....*....|....*....|....*.
gi 16131103 428 sDNAFQTSNPKIFAGGDIVRGSDLVVTAIAEGRKAA 463
Cdd:PRK13748 388 -DQGMRTSVPHIYAAGDCTDQPQFVYVAAAAGTRAA 422
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
154-182 |
3.71e-03 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 39.18 E-value: 3.71e-03
10 20
....*....|....*....|....*....
gi 16131103 154 AGPAGLACADVLTRNGVKAVVFDRHPEIG 182
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGSFPG 29
|
|
| PRK07538 |
PRK07538 |
hypothetical protein; Provisional |
148-181 |
5.34e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 236046 [Multi-domain] Cd Length: 413 Bit Score: 39.11 E-value: 5.34e-03
10 20 30
....*....|....*....|....*....|....
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEI 181
Cdd:PRK07538 2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEAAPEL 35
|
|
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
148-202 |
5.56e-03 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 38.96 E-value: 5.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131103 148 KVAIIGAGPAGLACADVLTRNGVKAVVFDRHPE----IGGlltfGIP-----AFKLEKEVMTRR 202
Cdd:PLN00093 41 RVAVIGGGPAGACAAETLAKGGIETFLIERKLDnakpCGG----AIPlcmvgEFDLPLDIIDRK 100
|
|
| PRK00711 |
PRK00711 |
D-amino acid dehydrogenase; |
335-400 |
6.15e-03 |
|
D-amino acid dehydrogenase;
Pssm-ID: 234819 [Multi-domain] Cd Length: 416 Bit Score: 39.01 E-value: 6.15e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131103 335 AREEGVEFKFNVQPLGIEVNGnGKVSGvkmVRTEMGepdakgrrraeivagsehIVPADAVIMAFG 400
Cdd:PRK00711 211 AEQLGVKFRFNTPVDGLLVEG-GRITG---VQTGGG------------------VITADAYVVALG 254
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
377-446 |
6.28e-03 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 39.00 E-value: 6.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131103 377 RRRAEIVAGSEHIVP--------ADAVIMAFGFRPhNMEWLAKHSVELDSQGRIIApegsDNAFQTSNPKIFAGGDIV 446
Cdd:PRK13512 207 RLNEEIDAINGNEVTfksgkvehYDMIIEGVGTHP-NSKFIESSNIKLDDKGFIPV----NDKFETNVPNIYAIGDII 279
|
|
| PRK07588 |
PRK07588 |
FAD-binding domain; |
147-215 |
6.94e-03 |
|
FAD-binding domain;
Pssm-ID: 169028 [Multi-domain] Cd Length: 391 Bit Score: 38.56 E-value: 6.94e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131103 147 KKVAIIGAGPAGLACADVLTRNGVKAVVFDRHPEI--GG-LLTFGIPAFklekEVMTRrreiftgMGIEFKL 215
Cdd:PRK07588 1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELrtGGyMVDFWGVGY----EVAKR-------MGITDQL 61
|
|
| |
