|
Name |
Accession |
Description |
Interval |
E-value |
| DHPD_FMN |
cd02940 |
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ... |
367-669 |
0e+00 |
|
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN, and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239244 Cd Length: 299 Bit Score: 556.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 367 DISVEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTFSLDKDIVTNVSPRIVRGTTSGPlygpGQGSFLNIE 446
Cdd:cd02940 1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVSPRIARLRTSGR----GQIGFNNIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 447 LISEKTAAYWCKSIAELKADFPNHVLIASIMCSYNRENWTELSKMAQVAGADALELNLSCPHGMGERGMGLACGQDPELV 526
Cdd:cd02940 77 LISEKPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 527 RNICRWVRQAVHIPFFAKLTPNVTDIVKIAMAAQEGGADGVTATNTVSGLMGLKADSTPwPAVGRGLRTTYGGVSGNAIR 606
Cdd:cd02940 157 EEICRWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTP-PAPGVEGKTTYGGYSGPAVK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032774312 607 PIALRAVSAIARAL-PGFPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGL 669
Cdd:cd02940 236 PIALRAVSQIARAPePGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
|
|
| PRK08318 |
PRK08318 |
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA; |
367-860 |
2.23e-129 |
|
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
Pssm-ID: 236237 [Multi-domain] Cd Length: 420 Bit Score: 394.31 E-value: 2.23e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 367 DISVEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTfsLDKDIVTNVSPRIvrgttsGPLYGPGQG--SFLN 444
Cdd:PRK08318 3 DLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKT--LGPPIVNVSSPRF------GALVKEDRRfiGFNN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 445 IELISEKTAAYWCKSIAELKADFPNHVLIASIMCSYNRENWTELSKMAQVAGADALELNLSCPHGMGERGMGLACGQDPE 524
Cdd:PRK08318 75 IELITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 525 LVRNICRWVRQAVHIPFFAKLTPNVTDIVKIAMAAQEGGADGVTATNTVSGLMGLKADS-TPWPAV-GRGlrtTYGGVSG 602
Cdd:PRK08318 155 LVEMYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRmIPMPIVnGKS---SHGGYCG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 603 NAIRPIALRAVSAIAR--ALPGFPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGlrallylksiee 680
Cdd:PRK08318 232 PAVKPIALNMVAEIARdpETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISG------------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 681 LEDWngqspatMrhqkgkpvprvadlmgkklpsfgpyleqrkkiiaenkiklkaqnmaaelpEKKHFvpkkpiPAVKDVI 760
Cdd:PRK08318 300 LSHY-------M--------------------------------------------------DEKGF------ASLEDMV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 761 GKALQYIGTYGDLCNTEQVVALIDEEMCINCGKCYMTCNDSGYQAIRFDPET--HLPTVTDSCTGCTLCLSVCPVIDCIR 838
Cdd:PRK08318 317 GLAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDEDGtrTPEVIEEECVGCNLCAHVCPVEGCIT 396
|
490 500
....*....|....*....|..
gi 2032774312 839 MVSRTTPYEPKRGLPLAVNPAR 860
Cdd:PRK08318 397 MGEVKFGKPYANWTTHPNNPAR 418
|
|
| DHOD_DHPD_FMN |
cd02810 |
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ... |
370-668 |
6.58e-93 |
|
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.
Pssm-ID: 239204 [Multi-domain] Cd Length: 289 Bit Score: 293.88 E-value: 6.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 370 VEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTFSLDkDIVTNVSPRIVRGTTSGPlYGPGQGSFLNIELIS 449
Cdd:cd02810 1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLH-PRPGNPLPRVARLPPEGE-SYPEQLGILNSFGLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 450 EKTAAYWCKSIAELKADFPNHVLIASIMCSyNRENWTELSKMAQVAGADALELNLSCPHGMGERGmglaCGQDPELVRNI 529
Cdd:cd02810 79 NLGLDVWLQDIAKAKKEFPGQPLIASVGGS-SKEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 530 CRWVRQAVHIPFFAKLTPNVT--DIVKIAMAAQEGGADGVTATNTVSGLMGLKadstpwPAVGRGLRTTYGGVSGNAIRP 607
Cdd:cd02810 154 LKAVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTISGRVVDL------KTVGPGPKRGTGGLSGAPIRP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032774312 608 IALRAVSAIARALP-GFPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTG 668
Cdd:cd02810 228 LALRWVARLAARLQlDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIKKE 289
|
|
| PLN02495 |
PLN02495 |
oxidoreductase, acting on the CH-CH group of donors |
367-688 |
1.68e-85 |
|
oxidoreductase, acting on the CH-CH group of donors
Pssm-ID: 215273 [Multi-domain] Cd Length: 385 Bit Score: 277.87 E-value: 1.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 367 DISVEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTFSLDKDIVTNVSPRIVR------GTTSGPLYGpgqg 440
Cdd:PLN02495 10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVTPRYARlraganGSAKGRVIG---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 441 sFLNIELISEKTAAYWCKSIAELKADFPNHVLIASIMCSYNRENWTELSKMAQVAGADALELNLSCPHGMGERGMGLACG 520
Cdd:PLN02495 86 -WQNIELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 521 QDPELVRNICRWVRQAVHIPFFAKLTPNVTDIVKIAMAAQEGGADGVTATNTVSGLMGLKADS-TPWPAVgRGLrTTYGG 599
Cdd:PLN02495 165 QDCDLLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLDTlRPEPCV-EGY-STPGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 600 VSGNAIRPIALRAVSAIARALPG-FP----ILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALLY 674
Cdd:PLN02495 243 YSSKAVRPIALAKVMAIAKMMKSeFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMK 322
|
330
....*....|....
gi 2032774312 675 LKSIEELEDWNGQS 688
Cdd:PLN02495 323 KHNFSSIEDFRGAS 336
|
|
| PyrD |
COG0167 |
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ... |
367-673 |
1.60e-83 |
|
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439937 [Multi-domain] Cd Length: 296 Bit Score: 269.25 E-value: 1.60e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 367 DISVEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTFSLDKdIVTNVSPRIVRgttsgpLygPGQGSFLNIE 446
Cdd:COG0167 1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEP-QPGNPRPRLFR------L--PEDSGLINRM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 447 LISEKTAAYWCKSIAELKAdfPNHVLIASIMCSyNRENWTELSKMAQVAGADALELNLSCPHGmgeRGMGLACGQDPELV 526
Cdd:COG0167 72 GLNNPGVDAFLERLLPAKR--YDVPVIVNIGGN-TVEDYVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 527 RNICRWVRQAVHIPFFAKLTPNVTDIVKIAMAAQEGGADGVTATNTVSGL-MGLKadsTPWPAVGRGlrttYGGVSGNAI 605
Cdd:COG0167 146 AELLAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGRaIDLE---TRRPVLANE----AGGLSGPAL 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032774312 606 RPIALRAVSAIARALPG-FPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALL 673
Cdd:COG0167 219 KPIALRMVREVAQAVGGdIPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYL 287
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
24-341 |
1.42e-78 |
|
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: 261.22 E-value: 1.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 24 KIALLGAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLGVKIIFRKGLAVDgMTL 103
Cdd:COG0493 123 KVAVVGSGPAGLAAAYQLARAGHE-VTVFEALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKD-ITL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 104 HTLKEDgYKAVFIGIG------LPEPNRDSifqglrmnQGFYTSKDFLPLVAMASKPGmcacnsPLPPIHGTVIVLGAGD 177
Cdd:COG0493 201 DELLEE-FDAVFLATGagkprdLGIPGEDL--------KGVHSAMDFLTAVNLGEAPD------TILAVGKRVVVIGGGN 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 178 TAFDCATSALRCGARRVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSPRKVVL-KGGQIVAMEFVRTE---QDSDGS 253
Cdd:COG0493 266 TAMDCARTALRLGAESVTIVYRRTREEMPASKEEVEEALEEGVEFLFLVAPVEIIGdENGRVTGLECVRMElgePDESGR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 254 WK--EDEDQVVRLKADVVISAFGSVLSDDKVREAMApIKFNRWGLPEIDPETMQTSEPWVFAGGDVGGLANTTVESVNDG 331
Cdd:COG0493 346 RRpvPIEGSEFTLPADLVILAIGQTPDPSGLEEELG-LELDKRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEG 424
|
330
....*....|
gi 2032774312 332 KQASWYMHRY 341
Cdd:COG0493 425 RKAARAIDRY 434
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
24-346 |
3.17e-72 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 244.70 E-value: 3.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 24 KIALLGAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLGVKiiFRKGLAVdGMTL 103
Cdd:PRK11749 142 KVAVIGAGPAGLTAAHRLARKGYD-VTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVE--IRTNTEV-GRDI 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 104 hTLKE--DGYKAVFIGIGLPEPNRDSIF-QGLrmnQGFYTSKDFLPLVAMASkpgmcacnSPLPPIHG-TVIVLGAGDTA 179
Cdd:PRK11749 218 -TLDElrAGYDAVFIGTGAGLPRFLGIPgENL---GGVYSAVDFLTRVNQAV--------ADYDLPVGkRVVVIGGGNTA 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 180 FDCATSALRCGARRVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSPRKVVLKGGQIVAMEFVRTE---QDSDGSWKE 256
Cdd:PRK11749 286 MDAARTAKRLGAESVTIVYRRGREEMPASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMElgePDASGRRRV 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 257 -DEDQVVRLKADVVISAFGSVlSDDKVREAMAPIKFNRWGLPEIDPETMQTSEPWVFAGGD-VGGlANTTVESVNDGKQA 334
Cdd:PRK11749 366 pIEGSEFTLPADLVIKAIGQT-PNPLILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDiVTG-AATVVWAVGDGKDA 443
|
330
....*....|..
gi 2032774312 335 SWYMHRYIQSLY 346
Cdd:PRK11749 444 AEAIHEYLEGAA 455
|
|
| PRK07259 |
PRK07259 |
dihydroorotate dehydrogenase; |
367-681 |
1.78e-61 |
|
dihydroorotate dehydrogenase;
Pssm-ID: 235982 Cd Length: 301 Bit Score: 210.01 E-value: 1.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 367 DISVEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTFSLDKDIvTNVSPRIVRgTTSG-----PLYGPGQGS 441
Cdd:PRK07259 1 RLSVELPGLKLKNPVMPASGTFGFGGEYARFYDLNGLGAIVTKSTTLEPRE-GNPTPRIAE-TPGGmlnaiGLQNPGVDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 442 FLNIELISEKtaaywcksiaelKADFPnhvLIASImCSYNRENWTEL-SKMAQVAGADALELNLSCPHGMGergMGLACG 520
Cdd:PRK07259 79 FIEEELPWLE------------EFDTP---IIANV-AGSTEEEYAEVaEKLSKAPNVDAIELNISCPNVKH---GGMAFG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 521 QDPELVRNICRWVRQAVHIPFFAKLTPNVTDIVKIAMAAQEGGADGVTATNTvsgLMGLKAD-STPWPAVGrglrTTYGG 599
Cdd:PRK07259 140 TDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAIDiKTRKPILA----NVTGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 600 VSGNAIRPIALRAVSAIARALpGFPILATGGIDSAETGLQFLHSGASVLQVCSAIQnQDFTVIDDYCTGLRALLY---LK 676
Cdd:PRK07259 213 LSGPAIKPIALRMVYQVYQAV-DIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDkygIK 290
|
....*
gi 2032774312 677 SIEEL 681
Cdd:PRK07259 291 SIEEI 295
|
|
| DHOD_1B_like |
cd04740 |
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ... |
369-688 |
6.95e-59 |
|
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240091 [Multi-domain] Cd Length: 296 Bit Score: 202.78 E-value: 6.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 369 SVEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTFSLDKDIvTNVSPRIVRgTTSG-----PLYGPGQGSFL 443
Cdd:cd04740 1 SVELAGLRLKNPVILASGTFGFGEELSRVADLGKLGAIVTKSITLEPRE-GNPPPRVVE-TPGGmlnaiGLQNPGVEAFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 444 NIELIsektaaywcksiAELKADFPnhvLIASIMCSyNRENWTELSKMAQVAGADALELNLSCPHgmgERGMGLACGQDP 523
Cdd:cd04740 79 EELLP------------WLREFGTP---VIASIAGS-TVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 524 ELVRNICRWVRQAVHIPFFAKLTPNVTDIVKIAMAAQEGGADGVTATNTvsgLMGLKADS-TPWPAVGRGlrttYGGVSG 602
Cdd:cd04740 140 EAVAEIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINT---LKGMAIDIeTRKPILGNV----TGGLSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 603 NAIRPIALRAVSAIARALpGFPILATGGIDSAETGLQFLHSGASVLQVCSAIQnQDFTVIDDYCTGLRALLYLKSIEELE 682
Cdd:cd04740 213 PAIKPIALRMVYQVYKAV-EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLDEEGIKSIE 290
|
....*.
gi 2032774312 683 DWNGQS 688
Cdd:cd04740 291 ELVGLA 296
|
|
| pyrD_sub1_fam |
TIGR01037 |
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ... |
368-681 |
3.32e-53 |
|
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.
Pssm-ID: 130109 [Multi-domain] Cd Length: 300 Bit Score: 187.25 E-value: 3.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 368 ISVEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTFSLDKDIvTNVSPRIVRgTTSG-----PLYGPGQGSF 442
Cdd:TIGR01037 1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLEPRP-GYRNPTIVE-TPCGmlnaiGLQNPGVEAF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 443 LNiELISEKTaaywcksiaelkaDFPNHvLIASIMCSyNRENWTELSKMAQVAG--ADALELNLSCPHGMGergMGLACG 520
Cdd:TIGR01037 79 LE-ELKPVRE-------------EFPTP-LIASVYGS-SVEEFAEVAEKLEKAPpyVDAYELNLSCPHVKG---GGIAIG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 521 QDPELVRNICRWVRQAVHIPFFAKLTPNVTDIVKIAMAAQEGGADGVTATNTvsgLMGLKAD-STPWPAvgrgLRTTYGG 599
Cdd:TIGR01037 140 QDPELSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKIDiKTGKPI----LANKTGG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 600 VSGNAIRPIALRAVSAIARALpGFPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFtVIDDYCTGLRALLY---LK 676
Cdd:TIGR01037 213 LSGPAIKPIALRMVYDVYKMV-DIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKaegFT 290
|
....*
gi 2032774312 677 SIEEL 681
Cdd:TIGR01037 291 SIEEL 295
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
24-344 |
1.41e-48 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 179.06 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 24 KIALLGAGPASLSCASFLARLGYsNITIFEKQEYLGGLSMSEIPQFRLPYD-VVNFEAELMKDLGVKI----IFRKGLAV 98
Cdd:PRK12831 142 KVAVIGSGPAGLTCAGDLAKMGY-DVTIFEALHEPGGVLVYGIPEFRLPKEtVVKKEIENIKKLGVKIetnvVVGKTVTI 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 99 DGMtlhtLKEDGYKAVFIGIGLPEPNRDSIfQGLRMNqGFYTSKDFLPLVAM--ASKPGMcacNSPLPpIHGTVIVLGAG 176
Cdd:PRK12831 221 DEL----LEEEGFDAVFIGSGAGLPKFMGI-PGENLN-GVFSANEFLTRVNLmkAYKPEY---DTPIK-VGKKVAVVGGG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 177 DTAFDCATSALRCGARrVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSP-RKVVLKGGQIVAMEFVRT---EQDSDG 252
Cdd:PRK12831 291 NVAMDAARTALRLGAE-VHIVYRRSEEELPARVEEVHHAKEEGVIFDLLTNPvEILGDENGWVKGMKCIKMelgEPDASG 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 253 SWK--EDEDQVVRLKADVVISAFGsvLSDDKVREAMAP-IKFNRWGLPEIDPETMQTSEPWVFAGGD-VGGLAnTTVESV 328
Cdd:PRK12831 370 RRRpvEIEGSEFVLEVDTVIMSLG--TSPNPLISSTTKgLKINKRGCIVADEETGLTSKEGVFAGGDaVTGAA-TVILAM 446
|
330
....*....|....*.
gi 2032774312 329 NDGKQASWYMHRYIQS 344
Cdd:PRK12831 447 GAGKKAAKAIDEYLSK 462
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
8-344 |
1.02e-47 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 181.86 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 8 NPSLPpleDMPEAYQVKIALLGAGPASLSCASFLARLGYsNITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLG 87
Cdd:PRK12778 420 NISVP---EVAEKNGKKVAVIGSGPAGLSFAGDLAKRGY-DVTVFEALHEIGGVLKYGIPEFRLPKKIVDVEIENLKKLG 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 88 VKIIFR----KGLAVDGMtlhtlKEDGYKAVFIGIGLPEPNRDSIfQGLRMNqGFYTSKDFLPLVAM--ASKPGmcacnS 161
Cdd:PRK12778 496 VKFETDvivgKTITIEEL-----EEEGFKGIFIASGAGLPNFMNI-PGENSN-GVMSSNEYLTRVNLmdAASPD-----S 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 162 PLPPIHG-TVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSPRKVV------LK 234
Cdd:PRK12778 564 DTPIKFGkKVAVVGGGNTAMDSARTAKRLGAERVTIVYRRSEEEMPARLEEVKHAKEEGIEFLTLHNPIEYLadekgwVK 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 235 GGQIVAMEFvrTEQDSDGSWK--EDEDQVVRLKADVVISAFGsVLSDDKVREAMAPIKFNRWGLPEIDPEtMQTSEPWVF 312
Cdd:PRK12778 644 QVVLQKMEL--GEPDASGRRRpvAIPGSTFTVDVDLVIVSVG-VSPNPLVPSSIPGLELNRKGTIVVDEE-MQSSIPGIY 719
|
330 340 350
....*....|....*....|....*....|..
gi 2032774312 313 AGGDVGGLANTTVESVNDGKQASWYMHRYIQS 344
Cdd:PRK12778 720 AGGDIVRGGATVILAMGDGKRAAAAIDEYLSS 751
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
24-343 |
3.25e-46 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 172.66 E-value: 3.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 24 KIALLGAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLGVKiiFRKGLAVDG-MT 102
Cdd:PRK12810 145 KVAVVGSGPAGLAAADQLARAGHK-VTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIE--FRTNVEVGKdIT 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 103 LHTLKEDgYKAVFIGIGLPEPnRDSIFQGlRMNQGFYTSKDFLP---LVAMASKPGmcacnsplPPIHGT---VIVLGAG 176
Cdd:PRK12810 222 AEELLAE-YDAVFLGTGAYKP-RDLGIPG-RDLDGVHFAMDFLIqntRRVLGDETE--------PFISAKgkhVVVIGGG 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 177 DTAFDCATSALRCGARRVfVVF----RKGFTHIRAVPE-------EMELAKEEKCEFLPFLSPRKVVLKGGQIVAMEFVR 245
Cdd:PRK12810 291 DTGMDCVGTAIRQGAKSV-TQRdimpMPPSRRNKNNPWpywpmklEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVR 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 246 TEqdsdgsWKEDEDQVV-----RLKADVVISAFGSVLSDDKVREAMApIKFNRWGLPEIDPETMQTSEPWVFAGGDVGGL 320
Cdd:PRK12810 370 TE------LGEGDFEPVegsefVLPADLVLLAMGFTGPEAGLLAQFG-VELDERGRVAAPDNAYQTSNPKVFAAGDMRRG 442
|
330 340
....*....|....*....|...
gi 2032774312 321 ANTTVESVNDGKQASWYMHRYIQ 343
Cdd:PRK12810 443 QSLVVWAIAEGRQAARAIDAYLM 465
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
24-341 |
5.02e-39 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 153.49 E-value: 5.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 24 KIALLGAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLGVKIifRKGLAV-DGMT 102
Cdd:PRK12771 139 RVAVIGGGPAGLSAAYHLRRMGHA-VTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGVEV--RLGVRVgEDIT 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 103 LHTLkEDGYKAVFIGIG------LPEPNRDSifqglrmnQGFYTSKDFLPLVAMASKPgmcacnsplpPIHGTVIVLGAG 176
Cdd:PRK12771 216 LEQL-EGEFDAVFVAIGaqlgkrLPIPGEDA--------AGVLDAVDFLRAVGEGEPP----------FLGKRVVVIGGG 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 177 DTAFDCATSALRCGARRVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSPRKVVLKGGQIVAM---EFVRTEQDSDGS 253
Cdd:PRK12771 277 NTAMDAARTARRLGAEEVTIVYRRTREDMPAHDEEIEEALREGVEINWLRTPVEIEGDENGATGLrviTVEKMELDEDGR 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 254 WKEDEDQVVRLKADVVISAFGSVlSDDKVREAMAPIKFNRwGLPEIDPETMQTSEPWVFAGGD-VGGLANTTVeSVNDGK 332
Cdd:PRK12771 357 PSPVTGEEETLEADLVVLAIGQD-IDSAGLESVPGVEVGR-GVVQVDPNFMMTGRPGVFAGGDmVPGPRTVTT-AIGHGK 433
|
....*....
gi 2032774312 333 QASWYMHRY 341
Cdd:PRK12771 434 KAARNIDAF 442
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
9-354 |
3.09e-37 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 149.11 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 9 PSLPPLEdmpEAYQVKIALLGAGPASLSCASFLARLGYsNITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLGV 88
Cdd:PRK12814 183 RYIPERA---PKSGKKVAIIGAGPAGLTAAYYLLRKGH-DVTIFDANEQAGGMMRYGIPRFRLPESVIDADIAPLRAMGA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 89 KIIFRKGLAVDgMTLHTLKEDgYKAVFIGIGLPEPNRDSIfQGLRMnQGFYTSKDFLPLVAM--ASKPGmcacnsplppi 166
Cdd:PRK12814 259 EFRFNTVFGRD-ITLEELQKE-FDAVLLAVGAQKASKMGI-PGEEL-PGVISGIDFLRNVALgtALHPG----------- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 167 hGTVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSPRKVVLKGGQIV--AMEFV 244
Cdd:PRK12814 324 -KKVVVIGGGNTAIDAARTALRLGAESVTILYRRTREEMPANRAEIEEALAEGVSLRELAAPVSIERSEGGLEltAIKMQ 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 245 RTEQDSDGSWKED--EDQVVRLKADVVISAFGSVLsdDKVREAMAPIKFNRWGLPEIDPETMQTSEPWVFAGGD-VGGlA 321
Cdd:PRK12814 403 QGEPDESGRRRPVpvEGSEFTLQADTVISAIGQQV--DPPIAEAAGIGTSRNGTVKVDPETLQTSVAGVFAGGDcVTG-A 479
|
330 340 350
....*....|....*....|....*....|...
gi 2032774312 322 NTTVESVNDGKQASWYMHRYiqsLYGVAVSTVP 354
Cdd:PRK12814 480 DIAINAVEQGKRAAHAIDLF---LNGKPVTAPV 509
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
2-344 |
5.35e-36 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 144.91 E-value: 5.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 2 NIPQIRNPSLppLEDMPEAYQVKIALLGAGPASLSCASFLARLGYsNITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAE 81
Cdd:PRK13984 265 NVPVEKYSEI--LDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 82 LMKDLGVKIIFRKGLAVDgMTLHTLKEdGYKAVFIGIGL--------PEPNRDSIFQGLRMNQGFytsKDFLplvamask 153
Cdd:PRK13984 342 FIEALGVKIHLNTRVGKD-IPLEELRE-KHDAVFLSTGFtlgrstriPGTDHPDVIQALPLLREI---RDYL-------- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 154 pgmcACNSPLPPIHGTVIVLGAGDTAFDCATSALRC-----GARRVFVV-FRKGFTHIRAVPEEMELAKEEKCEFLPFLS 227
Cdd:PRK13984 409 ----RGEGPKPKIPRSLVVIGGGNVAMDIARSMARLqkmeyGEVNVKVTsLERTFEEMPADMEEIEEGLEEGVVIYPGWG 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 228 PRKVVLKGGQIVAMEFVRTEQ--DSDGSW--KEDEDQVVRLKADVVISAFG-----SVLSDDkVREAMapiKFNRwglPE 298
Cdd:PRK13984 485 PMEVVIENDKVKGVKFKKCVEvfDEEGRFnpKFDESDQIIVEADMVVEAIGqapdySYLPEE-LKSKL---EFVR---GR 557
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2032774312 299 IDPETM-QTSEPWVFAGGD-VGGlaNTTVESVNDGKQASWYMHRYIQS 344
Cdd:PRK13984 558 ILTNEYgQTSIPWLFAGGDiVHG--PDIIHGVADGYWAAEGIDMYLRK 603
|
|
| DHO_dh |
pfam01180 |
Dihydroorotate dehydrogenase; |
369-673 |
7.34e-35 |
|
Dihydroorotate dehydrogenase;
Pssm-ID: 426103 Cd Length: 291 Bit Score: 134.78 E-value: 7.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 369 SVEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTFSLDKDiVTNVSPRIVRgttsgpLYGpgqgSFLN-IEL 447
Cdd:pfam01180 3 ATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQ-PGNPTPRVFR------LPE----GVLNrMGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 448 ISEKTAAYWCKSIAELKADFPNHV-LIASIMCSYNRENWTELSKMAQVAgaDALELNLSCPHGMGERgmglACGQDPELV 526
Cdd:pfam01180 72 NNPGLDAVLAELLKRRKEYPRPDLgINLSKAGMTVDDYVEVARKIGPFA--DYIELNVSCPNTPGLR----ALQTDPELA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 527 RNICRWVRQAVHIPFFAKLTPNVTDIVKIAMAAQEGGADGVTATN-TVSGLMGLKADSTPWPAVgrgLRTTYGGVSGNAI 605
Cdd:pfam01180 146 AILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINaTNTTVRGMRIDLKTEKPI---LANGTGGLSGPPI 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032774312 606 RPIALRAVSAIARAL-PGFPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALL 673
Cdd:pfam01180 223 KPIALKVIRELYQRTgPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
9-335 |
8.84e-34 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 140.08 E-value: 8.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 9 PSLPPleDMPEAYQvKIALLGAGPASLSCASFLARLGySNITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLGV 88
Cdd:PRK12775 420 PVKPP--RFSKKLG-KVAICGSGPAGLAAAADLVKYG-VDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGV 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 89 KIIFRKglaVDGMTL---HTLKEDGYKAVFIGIGLPEPNrdsiFQGL--RMNQGFYTSKDFLPLVAMASKPGMCACNSPL 163
Cdd:PRK12775 496 KIETNK---VIGKTFtvpQLMNDKGFDAVFLGVGAGAPT----FLGIpgEFAGQVYSANEFLTRVNLMGGDKFPFLDTPI 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 164 PpIHGTVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSPRKV-VLKGGQIVAM- 241
Cdd:PRK12775 569 S-LGKSVVVIGAGNTAMDCLRVAKRLGAPTVRCVYRRSEAEAPARIEEIRHAKEEGIDFFFLHSPVEIyVDAEGSVRGMk 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 242 --EFVRTEQDSDGSWKE-DEDQVVRLKADVVISAFGSVlSDDKVREAMAPIKFNRWGLPEID----PETMQTSEPWVFAG 314
Cdd:PRK12775 648 veEMELGEPDEKGRRKPmPTGEFKDLECDTVIYALGTK-ANPIITQSTPGLALNKWGNIAADdgklESTQSTNLPGVFAG 726
|
330 340
....*....|....*....|.
gi 2032774312 315 GDVGGLANTTVESVNDGKQAS 335
Cdd:PRK12775 727 GDIVTGGATVILAMGAGRRAA 747
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
18-342 |
1.68e-31 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 131.41 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 18 PEAYQVK-----IALLGAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLGVKIIF 92
Cdd:PRK12769 318 PDLSQVTksdkrVAIIGAGPAGLACADVLARNGVA-VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFEL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 93 RKGLAVDgMTLHTLKEDgYKAVFIGIGLPE------PNRDSifqglrmnQGFYtskDFLPLVAMASKPGMCACNSPLPPI 166
Cdd:PRK12769 397 NCEVGKD-ISLESLLED-YDAVFVGVGTYRsmkaglPNEDA--------PGVY---DALPFLIANTKQVMGLEELPEEPF 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 167 HGT----VIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSPRKVVL-KGGQIVAM 241
Cdd:PRK12769 464 INTaglnVVVLGGGDTAMDCVRTALRHGASNVTCAYRRDEANMPGSKKEVKNAREEGANFEFNVQPVALELnEQGHVCGI 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 242 EFVRT---EQDSDGSWK----EDEDQVvrLKADVVISAFGSVLSDDKVREAmAPIKFNRWGLPEIDPET---MQTSEPWV 311
Cdd:PRK12769 544 RFLRTrlgEPDAQGRRRpvpiPGSEFV--MPADAVIMAFGFNPHGMPWLES-HGVTVDKWGRIIADVESqyrYQTSNPKI 620
|
330 340 350
....*....|....*....|....*....|.
gi 2032774312 312 FAGGDVGGLANTTVESVNDGKQASWYMHRYI 342
Cdd:PRK12769 621 FAGGDAVRGADLVVTAMAEGRHAAQGIIDWL 651
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
781-839 |
2.94e-31 |
|
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: 434137 [Multi-domain] Cd Length: 59 Bit Score: 116.23 E-value: 2.94e-31
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2032774312 781 ALIDEEMCINCGKCYMTCNDSGYQAIRFDPETHLPTVTDSCTGCTLCLSVCPVIDCIRM 839
Cdd:pfam14697 1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVDDCITM 59
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
24-344 |
1.30e-30 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 123.95 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 24 KIALLGAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLGVKIIFRKGLAVDGMTL 103
Cdd:PRK12770 20 KVAIIGAGPAGLAAAGYLACLGYE-VHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTKVCCGEPLH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 104 H-----------TLKE--DGYKAVFIGIGLPEPNRDSIfQGLRMnQGFYTSKDFLpLVAMASKPGMcACNSPLPPIHG-T 169
Cdd:PRK12770 99 EeegdefverivSLEElvKKYDAVLIATGTWKSRKLGI-PGEDL-PGVYSALEYL-FRIRAAKLGY-LPWEKVPPVEGkK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 170 VIVLGAGDTAFDCATSALRCGARRVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSPRKVvLKGGQIVAMEFVRTE-Q 248
Cdd:PRK12770 175 VVVVGAGLTAVDAALEAVLLGAEKVYLAYRRTINEAPAGKYEIERLIARGVEFLELVTPVRI-IGEGRVEGVELAKMRlG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 249 DSDGSWKED----EDQVVRLKADVVISAFGSVLSDdKVREAMAPIKFNRWGlpEID-PETMQTSEPWVFAGGDV--G--- 318
Cdd:PRK12770 254 EPDESGRPRpvpiPGSEFVLEADTVVFAIGEIPTP-PFAKECLGIELNRKG--EIVvDEKHMTSREGVFAAGDVvtGpsk 330
|
330 340
....*....|....*....|....*..
gi 2032774312 319 -GLAnttvesVNDGKQASWYMHRYIQS 344
Cdd:PRK12770 331 iGKA------IKSGLRAAQSIHEWLDL 351
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
24-338 |
2.09e-30 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 127.83 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 24 KIALLGAGPASLSCASFLARLGYsNITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLGVKIIFRKGLAVDgMTL 103
Cdd:PRK12809 312 KVAVIGAGPAGLGCADILARAGV-QVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRD-ITF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 104 HTLKEDgYKAVFIGIG--------LPEPNRDSIFQGLrmnqgfytskdflPLVAMASKPGMCACNS---PLPPIHG-TVI 171
Cdd:PRK12809 390 SDLTSE-YDAVFIGVGtygmmradLPHEDAPGVIQAL-------------PFLTAHTRQLMGLPESeeyPLTDVEGkRVV 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 172 VLGAGDTAFDCATSALRCGARRVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSPRKVVL-KGGQIVAMEFVRTEQDS 250
Cdd:PRK12809 456 VLGGGDTTMDCLRTSIRLNAASVTCAYRRDEVSMPGSRKEVVNAREEGVEFQFNVQPQYIACdEDGRLTAVGLIRTAMGE 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 251 DGSWKEDEDQVV-----RLKADVVISAFGSVLSDDKVREAMApIKFNRWGLPEIDPE---TMQTSEPWVFAGGDVGGLAN 322
Cdd:PRK12809 536 PGPDGRRRPRPVagsefELPADVLIMAFGFQAHAMPWLQGSG-IKLDKWGLIQTGDVgylPTQTHLKKVFAGGDAVHGAD 614
|
330
....*....|....*.
gi 2032774312 323 TTVESVNDGKQASWYM 338
Cdd:PRK12809 615 LVVTAMAAGRQAARDM 630
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
25-335 |
6.84e-27 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 118.01 E-value: 6.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 25 IALLGAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMSEIPQFRLPYDVVNFEAELMKDLGVKiiFRKGLAV-DGMTL 103
Cdd:PRK12779 309 IAVVGSGPSGLINAYLLAVEGFP-VTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLLGGR--FVKNFVVgKTATL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 104 HTLKEDGYKAVFIGIGLPEPNRDSIfQGLRMNqGFYTSKDFLPLVAM--ASKPGMcacNSPLPPIHG-TVIVLGAGDTAF 180
Cdd:PRK12779 386 EDLKAAGFWKIFVGTGAGLPTFMNV-PGEHLL-GVMSANEFLTRVNLmrGLDDDY---ETPLPEVKGkEVFVIGGGNTAM 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 181 DCATSALRCGARrVFVVFRKGFTHIRAVPEEMELAKEEKCEFLPFLSPRKV-------VLKGGQIVAMEFvrTEQDSDGS 253
Cdd:PRK12779 461 DAARTAKRLGGN-VTIVYRRTKSEMPARVEELHHALEEGINLAVLRAPREFigddhthFVTHALLDVNEL--GEPDKSGR 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 254 WK-EDEDQVVRLKADVVISAFGSVlSDDKVREAMAPIKFNRWGLPEIDPETMQTSEPWVFAGGDVGGLANTTVESVNDGK 332
Cdd:PRK12779 538 RSpKPTGEIERVPVDLVIMALGNT-ANPIMKDAEPGLKTNKWGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQ 616
|
...
gi 2032774312 333 QAS 335
Cdd:PRK12779 617 AAA 619
|
|
| DHOD_2_like |
cd04738 |
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ... |
356-654 |
2.43e-23 |
|
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.
Pssm-ID: 240089 Cd Length: 327 Bit Score: 101.81 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 356 LPLFYTPIDLvdiSVEMAGLKFPNPFGLA-----SATpatsssMIRRAFEAGWGFAVTKTfsldkdiVT------NVSPR 424
Cdd:cd04738 30 LLLVYDDPRL---EVEVFGLTFPNPVGLAagfdkNAE------AIDALLALGFGFVEVGT-------VTprpqpgNPKPR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 425 IVRgttsgpLygPGQGSFLN--------IELISEKTAAYWcksiaelkadFPNHVLIASImcSYNREnwTELSK------ 490
Cdd:cd04738 94 LFR------L--PEDEALINrmgfnndgADAVAKRLKKRR----------PRGGPLGVNI--GKNKD--TPLEDavedyv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 491 --MAQVAG-ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAV-----HIPFFAKLTPNVTD--IVKIAMAAQ 560
Cdd:cd04738 152 igVRKLGPyADYLVVNVSSPNTPGLRDL-----QGKEALRELLTAVKEERnklgkKVPLLVKIAPDLSDeeLEDIADVAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 561 EGGADGVTATNTVSGLMGLKADStpwpavgrgLRTTYGGVSGNAIRPIALRAVSAIARALPG-FPILATGGIDSAETGLQ 639
Cdd:cd04738 227 EHGVDGIIATNTTISRPGLLRSP---------LANETGGLSGAPLKERSTEVLRELYKLTGGkIPIIGVGGISSGEDAYE 297
|
330
....*....|....*
gi 2032774312 640 FLHSGASVLQVCSAI 654
Cdd:cd04738 298 KIRAGASLVQLYTGL 312
|
|
| PRK05286 |
PRK05286 |
quinone-dependent dihydroorotate dehydrogenase; |
338-673 |
2.51e-19 |
|
quinone-dependent dihydroorotate dehydrogenase;
Pssm-ID: 235388 Cd Length: 344 Bit Score: 90.22 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 338 MHRYIQSLYGVAVSTVPELPLFYTPIDLvdiSVEMAGLKFPNPFGLA-----SATpatsssMIRrAFEA-GWGFA----V 407
Cdd:PRK05286 22 TIRALKRASRTPLLSLLRQRLTYTDPRL---PVTVMGLTFPNPVGLAagfdkNGE------AID-ALGAlGFGFVevgtV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 408 TKT----------FSLDKD---I---------VTNVSPRIVRGTTSGPLygpgqgsFLNIelisektaaywCKS----IA 461
Cdd:PRK05286 92 TPRpqpgnpkprlFRLPEDealInrmgfnndgADALAERLKKAYRGIPL-------GINI-----------GKNkdtpLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 462 ELKADFpnhvliasIMCsynrenwtelskMAQVAG-ADALELNLSCPHGMGERGMglacgQDPELVRNICRWVRQAVH-- 538
Cdd:PRK05286 154 DAVDDY--------LIC------------LEKLYPyADYFTVNISSPNTPGLRDL-----QYGEALDELLAALKEAQAel 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 539 ---IPFFAKLTPNVTD--IVKIAMAAQEGGADGVTATNTV---SGLMGLK-ADSTpwpavgrglrttyGGVSGNAIRPIA 609
Cdd:PRK05286 209 hgyVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIATNTTlsrDGLKGLPnADEA-------------GGLSGRPLFERS 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032774312 610 LRAVSAIARALPG-FPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALL 673
Cdd:PRK05286 276 TEVIRRLYKELGGrLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIYEGPGLVKEIVRGLARLL 340
|
|
| DHOD_like |
cd04739 |
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ... |
367-687 |
7.85e-18 |
|
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.
Pssm-ID: 240090 Cd Length: 325 Bit Score: 85.36 E-value: 7.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 367 DISVEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKtfSLDKDIVTNVSPRIVRGTTSGPLYGPGQGSFLNIE 446
Cdd:cd04739 1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLP--SLFEEQIEREAQELDRFLTYGSSFAEALSYFPEYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 447 LISEKTAAYwCKSIAELKA--DFPnhvLIASIMCsYNRENWTELSKMAQVAGADALELNLscphgmgergmgLACGQDPE 524
Cdd:cd04739 79 RYNLGPEEY-LELIRRAKRavSIP---VIASLNG-VSAGGWVDYARQIEEAGADALELNI------------YALPTDPD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 525 LVRN--------ICRWVRQAVHIPFFAKLTPNVTDIVKIAMAAQEGGADGVTATNTVsglmgLKAD-STPWPAVGRGLRT 595
Cdd:cd04739 142 ISGAeveqryldILRAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRF-----YQPDiDLETLEVVPNLLL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 596 TYGGVSGNAIRPIalravsAIARALPGFPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALLYL 675
Cdd:cd04739 217 SSPAEIRLPLRWI------AILSGRVKASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEE 290
|
330
....*....|..
gi 2032774312 676 KSIEELEDWNGQ 687
Cdd:cd04739 291 HGYESVQQLRGS 302
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
387-652 |
9.35e-18 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 82.63 E-value: 9.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 387 TPATSSSMIRRAFEAGWGFAVTKTFSLDKDIVTNVSPRIvrgttsgplygpgqgsflnielisektaaywcksiAELKAD 466
Cdd:cd04722 10 PSGDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEV-----------------------------------LKEVAA 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 467 FPNHVLIASIMCSYNRENWTELSKMAQVAGADALELNLSCPHGmgergmglacgqdPELVRNICRWVRQAV-HIPFFAKL 545
Cdd:cd04722 55 ETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYL-------------AREDLELIRELREAVpDVKVVVKL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 546 TPNVTDIvkiAMAAQEGGADGVTATNTVSGLMGLKADSTPWPAVgrglrttyggvsgnairpialravsAIARALPGFPI 625
Cdd:cd04722 122 SPTGELA---AAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLL-------------------------ILAKRGSKVPV 173
|
250 260
....*....|....*....|....*..
gi 2032774312 626 LATGGIDSAETGLQFLHSGASVLQVCS 652
Cdd:cd04722 174 IAGGGINDPEDAAEALALGADGVIVGS 200
|
|
| DHOD_1A_like |
cd04741 |
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ... |
370-673 |
1.11e-17 |
|
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.
Pssm-ID: 240092 Cd Length: 294 Bit Score: 84.68 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 370 VEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTFSLDKdivtnvsprivRGTTSGPLYGPGQGSFLNIELIS 449
Cdd:cd04741 1 VTPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAG-----------RPGNPEPRYYAFPLGSINSLGLP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 450 EKTAAYWCKSIAELKADFPNH--VLIASIMCSYNrENWTELSKMA--QVAGADALELNLSCPH--GMGERGMglacgqDP 523
Cdd:cd04741 70 NLGLDYYLEYIRTISDGLPGSakPFFISVTGSAE-DIAAMYKKIAahQKQFPLAMELNLSCPNvpGKPPPAY------DF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 524 ELVRNICRWVRQAVHIPFFAKLTPnVTDIVKIAMAAQ--EGGADG---VTATNTV-SGLMglkADSTPWPAVGRGlRTTY 597
Cdd:cd04741 143 DATLEYLTAVKAAYSIPVGVKTPP-YTDPAQFDTLAEalNAFACPisfITATNTLgNGLV---LDPERETVVLKP-KTGF 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032774312 598 GGVSGNAIRPIALRAVSAIARALPG-FPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALL 673
Cdd:cd04741 218 GGLAGAYLHPLALGNVRTFRRLLPSeIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
|
|
| PRK07565 |
PRK07565 |
dihydroorotate dehydrogenase-like protein; |
367-687 |
4.62e-17 |
|
dihydroorotate dehydrogenase-like protein;
Pssm-ID: 236051 Cd Length: 334 Bit Score: 83.38 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 367 DISVEMAGLKFPNPFgLASATPAT-SSSMIRRAFEAGWGFAVTKtfSLDKDIVTNVSPRIVRGTTSGPLYGPGQGSFlni 445
Cdd:PRK07565 2 DLSTTYLGLTLRNPL-VASASPLSeSVDNVKRLEDAGAGAVVLK--SLFEEQIRHEAAELDRHLTHGTESFAEALDY--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 446 elISEKTAAYW-----CKSIAELKA--DFPnhvLIASIMCSYNREnWTELSKMAQVAGADALELNLSCPHGmgerGMGLA 518
Cdd:PRK07565 76 --FPEPAKFYVgpeeyLELIRRAKEavDIP---VIASLNGSSAGG-WVDYARQIEQAGADALELNIYYLPT----DPDIS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 519 CGQDPELVRNICRWVRQAVHIPFFAKLTPNVTDIVKIAMAAQEGGADGVTATN-------------TVSGLMgLkadSTP 585
Cdd:PRK07565 146 GAEVEQRYLDILRAVKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNrfyqpdidletleVVPGLV-L---STP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 586 wpavgrglrttyggvsgNAIRpIALRAVsAIARALPGFPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDY 665
Cdd:PRK07565 222 -----------------AELR-LPLRWI-AILSGRVGADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTI 282
|
330 340
....*....|....*....|..
gi 2032774312 666 CTGLRALLYLKSIEELEDWNGQ 687
Cdd:PRK07565 283 LRGLEDWMERHGYESLQQFRGS 304
|
|
| pyrD_sub2 |
TIGR01036 |
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate ... |
350-653 |
3.81e-15 |
|
dihydroorotate dehydrogenase, subfamily 2; This model describes enzyme protein dihydroorotate dehydrogenase exclusively for subfamily 2. It includes members from bacteria, yeast, plants etc. The subfamilies 1 and 2 share extensive homology, particularly toward the C-terminus. This subfamily has a longer N-terminal region. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273408 Cd Length: 335 Bit Score: 77.52 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 350 VSTVPELPLFYTPIDLVD-ISVEMAGLKFPNPFGLAsATPATSSSMIRRAFEAGWGFAVTKTFSlDKDIVTNVSPRIVRG 428
Cdd:TIGR01036 27 GTGTPFLALLRSLFGASDpLEVTVLGLKFPNPLGLA-AGFDKDGEAIDALGAMGFGFLEIGTVT-PKPQPGNPRPRLFRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 429 ttsgplygPGQGSFLNIELISEKTAAYWCKSIAELKADFPNHVLIAS---IMCSYNRENWTELSKMAqVAGADALELNLS 505
Cdd:TIGR01036 105 --------IEDEALINRMGFNNHGADVLVERLKRARYKGPIGINIGKnkdTPSEDAKEDYAACLRKL-GPLADYLVVNVS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 506 CPHGMGERGMglacgQDPELVRNICRWVRQ-------AVHIPFFAKLTPNVT--DIVKIAMAAQEGGADGVTATNTV--- 573
Cdd:TIGR01036 176 SPNTPGLRDL-----QYKAELRDLLTAVKQeqdglrrVHRVPVLVKIAPDLTesDLEDIADSLVELGIDGVIATNTTvsr 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 574 SGLMGLKADSTPwpavgrglrttyGGVSGnaiRPIALRAVSAIAR---ALPG-FPILATGGIDSAETGLQFLHSGASVLQ 649
Cdd:TIGR01036 251 SLVQGPKNSDET------------GGLSG---KPLQDKSTEIIRRlyaELQGrLPIIGVGGISSAQDALEKIRAGASLLQ 315
|
....
gi 2032774312 650 VCSA 653
Cdd:TIGR01036 316 IYSG 319
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
783-843 |
6.97e-14 |
|
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: 67.77 E-value: 6.97e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032774312 783 IDEEMCINCGKCYMTCNDsgyQAIRFDPETHLPTVTDSCTGCTLCLSVCPViDCIRMVSRT 843
Cdd:COG1144 27 VDEDKCIGCGLCWIVCPD---GAIRVDDGKYYGIDYDYCKGCGICAEVCPV-KAIEMVPEE 83
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
24-318 |
4.47e-13 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 70.81 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 24 KIALLGAGPASLSCASFLARLGYSNITIFEKQEYLGGL---------SMSEIPQFRLPYDVVNFEAELMKDLGVKIIFRK 94
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCPYGGcvlskallgAAEAPEIASLWADLYKRKEEVVKKLNNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 95 GLAVDG-------MTLHTLKEDG-----YKAVFIGIGlPEPNRDSIfQGLRMNQGF----YTSKDFLplvamaskpgmca 158
Cdd:pfam07992 82 GTEVVSidpgakkVVLEELVDGDgetitYDRLVIATG-ARPRLPPI-PGVELNVGFlvrtLDSAEAL------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 159 cNSPLPPIHgtVIVLGAGDTAFDCATSALRCGARRVFVVFRKGFThiRAVPEEMELAKEEKceflpfLSPRKVVLKGGQI 238
Cdd:pfam07992 147 -RLKLLPKR--VVVVGGGYIGVELAAALAKLGKEVTLIEALDRLL--RAFDEEISAALEKA------LEKNGVEVRLGTS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 239 VamefVRTEQDSDGSWKEDEDqVVRLKADVVISAFGSVLSDDKVREamAPIKFNRWGLPEIDpETMQTSEPWVFAGGDVG 318
Cdd:pfam07992 216 V----KEIIGDGDGVEVILKD-GTEIDADLVVVAIGRRPNTELLEA--AGLELDERGGIVVD-EYLRTSVPGIYAAGDCR 287
|
|
| PRK02506 |
PRK02506 |
dihydroorotate dehydrogenase 1A; Reviewed |
367-687 |
1.27e-12 |
|
dihydroorotate dehydrogenase 1A; Reviewed
Pssm-ID: 235045 Cd Length: 310 Bit Score: 69.60 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 367 DISVEMAGLKFPNPFGLASATPATSSSMIRRAFEAGWGFAVTKTFSLDKDiVTNVSPRIVRgTTSGPLYG---PGQGsfl 443
Cdd:PRK02506 1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKSATLEPR-PGNPEPRYAD-TPLGSINSmglPNLG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 444 nielisektAAYWCKSIAELKADFPNHVLIASIMCSYNRENWTELSKMAQVAGADALELNLSCPHGMGERGMGLacgqDP 523
Cdd:PRK02506 76 ---------FDYYLDYVLELQKKGPNKPHFLSVVGLSPEETHTILKKIQASDFNGLVELNLSCPNVPGKPQIAY----DF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 524 ELVRNICRWVRQAVHIPFFAKLTPNVtDIVKIAMAA---QEGGADGVTATNTV-SGLMGLKADSTPW--PAVGrglrttY 597
Cdd:PRK02506 143 ETTEQILEEVFTYFTKPLGVKLPPYF-DIVHFDQAAaifNKFPLAFVNCINSIgNGLVIDPEDETVVikPKNG------F 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 598 GGVSGNAIRPIALRAVSAIARAL-PGFPILATGGIDSAETGLQFLHSGASVLQVCSAIQNQDFTVIDDYCTGLRALLYLK 676
Cdd:PRK02506 216 GGIGGDYIKPTALANVRAFYQRLnPSIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEK 295
|
330
....*....|.
gi 2032774312 677 SIEELEDWNGQ 687
Cdd:PRK02506 296 GYQSLEDFRGK 306
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
780-844 |
1.30e-12 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 63.59 E-value: 1.30e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032774312 780 VALIDEEMCINCGKCYMTCNdsgYQAIRFDPETHLPTVTDSCTGCTLCLSVCPViDCIRMVSRTT 844
Cdd:COG1149 5 IPVIDEEKCIGCGLCVEVCP---EGAIKLDDGGAPVVDPDLCTGCGACVGVCPT-GAITLEEREA 65
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
721-842 |
6.04e-11 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 63.59 E-value: 6.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 721 RKKIIAENKIKLKAQNMAAELPEKKHFVPKKPIPAVKDVIGKALQYIGTYGDLCNTEQVVALIDEEMCINCGKCYMTCnd 800
Cdd:COG1145 117 AVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVC-- 194
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2032774312 801 sGYQAIRFDPETHLPTV-TDSCTGCTLCLSVCPViDCIRMVSR 842
Cdd:COG1145 195 -PTGAIRLKDGKPQIVVdPDKCIGCGACVKVCPV-GAISLEPK 235
|
|
| PRK05113 |
PRK05113 |
electron transport complex protein RnfB; Provisional |
780-840 |
2.07e-10 |
|
electron transport complex protein RnfB; Provisional
Pssm-ID: 235347 [Multi-domain] Cd Length: 191 Bit Score: 60.73 E-value: 2.07e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032774312 780 VALIDEEMCINCGKCYMTCN-DSGYQAIRfdpetHLPTV-TDSCTGCTLCLSVCPViDCIRMV 840
Cdd:PRK05113 108 VAFIDEDNCIGCTKCIQACPvDAIVGATK-----AMHTViSDLCTGCDLCVAPCPT-DCIEMI 164
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
780-840 |
2.09e-10 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 60.20 E-value: 2.09e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032774312 780 VALIDEEMCINCGKCYMTCNdsgYQAIRFDPETHLPTVTDSCTGCTLCLSVCPViDCIRMV 840
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQACP---VDAIVGAAKAMHTVIADECTGCDLCVEPCPT-DCIEMI 163
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
780-846 |
5.55e-10 |
|
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: 60.78 E-value: 5.55e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032774312 780 VALI-----DEEMCINCGKCYMTCNdsgYQAIRFDPeTHLPTV-TDSCTGCTLCLSVCPViDCIRMVSRTTPY 846
Cdd:COG2878 126 AAVIggpkgCEYGCIGCGDCIKACP---FDAIVGAA-KGMHTVdEDKCTGCGLCVEACPV-DCIEMVPVSPTV 193
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
783-842 |
1.33e-09 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 55.10 E-value: 1.33e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032774312 783 IDEEMCINCGKCYMTCndsGYQAIRFDPETHLPTVT--DSCTGCTLCLSVCPViDCIRMVSR 842
Cdd:COG1146 5 IDTDKCIGCGACVEVC---PVDVLELDEEGKKALVInpEECIGCGACELVCPV-GAITVEDD 62
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
780-843 |
4.63e-09 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 58.27 E-value: 4.63e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032774312 780 VALIDEEMCINCGKCYMTCNdsgYQAIRFDPETHLPTVTDSCTGCTLCLSVCPViDCIRMVSRT 843
Cdd:PRK06991 79 VAVIDEQLCIGCTLCMQACP---VDAIVGAPKQMHTVLADLCTGCDLCVPPCPV-DCIDMVPVT 138
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
766-840 |
3.57e-08 |
|
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: 52.78 E-value: 3.57e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032774312 766 YIGTYGDLCNTEQVVALIDEEMCINCGKCYMTCNdsgYQAIRFDPEthLPTVTDS--CTGCTLCLSVCPViDCIRMV 840
Cdd:cd10549 58 ELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCP---VDAITLEDE--LEIVIDKekCIGCGICAEVCPV-NAIKLV 128
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
28-73 |
3.58e-08 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 50.99 E-value: 3.58e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2032774312 28 LGAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMS-EIPQFRLPY 73
Cdd:pfam13450 2 VGAGLAGLVAAALLAKRGFR-VLVLEKRDRLGGNAYSyRVPGYVFDY 47
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
783-842 |
4.09e-08 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 50.81 E-value: 4.09e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2032774312 783 IDEEMCINCGKCYMTCN----DSGYQAIRFDPethlptvtDSCTGCTLCLSVCPViDCIRMVSR 842
Cdd:COG4231 19 IDEDKCTGCGACVKVCPadaiEEGDGKAVIDP--------DLCIGCGSCVQVCPV-DAIKLEKR 73
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
788-833 |
4.66e-08 |
|
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: 50.22 E-value: 4.66e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2032774312 788 CINCGKCYMTCNdsgYQAIRFDPETHLPTVT------DSCTGCTLCLSVCPV 833
Cdd:pfam12838 1 CIGCGACVAACP---VGAITLDEVGEKKGTKtvvidpERCVGCGACVAVCPT 49
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
785-839 |
4.69e-08 |
|
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: 50.51 E-value: 4.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032774312 785 EEMCINCGKCYMTCNdsgYQAIRFDPETHLPTVT---DSCTGCTLCLSVCPViDCIRM 839
Cdd:COG1143 1 EDKCIGCGLCVRVCP---VDAITIEDGEPGKVYVidpDKCIGCGLCVEVCPT-GAISM 54
|
|
| PLN02826 |
PLN02826 |
dihydroorotate dehydrogenase |
368-653 |
1.11e-07 |
|
dihydroorotate dehydrogenase
Pssm-ID: 178421 Cd Length: 409 Bit Score: 55.13 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 368 ISVEMAGLKFPNPFGLAsATPATSSSMIRRAFEAGWGFAVTKTfsldkdiVT------NVSPRIVRGTTSGPLYGPGQGS 441
Cdd:PLN02826 74 LGVEVWGRTFSNPIGLA-AGFDKNAEAVEGLLGLGFGFVEIGS-------VTplpqpgNPKPRVFRLREEGAIINRYGFN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 442 FLNIELISEKTAAY-----------WCKSIAELKADFPNHVLIASIMCSYNRenwteLSK-MAQ--VAG-------ADAL 500
Cdd:PLN02826 146 SEGIVAVAKRLGAQhgkrkldetssSSFSSDDVKAGGKAGPGILGVNLGKNK-----TSEdAAAdyVQGvralsqyADYL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 501 ELNLSCPHGMGERGMglacgQDPELVRNICRWVR---------QAVHIPFFAKLTPNVT--DIVKIAMAAQEGGADGVTA 569
Cdd:PLN02826 221 VINVSSPNTPGLRKL-----QGRKQLKDLLKKVLaardemqwgEEGPPPLLVKIAPDLSkeDLEDIAAVALALGIDGLII 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 570 TNTVSglmglkadSTPWPAVGRGLRTTYGGVSGNAIRPIALRAVSAIARALPG-FPILATGGIDSAETGLQFLHSGASVL 648
Cdd:PLN02826 296 SNTTI--------SRPDSVLGHPHADEAGGLSGKPLFDLSTEVLREMYRLTRGkIPLVGCGGVSSGEDAYKKIRAGASLV 367
|
....*
gi 2032774312 649 QVCSA 653
Cdd:PLN02826 368 QLYTA 372
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
779-845 |
2.80e-07 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 48.57 E-value: 2.80e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032774312 779 VVALIDEEMCINCGKCYMTCNdsgYQAIRFDPETHLpTVTDSCTGCTLCLSVCPViDCIRMVSRTTP 845
Cdd:COG2768 4 GKPYVDEEKCIGCGACVKVCP---VGAISIEDGKAV-IDPEKCIGCGACIEVCPV-GAIKIEWEEDE 65
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
783-832 |
3.19e-07 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 48.02 E-value: 3.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2032774312 783 IDEEMCINCGKCYMTC--NDSGYQAIRFDPET-HLPTVTDSCTGCTLCLSVCP 832
Cdd:pfam13237 4 IDPDKCIGCGRCTAACpaGLTRVGAIVERLEGeAVRIGVWKCIGCGACVEACP 56
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
780-840 |
4.01e-07 |
|
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: 50.08 E-value: 4.01e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 780 VALIDEEMCINCGKCYMTCNdsgYQAIRFDPETHLPtvtDSCTGC---------TLCLSVCPViDCIRMV 840
Cdd:cd04410 74 IVLIDEDKCIGCGSCVEACP---YGAIVFDPEPGKA---VKCDLCgdrldeglePACVKACPT-GALTFG 136
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
783-833 |
5.30e-07 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 47.74 E-value: 5.30e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2032774312 783 IDEEMCINCGKCYMTCNDsgyQAIRFDpETHLPTVTDSCTGCTLCLSVCPV 833
Cdd:COG2221 12 IDEEKCIGCGLCVAVCPT---GAISLD-DGKLVIDEEKCIGCGACIRVCPT 58
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
780-833 |
7.50e-07 |
|
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: 319895 [Multi-domain] Cd Length: 154 Bit Score: 49.56 E-value: 7.50e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032774312 780 VALIDEEMCIN------CGKCYMTCNDSGYqAIRFDPETHLPTV-TDSCTGCTLCLSVCPV 833
Cdd:cd16373 85 VAVIDKDRCLAwqggtdCGVCVEACPTEAI-AIVLEDDVLRPVVdEDKCVGCGLCEYVCPV 144
|
|
| DusA |
COG0042 |
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ... |
487-645 |
8.94e-07 |
|
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 439812 [Multi-domain] Cd Length: 310 Bit Score: 51.63 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 487 ELSKMAQVAGADALELNLSCP------HGMGergmglAC-GQDPELVRNICRWVRQAVHIPFFAKL-------TPNVTDI 552
Cdd:COG0042 78 EAARIAEELGADEIDINMGCPvkkvtkGGAG------AAlLRDPELVAEIVKAVVEAVDVPVTVKIrlgwdddDENALEF 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 553 VKIamaAQEGGADGV-----TATNTVSGlmglKADstpWPAVGRglrttyggvsgnairpiaLRAVSAIaralpgfPILA 627
Cdd:COG0042 152 ARI---AEDAGAAALtvhgrTREQRYKG----PAD---WDAIAR------------------VKEAVSI-------PVIG 196
|
170
....*....|....*....
gi 2032774312 628 TGGIDSAETGLQFL-HSGA 645
Cdd:COG0042 197 NGDIFSPEDAKRMLeETGC 215
|
|
| DUS_like_FMN |
cd02801 |
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ... |
490-645 |
9.37e-07 |
|
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.
Pssm-ID: 239200 [Multi-domain] Cd Length: 231 Bit Score: 50.96 E-value: 9.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 490 KMAQVAGADALELNLSCP-----HGmgerGMGLACGQDPELVRNICRWVRQAVHIPFFAK---LTPNVTDIVKIAMAAQE 561
Cdd:cd02801 74 KIVEELGADGIDLNMGCPspkvtKG----GAGAALLKDPELVAEIVRAVREAVPIPVTVKirlGWDDEEETLELAKALED 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 562 GGADGVtatnTVSGlmglkadstpwpavgrglRTTYGGVSGNAIrpiaLRAVSAIARAlPGFPILATGGIDSAETGLQFL 641
Cdd:cd02801 150 AGASAL----TVHG------------------RTREQRYSGPAD----WDYIAEIKEA-VSIPVIANGDIFSLEDALRCL 202
|
....*
gi 2032774312 642 -HSGA 645
Cdd:cd02801 203 eQTGV 207
|
|
| Dus |
pfam01207 |
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ... |
486-645 |
1.18e-06 |
|
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.
Pssm-ID: 426126 Cd Length: 309 Bit Score: 51.17 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 486 TELSKMAQVAGADALELNLSCPHGMGERGMGLAC-GQDPELVRNICRWVRQAVHIPFFAKLT----PNVTDIVKIAMAAQ 560
Cdd:pfam01207 69 AEAAKLVEDRGADGIDINMGCPSKKVTRGGGGAAlLRNPDLVAQIVKAVVKAVGIPVTVKIRigwdDSHENAVEIAKIVE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 561 EGGADGVTATntvsglmglkadstpwpavGRGLRTTYGGvsgnairPIALRAVSAIARALPgFPILATGGIDSAETGLQF 640
Cdd:pfam01207 149 DAGAQALTVH-------------------GRTRAQNYEG-------TADWDAIKQVKQAVS-IPVIANGDITDPEDAQRC 201
|
....*.
gi 2032774312 641 L-HSGA 645
Cdd:pfam01207 202 LaYTGA 207
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
783-851 |
2.45e-06 |
|
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: 47.39 E-value: 2.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032774312 783 IDEEMCINCGKCYMTCNdsgYQAIRFDPETHLPTVT----DSCTGCTLCLSVCPViDCIRMVSRTTPYEPKRG 851
Cdd:cd10549 3 YDPEKCIGCGICVKACP---TDAIELGPNGAIARGPeideDKCVFCGACVEVCPT-GAIELTPEGKEYVPKEK 71
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
761-839 |
2.79e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 51.01 E-value: 2.79e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2032774312 761 GKALQYIGtyGDLCNTEQVVALIDEEMCINCGKCYMTCNdsgYQAIRFDPETHLPTVTDSCTGCTLCLSVCPViDCIRM 839
Cdd:COG1148 473 ARAIQLLS--KGELGVEPSVAEVDPEKCTGCGRCVEVCP---YGAISIDEKGVAEVNPALCKGCGTCAAACPS-GAISL 545
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
24-317 |
3.43e-06 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 49.73 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 24 KIALLGAGPASLSCASFLARLGYSnITIFEKQEyLGGlsmseipQFRLPYDVVNF----E----AELMKDL-------GV 88
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLK-TLVIEGGE-PGG-------QLATTKEIENYpgfpEgisgPELAERLreqaerfGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 89 KIIFRKGLAVD----GMTLHTLKEDGY--KAVFIGIGLpEPNRDSIfQGLR--MNQGFYTskdflplvamaskpgmCA-C 159
Cdd:COG0492 73 EILLEEVTSVDkddgPFRVTTDDGTEYeaKAVIIATGA-GPRKLGL-PGEEefEGRGVSY----------------CAtC 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 160 NSPLppIHG-TVIVLGAGDTAFDcatSALRCG--ARRVFVVFRKGftHIRAVPEEMELAKE-EKCEFLPflspRKVV--L 233
Cdd:COG0492 135 DGFF--FRGkDVVVVGGGDSALE---EALYLTkfASKVTLIHRRD--ELRASKILVERLRAnPKIEVLW----NTEVteI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 234 KGGQIVamEFVRTEQDSDGswkededQVVRLKADVVISAFGSVLSDDKVREamapikfnrWGLpEIDP-------ETMQT 306
Cdd:COG0492 204 EGDGRV--EGVTLKNVKTG-------EEKELEVDGVFVAIGLKPNTELLKG---------LGL-ELDEdgyivvdEDMET 264
|
330
....*....|.
gi 2032774312 307 SEPWVFAGGDV 317
Cdd:COG0492 265 SVPGVFAAGDV 275
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
780-840 |
3.77e-06 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 47.22 E-value: 3.77e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032774312 780 VALIDEEMCINCGKCYMTCNdsgYQAIrFDPETHLPTV-TDSCTGCTLCLSVCPViDCIRMV 840
Cdd:PRK08764 79 VAWIVEADCIGCTKCIQACP---VDAI-VGGAKHMHTViAPLCTGCELCVPACPV-DCIELH 135
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
796-842 |
6.84e-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: 6.84e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2032774312 796 MTCNDS-GYQAIRFDPETH---LPTV-TDSCTGCTLCLSVCPViDCIRMVSR 842
Cdd:cd10564 89 RSCQDAcPTQAIRFRPRLGgiaLPELdADACTGCGACVSVCPV-GAITLTPL 139
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
783-846 |
9.38e-06 |
|
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: 45.85 E-value: 9.38e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032774312 783 IDEEMCINCGKCYMTCndsGYQAIRFDPETHLPTVT--------DSCTGCTLCLSVCPViDCIRMVSRTTPY 846
Cdd:cd10549 37 IDEDKCVFCGACVEVC---PTGAIELTPEGKEYVPKekeaeideEKCIGCGLCVKVCPV-DAITLEDELEIV 104
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
787-837 |
4.74e-05 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 41.39 E-value: 4.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2032774312 787 MCINCGKCYMTCNDSGYQAIRFDPETHLPTVTDSCTGCTLCLSVCPViDCI 837
Cdd:pfam13187 1 KCTGCGACVAACPAGAIVPDLVGQTIRGDIAGLACIGCGACVDACPR-GAI 50
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
22-65 |
4.97e-05 |
|
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: 46.75 E-value: 4.97e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2032774312 22 QVKIALLGAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMSE 65
Cdd:COG1232 1 MKRVAVIGGGIAGLTAAYRLAKAGHE-VTVLEASDRVGGLIRTV 43
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
24-106 |
5.91e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 46.42 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 24 KIALLGAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMSeipqfrlpYDVVNFEAE---------------LMKDLGV 88
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHE-VTVFEADDQLGGLAAS--------FEFGGLPIErfyhhifksdealleLLDELGL 71
|
90 100
....*....|....*....|...
gi 2032774312 89 --KIIFRK---GLAVDGmTLHTL 106
Cdd:PRK07233 72 edKLRWREtktGYYVDG-KLYPL 93
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
29-87 |
8.35e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 46.00 E-value: 8.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2032774312 29 GAGPASLSCASFLARLGYSnITIFEKQEYLGGLSMS-EIPQFRL---PYDVVNFEA--ELMKDLG 87
Cdd:COG1233 10 GAGIGGLAAAALLARAGYR-VTVLEKNDTPGGRARTfERPGFRFdvgPSVLTMPGVleRLFRELG 73
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
783-833 |
9.00e-05 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 45.79 E-value: 9.00e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2032774312 783 IDEEMCINCGKCYMTCndsGYQAIRFDpETHLPTVTDSCTGCTLCLSVCPV 833
Cdd:COG4624 88 RDKEKCKNCYPCVRAC---PVKAIKVD-DGKAEIDEEKCISCGQCVAVCPF 134
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
784-843 |
1.64e-04 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 41.55 E-value: 1.64e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 784 DEEMCINCGKCYMTCNDSgyqAIRFDPETHLPTVTDSCTGCTLCLSVCPViDCIRMVSRT 843
Cdd:PRK09624 49 NRDKCVRCYLCYIYCPEP---AIYLDEEGYPVFDYDYCKGCGICANECPT-KAIEMVRET 104
|
|
| SIMIBI_bact_arch |
cd03110 |
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ... |
780-833 |
4.32e-04 |
|
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.
Pssm-ID: 349764 [Multi-domain] Cd Length: 246 Bit Score: 42.76 E-value: 4.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2032774312 780 VALIDEEMCINCGKCYMTCNdsgYQAIRFDPeTHLPTVTDSCTGCTLCLSVCPV 833
Cdd:cd03110 58 KAFIDQEKCIRCGNCERVCK---FGAILEFF-QKLIVDESLCEGCGACVIICPR 107
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
782-832 |
5.02e-04 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 41.86 E-value: 5.02e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 782 LIDEEMCINCGKCYMTCNdsgYQAIRFDPETHlptVTDSCTGC---------TLCLSVCP 832
Cdd:COG0437 86 LVDYDKCIGCRYCVAACP---YGAPRFNPETG---VVEKCTFCadrldegllPACVEACP 139
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
23-62 |
5.33e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 43.34 E-value: 5.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2032774312 23 VKIALLGAGPASLSCASFLARLGYSnITIFEKQEYLGGLS 62
Cdd:PRK07208 5 KSVVIIGAGPAGLTAAYELLKRGYP-VTVLEADPVVGGIS 43
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
780-833 |
6.10e-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: 319894 [Multi-domain] Cd Length: 125 Bit Score: 40.40 E-value: 6.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032774312 780 VALIDEEMCINCGKCYMTCNDSGYQ-------AIRFDPETHLPTVTdSCTGCTLCLSVCPV 833
Cdd:cd16372 2 LLVTDPEKCIGCLQCEEACSKTFFKeedreksCIRITETEGGYAIN-VCNQCGECIDVCPT 61
|
|
| ferrodoxin_EFR1 |
NF038196 |
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ... |
816-840 |
7.20e-04 |
|
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: 42.15 E-value: 7.20e-04
10 20
....*....|....*....|....*
gi 2032774312 816 TVTDSCTGCTLCLSVCPViDCIRMV 840
Cdd:NF038196 182 HVTDKCIGCGICAKVCPV-NNIEME 205
|
|
| DMSOR_beta_like |
cd16367 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
780-840 |
1.03e-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: 319889 [Multi-domain] Cd Length: 138 Bit Score: 39.98 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 780 VALIDEEMCINCGKCYMTCNDS----------GYQ-------------------------AIRFDPETHLpTVTDSCTGC 824
Cdd:cd16367 13 LLVIDLDRCIRCDNCEKACADThdghsrldrnGLRfgnllvptacrhcvdpvcmigcptgAIHRDDGGEV-VISDACCGC 91
|
90
....*....|....*.
gi 2032774312 825 TLCLSVCPvIDCIRMV 840
Cdd:cd16367 92 GNCASACP-YGAIQMV 106
|
|
| Fer4_17 |
pfam13534 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
788-832 |
1.08e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 433287 [Multi-domain] Cd Length: 61 Bit Score: 38.21 E-value: 1.08e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2032774312 788 CINCGKCYMTCnDSgYQAIRFDP-------------ETHLPTVTDSCTGCTLCLSVCP 832
Cdd:pfam13534 2 CIQCGCCVDEC-PR-YLLNGDEPkklmraaylgdleELQANKVANLCSECGLCEYACP 57
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
787-840 |
1.10e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 42.55 E-value: 1.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2032774312 787 MCINCGKCYMTCNDsgyQAI-RFDPETHLPTVTDSCTGCTLCLSVCPViDCIRMV 840
Cdd:PRK12771 511 NCFECDNCYGACPQ---DAIiKLGPGRRYHFDYDKCTGCHICADVCPC-GAIEMG 561
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
818-848 |
1.12e-03 |
|
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: 38.19 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|.
gi 2032774312 818 TDSCTGCTLCLSVCPViDCIRMVSRTTPYEP 848
Cdd:COG1143 1 EDKCIGCGLCVRVCPV-DAITIEDGEPGKVY 30
|
|
| GlpC |
COG0247 |
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ... |
786-855 |
1.21e-03 |
|
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];
Pssm-ID: 440017 [Multi-domain] Cd Length: 420 Bit Score: 42.37 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 786 EMCINCGKCYMTC---------NDS-------------GYQAIRFDPETHLptVTDSCTGCTLCLSVCPV-IDCIRMVSR 842
Cdd:COG0247 78 DACVGCGFCRAMCpsykatgdeKDSprgrinllrevleGELPLDLSEEVYE--VLDLCLTCKACETACPSgVDIADLIAE 155
|
90
....*....|....
gi 2032774312 843 TTP-YEPKRGLPLA 855
Cdd:COG0247 156 ARAqLVERGGRPLR 169
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
786-832 |
1.26e-03 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 39.73 E-value: 1.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2032774312 786 EMCINCGKCYMTCNDSgyqAIRFDPETHLPTVTDSCTGCTLCLSVCP 832
Cdd:PRK09625 59 EICINCFNCWVYCPDA---AILSRDKKLKGVDYSHCKGCGVCVEVCP 102
|
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
780-840 |
1.96e-03 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 38.77 E-value: 1.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2032774312 780 VALIDEEMCINCGKCYMTCNDSgyqAIRFDPETHLPTVTDSCTGCTLCLSVCPViDCIRMV 840
Cdd:PRK09623 45 MPVVDESKCVKCYICWKFCPEP---AIYIKEDGYVAIDYDYCKGCGICANECPT-KAITMV 101
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
782-833 |
1.98e-03 |
|
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: 39.29 E-value: 1.98e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2032774312 782 LIDEEMCINCGKCYMTC-------NDSGYQAIRF--DPETHLPTVTDSCTGCT--LCLSVCPV 833
Cdd:cd04410 2 VVDLDRCIGCGTCEVACkqehglrPGPDWSRIKVieGGGLERAFLPVSCMHCEdpPCVKACPT 64
|
|
| napG |
PRK09476 |
quinol dehydrogenase periplasmic component; Provisional |
782-831 |
2.19e-03 |
|
quinol dehydrogenase periplasmic component; Provisional
Pssm-ID: 236534 [Multi-domain] Cd Length: 254 Bit Score: 40.76 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032774312 782 LIDEEMCIN-----CGKCYMTCN--DsgyQAIRFD----PETH-----LPTV-TDSCTGCTLCLSVC 831
Cdd:PRK09476 133 LVDQENCLNfqglrCDVCYRVCPliD---KAITLElernERTGkhaffLPTVhSDACTGCGKCEKAC 196
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
817-850 |
2.38e-03 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 37.38 E-value: 2.38e-03
10 20 30
....*....|....*....|....*....|....
gi 2032774312 817 VTDSCTGCTLCLSVCPViDCIRMVSRTTPYEPKR 850
Cdd:COG1146 6 DTDKCIGCGACVEVCPV-DVLELDEEGKKALVIN 38
|
|
| eukary_SO_Moco |
cd02111 |
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ... |
443-496 |
2.76e-03 |
|
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.
Pssm-ID: 239029 [Multi-domain] Cd Length: 365 Bit Score: 40.84 E-value: 2.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2032774312 443 LNIELISEKTAAYwckSIAELKADFPNHVLIASIMCSYNRENwtELSKMAQVAG 496
Cdd:cd02111 48 LEVEGPDGTTLSL---SLEDLKSLFPKHEVTATLQCAGNRRS--EMTKVKKVKG 96
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
14-91 |
3.78e-03 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 40.55 E-value: 3.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032774312 14 LEDMPEayqvKIALLGAGPASLSCASFLARLGySNITIFEKQEYLGGLSMSEIPQFRLPYdvvnFEAELMKDLGVKII 91
Cdd:PRK06292 165 LDKLPK----SLAVIGGGVIGLELGQALSRLG-VKVTVFERGDRILPLEDPEVSKQAQKI----LSKEFKIKLGAKVT 233
|
|
| NapH |
COG0348 |
Polyferredoxin NapH [Energy production and conversion]; |
783-842 |
3.88e-03 |
|
Polyferredoxin NapH [Energy production and conversion];
Pssm-ID: 440117 [Multi-domain] Cd Length: 263 Bit Score: 40.05 E-value: 3.88e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2032774312 783 IDEEMCINCGKCYMTCnDSGyQAIRfdpetHLPTVTDSCTGCTLCLSVCPViDCIRMVSR 842
Cdd:COG0348 207 YDRGDCIDCGLCVKVC-PMG-IDIR-----KGEINQSECINCGRCIDACPK-DAIRFSSR 258
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
24-100 |
5.20e-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: 425450 [Multi-domain] Cd Length: 80 Bit Score: 36.80 E-value: 5.20e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2032774312 24 KIALLGAGPASLSCASFLARLGySNITIFEKQEYLGGLsmseipqfrLPYDVVNFEAELMKDLGVKIIFRKGL-AVDG 100
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLG-SKVTVVERRDRLLPG---------FDPEIAKILQEKLEKNGIEFLLNTTVeAIEG 68
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
772-832 |
5.68e-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: 37.70 E-value: 5.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2032774312 772 DLCNTEQV------VALIDEEMCINCGKCYMTCNdsgYQAIRFDPETHLPTvtdSCTGCTLCLSVCP 832
Cdd:cd16372 57 DVCPTGAItrdangVVMINKKLCVGCLMCVGFCP---EGAMFKHEDYPEPF---KCIACGICVKACP 117
|
|
| Fer4_8 |
pfam13183 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
787-833 |
7.51e-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: 35.75 E-value: 7.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2032774312 787 MCINCGKCYMTC--------NDSGY------QAIRFDPETH-LPTVTDSCTGCTLCLSVCPV 833
Cdd:pfam13183 1 RCIRCGACLAACpvylvtggRFPGDprggaaALLGRLEALEgLAEGLWLCTLCGACTEVCPV 62
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
24-60 |
8.21e-03 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 39.71 E-value: 8.21e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2032774312 24 KIALLGAGPASLSCASFLARlgYSNITIFEKQEYLGG 60
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSR--RHDVTLFEANDRLGG 39
|
|
| |
