|
Name |
Accession |
Description |
Interval |
E-value |
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
24-454 |
2.34e-155 |
|
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: 453.44 E-value: 2.34e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTAPCEKSCRKKDEGSPVDIRALKRFACDRHgvasph 103
Cdd:COG0493 32 CQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPAPCEGACVRGIVDEPVAIGALERFIADKA------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 104 avakrldelsqqaewvgdrtgnhiltMSRQFRKVKEARESSRKaaaRVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLP 183
Cdd:COG0493 106 --------------------------FEEGWVKPPPPAPRTGK---KVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 184 GGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLRAQgYEAVFITIGLQDPlRILDMEGTDLKGIYS 263
Cdd:COG0493 157 GGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEE-FDAVFLATGAGKP-RDLGIPGEDLKGVHS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 264 GVDYVRDYEK-------ISLGKRCLVIGGGGVAIDCAQHAVRQGAGQVMIACLESWETMPASLSEKEDAQEEGIVFHPSL 336
Cdd:COG0493 235 AMDFLTAVNLgeapdtiLAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLFLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 337 GPRRFLGHE-GRVTRVEFLKV-SSVFDAEGKFSPTFVPNSTTILEVDSVILAVGQASTAPSLSGLEGLEMTPNGLIRA-A 413
Cdd:COG0493 315 APVEIIGDEnGRVTGLECVRMeLGEPDESGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVVdE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2017541172 414 EDMSTNLPGVFVGGDVRwRFTRNATDAIADGQKAARAIHGY 454
Cdd:COG0493 395 ETYQTSLPGVFAGGDAV-RGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
24-458 |
4.98e-126 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 379.14 E-value: 4.98e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTAP--CEKSCRKKDEGSPVDIRALKRFACDRHgvas 101
Cdd:PRK11749 50 CVKACPVSIDIPEFIRLIAEGNLKGAAETILETNPLPAVCGRVCPQErlCEGACVRGKKGEPVAIGRLERYITDWA---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 102 phavakrldelsqqaewvgdrtgnhiltMSRQFRKVKEARESSRKaaarVAIVGSGPTGLSAAHDLALLGYRVTIFEAAS 181
Cdd:PRK11749 126 ----------------------------METGWVLFKRAPKTGKK----VAVIGAGPAGLTAAHRLARKGYDVTIFEARD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 182 LPGGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLRaQGYEAVFITIGLQDPlRILDMEGTDLKGI 261
Cdd:PRK11749 174 KAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELR-AGYDAVFIGTGAGLP-RFLGIPGENLGGV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 262 YSGVDY------VRDYEKISLGKRCLVIGGGGVAIDCAQHAVRQGAGQVMIACLESWETMPASLSEKEDAQEEGIVFHPS 335
Cdd:PRK11749 252 YSAVDFltrvnqAVADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAESVTIVYRRGREEMPASEEEVEHAKEEGVEFEWL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 336 LGPRRFLGHEGRVTRVEFLKVSSVFDAEGKFSPTFVPNSTTILEVDSVILAVGQASTAPSLSGLEGLEMTPNGLIRAAE- 414
Cdd:PRK11749 332 AAPVEILGDEGRVTGVEFVRMELGEPDASGRRRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTPGLELNRWGTIIADDe 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2017541172 415 DMSTNLPGVFVGGDVRwrfTRNAT--DAIADGQKAARAIHGYLGGK 458
Cdd:PRK11749 412 TGRTSLPGVFAGGDIV---TGAATvvWAVGDGKDAAEAIHEYLEGA 454
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
24-606 |
1.04e-121 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 371.90 E-value: 1.04e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTAPCEKSCRKKDEGSPVDIRALKRFACDrhgvaspH 103
Cdd:PRK12771 49 CNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHPCESGCNRGQVDDAVGINAVERFLGD-------Y 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 104 AVAKRLdelsqqaewvgdrtgnhiltmsrqfrKVKEARESSRKaaaRVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLP 183
Cdd:PRK12771 122 AIANGW--------------------------KFPAPAPDTGK---RVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 184 GGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLrAQGYEAVFITIGLQDPlRILDMEGTDLKGIYS 263
Cdd:PRK12771 173 GGMMRYGIPAYRLPREVLDAEIQRILDLGVEVRLGVRVGEDITLEQL-EGEFDAVFVAIGAQLG-KRLPIPGEDAAGVLD 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 264 GVDYVRDY---EKISLGKRCLVIGGGGVAIDCAQHAVRQGAGQVMIACLESWETMPASLSEKEDAQEEGIVFHPSLGPRR 340
Cdd:PRK12771 251 AVDFLRAVgegEPPFLGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 341 FLGHEGRVTRVEFLKVS-SVFDAEGKFSPtfVPNSTTILEVDSVILAVGQAStapSLSGLEGLEMTPN--GLIRAAED-M 416
Cdd:PRK12771 331 IEGDENGATGLRVITVEkMELDEDGRPSP--VTGEEETLEADLVVLAIGQDI---DSAGLESVPGVEVgrGVVQVDPNfM 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 417 STNLPGVFVGGDVRwRFTRNATDAIADGQKAARAIHGYLGGKTLEVRKKGYMRALAPDFENTRCETiAPIKIPKRAASER 496
Cdd:PRK12771 406 MTGRPGVFAGGDMV-PGPRTVTTAIGHGKKAARNIDAFLGGEPYEHRPKREIVKFDKLNLWYFTDA-PRAQRPELDADER 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 497 IRTKEEITLGYDEAQARQQAARCRQCSIqavfdrsrCLLCGTCAETCVNGAlrLVRVADIQGDEkvaklTDAlekasprt 576
Cdd:PRK12771 484 VGDFDEVLGGLTEEEARQEAARCLSCGN--------CFECDNCYGACPQDA--IIKLGPGRRYH-----FDY-------- 540
|
570 580 590
....*....|....*....|....*....|
gi 2017541172 577 rgmtaiikdeSRCVSCGMCARRCPGGAITM 606
Cdd:PRK12771 541 ----------DKCTGCHICADVCPCGAIEM 560
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
24-605 |
8.15e-110 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 344.02 E-value: 8.15e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTAPCEKSCRKKDEGSPVDIRALKRFACDRHgvasph 103
Cdd:PRK12814 104 CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAPCEEACRRHGVDEPVSICALKRYAADRD------ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 104 avakrldelSQQAEwvgdrtgnhiltmsrqfRKVKEARESSRKaaaRVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLP 183
Cdd:PRK12814 178 ---------MESAE-----------------RYIPERAPKSGK---KVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 184 GGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLRAQgYEAVFITIGLQDPLRiLDMEGTDLKGIYS 263
Cdd:PRK12814 229 GGMMRYGIPRFRLPESVIDADIAPLRAMGAEFRFNTVFGRDITLEELQKE-FDAVLLAVGAQKASK-MGIPGEELPGVIS 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 264 GVDYVRDY---EKISLGKRCLVIGGGGVAIDCAQHAVRQGAGQVMIACLESWETMPASLSEKEDAQEEGIVFHPSLGPRR 340
Cdd:PRK12814 307 GIDFLRNValgTALHPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 341 FLGHEGRVTRVEFLKVSSVFDAEGKFSPTFVPNSTTILEVDSVILAVGQaSTAPSLSGLEGLEMTPNGLIRA-AEDMSTN 419
Cdd:PRK12814 387 IERSEGGLELTAIKMQQGEPDESGRRRPVPVEGSEFTLQADTVISAIGQ-QVDPPIAEAAGIGTSRNGTVKVdPETLQTS 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 420 LPGVFVGGD-VRWRFTrnATDAIADGQKAARAIHGYLGGKTLEVRKKGY-----MRALAPDFENTRCETIAPIKIPKRAA 493
Cdd:PRK12814 466 VAGVFAGGDcVTGADI--AINAVEQGKRAAHAIDLFLNGKPVTAPVQPFnssygPRDKAPEAFYDRAQPAPRVALPELPL 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 494 SERIRTKEEITLGYDEAQARQQAARCRQCSIQAVfdrsrcllcgtcaETCvngalRLVRVADIQGDEKVAKLTDALEKAs 573
Cdd:PRK12814 544 EERTGGFEEVVTGYSPEQAREEALRCLRCRCNAV-------------DDC-----RLRDLATRYLPDTPCKEEEHEGFS- 604
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2017541172 574 pRTRGmTAIIKDESRCVSCGMCAR------------------RCPGGAIT 605
Cdd:PRK12814 605 -ITRN-GDIRFEREKCVDCGICVRtleeygaegntdievlaeSCPTGALS 652
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
24-459 |
1.42e-92 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 293.08 E-value: 1.42e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVC--TAPCEKSCRKKDEGSPVDIRALKRFACD---RHG 98
Cdd:PRK12831 50 CVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCpqESQCEGKCVLGIKGEPVAIGKLERFVADwarENG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 99 VasphavakrldelsqqaewvgdrtgnhiltmsrqfrKVKEARESSRKaaaRVAIVGSGPTGLSAAHDLALLGYRVTIFE 178
Cdd:PRK12831 130 I------------------------------------DLSETEEKKGK---KVAVIGSGPAGLTCAGDLAKMGYDVTIFE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 179 AASLPGGMLRTGIPGFRLPKE-ILQQEIDAILELGVELKLNSPIGRDQSLADLRAQ-GYEAVFITIGLQDPlRILDMEGT 256
Cdd:PRK12831 171 ALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGKTVTIDELLEEeGFDAVFIGSGAGLP-KFMGIPGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 257 DLKGIYSGVD----------YVRDYEK-ISLGKRCLVIGGGGVAIDCAQHAVRQGAgQVMIACLESWETMPASLSEKEDA 325
Cdd:PRK12831 250 NLNGVFSANEfltrvnlmkaYKPEYDTpIKVGKKVAVVGGGNVAMDAARTALRLGA-EVHIVYRRSEEELPARVEEVHHA 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 326 QEEGIVFHPSLGPRRFLGHE-GRVTRVEFLKVS-SVFDAEGKFSPTFVPNSTTILEVDSVILAVGQASTAPSLSGLEGLE 403
Cdd:PRK12831 329 KEEGVIFDLLTNPVEILGDEnGWVKGMKCIKMElGEPDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTKGLK 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541172 404 MTPNGLIRAAEDM-STNLPGVFVGGDVrwrFTRNAT--DAIADGQKAARAIHGYLGGKT 459
Cdd:PRK12831 409 INKRGCIVADEETgLTSKEGVFAGGDA---VTGAATviLAMGAGKKAAKAIDEYLSKKW 464
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
24-459 |
9.29e-92 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 291.30 E-value: 9.29e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTAPCEKSCRKKDEGSPVDIRALKRFACDR---HGVA 100
Cdd:PRK12810 54 CHWGCPVHNYIPEWNDLVYRGRWEEAAERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKafeEGWV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 101 SPHAVAKRldelsqqaewvgdrTGNhiltmsrqfrkvkearessrkaaaRVAIVGSGPTGLSAAHDLALLGYRVTIFEAA 180
Cdd:PRK12810 134 KPDPPVKR--------------TGK------------------------KVAVVGSGPAGLAAADQLARAGHKVTVFERA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 181 SLPGGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLRAQgYEAVFITIGLQDPlRILDMEGTDLKG 260
Cdd:PRK12810 176 DRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAE-YDAVFLGTGAYKP-RDLGIPGRDLDG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 261 IYSGVDY-------VRDYEK---ISL-GKRCLVIGGGGVAIDCAQHAVRQGAGQVM---IacleswETMPAS-------- 318
Cdd:PRK12810 254 VHFAMDFliqntrrVLGDETepfISAkGKHVVVIGGGDTGMDCVGTAIRQGAKSVTqrdI------MPMPPSrrnknnpw 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 319 -----LSEKEDAQEEGIVFHPSLGPRRFLGHEGRVTRVEFLKVSSVfdaEGKFSPtfVPNSTTILEVDSVILAVGQASTA 393
Cdd:PRK12810 328 pywpmKLEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELG---EGDFEP--VEGSEFVLPADLVLLAMGFTGPE 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017541172 394 PSLSGLEGLEMTPNGLIRAAE-DMSTNLPGVFVGGDVR-------WrftrnatdAIADGQKAARAIHGYLGGKT 459
Cdd:PRK12810 403 AGLLAQFGVELDERGRVAAPDnAYQTSNPKVFAAGDMRrgqslvvW--------AIAEGRQAARAIDAYLMGST 468
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
24-458 |
1.85e-91 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 294.37 E-value: 1.85e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTAPCEKSCRKKDEGSPVDIRALKRFACDRhgvasph 103
Cdd:PRK13984 193 CTDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVCGRVCTHKCETVCSIGHRGEPIAIRWLKRYIVDN------- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 104 avakrldelsqqaewvgdrtgnhilTMSRQFRKVkeARESSRKAAARVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLP 183
Cdd:PRK13984 266 -------------------------VPVEKYSEI--LDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKP 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 184 GGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLRaQGYEAVFITIGLQDPlRILDMEGTDLKGIYS 263
Cdd:PRK13984 319 GGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELR-EKHDAVFLSTGFTLG-RSTRIPGTDHPDVIQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 264 GVDY---VRDY-----EKISLGKRCLVIGGGGVAIDCAQHAVR-----QGAGQVMIACLE-SWETMPASLSEKEDAQEEG 329
Cdd:PRK13984 397 ALPLlreIRDYlrgegPKPKIPRSLVVIGGGNVAMDIARSMARlqkmeYGEVNVKVTSLErTFEEMPADMEEIEEGLEEG 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 330 IVFHPSLGPRRFLGHEGRVTRVEFLKVSSVFDAEGKFSPTFVPNSTTILEVDSVILAVGQastAPSLSGL-----EGLEM 404
Cdd:PRK13984 477 VVIYPGWGPMEVVIENDKVKGVKFKKCVEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQ---APDYSYLpeelkSKLEF 553
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2017541172 405 TpNGLIRAAEDMSTNLPGVFVGGDVrwrftRNATD---AIADGQKAARAIHGYLGGK 458
Cdd:PRK13984 554 V-RGRILTNEYGQTSIPWLFAGGDI-----VHGPDiihGVADGYWAAEGIDMYLRKQ 604
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
23-458 |
2.87e-84 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 279.32 E-value: 2.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 23 ACQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVC--TAPCEKSC-RKKDEGSPVDIRALKRFAcdrhgv 99
Cdd:PRK12778 338 GCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCpqEKQCESKCiHGKMGEEAVAIGYLERFV------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 100 asphavakrldelsqqAEWVgdRTGNHIltmsrqfrkvkEARESSRKAAARVAIVGSGPTGLSAAHDLALLGYRVTIFEA 179
Cdd:PRK12778 412 ----------------ADYE--RESGNI-----------SVPEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEA 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 180 ASLPGGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLRAQGYEAVFITIGLQDPlRILDMEGTDLK 259
Cdd:PRK12778 463 LHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEGFKGIFIASGAGLP-NFMNIPGENSN 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 260 GIYSGVDYV------RDYEK-----ISLGKRCLVIGGGGVAIDCAQHAVRQGAGQVMIACLESWETMPASLSEKEDAQEE 328
Cdd:PRK12778 542 GVMSSNEYLtrvnlmDAASPdsdtpIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARLEEVKHAKEE 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 329 GIVFHPSLGPRRFLGHE-GRVTRVEFLKVS-SVFDAEGKFSPTFVPNSTTILEVDSVILAVGQASTAPSLSGLEGLEMTP 406
Cdd:PRK12778 622 GIEFLTLHNPIEYLADEkGWVKQVVLQKMElGEPDASGRRRPVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSIPGLELNR 701
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2017541172 407 NGLIRAAEDMSTNLPGVFVGGDVrwrFTRNAT--DAIADGQKAARAIHGYLGGK 458
Cdd:PRK12778 702 KGTIVVDEEMQSSIPGIYAGGDI---VRGGATviLAMGDGKRAAAAIDEYLSSK 752
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
24-455 |
1.07e-79 |
|
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: 259.03 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTAP--CEKSC----RKKDEGSPVDIRALKRFacdrh 97
Cdd:TIGR01316 38 CIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRVCPQErqCEGQCtvgkMFKDVGKPVSIGALERF----- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 98 gvasphavakrldelsqqaewVGDRTGNHiltmsrqfrKVKEARESSRKAAARVAIVGSGPTGLSAAHDLALLGYRVTIF 177
Cdd:TIGR01316 113 ---------------------VADWERQH---------GIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVTVF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 178 EAASLPGGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLRAQgYEAVFITIGLQDPlRILDMEGTD 257
Cdd:TIGR01316 163 EALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQ-YDAVFIGTGAGLP-KLMNIPGEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 258 LKGIYSGVDYV------RDYE------KISLGKRCLVIGGGGVAIDCAQHAVRQGAgQVMIACLESWETMPASLSEKEDA 325
Cdd:TIGR01316 241 LCGVYSANDFLtranlmKAYEfphadtPVYAGKSVVVIGGGNTAVDSARTALRLGA-EVHCLYRRTREDMTARVEEIAHA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 326 QEEGIVFHPSLGPRRFLGHE-GRVTRVEFLKVSSVFDAE-GKFSPTFVPNSTTILEVDSVILAVGQASTaPSLSGLEGLE 403
Cdd:TIGR01316 320 EEEGVKFHFLCQPVEIIGDEeGNVRAVKFRKMDCQEQIDsGERRFLPCGDAECKLEADAVIVAIGNGSN-PIMAETTRLK 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2017541172 404 MTPNGLIRAAEDMSTNLPGVFVGGDVrWRFTRNATDAIADGQKAARAIHGYL 455
Cdd:TIGR01316 399 TSERGTIVVDEDQRTSIPGVFAGGDI-ILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
141-458 |
7.93e-63 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 211.39 E-value: 7.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 141 RESSRKAAARVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSP 220
Cdd:PRK12770 11 KEKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 221 I---------------GRDQSLADLrAQGYEAVFITIGLQDPlRILDMEGTDLKGIYSGVDYV----------RDYEKI- 274
Cdd:PRK12770 91 VccgeplheeegdefvERIVSLEEL-VKKYDAVLIATGTWKS-RKLGIPGEDLPGVYSALEYLfriraaklgyLPWEKVp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 275 -SLGKRCLVIGGGGVAIDCAQHAVRQGAGQVMIACLESWETMPASLSEKEDAQEEGIVFHPSLGPRRFLGhEGRVTRVEF 353
Cdd:PRK12770 169 pVEGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRIIG-EGRVEGVEL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 354 LKVSSV-FDAEGKFSPTFVPNSTTILEVDSVILAVGQASTAPSLSGLEGLEMTPNGLIRAAEDMSTNLPGVFVGGDVRwR 432
Cdd:PRK12770 248 AKMRLGePDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKGEIVVDEKHMTSREGVFAAGDVV-T 326
|
330 340
....*....|....*....|....*.
gi 2017541172 433 FTRNATDAIADGQKAARAIHGYLGGK 458
Cdd:PRK12770 327 GPSKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
24-455 |
6.04e-53 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 195.55 E-value: 6.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVC--TAPCEKSC--RKKDEgsPVDIRALKRFacdrhgv 99
Cdd:PRK12775 341 CIAGCPVQIDIPVFIRHVVVRDFDGALEVIYEASIFPSICGRVCpqETQCEAQCiiAKKHE--SVGIGRLERF------- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 100 asphavakrldelsqqaewVGDRTgnhiltmsrQFRKVKEARESsrKAAARVAIVGSGPTGLSAAHDLALLGYRVTIFEA 179
Cdd:PRK12775 412 -------------------VGDNA---------RAKPVKPPRFS--KKLGKVAICGSGPAGLAAAADLVKYGVDVTVYEA 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 180 ASLPGGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADL-RAQGYEAVFITIGLQDPlRILDMEGTDL 258
Cdd:PRK12775 462 LHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLmNDKGFDAVFLGVGAGAP-TFLGIPGEFA 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 259 KGIYSGVDYVRDYE------------KISLGKRCLVIGGGGVAIDCAQHAVRQGAGQVMIACLESWETMPASLSEKEDAQ 326
Cdd:PRK12775 541 GQVYSANEFLTRVNlmggdkfpfldtPISLGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAK 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 327 EEGIVFHPSLGPRRFLGHEG---RVTRVEFLKVSSVfDAEGKFSPtfVPNSTTI-LEVDSVILAVGQASTAPSLSGLEGL 402
Cdd:PRK12775 621 EEGIDFFFLHSPVEIYVDAEgsvRGMKVEEMELGEP-DEKGRRKP--MPTGEFKdLECDTVIYALGTKANPIITQSTPGL 697
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 403 EMTPNGLIRAAEDM-----STNLPGVFVGGDVrwrFTRNATD--AIADGQKAARAIHGYL 455
Cdd:PRK12775 698 ALNKWGNIAADDGKlestqSTNLPGVFAGGDI---VTGGATVilAMGAGRRAARSIATYL 754
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
28-497 |
2.75e-46 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 175.79 E-value: 2.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 28 CPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTAP--CEKSCRKKDEgsPVDIRALKRFACDRHGVASPHAV 105
Cdd:PRK12779 214 CPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQElqCQGVCTHTKR--PIEIGQLEWYLPQHEKLVNPNAN 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 106 AKRLDELSqqaEWVgdrtgnhiltmsrqfrkvkearessrkAAAR--VAIVGSGPTGLSAAHDLALLGYRVTIFEAASLP 183
Cdd:PRK12779 292 ERFAGRIS---PWA---------------------------AAVKppIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 184 GGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLRAQGYEAVFITIGLQDPlRILDMEGTDLKGIYS 263
Cdd:PRK12779 342 GGVLRYGIPEFRLPNQLIDDVVEKIKLLGGRFVKNFVVGKTATLEDLKAAGFWKIFVGTGAGLP-TFMNVPGEHLLGVMS 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 264 G------VDYVR----DYEKI---SLGKRCLVIGGGGVAIDCAQHAVRQGaGQVMIACLESWETMPASLSEKEDAQEEGI 330
Cdd:PRK12779 421 AnefltrVNLMRglddDYETPlpeVKGKEVFVIGGGNTAMDAARTAKRLG-GNVTIVYRRTKSEMPARVEELHHALEEGI 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 331 VFHPSLGPRRFLG--HEGRVTRVeFLKVSSVF--DAEGKFSPTfvPNSTTI-LEVDSVILAVGQASTaPSLSGLE-GLEM 404
Cdd:PRK12779 500 NLAVLRAPREFIGddHTHFVTHA-LLDVNELGepDKSGRRSPK--PTGEIErVPVDLVIMALGNTAN-PIMKDAEpGLKT 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 405 TPNGLIRAAED-MSTNLPGVFVGGDVRwRFTRNATDAIADGQKAARAIHGYLGGKTLEVRKkgyMRALAPDFenTRCETI 483
Cdd:PRK12779 576 NKWGTIEVEKGsQRTSIKGVYSGGDAA-RGGSTAIRAAGDGQAAAKEIVGEIPFTPAEIKD---RVERAARY--TELGQI 649
|
490
....*....|....
gi 2017541172 484 APIKIPKRAASERI 497
Cdd:PRK12779 650 PQTIVGKVQLAGGI 663
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
24-456 |
5.92e-46 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 172.62 E-value: 5.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTAP--CEKSCRKKDEGSPVDIRALKRFACDRhgvas 101
Cdd:PRK12769 236 CEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLPEITGRVCPQDrlCEGACTLRDEYGAVTIGNIERYISDQ----- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 102 phAVAKrldelsqqaEWVGDRTGnhiltmsrqfrkVKearessrKAAARVAIVGSGPTGLSAAHDLALLGYRVTIFEAAS 181
Cdd:PRK12769 311 --ALAK---------GWRPDLSQ------------VT-------KSDKRVAIIGAGPAGLACADVLARNGVAVTVYDRHP 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 182 LPGGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLRAQgYEAVFITIGLQDPLRIlDMEGTDLKGI 261
Cdd:PRK12769 361 EIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLED-YDAVFVGVGTYRSMKA-GLPNEDAPGV 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 262 YSGVDY-------VRDYEK------ISL-GKRCLVIGGGGVAIDCAQHAVRQGAGQVMIACLESWETMPASLSEKEDAQE 327
Cdd:PRK12769 439 YDALPFliantkqVMGLEElpeepfINTaGLNVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNARE 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 328 EGIVFHPSLGPRRF-LGHEGRVTRVEFLKVS-SVFDAEGKFSPTFVPNSTTILEVDSVILAVG-QASTAPSLSGlEGLEM 404
Cdd:PRK12769 519 EGANFEFNVQPVALeLNEQGHVCGIRFLRTRlGEPDAQGRRRPVPIPGSEFVMPADAVIMAFGfNPHGMPWLES-HGVTV 597
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541172 405 TPNGLIRAAED----MSTNLPGVFVGGDVrwrfTRNA---TDAIADGQKAARAIHGYLG 456
Cdd:PRK12769 598 DKWGRIIADVEsqyrYQTSNPKIFAGGDA----VRGAdlvVTAMAEGRHAAQGIIDWLG 652
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
24-449 |
5.95e-44 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 166.74 E-value: 5.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTAP--CEKSCRKKDEGSPVDIRALKRFACDRhgvas 101
Cdd:PRK12809 219 CNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDT----- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 102 phavakrldelSQQAEWVGDrtgnhiltmsrqFRKVKEAREssrkaaaRVAIVGSGPTGLSAAHDLALLGYRVTIFEAAS 181
Cdd:PRK12809 294 -----------ALAMGWRPD------------VSKVVPRSE-------KVAVIGAGPAGLGCADILARAGVQVDVFDRHP 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 182 LPGGMLRTGIPGFRLPKEILQQEIDAILELGVELKLNSPIGRDQSLADLrAQGYEAVFITIGLQDPLRIlDMEGTDLKGI 261
Cdd:PRK12809 344 EIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDL-TSEYDAVFIGVGTYGMMRA-DLPHEDAPGV 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 262 YSGVDYV----RDY------EKISL----GKRCLVIGGGGVAIDCAQHAVRQGAGQVMIACLESWETMPASLSEKEDAQE 327
Cdd:PRK12809 422 IQALPFLtahtRQLmglpesEEYPLtdveGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNARE 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 328 EGIVFHPSLGPRRFLGHE-GRVTRVEFLKVS-SVFDAEGKFSPTFVPNSTTILEVDSVILAVG-QASTAPSLSGLeGLEM 404
Cdd:PRK12809 502 EGVEFQFNVQPQYIACDEdGRLTAVGLIRTAmGEPGPDGRRRPRPVAGSEFELPADVLIMAFGfQAHAMPWLQGS-GIKL 580
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2017541172 405 TPNGLIRAAE----DMSTNLPGVFVGGDVRWRFTRNATdAIADGQKAAR 449
Cdd:PRK12809 581 DKWGLIQTGDvgylPTQTHLKKVFAGGDAVHGADLVVT-AMAAGRQAAR 628
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-444 |
4.01e-27 |
|
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: 111.64 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFEAAS--------LPGGMLRTG--IPGFRLPKEILQ--QEIDAILELGVELKL 217
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGtcpyggcvLSKALLGAAeaPEIASLWADLYKrkEEVVKKLNNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 218 NSP-----------IGRDQSLADLRAQGYEAVFITIGLQDplRILDMEGTDLKGIYsGVDYVRDYEKISLG---KRCLVI 283
Cdd:pfam07992 82 GTEvvsidpgakkvVLEELVDGDGETITYDRLVIATGARP--RLPPIPGVELNVGF-LVRTLDSAEALRLKllpKRVVVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 284 GGGGVAIDCAQHAVRQGAgQVMIACLESW--ETMPASLSE--KEDAQEEGIVFHPSLGPRRFLGHEGRVTrveflkvssV 359
Cdd:pfam07992 159 GGGYIGVELAAALAKLGK-EVTLIEALDRllRAFDEEISAalEKALEKNGVEVRLGTSVKEIIGDGDGVE---------V 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 360 FDAEGkfsptfvpnstTILEVDSVILAVGQastAPSLSGLE--GLEMTPNGLIRAAEDMSTNLPGVFVGGDVRWRFTRNA 437
Cdd:pfam07992 229 ILKDG-----------TEIDADLVVVAIGR---RPNTELLEaaGLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELA 294
|
....*..
gi 2017541172 438 TDAIADG 444
Cdd:pfam07992 295 QNAVAQG 301
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
151-458 |
7.85e-27 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 110.98 E-value: 7.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 151 VAIVGSGPTGLSAAHDLALLGYRVTIFEAaSLPGGMLRTG-----IPGFrlPKEILQQE-----IDAILELGVELKLNSP 220
Cdd:COG0492 3 VVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLATTkeienYPGF--PEGISGPElaerlREQAERFGAEILLEEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 221 IGrdqslADLRAQGYE------------AVFITIGLQDplRILDMEGTDL---KGIYSGV----DYVRdyekislGKRCL 281
Cdd:COG0492 80 TS-----VDKDDGPFRvttddgteyeakAVIIATGAGP--RKLGLPGEEEfegRGVSYCAtcdgFFFR-------GKDVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 282 VIGGGGVAID----CAQHA------VRQG---AGQVMIACLESWEtmpaslsekedaqeeGIVFHPSLGPRRFLGhEGRV 348
Cdd:COG0492 146 VVGGGDSALEealyLTKFAskvtliHRRDelrASKILVERLRANP---------------KIEVLWNTEVTEIEG-DGRV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 349 TRVEFLKVssvfdaegkfsptfVPNSTTILEVDSVILAVGqasTAPSLSGLE--GLEMTPNGLIRAAEDMSTNLPGVFVG 426
Cdd:COG0492 210 EGVTLKNV--------------KTGEEKELEVDGVFVAIG---LKPNTELLKglGLELDEDGYIVVDEDMETSVPGVFAA 272
|
330 340 350
....*....|....*....|....*....|..
gi 2017541172 427 GDVRWRFTRNATDAIADGQKAARAIHGYLGGK 458
Cdd:COG0492 273 GDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
24-97 |
7.31e-19 |
|
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: 7.31e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2017541172 24 CQSACPLGTDTKRYVKAITDGDYEKAFLIARQTNPLVSVCSRVCTA--PCEKSC-RKKDEGSPVDIRALKRFACDRH 97
Cdd:pfam14691 32 CVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQerQCEGACvLGKKGFEPVAIGRLERFAADWA 108
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
173-453 |
9.67e-13 |
|
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: 69.45 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 173 RVTIFEAASLPGGmLRTGIP-----GFRLPKEILQQEIDAILELGVELKLNSP---IGRDQ---SLADLRAQGYEAVFIT 241
Cdd:COG0446 7 EITVIEKGPHHSY-QPCGLPyyvggGIKDPEDLLVRTPESFERKGIDVRTGTEvtaIDPEAktvTLRDGETLSYDKLVLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 242 IGLQdpLRILDMEGTDLKGIYS-----GVDYVRDYEKISLGKRCLVIGGGGVAIDCAQHAVRQGAgQVMIacLES----W 312
Cdd:COG0446 86 TGAR--PRPPPIPGLDLPGVFTlrtldDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGL-KVTL--VERaprlL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 313 ETMPASLSE--KEDAQEEGIVFHPSLGPRRFLGHEGrvTRVEFlkvssvfdaegkfsptfvpNSTTILEVDSVILAVGQA 390
Cdd:COG0446 161 GVLDPEMAAllEEELREHGVELRLGETVVAIDGDDK--VAVTL-------------------TDGEEIPADLVVVAPGVR 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2017541172 391 STApSLSGLEGLEMTPNGLIRAAEDMSTNLPGVFVGGDV---------RWRFTRNATDAIADGQKAARAIHG 453
Cdd:COG0446 220 PNT-ELAKDAGLALGERGWIKVDETLQTSDPDVYAAGDCaevphpvtgKTVYIPLASAANKQGRVAAENILG 290
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
150-609 |
2.68e-11 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 66.42 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGM---LRTGIPGFRLPKEILQQEIDAILE-LGVELKLNSPIgrdq 225
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDCPQCILEPLIAEVEAnPNITVYTGAEV---- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 226 sladLRAQGYEAVFITIGLQDPLRILDME--------GTDLK----------GIYSGVDYVRDYEKISLGKRCLVIGGGG 287
Cdd:COG1148 218 ----EEVSGYVGNFTVTIKKGPREEIEIEvgaivlatGFKPYdptklgeygyGKYPNVITNLELERLLAAGKILRPSDGK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 288 VA-----IDCA-----------------QHAVRQGagqvmIACLESWETMPASL--------SEKED----AQEEGIVFH 333
Cdd:COG1148 294 EPksvafIQCVgsrdeenglpycsrvccMYALKQA-----LYLKEKNPDADVYIfyrdirtyGKYEEfyrrAREDGVRFI 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 334 PslgprrflgheGRVTRVE-----FLKVSsVFDAEGkfsptfvpNSTTILEVDSVILAVGQ--ASTAPSLSGLEGLEMTP 406
Cdd:COG1148 369 R-----------GRVAEIEedeggKLVVT-VEDTLL--------GEPVEIEADLVVLATGMvpSEDNEELAKLLKLPLDQ 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 407 NGLIRAAED----MSTNLPGVFVGGDVRWrfTRNATDAIADGQKAA-RAIhGYLGGKTLEVrkkgymralapdfentrce 481
Cdd:COG1148 429 DGFFLEAHPklrpVETATDGIFLAGAAHG--PKDIPESIAQATAAAaRAI-QLLSKGELGV------------------- 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 482 tiAPIKipkraaserirtkeeitlgydeaqarqqaarcrqcsiqAVFDRSRCLLCGTCAETCVNGALRLVrvadiqgDEK 561
Cdd:COG1148 487 --EPSV--------------------------------------AEVDPEKCTGCGRCVEVCPYGAISID-------EKG 519
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2017541172 562 VAKLtdalekasprtrgmtaiikDESRCVSCGMCARRCPGGAITMAEF 609
Cdd:COG1148 520 VAEV-------------------NPALCKGCGTCAAACPSGAISLKGF 548
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
150-189 |
2.83e-11 |
|
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: 66.01 E-value: 2.83e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRT 189
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRT 42
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
150-302 |
5.41e-11 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 65.10 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 150 RVAIVGSGPTGLSAAHDL--ALLGYRVTIFEAASLPGGMLRTGIPGFRLPKEILQQEIDAILELG-VELKLNSPIGRDQS 226
Cdd:PLN02852 28 HVCVVGSGPAGFYTADKLlkAHDGARVDIIERLPTPFGLVRSGVAPDHPETKNVTNQFSRVATDDrVSFFGNVTLGRDVS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 227 LADLRAQgYEAVFITIGLQ-DplRILDMEGTDLKGIYSGVDYVRDYE----------KISLGKRCLVIGGGGVAIDCA-- 293
Cdd:PLN02852 108 LSELRDL-YHVVVLAYGAEsD--RRLGIPGEDLPGVLSAREFVWWYNghpdcvhlppDLKSSDTAVVLGQGNVALDCAri 184
|
170 180
....*....|....*....|...
gi 2017541172 294 --------------QHAVRQGAG 302
Cdd:PLN02852 185 llrptdelastdiaEHALEALRG 207
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
150-189 |
7.88e-11 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 64.52 E-value: 7.88e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRT 189
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAAS 40
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
527-606 |
4.40e-10 |
|
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: 57.79 E-value: 4.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 527 VFDRSRCLLCGTCAETCVNGALRLVRVADIQGDE-------------------KVAKLTDALEKASPRTRGmtAIIkDES 587
Cdd:cd10549 2 KYDPEKCIGCGICVKACPTDAIELGPNGAIARGPeidedkcvfcgacvevcptGAIELTPEGKEYVPKEKE--AEI-DEE 78
|
90
....*....|....*....
gi 2017541172 588 RCVSCGMCARRCPGGAITM 606
Cdd:cd10549 79 KCIGCGLCVKVCPVDAITL 97
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
150-195 |
7.27e-10 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 61.79 E-value: 7.27e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRTG-IPGFR 195
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFeRPGFR 51
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
422-608 |
1.60e-09 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 58.58 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 422 GVFVGGDVRWRFTRNATDAIADGQKAARAIHGYLGGKTLEVRKKGYMRALAPDFENTRCETIAPIKIPKRAASERIRTKE 501
Cdd:COG1145 78 AGEIVRVGIAAADLNLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 502 EITLGYDEAQARQQAARCRqcsiqAVFDRSRCLLCGTCAETCVNGALRLVRvadiqgdekvakltdalekasprtrGMTA 581
Cdd:COG1145 158 ISGGKKIEEELKIAIKKAK-----AVIDAEKCIGCGLCVKVCPTGAIRLKD-------------------------GKPQ 207
|
170 180
....*....|....*....|....*..
gi 2017541172 582 IIKDESRCVSCGMCARRCPGGAITMAE 608
Cdd:COG1145 208 IVVDPDKCIGCGACVKVCPVGAISLEP 234
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
526-608 |
2.00e-09 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 53.96 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 526 AVFDRSRCLLCGTCAETCVNGALRLVrvadiqgdekvakltdalekasprtrGMTAIIKDESRCVSCGMCARRCPGGAIT 605
Cdd:COG1149 6 PVIDEEKCIGCGLCVEVCPEGAIKLD--------------------------DGGAPVVDPDLCTGCGACVGVCPTGAIT 59
|
...
gi 2017541172 606 MAE 608
Cdd:COG1149 60 LEE 62
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
153-197 |
4.32e-09 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 52.92 E-value: 4.32e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2017541172 153 IVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRTG-IPGFRLP 197
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYrVPGYVFD 46
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
527-606 |
8.67e-09 |
|
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: 53.94 E-value: 8.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 527 VFDRSRCLLCGTCAETCVNGALRLVRVADIQGDEKVAKLTD--------ALEKASP-----RTRGMTAIIkDESRCVSCG 593
Cdd:cd10549 36 EIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEKEAEIDeekcigcgLCVKVCPvdaitLEDELEIVI-DKEKCIGCG 114
|
90
....*....|...
gi 2017541172 594 MCARRCPGGAITM 606
Cdd:cd10549 115 ICAEVCPVNAIKL 127
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
143-194 |
3.60e-08 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 56.08 E-value: 3.60e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2017541172 143 SSRKAAARVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRTGIPGF 194
Cdd:COG1231 2 SRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGD 53
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
147-185 |
6.33e-08 |
|
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: 55.25 E-value: 6.33e-08
10 20 30
....*....|....*....|....*....|....*....
gi 2017541172 147 AAARVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGG 185
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
527-605 |
6.64e-08 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 49.66 E-value: 6.64e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541172 527 VFDRSRCLLCGTCAETCVNGALRLVrvadiqgdekvakltdalekasprtrGMTAIIkDESRCVSCGMCARRCPGGAIT 605
Cdd:COG2221 11 KIDEEKCIGCGLCVAVCPTGAISLD--------------------------DGKLVI-DEEKCIGCGACIRVCPTGAIK 62
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
523-608 |
1.02e-07 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 49.67 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 523 SIQAVFDRSRCLLCGTCAETCVNGALRLVrvadiqgDEKVAKLtdalekasprtrgmtaiikDESRCVSCGMCARRCPGG 602
Cdd:COG1144 22 VERPVVDEDKCIGCGLCWIVCPDGAIRVD-------DGKYYGI-------------------DYDYCKGCGICAEVCPVK 75
|
....*.
gi 2017541172 603 AITMAE 608
Cdd:COG1144 76 AIEMVP 81
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
526-610 |
2.48e-07 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 48.17 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 526 AVFDRSRCLLCGTCAETCVNGALRLVRvadiqgdekvakltdalekasprtRGMTAIIKDESRCVSCGMCARRCPGGAIT 605
Cdd:COG1146 3 PVIDTDKCIGCGACVEVCPVDVLELDE------------------------EGKKALVINPEECIGCGACELVCPVGAIT 58
|
....*
gi 2017541172 606 MAEFY 610
Cdd:COG1146 59 VEDDE 63
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
530-609 |
3.11e-07 |
|
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: 47.82 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 530 RSRCLLCGTCAETCVNGALRLVRVadiqgdekvakltdalekasprtRGMTAIIKDESRCVSCGMCARRCPGGAITMAEF 609
Cdd:COG1143 1 EDKCIGCGLCVRVCPVDAITIEDG-----------------------EPGKVYVIDPDKCIGCGLCVEVCPTGAISMTPF 57
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
522-605 |
6.69e-07 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 51.95 E-value: 6.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 522 CSIQAVFDRSRCLLCGTCAETCVNGAlrlvrvadIQGDEKVAKLtdalekasprtrgmtaiikDESRCVSCGMCARRCPG 601
Cdd:COG4624 82 RGPSIIRDKEKCKNCYPCVRACPVKA--------IKVDDGKAEI-------------------DEEKCISCGQCVAVCPF 134
|
....
gi 2017541172 602 GAIT 605
Cdd:COG4624 135 GAIT 138
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
150-191 |
1.20e-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: 50.86 E-value: 1.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPG--------GMLRTGI 191
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGL 50
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
523-611 |
1.49e-06 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 46.26 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 523 SIQAVFDRSRCLLCGTCAETCVNGAlrlvrvadIQGDEKVAKLtdalekasprtrgmtaiikDESRCVSCGMCARRCPGG 602
Cdd:COG2768 3 LGKPYVDEEKCIGCGACVKVCPVGA--------ISIEDGKAVI-------------------DPEKCIGCGACIEVCPVG 55
|
....*....
gi 2017541172 603 AITMAEFYS 611
Cdd:COG2768 56 AIKIEWEED 64
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
150-185 |
1.57e-06 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 50.88 E-value: 1.57e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2017541172 150 RVAIVGSGPTGLSAAHdlaLLG--YRVTIFEAASLPGG 185
Cdd:COG2907 5 RIAVIGSGISGLTAAW---LLSrrHDVTLFEANDRLGG 39
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
150-188 |
1.62e-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: 50.32 E-value: 1.62e-06
10 20 30
....*....|....*....|....*....|....*....
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLR 188
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGR 43
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
151-189 |
2.81e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 50.27 E-value: 2.81e-06
10 20 30
....*....|....*....|....*....|....*....
gi 2017541172 151 VAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRT 189
Cdd:PRK07208 7 VVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRT 45
|
|
| PRK05888 |
PRK05888 |
NADH-quinone oxidoreductase subunit NuoI; |
573-606 |
3.70e-06 |
|
NADH-quinone oxidoreductase subunit NuoI;
Pssm-ID: 235637 [Multi-domain] Cd Length: 164 Bit Score: 47.18 E-value: 3.70e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2017541172 573 SPRTRGMTAIIKDES---RCVSCGMCARRCPGGAITM 606
Cdd:PRK05888 41 SPRFRGRHALRRDPNgeeRCIACKLCAAICPADAITI 77
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
147-197 |
3.89e-06 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 49.52 E-value: 3.89e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2017541172 147 AAARVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLP-------GGMLRTGIPGFRLP 197
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGsgasgrnAGQLRPGLAALADR 58
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
528-608 |
4.40e-06 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 46.47 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 528 FDRSRCLLCGTCAETCVNGALRLVRVADIQ-----GDEKVAKL------------TDALeKASPRTRGMTAIIKDESRCV 590
Cdd:cd10564 42 FSRGECTFCGACAEACPEGALDPAREAPWPlraeiGDSCLALQgvecrscqdacpTQAI-RFRPRLGGIALPELDADACT 120
|
90
....*....|....*...
gi 2017541172 591 SCGMCARRCPGGAITMAE 608
Cdd:cd10564 121 GCGACVSVCPVGAITLTP 138
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
482-522 |
7.90e-06 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 48.64 E-value: 7.90e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2017541172 482 TIAPIKIPKRAASERIRTKEEITLGYDEAQARQQAARCRQC 522
Cdd:PRK11749 5 TTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQC 45
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
513-610 |
9.98e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 48.61 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 513 RQQAARCRQCSIQavfDRSRCLLCGTCAETCVNGALRLVRVADIQGDEKVAKLTDALekasprtrgmtaiikDESRCVSC 592
Cdd:PRK13984 30 REAAERYRGFHIN---DWEKCIGCGTCSKICPTDAITMVEVPDLPQEYGKKPQRPVI---------------DYGRCSFC 91
|
90
....*....|....*...
gi 2017541172 593 GMCARRCPGGAITMAEFY 610
Cdd:PRK13984 92 ALCVDICTTGSLKMTREY 109
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
146-221 |
1.02e-05 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 48.21 E-value: 1.02e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541172 146 KAAARVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPggMLRTgipgfrLPKE---ILQQeidAILELGVELKLNSPI 221
Cdd:COG1251 140 APGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRL--LPRQ------LDEEagaLLQR---LLEALGVEVRLGTGV 207
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
151-453 |
1.19e-05 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 48.16 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 151 VAIVGSGPTGLSAAHDLALLGYRVTIFEAASLpGG------------MLRT-------------GI----PGFRLPKeiL 201
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGRL-GGtclnvgcipskaLLHAaevahearhaaefGIsagaPSVDWAA--L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 202 QQEIDAILElgvelKLNSpiGRDQSLADLRAQGY--EAVFI---TIGLQDPLRI---------------LDMEGTDLKGI 261
Cdd:COG1249 83 MARKDKVVD-----RLRG--GVEELLKKNGVDVIrgRARFVdphTVEVTGGETLtadhiviatgsrprvPPIPGLDEVRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 262 YsgvdyvrDYEKI----SLGKRCLVIGGGGVAIDCAQHAVRQGAgQVMIacLESWET----MPASLSE--KEDAQEEGIV 331
Cdd:COG1249 156 L-------TSDEAleleELPKSLVVIGGGYIGLEFAQIFARLGS-EVTL--VERGDRllpgEDPEISEalEKALEKEGID 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 332 FHpslgprrfLGHegRVTRVEflkvssvfDAEGKFSPTF-VPNSTTILEVDSVILAVG-QASTApSLsGLE--GLEMTPN 407
Cdd:COG1249 226 IL--------TGA--KVTSVE--------KTGDGVTVTLeDGGGEEAVEADKVLVATGrRPNTD-GL-GLEaaGVELDER 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2017541172 408 GLIRAAEDMSTNLPGVFVGGDV--RWRFtrnATDAIADGQKAARAIHG 453
Cdd:COG1249 286 GGIKVDEYLRTSVPGIYAIGDVtgGPQL---AHVASAEGRVAAENILG 330
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
533-603 |
1.23e-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: 42.90 E-value: 1.23e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2017541172 533 CLLCGTCAETCVNGALRLVRVADIQGDEKVAKltdalekasprtrgmtaiikDESRCVSCGMCARRCPGGA 603
Cdd:pfam12838 1 CIGCGACVAACPVGAITLDEVGEKKGTKTVVI--------------------DPERCVGCGACVAVCPTGA 51
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-219 |
1.27e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 425450 [Multi-domain] Cd Length: 80 Bit Score: 43.73 E-value: 1.27e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMlrtgipgfrLPKEILQQEIDAILELGVELKLNS 219
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPG---------FDPEIAKILQEKLEKNGIEFLLNT 61
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
526-608 |
1.58e-05 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 43.11 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 526 AVFDRSRCLLCGTCAETCVNGALRLvrvadiqGDEKVAkltdalekasprtrgmtaiIkDESRCVSCGMCARRCPGGAIT 605
Cdd:COG4231 17 YVIDEDKCTGCGACVKVCPADAIEE-------GDGKAV-------------------I-DPDLCIGCGSCVQVCPVDAIK 69
|
...
gi 2017541172 606 MAE 608
Cdd:COG4231 70 LEK 72
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
267-427 |
1.71e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 46.83 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 267 YVRDYEKISlGKRCLVIGGGGVAIDCAQHAVRQGAGQVMI---ACLESWETMPaSLSEKEDAQE--EGIVFHPSLgprRF 341
Cdd:pfam13738 146 YVKDFHPYA-GQKVVVIGGYNSAVDAALELVRKGARVTVLyrgSEWEDRDSDP-SYSLSPDTLNrlEELVKNGKI---KA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 342 LGHEgRVTRVEFLKVSSVfdaegkfspTFVPNSTTILEVDSVILAVGQASTAPSLSGlEGLEMTPNGLIR-AAEDMSTNL 420
Cdd:pfam13738 221 HFNA-EVKEITEVDVSYK---------VHTEDGRKVTSNDDPILATGYHPDLSFLKK-GLFELDEDGRPVlTEETESTNV 289
|
....*..
gi 2017541172 421 PGVFVGG 427
Cdd:pfam13738 290 PGLFLAG 296
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
150-196 |
2.25e-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: 47.16 E-value: 2.25e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRTGI-PGFRL 196
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTWRDNRyPGLRL 55
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
147-213 |
3.19e-05 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 45.54 E-value: 3.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541172 147 AAARVAIVGSGPTGLSAAHDLAL-LGYRVTIFEAASLPGGMLRTGIPGFrlPKEILQQEIDAIL-ELGV 213
Cdd:pfam01946 16 AESDVVIVGAGSSGLTAAYYLAKnRGLKVAIIERSVSPGGGAWLGGQLF--SAMVVRKPAHLFLdEFGI 82
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
527-606 |
3.39e-05 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 43.92 E-value: 3.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 527 VFDRSRCLLCGTCAETC-----VNGALRLVRVADIQGDEKVAKL------------------TDALEKaspRTRGMTAIi 583
Cdd:cd04410 2 VVDLDRCIGCGTCEVACkqehgLRPGPDWSRIKVIEGGGLERAFlpvscmhcedppcvkacpTGAIYK---DEDGIVLI- 77
|
90 100
....*....|....*....|...
gi 2017541172 584 kDESRCVSCGMCARRCPGGAITM 606
Cdd:cd04410 78 -DEDKCIGCGSCVEACPYGAIVF 99
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
150-189 |
3.51e-05 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 46.77 E-value: 3.51e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLG--YRVTIFEAASLPGGMLRT 189
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQT 43
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
578-608 |
4.55e-05 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 41.58 E-value: 4.55e-05
10 20 30
....*....|....*....|....*....|.
gi 2017541172 578 GMTAIIKDESRCVSCGMCARRCPGGAITMAE 608
Cdd:COG2221 6 GTWPPKIDEEKCIGCGLCVAVCPTGAISLDD 36
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
527-608 |
4.64e-05 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 43.42 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 527 VFDRSRCLLCGTCAETCVNGAlrlvrvadIQGDEKVAKltdalekasprtrgmtAIIkdesrCVSCGMCARRCPGGAITM 606
Cdd:cd16370 79 VLDKEKCIGCGNCVKACIVGA--------IFWDEETNK----------------PII-----CIHCGYCARYCPHDVLAM 129
|
..
gi 2017541172 607 AE 608
Cdd:cd16370 130 EE 131
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
153-434 |
7.61e-05 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 45.58 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 153 IVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRTG-IP--------------------GFRLPKEIlqqEID--AIL 209
Cdd:PRK06370 10 VIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGcVPtktliasaraahlarraaeyGVSVGGPV---SVDfkAVM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 210 ELGVELKLNSPIGRDQSLADLRA----QGyEAVFI---TIGLQDPL----RILDMEGT-----DLKGIySGVDYVRDYEK 273
Cdd:PRK06370 87 ARKRRIRARSRHGSEQWLRGLEGvdvfRG-HARFEspnTVRVGGETlrakRIFINTGAraaipPIPGL-DEVGYLTNETI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 274 ISLG---KRCLVIGGGGVAIDCAQHAVRQGAgQVMIacLESWETmpasLSEKEDAQEEGIVfhpslgpRRFLGHEGrvtr 350
Cdd:PRK06370 165 FSLDelpEHLVIIGGGYIGLEFAQMFRRFGS-EVTV--IERGPR----LLPREDEDVAAAV-------REILEREG---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 351 VEFL---KVSSVFDAEGKFSPTFVPNS-TTILEVDSVILAVGQASTAPSLsGLE--GLEMTPNGLIRAAEDMSTNLPGVF 424
Cdd:PRK06370 227 IDVRlnaECIRVERDGDGIAVGLDCNGgAPEITGSHILVAVGRVPNTDDL-GLEaaGVETDARGYIKVDDQLRTTNPGIY 305
|
330
....*....|..
gi 2017541172 425 VGGDV--RWRFT 434
Cdd:PRK06370 306 AAGDCngRGAFT 317
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
489-524 |
8.32e-05 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 45.54 E-value: 8.32e-05
10 20 30
....*....|....*....|....*....|....*.
gi 2017541172 489 PKRAASERIRTKEEITLGYDEAQARQQAARCRQCSI 524
Cdd:PRK12810 16 KKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGI 51
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
526-609 |
9.08e-05 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 44.54 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 526 AVFDRSRCLLCGTCAETCVNGALRLvrvadIQGDEKVAkltdalekASPRTRGMTAIIKD--ESRCVSCGMCARRCPGGA 603
Cdd:PRK07118 163 PVVDEDKCTGCGACVKACPRNVIEL-----IPKSARVF--------VACNSKDKGKAVKKvcEVGCIGCGKCVKACPAGA 229
|
....*.
gi 2017541172 604 ITMAEF 609
Cdd:PRK07118 230 ITMENN 235
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
527-612 |
1.09e-04 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 42.34 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 527 VFDRSRCLLCGTCAETCV---NGALRLVRVADIQGdEKVAKLTDAL----------EKASPR---TRGMTAIIKDESRCV 590
Cdd:COG1142 6 IADPEKCIGCRTCEAACAvahEGEEGEPFLPRIRV-VRKAGVSAPVqcrhcedapcAEVCPVgaiTRDDGAVVVDEEKCI 84
|
90 100
....*....|....*....|..
gi 2017541172 591 SCGMCARRCPGGAITMAEFYSQ 612
Cdd:COG1142 85 GCGLCVLACPFGAITMVGEKSR 106
|
|
| PLN02576 |
PLN02576 |
protoporphyrinogen oxidase |
146-189 |
1.16e-04 |
|
protoporphyrinogen oxidase
Pssm-ID: 215314 [Multi-domain] Cd Length: 496 Bit Score: 45.00 E-value: 1.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2017541172 146 KAAARVAIVGSGPTGLSAAHDLAL-LGYRVTIFEAASLPGGMLRT 189
Cdd:PLN02576 10 ASSKDVAVVGAGVSGLAAAYALASkHGVNVLVTEARDRVGGNITS 54
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
151-429 |
1.21e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 44.78 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 151 VAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRTG-IP------------------GFRLPKEILQQEIDAILE- 210
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVGcIPskaliaaaeafheakhaeEFGIHADGPKIDFKKVMAr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 211 ---------LGVELKLnspigrDQSLADLRAQGY------------------EAVFITIGLQDPlRILDMEGTDLKGIYS 263
Cdd:PRK06292 86 vrrerdrfvGGVVEGL------EKKPKIDKIKGTarfvdpntvevngerieaKNIVIATGSRVP-PIPGVWLILGDRLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 264 GvDYVRDYEKisLGKRCLVIGGGGVAIDCAQHAVRQGAgQVMIacLESWETMpASLSEKEDAQEegivFHPSLGpRRF-- 341
Cdd:PRK06292 159 S-DDAFELDK--LPKSLAVIGGGVIGLELGQALSRLGV-KVTV--FERGDRI-LPLEDPEVSKQ----AQKILS-KEFki 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 342 -LGHEgrVTRVEFLK--VSSVFDAEGKfsptfvpnsTTILEVDSVILAVGQASTAPSLsGLE--GLEMTPNGLIRAAEDM 416
Cdd:PRK06292 227 kLGAK--VTSVEKSGdeKVEELEKGGK---------TETIEADYVLVATGRRPNTDGL-GLEntGIELDERGRPVVDEHT 294
|
330
....*....|...
gi 2017541172 417 STNLPGVFVGGDV 429
Cdd:PRK06292 295 QTSVPGIYAAGDV 307
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
576-608 |
1.25e-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: 40.48 E-value: 1.25e-04
10 20 30
....*....|....*....|....*....|...
gi 2017541172 576 TRGMTAIIkDESRCVSCGMCARRCPGGAITMAE 608
Cdd:COG1149 1 VKRKIPVI-DEEKCIGCGLCVEVCPEGAIKLDD 32
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
582-605 |
1.85e-04 |
|
4Fe-4S binding 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.
Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 38.77 E-value: 1.85e-04
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
566-606 |
2.52e-04 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 41.41 E-value: 2.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2017541172 566 TDALEKaSPRTRgmtAIIKDESRCVSCGMCARRCPGGAITM 606
Cdd:cd10550 63 VGAISR-DEETG---AVVVDEDKCIGCGMCVEACPFGAIRV 99
|
|
| PRK14028 |
PRK14028 |
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional |
525-606 |
2.61e-04 |
|
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
Pssm-ID: 172522 [Multi-domain] Cd Length: 312 Bit Score: 43.45 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 525 QAVFDRSRCLLCGTCAETCVNGALrlvrvadiqgdekvakLTDALEKASPRTRG--MTAIIKDESRCVSCGMCARRCPGG 602
Cdd:PRK14028 241 KPVIDHSKCIMCRKCWLYCPDDAI----------------IEAWREAEGPRGRKfrMKMIDFDYQYCKGCGVCAEVCPTG 304
|
....
gi 2017541172 603 AITM 606
Cdd:PRK14028 305 AIQM 308
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
486-522 |
2.79e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 43.85 E-value: 2.79e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2017541172 486 IKIPKRAASERIRTKEEITLGYDEAQARQQAARCRQC 522
Cdd:PRK12831 9 VPVREQDPEVRATNFEEVCLGYNEEEAVKEASRCLQC 45
|
|
| DMSOR_beta_like |
cd16367 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
527-607 |
3.01e-04 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319889 [Multi-domain] Cd Length: 138 Bit Score: 41.14 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 527 VFDRSRCLLCGTCAETCV---NGALRLVRVADIQGDEKVAK----------LTDALEKASPRTRGMTAIIKDesRCVSCG 593
Cdd:cd16367 15 VIDLDRCIRCDNCEKACAdthDGHSRLDRNGLRFGNLLVPTacrhcvdpvcMIGCPTGAIHRDDGGEVVISD--ACCGCG 92
|
90
....*....|....
gi 2017541172 594 MCARRCPGGAITMA 607
Cdd:cd16367 93 NCASACPYGAIQMV 106
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
108-189 |
3.54e-04 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 43.70 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 108 RLDELSQQAEWVGDRTGNHILTMSRQFRKvkearessrkaaaRVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGML 187
Cdd:PLN02976 666 RNELQSVQSNSCIEMGGNHCVLCDSVDRK-------------KIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRV 732
|
..
gi 2017541172 188 RT 189
Cdd:PLN02976 733 YT 734
|
|
| HycB_like |
cd10554 |
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
516-614 |
3.56e-04 |
|
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.
Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 41.09 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 516 AARCRQCSIQAvfdrsrcllcgtCAETCVNGALRlvrvadiqgdekvakltdalekaspRTRGMTAIikDESRCVSCGMC 595
Cdd:cd10554 53 PVQCRQCEDAP------------CANVCPVGAIS-------------------------QEDGVVQV--DEERCIGCKLC 93
|
90
....*....|....*....
gi 2017541172 596 ARRCPGGAITMAEFYSQEE 614
Cdd:cd10554 94 VLACPFGAIEMAPTTVPGV 112
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
145-219 |
3.93e-04 |
|
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: 42.88 E-value: 3.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2017541172 145 RKAAARVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGmlrtgipgfRLPKEILQQEIDAILELGVELKLNS 219
Cdd:COG0446 121 EFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLG---------VLDPEMAALLEEELREHGVELRLGE 186
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
137-189 |
4.96e-04 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 43.06 E-value: 4.96e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2017541172 137 VKEA--RESSRKAAARVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRT 189
Cdd:PLN02328 225 IKEAqlRSFEGVEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKT 279
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
582-608 |
6.12e-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: 40.07 E-value: 6.12e-04
10 20
....*....|....*....|....*..
gi 2017541172 582 IIKDESRCVSCGMCARRCPGGAITMAE 608
Cdd:cd10549 1 LKYDPEKCIGCGICVKACPTDAIELGP 27
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
136-189 |
6.25e-04 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 43.08 E-value: 6.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2017541172 136 KVKEARESSRKAaarVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGGMLRT 189
Cdd:PLN03000 175 KDKFPAQSSKSS---VVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYT 225
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
151-178 |
8.69e-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: 41.93 E-value: 8.69e-04
10 20
....*....|....*....|....*...
gi 2017541172 151 VAIVGSGPTGLSAAHDLALLGYRVTIFE 178
Cdd:pfam01494 4 VLIVGGGPAGLMLALLLARAGVRVVLVE 31
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
496-522 |
9.24e-04 |
|
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: 39.06 E-value: 9.24e-04
10 20
....*....|....*....|....*..
gi 2017541172 496 RIRTKEEITLGYDEAQARQQAARCRQC 522
Cdd:pfam14691 1 RIKNFEEVALGYTEEEAIAEASRCLQC 27
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
150-428 |
1.06e-03 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 41.95 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALL--GYRVTIFE--------AASLP---GGMLRTgiPGF---RLPKEILQQEIDAILE--- 210
Cdd:PRK09564 2 KIIIIGGTAAGMSAAAKAKRLnkELEITVYEktdivsfgACGLPyfvGGFFDD--PNTmiaRTPEEFIKSGIDVKTEhev 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 211 LGVELKLNSPIGRDQSLADLRAQGYEAVFITIGLQdPLrILDMEGTDLKGIYSGVD-----YVRDYEKISLGKRCLVIGG 285
Cdd:PRK09564 80 VKVDAKNKTITVKNLKTGSIFNDTYDKLMIATGAR-PI-IPPIKNINLENVYTLKSmedglALKELLKDEEIKNIVIIGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 286 GGVAIDCAQHAVRQGAgQVMIACLESwETMPASLSEK------EDAQEEGIVFHPSLGPRRFLGhEGRVTRVEFLKvssv 359
Cdd:PRK09564 158 GFIGLEAVEAAKHLGK-NVRIIQLED-RILPDSFDKEitdvmeEELRENGVELHLNEFVKSLIG-EDKVEGVVTDK---- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541172 360 fdaeGKFsptfvpnsttilEVDSVILAVGQASTAPSLSGlEGLEMTPNGLIRAAEDMSTNLPGVFVGGD 428
Cdd:PRK09564 231 ----GEY------------EADVVIVATGVKPNTEFLED-TGLKTLKNGAIIVDEYGETSIENIYAAGD 282
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
587-606 |
1.16e-03 |
|
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).
Pssm-ID: 468407 [Multi-domain] Cd Length: 243 Bit Score: 41.00 E-value: 1.16e-03
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
151-178 |
1.23e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 41.82 E-value: 1.23e-03
10 20
....*....|....*....|....*...
gi 2017541172 151 VAIVGSGPTGLSAAHDLALLGYRVTIFE 178
Cdd:PRK06183 13 VVIVGAGPVGLTLANLLGQYGVRVLVLE 40
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
150-178 |
1.28e-03 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 41.55 E-value: 1.28e-03
10 20
....*....|....*....|....*....
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFE 178
Cdd:PRK12409 3 HIAVIGAGITGVTTAYALAQRGYQVTVFD 31
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
278-432 |
1.65e-03 |
|
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: 41.50 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 278 KRCLVIGGGGVAIDCAQ--HAVRQGAGQVMIA-----CLESW-ETMPASLSEKEDAQeeGIVFHPSLGPRrflghegrvt 349
Cdd:TIGR01423 188 RRVLTVGGGFISVEFAGifNAYKPRGGKVTLCyrnnmILRGFdSTLRKELTKQLRAN--GINIMTNENPA---------- 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 350 rveflKVSsvFDAEGKFSPTFvpNSTTILEVDSVILAVGQASTAPSLS-GLEGLEMTPNGLIRAAEDMSTNLPGVFVGGD 428
Cdd:TIGR01423 256 -----KVT--LNADGSKHVTF--ESGKTLDVDVVMMAIGRVPRTQTLQlDKVGVELTKKGAIQVDEFSRTNVPNIYAIGD 326
|
....
gi 2017541172 429 VRWR 432
Cdd:TIGR01423 327 VTDR 330
|
|
| CooF_like |
cd10563 |
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ... |
516-605 |
2.20e-03 |
|
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.
Pssm-ID: 319885 [Multi-domain] Cd Length: 140 Bit Score: 38.78 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 516 AARCRQCSIQAvfdrsrcllcgtCAETCVNGALRlvrvadiqgdekvakltdalekaspRTRGMTAIIKDESRCVSCGMC 595
Cdd:cd10563 54 PLQCRHCDEPP------------CVKACMSGAMH-------------------------KDPETGIVIHDEEKCVGCWMC 96
|
90
....*....|
gi 2017541172 596 ARRCPGGAIT 605
Cdd:cd10563 97 VMVCPYGAIR 106
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
151-185 |
2.31e-03 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 40.59 E-value: 2.31e-03
10 20 30
....*....|....*....|....*....|....*
gi 2017541172 151 VAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGG 185
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
490-569 |
2.38e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 40.89 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 490 KRAASERIRTKEEITLGYDEAQARQQAARCRQCSIQAVfdrsrcllcgtCAETC-----VNGALRLVRVADIQGDEKVAK 564
Cdd:PRK12769 198 KLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEHSI-----------CEWTCplhnhIPQWIELVKAGNIDAAVELSH 266
|
....*
gi 2017541172 565 LTDAL 569
Cdd:PRK12769 267 QTNSL 271
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
378-429 |
2.55e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 40.68 E-value: 2.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2017541172 378 LEVDSVILAVGQASTAPSLsGLE--GLEMTPNGLIRAAEDMSTNLPGVFVGGDV 429
Cdd:PRK06327 271 LEVDKLIVSIGRVPNTDGL-GLEavGLKLDERGFIPVDDHCRTNVPNVYAIGDV 323
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
526-616 |
2.83e-03 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 40.84 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 526 AVFDRSRCLLCGTCAETCVN----GALRLVR----VADIQGDEKVAKltDALEKASPRTRGMTAIIKDES-RCVSCGMCA 596
Cdd:PRK08493 136 INYDPSLCIVCERCVTVCKDkigeSALKTVPrgldAPDKSFKESMPK--DAYAVWSKKQKSLIGPVGGETlDCSFCGECI 213
|
90 100
....*....|....*....|.
gi 2017541172 597 RRCPGGAITMAEF-YSQEEWE 616
Cdd:PRK08493 214 AVCPVGALSSSDFqYTSNAWE 234
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
532-604 |
3.13e-03 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 35.99 E-value: 3.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2017541172 532 RCLLCGTCAETCVNGALRLVRVAdiqgdekvakltdalekasprtrGMTAIIKDESRCVSCGMCARRCPGGAI 604
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVG-----------------------QTIRGDIAGLACIGCGACVDACPRGAI 50
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
532-600 |
3.16e-03 |
|
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: 433017 [Multi-domain] Cd Length: 64 Bit Score: 36.52 E-value: 3.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2017541172 532 RCLLCGTCAETCVNGALRLVRVADIQGDEKVAKLtDALEKASPRTRGMtaiikdeSRCVSCGMCARRCP 600
Cdd:pfam13183 1 RCIRCGACLAACPVYLVTGGRFPGDPRGGAAALL-GRLEALEGLAEGL-------WLCTLCGACTEVCP 61
|
|
| PRK08132 |
PRK08132 |
FAD-dependent oxidoreductase; Provisional |
130-180 |
3.62e-03 |
|
FAD-dependent oxidoreductase; Provisional
Pssm-ID: 236158 [Multi-domain] Cd Length: 547 Bit Score: 40.24 E-value: 3.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2017541172 130 MSRQFRK--VKEARESSRKAAAR--VAIVGSGPTGLSAAHDLALLGYRVTIFEAA 180
Cdd:PRK08132 1 IDYQTPKfpYRPHADQDADDPARhpVVVVGAGPVGLALAIDLAQQGVPVVLLDDD 55
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
149-223 |
3.97e-03 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 40.00 E-value: 3.97e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2017541172 149 ARVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLpggmlrtgipgfRLPKE--ILQQEIDAIL-ELGVELKLNSPIGR 223
Cdd:PRK08010 159 GHLGILGGGYIGVEFASMFANFGSKVTILEAASL------------FLPREdrDIADNIATILrDQGVDIILNAHVER 224
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
479-522 |
4.40e-03 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 40.31 E-value: 4.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2017541172 479 RCETIAP--IKIPKRAASERIRTKEEITLGYDEAQARQQAARCRQC 522
Cdd:PRK12775 291 KLKTLVPhqTPMPERDAVERARNFKEVNLGYSLEDALQEAERCIQC 336
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
126-233 |
4.71e-03 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 39.51 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 126 HILTM-SRQFRKVKEARESSrkaAARVAIVGSGPTGLSAAHDLALLGYRVTIFE-AASLPGGMlrtgipgfrLPKEI--- 200
Cdd:PRK04965 121 LMLTLnSQQEYRAAETQLRD---AQRVLVVGGGLIGTELAMDLCRAGKAVTLVDnAASLLASL---------MPPEVssr 188
|
90 100 110
....*....|....*....|....*....|....
gi 2017541172 201 LQQeidAILELGVELKLNSPIGR-DQSLADLRAQ 233
Cdd:PRK04965 189 LQH---RLTEMGVHLLLKSQLQGlEKTDSGIRAT 219
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
157-184 |
7.49e-03 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 38.80 E-value: 7.49e-03
10 20
....*....|....*....|....*...
gi 2017541172 157 GPTGLSAAHDLALLGYRVTIFEAASLPG 184
Cdd:COG0644 2 GPAGSAAARRLARAGLSVLLLEKGSFPG 29
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
147-192 |
7.57e-03 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 39.17 E-value: 7.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2017541172 147 AAARVAIVGSGPTGLSAAHDLALLGY---RVTIFEAASLPGgmlrTGIP 192
Cdd:COG4529 4 ARKRIAIIGGGASGTALAIHLLRRAPeplRITLFEPRPELG----RGVA 48
|
|
| PRK08348 |
PRK08348 |
NADH-plastoquinone oxidoreductase subunit; Provisional |
527-607 |
8.03e-03 |
|
NADH-plastoquinone oxidoreductase subunit; Provisional
Pssm-ID: 181399 [Multi-domain] Cd Length: 120 Bit Score: 36.74 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 527 VFDRSRCLLCGTCAETCVNGALrlVRVADIQgdeKVAKLTdalekasprtrgmtaiikdeSRCVSCGMCARRCPGGAITM 606
Cdd:PRK08348 38 LYDVDKCVGCRMCVTVCPAGVF--VYLPEIR---KVALWT--------------------GRCVFCGQCVDVCPTGALQM 92
|
.
gi 2017541172 607 A 607
Cdd:PRK08348 93 S 93
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
533-606 |
8.25e-03 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 38.44 E-value: 8.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2017541172 533 CLLCGTCAETCVNGAlrlvrvadIQGDEKvakltdalekasprtrGMTAIIKDEsrCVSCGMCARRCPGGAITM 606
Cdd:COG2878 139 CIGCGDCIKACPFDA--------IVGAAK----------------GMHTVDEDK--CTGCGLCVEACPVDCIEM 186
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
150-185 |
8.62e-03 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 39.01 E-value: 8.62e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2017541172 150 RVAIVGSGPTGLSAAHDLALLGYRVTIFEAASLPGG 185
Cdd:PLN02487 77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGG 112
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
278-427 |
9.48e-03 |
|
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: 38.45 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 278 KRCLVIGGGGVAIDCAQHAVRQGAGQVMI---------ACLESwETMPASLSEKEDAQE--------EGIVFHPSLGPRR 340
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIedegtcpygGCVLS-KALLGAAEAPEIASLwadlykrkEEVVKKLNNGIEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 341 FLGHEgrvtrveflkVSSVFDAEGKF-SPTFVPNSTTILEVDSVILAVGQASTAPslsGLEGLEMTPNGLIRAAEDM--- 416
Cdd:pfam07992 80 LLGTE----------VVSIDPGAKKVvLEELVDGDGETITYDRLVIATGARPRLP---PIPGVELNVGFLVRTLDSAeal 146
|
170
....*....|....
gi 2017541172 417 -STNLPG--VFVGG 427
Cdd:pfam07992 147 rLKLLPKrvVVVGG 160
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
533-612 |
9.64e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 36.54 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2017541172 533 CLLCGTCAETCVNGALRlvrvADIQGdekvakltdalekasprtrgmtAIIKDESRCVSCGMCARRCPGGAITMAEFYSQ 612
Cdd:cd16372 49 CNQCGECIDVCPTGAIT----RDANG----------------------VVMINKKLCVGCLMCVGFCPEGAMFKHEDYPE 102
|
|
| |
