|
Name |
Accession |
Description |
Interval |
E-value |
| Se_ygfK |
TIGR03315 |
putative selenate reductase, YgfK subunit; Members of this protein family are YgfK, predicted ... |
2-1027 |
0e+00 |
|
putative selenate reductase, YgfK subunit; Members of this protein family are YgfK, predicted to be one subunit of a three-subunit, molybdopterin-containing selenate reductase. This enzyme is found, typically, in genomic regions associated with xanthine dehydrogenase homologs predicted to belong to the selenium-dependent molybdenum hydroxylases (SDMH). Therefore, the selenate reductase is suggested to play a role in furnishing selenide for SelD, the selenophosphate synthase.
Pssm-ID: 132358 [Multi-domain] Cd Length: 1012 Bit Score: 1867.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 2 GDIMRPIPFEELLTRIFDEYQQQRSIFGIPEQQFYSPVKGKTVSVFGETCATPVGPAAGPHTQLAQNIVTSWLTGGRFIE 81
Cdd:TIGR03315 1 GDIMRPIPFKKLLNWIFEEYKEDGSIFGIPKRKFYRADPGKYISLFGEKLETPVGPAAGPHTQLAQNIVASYLTGGRFFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 82 LKTVQILDRLELEKPCIDAEDECFNTEWSTEFTLLKAWDEYLKAWFALHLLEAMFQPSDSgKSFIFNMSVGYNLEGIKQP 161
Cdd:TIGR03315 81 LKTVQVLDGLDLPKPCIDAADECYNVEWSTELTVPEAYDEYVKAWFLLHLLEKEFELGDP-RGFMFNMSVGYDLAGIKSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 162 PMQQFIDNMMDASDHPKFAQYRDTLNKLLQ-----DDAFLARhglqekreslqalparIPTSMVHGVTLSTMHGCPPHEI 236
Cdd:TIGR03315 160 KVDRYIEEMQDASGTPIFAECRATLKKYIDyfkkvDDEFIDA----------------ISPKVCHSVTLSTMHGCPPDEI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 237 EAICRYMLEEKGLNTFVKLNPTLLGYARVREILDVCGFGYIGLKEESFDHDLKLTQALEMLERLMALAKEKSLGFGVKLT 316
Cdd:TIGR03315 224 EAICRYLLEEKGLHTFVKLNPTLLGYKFVRDTMDEMGFDYIVLKEESFSHDLQYEDAVAMLQRLQLLAKEKGLGFGVKLT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 317 NTLGTINNKGALPGEEMYMSGRALFPLSINVAAVLSRAFDGKLPISYSGGASQLTIRDIFDTGIRPITMATDLLKPGGYL 396
Cdd:TIGR03315 304 NTLPVTIAKGELPGEEMYMSGRALFPLSINLAAKLSREFDGKLQISYSGGADIFNIKEIFDTGIWPITMATTLLKPGGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 397 RLSACMRELEGSDAWGLDHVDVERLNRLAADALTMEYTQKHWKPEERIEVAEDLPLTDCYVAPCVTACAIKQDIPEYIRL 476
Cdd:TIGR03315 384 RLNQCANELETSEYWGMGHVDLDKLAQLAAKALTDEYTQKEWRPVESRKLRKTLPLTDCYVAPCTTGCPINQDIPEYIRL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 477 LGEHRYADALELIYQRNALPAITGHICDHQCQYNCTRLDYDSALNIRELKKVALEKGWDEYKQRWHKPAGSGSRHPVAVI 556
Cdd:TIGR03315 464 VGEKRYLEALEVIYDKNPLPAITGTICDHQCQYKCTRLDYDESVNIREMKKVAAEKGYDEYKTRWHKPQGKSSAHKVAVI 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 557 GAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQHDIDFVAAHGVKFEYGCSPDLTIEQLKNQGFH 636
Cdd:TIGR03315 544 GAGPAGLSAGYFLARAGHPVTVFEKKEKPGGVVKNIIPEFRISAESIQKDIELVKFHGVEFKYGCSPDLTVAELKNQGYK 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 637 YVLIATGTDKNSGVKLAGDNQNVWKSLPFLREYNKG-TALKLGKHVVVVGAGNTAMDCARAALRVPGVEKATIVYRRSLQ 715
Cdd:TIGR03315 624 YVILAIGAWKHGPLRLEGGGERVLKSLEFLRAFKEGpTINPLGKHVVVVGGGNTAMDAARAALRVPGVEKVTVVYRRTKR 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 716 EMPAWREEYEEALHDGVEFRFLNNPERFDaDGTLTLRVMSLGEPDEKGRRRPVETNETVTLLVDSLITAIGEQQDTEALN 795
Cdd:TIGR03315 704 YMPASREELEEALEDGVDFKELLSPESFE-DGTLTCEVMKLGEPDASGRRRPVGTGETVDLPADTVIAAVGEQVDTDLLQ 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 796 AMGVPLDKNGWPDVDHN-GETRLTDVFMIGDVQRGPSSIVAAVGTARRATDAILSRENIRSHQNDkYW---NNVNPAEIY 871
Cdd:TIGR03315 783 KNGIPLDEYGWPVVNQAtGETNITNVFVIGDANRGPATIVEAIADGRKAANAILSREGLNSDVDK-VFpinEEVRLAEVY 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 872 QRKGDISItlvnsDDRDAFVAQEAARCLECNYVCSKCVDVCPNRANVSIAVPGFQNRFQTLHLDAYCNECGNCAQFCPWN 951
Cdd:TIGR03315 862 QKKGILVI-----DDHSCFPEQESQRCLECSYVCEKCVDVCPNRANIVIYVPGFRDQFQIVHLDGMCNECGNCATFCPYD 936
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130780 952 GKPYKDKITVFSLAQDFDNSSNPGFLVEDCRV---RVRLNNQSWVLNIDSKGQFNNVPPELNDMcrIISHVHQhHHYLL 1027
Cdd:TIGR03315 937 GAPYKDKLTLFWLEEDFYNSTNSGFLVEDPVVkicKVRLNGEVSTIQIDDQGKENDVPEELIDL--IITMVHE-YHYLL 1012
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
440-847 |
3.44e-142 |
|
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: 432.64 E-value: 3.44e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 440 PEERIEVAEdlPLTDCYVAPCVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHICDHQCQYNCTRLDYDSA 519
Cdd:COG0493 14 EEEAIEQAA--RCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPAPCEGACVRGIVDEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 520 LNIRELKKVALEKGWDEYKQRWHKPAGSgSRHPVAVIgagpaglaagYFLARAGHPVTLFEREANAGGVVKNIIPQFRIP 599
Cdd:COG0493 92 VAIGALERFIADKAFEEGWVKPPPPAPR-TGKKVAVVgsgpaglaaaYQLARAGHEVTVFEALDKPGGLLRYGIPEFRLP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 600 AELIQHDIDFVAAHGVKFEYGCSP--DLTIEQLKNQgFHYVLIATGTDKNSGVKLAGDN-QNVWKSLPFLREYNKGTA-- 674
Cdd:COG0493 171 KDVLDREIELIEALGVEFRTNVEVgkDITLDELLEE-FDAVFLATGAGKPRDLGIPGEDlKGVHSAMDFLTAVNLGEApd 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 675 --LKLGKHVVVVGAGNTAMDCARAALRVpGVEKATIVYRRSLQEMPAWREEYEEALHDGVEFRFLNNPERF--DADGTLT 750
Cdd:COG0493 250 tiLAVGKRVVVIGGGNTAMDCARTALRL-GAESVTIVYRRTREEMPASKEEVEEALEEGVEFLFLVAPVEIigDENGRVT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 751 ---LRVMSLGEPDEKGRRRPVE-TNETVTLLVDSLITAIGEQQDTEAL-NAMGVPLDKNGWPDVDH-NGETRLTDVFMIG 824
Cdd:COG0493 329 gleCVRMELGEPDESGRRRPVPiEGSEFTLPADLVILAIGQTPDPSGLeEELGLELDKRGTIVVDEeTYQTSLPGVFAGG 408
|
410 420
....*....|....*....|...
gi 16130780 825 DVQRGPSSIVAAVGTARRATDAI 847
Cdd:COG0493 409 DAVRGPSLVVWAIAEGRKAARAI 431
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
455-949 |
3.79e-98 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 321.05 E-value: 3.79e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 455 CYV---APCVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHICDHQCQYNCTRLDYDSALNIRELKKV--- 528
Cdd:PRK12771 41 VYVdqtPPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHPCESGCNRGQVDDAVGINAVERFlgd 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 529 -ALEKGWDeykqrwHKPAGSGSRHPVAVIGAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQHDI 607
Cdd:PRK12771 121 yAIANGWK------FPAPAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 608 DFVAAHGVKFEYGCS--PDLTIEQLKNqGFHYVLIATGTDKNSGVKLAG-DNQNVWKSLPFLREYNKGTALKLGKHVVVV 684
Cdd:PRK12771 195 QRILDLGVEVRLGVRvgEDITLEQLEG-EFDAVFVAIGAQLGKRLPIPGeDAAGVLDAVDFLRAVGEGEPPFLGKRVVVI 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 685 GAGNTAMDCARAALRVpGVEKATIVYRRSLQEMPAWREEYEEALHDGVEFRFLNNPERF--DADGTLTLRV--MSLGEPD 760
Cdd:PRK12771 274 GGGNTAMDAARTARRL-GAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIegDENGATGLRVitVEKMELD 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 761 EKGRRRPVeTNETVTLLVDSLITAIGEQQDTEALNAMGVPLDKNGWPDVDHNgeTRLTD---VFMIGDVQRGPSSIVAAV 837
Cdd:PRK12771 353 EDGRPSPV-TGEEETLEADLVVLAIGQDIDSAGLESVPGVEVGRGVVQVDPN--FMMTGrpgVFAGGDMVPGPRTVTTAI 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 838 GTARRATDAI------------LSRENIR-SHQNDKYWNNVNPA-----EIYQRKGDISITLVNSDDRDAfvAQEAARCL 899
Cdd:PRK12771 430 GHGKKAARNIdaflggepyehrPKREIVKfDKLNLWYFTDAPRAqrpelDADERVGDFDEVLGGLTEEEA--RQEAARCL 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 16130780 900 ECN--YVCSKCVDVCPNRAnvsIAVPGFQNRFQTLHldAYCNECGNCAQFCP 949
Cdd:PRK12771 508 SCGncFECDNCYGACPQDA---IIKLGPGRRYHFDY--DKCTGCHICADVCP 554
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
440-847 |
1.05e-97 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 316.35 E-value: 1.05e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 440 PEERI----EVAedLPLTD------------CYVAPCVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHIC 503
Cdd:PRK11749 16 AEERAqnfdEVA--PGYTPeeaieeasrclqCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVC 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 504 DH--QCQYNCTRLDYDSALNIRELKK----VALEKGWDEYKqrwhKPAGSGSRhpVAVIGAGPAGLAAGYFLARAGHPVT 577
Cdd:PRK11749 94 PQerLCEGACVRGKKGEPVAIGRLERyitdWAMETGWVLFK----RAPKTGKK--VAVIGAGPAGLTAAHRLARKGYDVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 578 LFEREANAGGVVKNIIPQFRIPAELIQHDIDFVAAHGVKFEYGCS--PDLTIEQLKnQGFHYVLIATGTDKNSGVKLAGD 655
Cdd:PRK11749 168 IFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEvgRDITLDELR-AGYDAVFIGTGAGLPRFLGIPGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 656 N-QNVWKSLPFLREYNKG---TALKLGKHVVVVGAGNTAMDCARAALRVpGVEKATIVYRRSLQEMPAWREEYEEALHDG 731
Cdd:PRK11749 247 NlGGVYSAVDFLTRVNQAvadYDLPVGKRVVVIGGGNTAMDAARTAKRL-GAESVTIVYRRGREEMPASEEEVEHAKEEG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 732 VEFRFLNNPERFDADG----TLTLRVMSLGEPDEKGRRRPVETNETVTLLVDSLITAIGeqQDTEALNAMGVP---LDKN 804
Cdd:PRK11749 326 VEFEWLAAPVEILGDEgrvtGVEFVRMELGEPDASGRRRVPIEGSEFTLPADLVIKAIG--QTPNPLILSTTPgleLNRW 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 16130780 805 GWPDVDH-NGETRLTDVFMIGDVQRGPSSIVAAVGTARRATDAI 847
Cdd:PRK11749 404 GTIIADDeTGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAI 447
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
454-944 |
3.01e-84 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 286.24 E-value: 3.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 454 DCyVAPCVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHICDHQCQYNCTRLDYDSALNIRELKKVALEKG 533
Cdd:PRK12814 99 DC-LGPCELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAPCEEACRRHGVDEPVSICALKRYAADRD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 534 wDEYKQRWHKPAGSGSRHPVAVIGAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQHDIDFVAAH 613
Cdd:PRK12814 178 -MESAERYIPERAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 614 GVKFEYGC--SPDLTIEQLKNQgFHYVLIATGTDKNSGVKLAG-DNQNVWKSLPFLREYNKGTALKLGKHVVVVGAGNTA 690
Cdd:PRK12814 257 GAEFRFNTvfGRDITLEELQKE-FDAVLLAVGAQKASKMGIPGeELPGVISGIDFLRNVALGTALHPGKKVVVIGGGNTA 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 691 MDCARAALRVpGVEKATIVYRRSLQEMPAWREEYEEALHDGVEFRFLNNP---ERFDADGTLTLRVMSLGEPDEKGRRRP 767
Cdd:PRK12814 336 IDAARTALRL-GAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPvsiERSEGGLELTAIKMQQGEPDESGRRRP 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 768 VETNET-VTLLVDSLITAIGEQQDTEALNAMGVPLDKNGWPDVDhnGETRLTD---VFMIGDVQRGPSSIVAAVGTARRA 843
Cdd:PRK12814 415 VPVEGSeFTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVD--PETLQTSvagVFAGGDCVTGADIAINAVEQGKRA 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 844 TDAI---LSRENI-------------RSHQNDKYWNNVNPAE--------IYQRKGDISITLVNSDDRDAfvAQEAARCL 899
Cdd:PRK12814 493 AHAIdlfLNGKPVtapvqpfnssygpRDKAPEAFYDRAQPAPrvalpelpLEERTGGFEEVVTGYSPEQA--REEALRCL 570
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130780 900 ECNyvCSKcVDVCPNRANVSIAVPGFQNRfQTLHLDAY-------------CNECGNC 944
Cdd:PRK12814 571 RCR--CNA-VDDCRLRDLATRYLPDTPCK-EEEHEGFSitrngdirferekCVDCGIC 624
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
420-847 |
1.92e-76 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 266.99 E-value: 1.92e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 420 RLNRLAADALTMEYTQKHWKPEERIEVAEDLPLT------DCYVAPCVTACAIKQDIPEYIRLLGEHRYADALELIYQRN 493
Cdd:PRK12778 293 AIERVPMPELDPEYRAHNRFEEVNLGLTKEQAMTeakrclDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 494 ALPAITGHIC--DHQCQYNCTRLDYDS-ALNIRELKKVALEkgWDEYKQRWHKP-AGSGSRHPVAVIGAGPAGLAAGYFL 569
Cdd:PRK12778 373 ALPAVCGRVCpqEKQCESKCIHGKMGEeAVAIGYLERFVAD--YERESGNISVPeVAEKNGKKVAVIGSGPAGLSFAGDL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 570 ARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQHDIDFVAAHGVKFEYGC--SPDLTIEQLKNQGFHYVLIATGTDKN 647
Cdd:PRK12778 451 AKRGYDVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVivGKTITIEELEEEGFKGIFIASGAGLP 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 648 SGVKLAGDNQN-VWKSLPFL------REYNKGTA--LKLGKHVVVVGAGNTAMDCARAALRVpGVEKATIVYRRSLQEMP 718
Cdd:PRK12778 531 NFMNIPGENSNgVMSSNEYLtrvnlmDAASPDSDtpIKFGKKVAVVGGGNTAMDSARTAKRL-GAERVTIVYRRSEEEMP 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 719 AWREEYEEALHDGVEFRFLNNPERFDAD--GTLT---LRVMSLGEPDEKGRRRPVE-TNETVTLLVDSLITAIGEQQDTE 792
Cdd:PRK12778 610 ARLEEVKHAKEEGIEFLTLHNPIEYLADekGWVKqvvLQKMELGEPDASGRRRPVAiPGSTFTVDVDLVIVSVGVSPNPL 689
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16130780 793 ALNAM-GVPLDKNGWPDVDHNGETRLTDVFMIGDVQRGPSSIVAAVGTARRATDAI 847
Cdd:PRK12778 690 VPSSIpGLELNRKGTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAI 745
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
455-847 |
1.63e-73 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 251.09 E-value: 1.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 455 CYVAPCVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHIC--DHQCQYNCTRLDYDSALNIRELKK-VAle 531
Cdd:PRK12831 45 CKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCpqESQCEGKCVLGIKGEPVAIGKLERfVA-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 532 kgwDEYKQRWHKPAGSGSRH--PVAVIGAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELI-QHDID 608
Cdd:PRK12831 123 ---DWARENGIDLSETEEKKgkKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLVYGIPEFRLPKETVvKKEIE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 609 FVAAHGVKFE--YGCSPDLTIEQL-KNQGFHYVLIAT--GTDKNSGVKlaGDNQN-VWKSLPFLREYNKG--------TA 674
Cdd:PRK12831 200 NIKKLGVKIEtnVVVGKTVTIDELlEEEGFDAVFIGSgaGLPKFMGIP--GENLNgVFSANEFLTRVNLMkaykpeydTP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 675 LKLGKHVVVVGAGNTAMDCARAALRVpGVEkATIVYRRSLQEMPAWREEYEEALHDGVEFRFLNNPERF--DADGTLT-- 750
Cdd:PRK12831 278 IKVGKKVAVVGGGNVAMDAARTALRL-GAE-VHIVYRRSEEELPARVEEVHHAKEEGVIFDLLTNPVEIlgDENGWVKgm 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 751 -LRVMSLGEPDEKGRRRPVE-TNETVTLLVDSLITAIGEQQDTEALNAM-GVPLDKNGWPDVDHN-GETRLTDVFMIGDV 826
Cdd:PRK12831 356 kCIKMELGEPDASGRRRPVEiEGSEFVLEVDTVIMSLGTSPNPLISSTTkGLKINKRGCIVADEEtGLTSKEGVFAGGDA 435
|
410 420
....*....|....*....|.
gi 16130780 827 QRGPSSIVAAVGTARRATDAI 847
Cdd:PRK12831 436 VTGAATVILAMGAGKKAAKAI 456
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
464-873 |
9.42e-56 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 209.69 E-value: 9.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 464 CAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHICDH--QCQYNCTRldydsalnirelKKVALEKGWDEYKQRW 541
Cdd:PRK12779 214 CPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQelQCQGVCTH------------TKRPIEIGQLEWYLPQ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 542 HK----------------PAGSGSRHPVAVIGAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQH 605
Cdd:PRK12779 282 HEklvnpnanerfagrisPWAAAVKPPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDD 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 606 DIDFVAAHGVKF--EYGCSPDLTIEQLKNQGFHYVLIATGTDKNSGVKLAGDN-QNVWKSLPFLREYNKGTALK------ 676
Cdd:PRK12779 362 VVEKIKLLGGRFvkNFVVGKTATLEDLKAAGFWKIFVGTGAGLPTFMNVPGEHlLGVMSANEFLTRVNLMRGLDddyetp 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 677 ----LGKHVVVVGAGNTAMDCARAALRVPGveKATIVYRRSLQEMPAWREEYEEALHDGVEFRFLNNPERFDADG----- 747
Cdd:PRK12779 442 lpevKGKEVFVIGGGNTAMDAARTAKRLGG--NVTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFIGDDhthfv 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 748 -TLTLRVMSLGEPDEKGRRRPVETNETVTLLVDSLITAIGEQ-----QDTEAlnamGVPLDKNGWPDVDHNG-ETRLTDV 820
Cdd:PRK12779 520 tHALLDVNELGEPDKSGRRSPKPTGEIERVPVDLVIMALGNTanpimKDAEP----GLKTNKWGTIEVEKGSqRTSIKGV 595
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 16130780 821 FMIGDVQRGPSSIVAAVGTARRAtdailSRENIRShqndkywNNVNPAEIYQR 873
Cdd:PRK12779 596 YSGGDAARGGSTAIRAAGDGQAA-----AKEIVGE-------IPFTPAEIKDR 636
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
455-847 |
3.61e-52 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 199.01 E-value: 3.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 455 CYVAPCVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHIC--DHQCQYNCTRLDYDSALNIRELKKVAlek 532
Cdd:PRK12775 336 CAKPTCIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCpqETQCEAQCIIAKKHESVGIGRLERFV--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 533 gWDEYKQRWHKPAG-SGSRHPVAVIGAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQHDIDFVA 611
Cdd:PRK12775 413 -GDNARAKPVKPPRfSKKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLV 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 612 AHGVKFEYG--CSPDLTIEQLKN-QGFHYVLIATGTDKNSGVKLAGDNQN-VWKSLPFLREYN---------KGTALKLG 678
Cdd:PRK12775 492 DIGVKIETNkvIGKTFTVPQLMNdKGFDAVFLGVGAGAPTFLGIPGEFAGqVYSANEFLTRVNlmggdkfpfLDTPISLG 571
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 679 KHVVVVGAGNTAMDCARAALRVpGVEKATIVYRRSLQEMPAWREEYEEALHDGVEFRFLNNPERF--DADGT---LTLRV 753
Cdd:PRK12775 572 KSVVVIGAGNTAMDCLRVAKRL-GAPTVRCVYRRSEAEAPARIEEIRHAKEEGIDFFFLHSPVEIyvDAEGSvrgMKVEE 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 754 MSLGEPDEKGRRRPVETNETVTLLVDSLITAIGEQQD---TEALNAMGVpldkNGWPDV-------DHNGETRLTDVFMI 823
Cdd:PRK12775 651 MELGEPDEKGRRKPMPTGEFKDLECDTVIYALGTKANpiiTQSTPGLAL----NKWGNIaaddgklESTQSTNLPGVFAG 726
|
410 420
....*....|....*....|....
gi 16130780 824 GDVQRGPSSIVAAVGTARRATDAI 847
Cdd:PRK12775 727 GDIVTGGATVILAMGAGRRAARSI 750
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
440-848 |
7.31e-51 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 186.91 E-value: 7.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 440 PEERI----EVAEDLPLT----------DCYVAPCVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHICDH 505
Cdd:PRK12810 20 VAERIkdfkEFYEPFSEEqakiqaarcmDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 506 QCQYNCTRLDYDSALNIRELKKVALEKGWDEykqRWHKP----AGSGSRhpVAVIGAGPAGLAAGYFLARAGHPVTLFER 581
Cdd:PRK12810 100 PCEGACTLNINFGPVTIKNIERYIIDKAFEE---GWVKPdppvKRTGKK--VAVVGSGPAGLAAADQLARAGHKVTVFER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 582 EANAGGVVKNIIPQFRIPAELIQHDIDFVAAHGVKFEYGCSP--DLTIEQLKNQgFHYVLIATGTDKNSGVKLAG-DNQN 658
Cdd:PRK12810 175 ADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVgkDITAEELLAE-YDAVFLGTGAYKPRDLGIPGrDLDG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 659 VWKSLPFLREYNK---GTALKL-----GKHVVVVGAGNTAMDCARAALRvpgvEKATIVYRRSLQEMPAWRE-------- 722
Cdd:PRK12810 254 VHFAMDFLIQNTRrvlGDETEPfisakGKHVVVIGGGDTGMDCVGTAIR----QGAKSVTQRDIMPMPPSRRnknnpwpy 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 723 -----EYEEALHDGVEFRFLNNPERFD-ADGTLT-LRV--MSLGEPDekgrRRPVETNETVtLLVDSLITAIG-EQQDTE 792
Cdd:PRK12810 330 wpmklEVSNAHEEGVEREFNVQTKEFEgENGKVTgVKVvrTELGEGD----FEPVEGSEFV-LPADLVLLAMGfTGPEAG 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130780 793 ALNAMGVPLDKNGWPDVDHNG-ETRLTDVFMIGDVQRGPSSIVAAVGTARRATDAIL 848
Cdd:PRK12810 405 LLAQFGVELDERGRVAAPDNAyQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAID 461
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
460-847 |
2.92e-48 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 182.27 E-value: 2.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 460 CVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHICDHQCQYNCTRLDYDSALNIRELKK-VALEKGWDEYK 538
Cdd:PRK13984 193 CTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVCTHKCETVCSIGHRGEPIAIRWLKRyIVDNVPVEKYS 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 539 QRWHKPAGSGSRHpVAVIGAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQHDIDFVAAHGVKFE 618
Cdd:PRK13984 273 EILDDEPEKKNKK-VAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 619 YGCS--PDLTIEQLKnQGFHYVLIATGTDKNSGVKLAG-DNQNVWKSLPFLRE-----YNKGTALKLGKHVVVVGAGNTA 690
Cdd:PRK13984 352 LNTRvgKDIPLEELR-EKHDAVFLSTGFTLGRSTRIPGtDHPDVIQALPLLREirdylRGEGPKPKIPRSLVVIGGGNVA 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 691 MDCARAALRVPGVEKATI-----VYRRSLQEMPAWREEYEEALHDGVEFRFLNNPER--FDAD---GTLTLRVMSLGepD 760
Cdd:PRK13984 431 MDIARSMARLQKMEYGEVnvkvtSLERTFEEMPADMEEIEEGLEEGVVIYPGWGPMEvvIENDkvkGVKFKKCVEVF--D 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 761 EKGRRRP-VETNETVTLLVDSLITAIGEQQDTEALnamGVPLDKN-----GWPDVDHNGETRLTDVFMIGDVQRGPsSIV 834
Cdd:PRK13984 509 EEGRFNPkFDESDQIIVEADMVVEAIGQAPDYSYL---PEELKSKlefvrGRILTNEYGQTSIPWLFAGGDIVHGP-DII 584
|
410
....*....|...
gi 16130780 835 AAVGTARRATDAI 847
Cdd:PRK13984 585 HGVADGYWAAEGI 597
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
458-849 |
6.33e-46 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 175.98 E-value: 6.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 458 APCVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHIC--DHQCQYNCTRLDYDSALNIRELKK----VALE 531
Cdd:PRK12809 217 ANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCpqDRLCEGACTLKDHSGAVSIGNLERyitdTALA 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 532 KGWdeykqrwhKPAGSG---SRHPVAVIGAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQHDID 608
Cdd:PRK12809 297 MGW--------RPDVSKvvpRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRRE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 609 FVAAHGVKFEYGCS--PDLTIEQLKNQgFHYVLIATGTDKNSGVKLAG-DNQNVWKSLPFLREYNKG------------T 673
Cdd:PRK12809 369 IFTAMGIDFHLNCEigRDITFSDLTSE-YDAVFIGVGTYGMMRADLPHeDAPGVIQALPFLTAHTRQlmglpeseeyplT 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 674 ALKlGKHVVVVGAGNTAMDCARAALRVpGVEKATIVYRRSLQEMPAWREEYEEALHDGVEFRFLNNPERF--DADGTLT- 750
Cdd:PRK12809 448 DVE-GKRVVVLGGGDTTMDCLRTSIRL-NAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIacDEDGRLTa 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 751 --LRVMSLGEPDEKGRRR--PVETNEtVTLLVDSLITAIGEQ-QDTEALNAMGVPLDKngWPDVDHNGETRLT------D 819
Cdd:PRK12809 526 vgLIRTAMGEPGPDGRRRprPVAGSE-FELPADVLIMAFGFQaHAMPWLQGSGIKLDK--WGLIQTGDVGYLPtqthlkK 602
|
410 420 430
....*....|....*....|....*....|
gi 16130780 820 VFMIGDVQRGPSSIVAAVGTARRATDAILS 849
Cdd:PRK12809 603 VFAGGDAVHGADLVVTAMAAGRQAARDMLT 632
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
460-848 |
3.66e-43 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 168.00 E-value: 3.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 460 CVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHIC--DHQCQYNCTRLDYDSALNI----RELKKVALEKG 533
Cdd:PRK12769 236 CEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLPEITGRVCpqDRLCEGACTLRDEYGAVTIgnieRYISDQALAKG 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 534 WdeykqrwhKPAGSG---SRHPVAVIGAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQHDIDFV 610
Cdd:PRK12769 316 W--------RPDLSQvtkSDKRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIF 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 611 AAHGVKFEYGCS--PDLTIEQLKNQgFHYVLIATGTDKNSGVKLAG-DNQNVWKSLPFLREYNK--------------GT 673
Cdd:PRK12769 388 SAMGIEFELNCEvgKDISLESLLED-YDAVFVGVGTYRSMKAGLPNeDAPGVYDALPFLIANTKqvmgleelpeepfiNT 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 674 AlklGKHVVVVGAGNTAMDCARAALRvPGVEKATIVYRRSLQEMPAWREEYEEALHDGVEFRFLNNPER--FDADGTLT- 750
Cdd:PRK12769 467 A---GLNVVVLGGGDTAMDCVRTALR-HGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVAleLNEQGHVCg 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 751 ---LRVmSLGEPDEKGRRR--PVETNETVtLLVDSLITAIGEQQDTEA-LNAMGVPLDKNGW----PDVDHNGETRLTDV 820
Cdd:PRK12769 543 irfLRT-RLGEPDAQGRRRpvPIPGSEFV-MPADAVIMAFGFNPHGMPwLESHGVTVDKWGRiiadVESQYRYQTSNPKI 620
|
410 420
....*....|....*....|....*...
gi 16130780 821 FMIGDVQRGPSSIVAAVGTARRATDAIL 848
Cdd:PRK12769 621 FAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
543-847 |
5.48e-41 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 154.76 E-value: 5.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 543 KPAGSGSRhpVAVIGAGPAGLAAGYFLARAGHPVTLFEREANAGGVVKNIIPQFRIPAELIQHDIDFVAAHGVKFE---- 618
Cdd:PRK12770 13 KPPPTGKK--VAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHtrtk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 619 -YGCSP------------DLTIEQLKNQgFHYVLIATGTDKNSGVKLAGDN-QNVWKSLPFL---REYNKGTALK----- 676
Cdd:PRK12770 91 vCCGEPlheeegdefverIVSLEELVKK-YDAVLIATGTWKSRKLGIPGEDlPGVYSALEYLfriRAAKLGYLPWekvpp 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 677 -LGKHVVVVGAGNTAMDCARAALRVpGVEKATIVYRRSLQEMPAWREEYEEALHDGVEFRFLNNPERFDADGTLT---LR 752
Cdd:PRK12770 170 vEGKKVVVVGAGLTAVDAALEAVLL-GAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIGEGRVEgveLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 753 VMSLGEPDEKGRRRPVE-TNETVTLLVDSLITAIGEQQDTE-ALNAMGVPLDKNGWPDVDHNGETRLTDVFMIGDVQRGP 830
Cdd:PRK12770 249 KMRLGEPDESGRPRPVPiPGSEFVLEADTVVFAIGEIPTPPfAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGP 328
|
330
....*....|....*..
gi 16130780 831 SSIVAAVGTARRATDAI 847
Cdd:PRK12770 329 SKIGKAIKSGLRAAQSI 345
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
568-840 |
1.90e-35 |
|
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: 137.06 E-value: 1.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 568 FLARAGHPVTLFERE---ANAGGVVKNIIPQFRIPAELIQHDIDFVA------------------AHGVKFEYGCSpDLT 626
Cdd:pfam07992 18 TLAQLGGKVTLIEDEgtcPYGGCVLSKALLGAAEAPEIASLWADLYKrkeevvkklnngievllgTEVVSIDPGAK-KVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 627 IEQLK-----NQGFHYVLIATG-TDKNSGVKlaGDNQNVWKSLPFLREYNKGTALKLGKHVVVVGAGNTAMDCARAALRV 700
Cdd:pfam07992 97 LEELVdgdgeTITYDRLVIATGaRPRLPPIP--GVELNVGFLVRTLDSAEALRLKLLPKRVVVVGGGYIGVELAAALAKL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 701 pGVEkATIVYRRSL---QEMPAWREEYEEAL-HDGVEFRFLNNPERFDADGTLTLrvmslgepdekgrrrpVETNETVTL 776
Cdd:pfam07992 175 -GKE-VTLIEALDRllrAFDEEISAALEKALeKNGVEVRLGTSVKEIIGDGDGVE----------------VILKDGTEI 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130780 777 LVDSLITAIGEQQDTEALNAMGVPLDKNGWPDVDHNGETRLTDVFMIGDV-QRGPSSIVAAVGTA 840
Cdd:pfam07992 237 DADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCrVGGPELAQNAVAQG 301
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
454-534 |
1.55e-18 |
|
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: 82.20 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 454 DCYVAPCVTACAIKQDIPEYIRLLGEHRYADALELIYQRNALPAITGHICDH--QCQYNCTR-LDYDSALNIRELKK--- 527
Cdd:pfam14691 26 QCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQerQCEGACVLgKKGFEPVAIGRLERfaa 105
|
....*...
gi 16130780 528 -VALEKGW 534
Cdd:pfam14691 106 dWARENGI 113
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
569-843 |
4.41e-17 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 83.25 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 569 LARAGHPVTLFEREAnAGGVVKNI-----IPQFRIP---AELIQHDIDFVAAHGVKFEYGcspdlTIEQLK--NQGFH-- 636
Cdd:COG0492 19 AARAGLKTLVIEGGE-PGGQLATTkeienYPGFPEGisgPELAERLREQAERFGAEILLE-----EVTSVDkdDGPFRvt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 637 ----------YVLIATGtdknsgvklAGDNqnvWKSLPFLREY-NKG--------TALKLGKHVVVVGAGNTAMD----C 693
Cdd:COG0492 93 tddgteyeakAVIIATG---------AGPR---KLGLPGEEEFeGRGvsycatcdGFFFRGKDVVVVGGGDSALEealyL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 694 ARAALRVpgvekaTIVYRR-SLQEMPAWREEYEEalHDGVEFRFLNNPERFDADGTLT-LRVmslgepdekgrrRPVETN 771
Cdd:COG0492 161 TKFASKV------TLIHRRdELRASKILVERLRA--NPKIEVLWNTEVTEIEGDGRVEgVTL------------KNVKTG 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130780 772 ETVTLLVDSLITAIGEQQDTEALNAMGVPLDKNGWPDVDHNGETRLTDVFMIGDVQRGPS-SIVAAVGTARRA 843
Cdd:COG0492 221 EEKELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYrQAATAAGEGAIA 293
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
576-826 |
8.70e-15 |
|
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: 76.77 E-value: 8.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 576 VTLFEREANA-----------GGVVKNII-PQFRIPAELIQHDIDFVAAHGVKfeyGCSPD---LTIEQLKNQGFHYVLI 640
Cdd:COG0446 8 ITVIEKGPHHsyqpcglpyyvGGGIKDPEdLLVRTPESFERKGIDVRTGTEVT---AIDPEaktVTLRDGETLSYDKLVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 641 ATG----TDKNSGVKLAGdnqnvwksLPFLREYNKGTALKL------GKHVVVVGAGNTAMDCArAALRVPGVeKATIVY 710
Cdd:COG0446 85 ATGarprPPPIPGLDLPG--------VFTLRTLDDADALREalkefkGKRAVVIGGGPIGLELA-EALRKRGL-KVTLVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 711 RRSlQEMPAWREEYEEALHD-----GVEFRFLNNPERFDADGTLTLRVmslgepdEKGRRRPVetnetvtllvDSLITAI 785
Cdd:COG0446 155 RAP-RLLGVLDPEMAALLEEelrehGVELRLGETVVAIDGDDKVAVTL-------TDGEEIPA----------DLVVVAP 216
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 16130780 786 GEQQDTEALNAMGVPLDKNGWPDVDHNGETRLTDVFMIGDV 826
Cdd:COG0446 217 GVRPNTELAKDAGLALGERGWIKVDETLQTSDPDVYAAGDC 257
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
580-830 |
3.26e-10 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 63.66 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 580 EREANAGGVVKNIipqFRIPAE-LIQHDIDFVAAHGVKFEygcspDLTIEqlknqgFHYVLIATGTDKNS--GVKLAgDN 656
Cdd:PRK06292 89 ERDRFVGGVVEGL---EKKPKIdKIKGTARFVDPNTVEVN-----GERIE------AKNIVIATGSRVPPipGVWLI-LG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 657 QNVWKSlpflreynkGTAL---KLGKHVVVVGAGNTAMDCArAALRVPGVEKATIVYRRSL--QEMPAWREEYEEALHDg 731
Cdd:PRK06292 154 DRLLTS---------DDAFeldKLPKSLAVIGGGVIGLELG-QALSRLGVKVTVFERGDRIlpLEDPEVSKQAQKILSK- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 732 vEFRFlnnpeRFDAdgtltlRVMSLGEPDEKGRRRPVETNETVTLLVDSLITAIGEQQDTEALN--AMGVPLDKNGWPDV 809
Cdd:PRK06292 223 -EFKI-----KLGA------KVTSVEKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGLGleNTGIELDERGRPVV 290
|
250 260
....*....|....*....|.
gi 16130780 810 DHNGETRLTDVFMIGDVQRGP 830
Cdd:PRK06292 291 DEHTQTSVPGIYAAGDVNGKP 311
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
883-951 |
9.95e-08 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 54.34 E-value: 9.95e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130780 883 NSDDRDAFVAQEAARCLECNyvcsKCVDVCPNRANVSIavpgfQNRFQTLHLDAYCNECGNCAQFCPWN 951
Cdd:COG1145 169 KIAIKKAKAVIDAEKCIGCG----LCVKVCPTGAIRLK-----DGKPQIVVDPDKCIGCGACVKVCPVG 228
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
772-830 |
4.55e-07 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 53.78 E-value: 4.55e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130780 772 ETVTLLVDSLITAIGEQQDTEALNA--MGVPLDKNGWPDVDHNGETRLTDVFMIGDVQRGP 830
Cdd:PRK06327 267 EAQTLEVDKLIVSIGRVPNTDGLGLeaVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGP 327
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
635-830 |
2.39e-06 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 51.24 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 635 FHYVLIATGTdknsgvklagdnqnVWKSLPFLREYNKG-----TAL---KLGKHVVVVGAGNTAMDCARAALRVpGVEkA 706
Cdd:COG1249 131 ADHIVIATGS--------------RPRVPPIPGLDEVRvltsdEALeleELPKSLVVIGGGYIGLEFAQIFARL-GSE-V 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 707 TIVYRRS--LQEMPAW-REEYEEAL-HDGVEFRFLNNPERFDADG---TLTLrvmslgepdEKGrrrpvetNETVTLLVD 779
Cdd:COG1249 195 TLVERGDrlLPGEDPEiSEALEKALeKEGIDILTGAKVTSVEKTGdgvTVTL---------EDG-------GGEEAVEAD 258
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16130780 780 SLITAIGEQQDTEALN--AMGVPLDKNGWPDVDHNGETRLTDVFMIGDVQRGP 830
Cdd:COG1249 259 KVLVATGRRPNTDGLGleAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTGGP 311
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
589-835 |
3.43e-06 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 50.85 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 589 VKNIIPQFripAELIQHDidFVAAHG-VKFeygcSPDLTIEQLKnQGFHYVLIATGTDKNSGVKLAG-DNQNVWKSLPFL 666
Cdd:PLN02852 78 TKNVTNQF---SRVATDD--RVSFFGnVTL----GRDVSLSELR-DLYHVVVLAYGAESDRRLGIPGeDLPGVLSAREFV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 667 REYNK-------GTALKLGKHVVVVGAGNTAMDCAR-------------------AALRVPGVEKATIVYRR-------- 712
Cdd:PLN02852 148 WWYNGhpdcvhlPPDLKSSDTAVVLGQGNVALDCARillrptdelastdiaehalEALRGSSVRKVYLVGRRgpvqaact 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 713 --SLQEM------------------PAWREE----------YE--------EALHDG-----VEFRFLNNPERFDA--DG 747
Cdd:PLN02852 228 akELRELlglknvrvrikeadltlsPEDEEElkasrpkrrvYEllskaaaaGKCAPSggqreLHFVFFRNPTRFLDsgDG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 748 TLTLRVMSLG----EPDE-KGRRRPVETNETVTLLVDSLITAIGEQqdteALNAMGVPLD-KNGW-PDV------DHNGE 814
Cdd:PLN02852 308 NGHVAGVKLErtvlEGAAgSGKQVAVGTGEFEDLPCGLVLKSIGYK----SLPVDGLPFDhKRGVvPNVhgrvlsSASGA 383
|
330 340
....*....|....*....|.
gi 16130780 815 TRLTDVFMIGDVQRGPSSIVA 835
Cdd:PLN02852 384 DTEPGLYVVGWLKRGPTGIIG 404
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
894-949 |
1.60e-05 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 43.39 E-value: 1.60e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130780 894 EAARCLECNyvcsKCVDVCP-NRANVSIAVPGFQNrFQTLHLDAYCNECGNCAQFCP 949
Cdd:pfam13237 5 DPDKCIGCG----RCTAACPaGLTRVGAIVERLEG-EAVRIGVWKCIGCGACVEACP 56
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
561-949 |
2.13e-05 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 48.32 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 561 AGLAAGYFLARAGHPVTLFEREANAGGVVKNI---IPQFRIPAELIQHDIDFVAAHG----------VKFE-YGCSPDLT 626
Cdd:COG1148 151 AGMTAALELAEQGYEVYLVEKEPELGGRAAQLhktFPGLDCPQCILEPLIAEVEANPnitvytgaevEEVSgYVGNFTVT 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 627 IEQ--LKNQGFHY--VLIATGTDKNSGVKLA----GDNQNVWKSLPFLREYNKGTALKL--GKHV--VV----VGAGNTA 690
Cdd:COG1148 231 IKKgpREEIEIEVgaIVLATGFKPYDPTKLGeygyGKYPNVITNLELERLLAAGKILRPsdGKEPksVAfiqcVGSRDEE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 691 MD-------CARAAL--------RVPGVEkATIVYR--RslqeMPAWREE-YEEALHDGVEF-RF-LNNPERfDADGTLT 750
Cdd:COG1148 311 NGlpycsrvCCMYALkqalylkeKNPDAD-VYIFYRdiR----TYGKYEEfYRRAREDGVRFiRGrVAEIEE-DEGGKLV 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 751 LRVM--SLGEPdekgrrrpveTNETVTLLVdsLITAIGEQQDTEALNAM-GVPLDKNGWPDVDH----NGETRLTDVFMI 823
Cdd:COG1148 385 VTVEdtLLGEP----------VEIEADLVV--LATGMVPSEDNEELAKLlKLPLDQDGFFLEAHpklrPVETATDGIFLA 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 824 GDVQrGPSSIVAAV----GTARRATdAILSRENIrshqndkywnnvnpaeiyqrkgdisitlvnsdDRDAFVAQ-EAARC 898
Cdd:COG1148 453 GAAH-GPKDIPESIaqatAAAARAI-QLLSKGEL--------------------------------GVEPSVAEvDPEKC 498
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 16130780 899 LecnyVCSKCVDVCPNRAnvsiavPGFQNRFQTLHLDAYCNECGNCAQFCP 949
Cdd:COG1148 499 T----GCGRCVEVCPYGA------ISIDEKGVAEVNPALCKGCGTCAAACP 539
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
905-951 |
2.45e-05 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 42.51 E-value: 2.45e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 16130780 905 CSKCVDVCPNRANVSIAVPGFQNRFQTLHLDAYCNECGNCAQFCPWN 951
Cdd:pfam12838 4 CGACVAACPVGAITLDEVGEKKGTKTVVIDPERCVGCGACVAVCPTG 50
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
678-847 |
5.89e-05 |
|
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: 46.78 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 678 GKHVVVVGAGNTAMDCARAALRVpgVEKATIVYRRslqemPAW---REEYEEALHDGVEFRFLNNPERF-DADGTLTLRV 753
Cdd:COG2072 171 GKRVLVVGTGASAVQIAPELARV--AAHVTVFQRT-----PPWvlpRPNYDPERGRPANYLGLEAPPALnRRDARAWLRR 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 754 MSLGE----------PD-EKGRRRPVETNE--------TVTLL---------------------VDSLITAIGEQQDTEA 793
Cdd:COG2072 244 LLRAQvkdpelglltPDyPPGCKRPLLSTDyyealrrgNVELVtggieritedgvvfadgteheVDVIVWATGFRADLPW 323
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130780 794 LNAMGVpLDKNGWPDVDHNGETRLTDV---FMIG-DVQRGPSSIVAAVG-TARRATDAI 847
Cdd:COG2072 324 LAPLDV-RGRDGRSGPRAYLGVVVPGFpnlFFLGpNSPSGHSSLTLGAErQARYIARLI 381
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
905-949 |
1.35e-04 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 40.88 E-value: 1.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 16130780 905 CSKCVDVCPNRAnvsIAVPGFQNRFqTLHLD-AYCNECGNCAQFCP 949
Cdd:COG1143 7 CGLCVRVCPVDA---ITIEDGEPGK-VYVIDpDKCIGCGLCVEVCP 48
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
597-825 |
2.09e-04 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 45.03 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 597 RIPAELIQHDIDFVAAHGV-KFEYGcSPDLTIEQLKNQGF---HY--VLIATGTD----KNSGVKLagdnQNVWKslpfL 666
Cdd:PRK09564 61 RTPEEFIKSGIDVKTEHEVvKVDAK-NKTITVKNLKTGSIfndTYdkLMIATGARpiipPIKNINL----ENVYT----L 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 667 REYNKGTALKLG------KHVVVVGAGNTAMDCARAALrvpGVEKATIVYRRSLQEMP-AWREEY----EEALHD-GVEF 734
Cdd:PRK09564 132 KSMEDGLALKELlkdeeiKNIVIIGAGFIGLEAVEAAK---HLGKNVRIIQLEDRILPdSFDKEItdvmEEELREnGVEL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 735 RFLNNPERFDADGTLTLRVMSLGEPDekgrrrpvetnetvtllVDSLITAIGEQQDTEALNAMGVPLDKNGWPDVDHNGE 814
Cdd:PRK09564 209 HLNEFVKSLIGEDKVEGVVTDKGEYE-----------------ADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGE 271
|
250
....*....|.
gi 16130780 815 TRLTDVFMIGD 825
Cdd:PRK09564 272 TSIENIYAAGD 282
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
905-951 |
2.37e-04 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 42.00 E-value: 2.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 16130780 905 CSKCVDVCPNRAnvsIAVPgfqNRFQTLHLDAYCNECGNCAQFCPWN 951
Cdd:cd10549 83 CGLCVKVCPVDA---ITLE---DELEIVIDKEKCIGCGICAEVCPVN 123
|
|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
905-951 |
3.35e-04 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 39.78 E-value: 3.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130780 905 CSKCVDVCPNRA---------------NVSIAVPGFQNRFQTLHLDAYCNECGNCAQFCPWN 951
Cdd:pfam13484 4 CGKCIDACPTGAivgpegvldarrcisYLTIEKKGLIPDELRCLLGNRCYGCDICQDVCPWN 65
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
901-949 |
3.37e-04 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 39.71 E-value: 3.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 16130780 901 CNYvCSKCVDVCPNRAnvsIAvpgFQNRFQTLHLDAYCNECGNCAQFCP 949
Cdd:COG1149 13 CIG-CGLCVEVCPEGA---IK---LDDGGAPVVDPDLCTGCGACVGVCP 54
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
680-747 |
8.91e-04 |
|
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: 39.11 E-value: 8.91e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130780 680 HVVVVGAGNTAMDCArAALRVPGVeKATIVYRRSL------QEMPAWREEYEEALhdGVEFRFLNNPERFDADG 747
Cdd:pfam00070 1 RVVVVGGGYIGLELA-GALARLGS-KVTVVERRDRllpgfdPEIAKILQEKLEKN--GIEFLLNTTVEAIEGNG 70
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
599-826 |
1.11e-03 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 42.44 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 599 PAELIQHDIDFVAAHGVKFEYGCS-----PD---LTIEQLKNQGFHYVLIATGTD----KNSGVKLAG-----DNQNVWK 661
Cdd:COG1251 55 EEDLLLRPADFYEENGIDLRLGTRvtaidRAartVTLADGETLPYDKLVLATGSRprvpPIPGADLPGvftlrTLDDADA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 662 slpfLREynkgtALKLGKHVVVVGAGNTAMDCArAALRVPGVEkATIVYR------RSL-QEMPAW-REEYEEAlhdGVE 733
Cdd:COG1251 135 ----LRA-----ALAPGKRVVVIGGGLIGLEAA-AALRKRGLE-VTVVERaprllpRQLdEEAGALlQRLLEAL---GVE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130780 734 FRFLNNPERFDADGTLTLRVMSLGEpdekgrrrpvetnetvTLLVDSLITAIGEQQDTEALNAMGVPLDkNGwPDVDHNG 813
Cdd:COG1251 201 VRLGTGVTEIEGDDRVTGVRLADGE----------------ELPADLVVVAIGVRPNTELARAAGLAVD-RG-IVVDDYL 262
|
250
....*....|...
gi 16130780 814 ETRLTDVFMIGDV 826
Cdd:COG1251 263 RTSDPDIYAAGDC 275
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
905-949 |
1.46e-03 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 37.53 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 16130780 905 CSKCVDVCPNRANVSIAVPGFqNRFQtlHLDAYCNECGNCAQFCP 949
Cdd:pfam13187 5 CGACVAACPAGAIVPDLVGQT-IRGD--IAGLACIGCGACVDACP 46
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
905-951 |
1.51e-03 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 38.49 E-value: 1.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 16130780 905 CSKCVDVCPnranvSIAVpGFQNRFQTLHLDAyCNECGNCAQFCPWN 951
Cdd:COG4231 27 CGACVKVCP-----ADAI-EEGDGKAVIDPDL-CIGCGSCVQVCPVD 66
|
|
| napF |
TIGR00402 |
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ... |
878-951 |
1.76e-03 |
|
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]
Pssm-ID: 273060 [Multi-domain] Cd Length: 101 Bit Score: 38.77 E-value: 1.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130780 878 SITLVNSDDRDAFVAQEAARCLECNYvCSKCVDVCPNranvSIAVPGfQNRFQTLHLD-AYCNECGNCAQFCPWN 951
Cdd:TIGR00402 13 SSTIEKTQIRPPWSARESLFSAVCTR-CGECASACEN----NILQLG-QQGQPTVEFDnAECDFCGKCAEACPTN 81
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
905-949 |
4.34e-03 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 36.95 E-value: 4.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 16130780 905 CSKCVDVCPNRAnvsIAVPGFqnrfqTLHLDA-YCNECGNCAQFCP 949
Cdd:COG2221 20 CGLCVAVCPTGA---ISLDDG-----KLVIDEeKCIGCGACIRVCP 57
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
905-949 |
8.73e-03 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 36.25 E-value: 8.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 16130780 905 CSKCVDVCPNRANVsiavpgFQNRFQTLHLDAyCNECGNCAQFCP 949
Cdd:COG2768 16 CGACVKVCPVGAIS------IEDGKAVIDPEK-CIGCGACIEVCP 53
|
|
| |
