|
Name |
Accession |
Description |
Interval |
E-value |
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
332-598 |
9.31e-50 |
|
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.
Pssm-ID: 99783 [Multi-domain] Cd Length: 210 Bit Score: 171.33 E-value: 9.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 332 IISVISHP-SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLL 407
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 408 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 486
Cdd:cd06186 81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 487 IQSFRWFADLLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVF 566
Cdd:cd06186 150 REDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VV 180
|
250 260 270
....*....|....*....|....*....|..
gi 221042164 567 CCGPNSLSKTLHKLSNQNNsyGTRFEYNKESF 598
Cdd:cd06186 181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
444-581 |
6.46e-27 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 106.66 E-value: 6.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 444 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYV 513
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221042164 514 NIQLYLSQTD-GIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 581
Cdd:pfam08030 81 SDQSDSSIRSeNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
90-500 |
5.11e-16 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 81.43 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 90 SLILLPMCRTL-LAYLRGSQKVPSRRtrrlldksrtFHITCGVTICIFSGVHVAAHLvnalnfsvnysedFVELNAARYR 168
Cdd:PLN02844 168 ALLLLPVLRGLaLFRLLGIQFEASVR----------YHVWLGTSMIFFATVHGASTL-------------FIWGISHHIQ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 169 DEdPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgci 248
Cdd:PLN02844 225 DE-IWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG------------------ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 249 slnrtssqnislpeyfSEHFHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNK 328
Cdd:PLN02844 286 ----------------DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRP 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 329 PVTIISVISHPSDVMEIRMVKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLL 407
Cdd:PLN02844 313 ETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQ 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 408 PPSSQDSEILPFIQSRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCR 485
Cdd:PLN02844 393 AELDSETNQMNCIPVA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVK 466
|
410
....*....|....*
gi 221042164 486 DIQSfrwfadlLCML 500
Cdd:PLN02844 467 KSQD-------ICLL 474
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
295-486 |
1.93e-14 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 75.70 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 295 PRFQANFPQTWLWIS-GPLCLYCAerLYRYIRSN-----KPVTIISVISHPSDVMEIRMVKEN---FKARPGQ--YITLH 363
Cdd:COG4097 178 GPFYWSPPAGVLWAAlAAAGLAAA--VYSRLGRPlrsrrHPYRVESVEPEAGDVVELTLRPEGgrwLGHRAGQfaFLRFD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 364 CPSVSaLENHPFTLTMCPTET-KATFGVhlKIVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEES 441
Cdd:COG4097 256 GSPFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRR 315
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221042164 442 LNYEVSLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 486
Cdd:COG4097 316 DTAPRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
90-226 |
3.97e-14 |
|
Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.
Pssm-ID: 426438 [Multi-domain] Cd Length: 121 Bit Score: 69.22 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 90 SLILLPMcrTLLAYLRGSqkVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRD 169
Cdd:pfam01794 5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 221042164 170 edprkllfttvpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 226
Cdd:pfam01794 78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
194-467 |
2.79e-10 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 63.35 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 194 LMITASTY-AIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrTSSQNISLPEYFsehfhepf 272
Cdd:PLN02292 261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG----------------------ISFALISFPGFY-------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 273 pegfskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVKEN- 351
Cdd:PLN02292 311 -----------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 352 FKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLlppSSQDSeilpfiqsRNYPKLYID 431
Cdd:PLN02292 350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSDQ--------IDRLAVSVE 418
|
250 260 270
....*....|....*....|....*....|....*.
gi 221042164 432 GPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 467
Cdd:PLN02292 419 GPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
332-598 |
9.31e-50 |
|
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as superoxide and hydrogen peroxide. ROS were originally identified as bactericidal agents in phagocytes, but are now also implicated in cell signaling and metabolism. NOX has a 6-alpha helix heme-binding transmembrane domain fused to a flavoprotein with the nucleotide binding domain located in the cytoplasm. Duox enzymes link a peroxidase domain to the NOX domain via a single transmembrane and EF-hand Ca2+ binding sites. The flavoprotein module has a ferredoxin like FAD/NADPH binding domain. In classical phagocytic NOX2, electron transfer occurs from NADPH to FAD to the heme of cytb to oxygen leading to superoxide formation.
Pssm-ID: 99783 [Multi-domain] Cd Length: 210 Bit Score: 171.33 E-value: 9.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 332 IISVISHP-SDVMEIRMVKE-NFKARPGQYITLHCPSV-SALENHPFTLTMCPTETKATFGVHLKIV-GDWTERFRDLLL 407
Cdd:cd06186 1 IATVELLPdSDVIRLTIPKPkPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDEQDTLSLIIRAKkGFTTRLLRKALK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 408 PPSSQDSeilpfiqsrnyPKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDW-KPYKLRRLYFIWVCRD 486
Cdd:cd06186 81 SPGGGVS-----------LKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSsKTSRTRRVKLVWVVRD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 487 IQSFRWFADLLCMlhnkfWQENRPDYvNIQLYLSQtdgiqkiigekyhalnsrlfigrprwkllfdeiakynrgktvgVF 566
Cdd:cd06186 150 REDLEWFLDELRA-----AQELEVDG-EIEIYVTR-------------------------------------------VV 180
|
250 260 270
....*....|....*....|....*....|..
gi 221042164 567 CCGPNSLSKTLHKLSNQNNsyGTRFEYNKESF 598
Cdd:cd06186 181 VCGPPGLVDDVRNAVAKKG--GTGVEFHEESF 210
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
444-581 |
6.46e-27 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 106.66 E-value: 6.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 444 YEVSLCVAGGIGVTPFASILNTLLDDWKPYKLRRLYFIWVCRDIQSFRWFADLLCML----------HNKFWQENRPDYV 513
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKKLKTKKIKFYWVVRDLSSLEWFKDVLNELeelkelnieiHIYLTGEYEAEDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221042164 514 NIQLYLSQTD-GIQKIIGEKYHALNSRLFIGRPRWKLLFDEIAKYNRGKTVGVFCCGPNSLSKTLHKLS 581
Cdd:pfam08030 81 SDQSDSSIRSeNFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNLV 149
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
90-500 |
5.11e-16 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 81.43 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 90 SLILLPMCRTL-LAYLRGSQKVPSRRtrrlldksrtFHITCGVTICIFSGVHVAAHLvnalnfsvnysedFVELNAARYR 168
Cdd:PLN02844 168 ALLLLPVLRGLaLFRLLGIQFEASVR----------YHVWLGTSMIFFATVHGASTL-------------FIWGISHHIQ 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 169 DEdPRKLLFTTVPGLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgci 248
Cdd:PLN02844 225 DE-IWKWQKTGRIYLAGEIALVTGLVIWITSLPQIRRKRFEIFYYTHHLYIVFLIFFLFHAG------------------ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 249 slnrtssqnislpeyfSEHFHEPFPEGFskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNK 328
Cdd:PLN02844 286 ----------------DRHFYMVFPGIF-------------------------------------LFGLDKLLRIVQSRP 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 329 PVTIISVISHPSDVMEIRMVKE-NFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLL 407
Cdd:PLN02844 313 ETCILSARLFPCKAIELVLPKDpGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNIDDHTMSVIIKCEGGWTNSLYNKIQ 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 408 PPSSQDSEILPFIQSRnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP-YKL-RRLYFIWVCR 485
Cdd:PLN02844 393 AELDSETNQMNCIPVA------IEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSrYRFpKRVQLIYVVK 466
|
410
....*....|....*
gi 221042164 486 DIQSfrwfadlLCML 500
Cdd:PLN02844 467 KSQD-------ICLL 474
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
328-437 |
1.59e-15 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 72.75 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 328 KPVTIISVISHPSDVMEIRMVKEN--FKARPGQYITLHC-PSVSALENHPFTLTMCPTETKATfgVHLKIVGDWTERFRD 404
Cdd:pfam08022 2 FGVPKAKVALLPDNVLKLRVSKPKkpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLS--LHIKVKGGWTRKLAN 79
|
90 100 110
....*....|....*....|....*....|...
gi 221042164 405 LLLPpssqdSEILPFIQSRNYPKLYIDGPFGSP 437
Cdd:pfam08022 80 YLSS-----SCPKSPENGKDKPRVLIEGPYGPP 107
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
341-570 |
3.46e-15 |
|
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 75.18 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 341 DVMEIRMVKEN-FKARPGQYITLHCPSVSALENHPFTLTMCPTETKA-TFGVHLKIVGDWTERFRDLLLppssqDSEILp 418
Cdd:cd00322 9 DVRLFRLQLPNgFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGElELTVKIVPGGPFSAWLHDLKP-----GDEVE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 419 fiqsrnypklyIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFrWFADLLC 498
Cdd:cd00322 83 -----------VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPG---GEITLLYGARTPADL-LFLDELE 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221042164 499 MLHNKFwqenrpdyVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPRWKLLFDEIAKY-NRGKTVGVFCCGP 570
Cdd:cd00322 148 ELAKEG--------PNFRLVLALSRE-------------SEAKLGPGGRIDREAEILALlPDDSGALVYICGP 199
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
295-486 |
1.93e-14 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 75.70 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 295 PRFQANFPQTWLWIS-GPLCLYCAerLYRYIRSN-----KPVTIISVISHPSDVMEIRMVKEN---FKARPGQ--YITLH 363
Cdd:COG4097 178 GPFYWSPPAGVLWAAlAAAGLAAA--VYSRLGRPlrsrrHPYRVESVEPEAGDVVELTLRPEGgrwLGHRAGQfaFLRFD 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 364 CPSVSaLENHPFTLTMCPTET-KATFGVhlKIVGDWTERFRDLllPPSSqdseilpfiqsrnypKLYIDGPFGS-PFEES 441
Cdd:COG4097 256 GSPFW-EEAHPFSISSAPGGDgRLRFTI--KALGDFTRRLGRL--KPGT---------------RVYVEGPYGRfTFDRR 315
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 221042164 442 LNYEVSLCVAGGIGVTPFASILNTLldDWKPYKLRRLYFIWVCRD 486
Cdd:COG4097 316 DTAPRQVWIAGGIGITPFLALLRAL--AARPGDQRPVDLFYCVRD 358
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
90-226 |
3.97e-14 |
|
Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.
Pssm-ID: 426438 [Multi-domain] Cd Length: 121 Bit Score: 69.22 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 90 SLILLPMcrTLLAYLRGSqkVPSRRTRRLLDKSRTFHITCGVTICIFSGVHVAAHLVNALNFSVnysEDFVELNAARYRD 169
Cdd:pfam01794 5 ALALLPL--LLLLALRNN--PLEWLTGLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSL---EGILDLLLKRPYN 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 221042164 170 edprkllfttvpgLTGVCMVVVLFLMITASTYAIRVSNYDIFWYTHNLFFVFYMLLT 226
Cdd:pfam01794 78 -------------ILGIIALVLLVLLAITSLPPFRRLSYELFLYLHILLAVAFLLLV 121
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
331-486 |
4.96e-14 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 72.20 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 331 TIISVISHPSDV--MEIRMVKENFKARPGQYITLHCPSvsALENHPFTLTMCPTEtKATFGVHLKIVGDWTERFRDLllp 408
Cdd:COG0543 1 KVVSVERLAPDVylLRLEAPLIALKFKPGQFVMLRVPG--DGLRRPFSIASAPRE-DGTIELHIRVVGKGTRALAEL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 409 pssQDSEilpfiqsrnypKLYIDGPFGSPFEeslnYEVS----LCVAGGIGVTPFASILNTLLDdwkpyKLRRLYFIWVC 484
Cdd:COG0543 75 ---KPGD-----------ELDVRGPLGNGFP----LEDSgrpvLLVAGGTGLAPLRSLAEALLA-----RGRRVTLYLGA 131
|
..
gi 221042164 485 RD 486
Cdd:COG0543 132 RT 133
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
338-599 |
1.59e-10 |
|
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99795 [Multi-domain] Cd Length: 216 Bit Score: 61.12 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 338 HPSDVMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLTMCPTETK-ATFGVhlKIVGDWTERFRDLLLPPSsqdsei 416
Cdd:cd06198 7 RPTTTLTLEPRGPALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTI--KALGDYTRRLAERLKPGT------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 417 lpfiqsrnypKLYIDGPFGSpFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQSFrWFADL 496
Cdd:cd06198 79 ----------RVTVEGPYGR-FTFDDRRARQIWIAGGIGITPFLALLEALAARGDA---RPVTLFYCVRDPEDA-VFLDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 497 LcmlhnkfWQENRPDYVNIQLYLSQTDGiqkiigekyhalnsRLFIGRPRWKLLFDeiakynrGKTVGVFCCGPNSLSKT 576
Cdd:cd06198 144 L-------RALAAAAGVVLHVIDSPSDG--------------RLTLEQLVRALVPD-------LADADVWFCGPPGMADA 195
|
250 260
....*....|....*....|...
gi 221042164 577 LHKLSNQNNSYGTRFEYnkESFS 599
Cdd:cd06198 196 LEKGLRALGVPARRFHY--ERFE 216
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
194-467 |
2.79e-10 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 63.35 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 194 LMITASTY-AIRVSNYDIFWYTHNLFFVFYMLLTLHVSggllkyqtnldthppgcislnrTSSQNISLPEYFsehfhepf 272
Cdd:PLN02292 261 LVMWATTYpKIRRRFFEVFFYTHYLYIVFMLFFVFHVG----------------------ISFALISFPGFY-------- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 273 pegfskpaeftqhkfvkicmeeprfqanfpqtwlwisgplcLYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVKEN- 351
Cdd:PLN02292 311 -----------------------------------------IFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFSKNPm 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 352 FKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHLKIVGDWTERFRDLLlppSSQDSeilpfiqsRNYPKLYID 431
Cdd:PLN02292 350 LMYSPTSIMFVNIPSISKLQWHPFTITSSSKLEPEKLSVMIKSQGKWSTKLYHML---SSSDQ--------IDRLAVSVE 418
|
250 260 270
....*....|....*....|....*....|....*.
gi 221042164 432 GPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLL 467
Cdd:PLN02292 419 GPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
314-496 |
3.43e-10 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 63.14 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 314 LYCAERLYRYIRSNKPVTIISVISHPSDVMEIRMVK-ENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGVHL 392
Cdd:PLN02631 294 LFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKtPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNLEKDTLSVVI 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 393 KIVGDWTERFRDLLlpPSSQDSEilpfiqsrnypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKP 472
Cdd:PLN02631 374 RRQGSWTQKLYTHL--SSSIDSL-----------EVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELIFQSQN 440
|
170 180
....*....|....*....|....
gi 221042164 473 YKLRRLYFIWVCrdiqSFRWFADL 496
Cdd:PLN02631 441 PSTKLPDVLLVC----SFKHYHDL 460
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
329-570 |
3.36e-08 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 54.41 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 329 PVTIISVISHPSDVMEIRMV----KENFKARPGQYITLHCPSVSALENHPFTLTMCPTETKATFGV-------------- 390
Cdd:COG1018 5 PLRVVEVRRETPDVVSFTLEppdgAPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVkrvpggggsnwlhd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 391 HLKiVGDwterfrdlllppssqdseilpfiqsrnypKLYIDGPFGS---PFEESLNYevsLCVAGGIGVTPFASILNTLL 467
Cdd:COG1018 85 HLK-VGD-----------------------------TLEVSGPRGDfvlDPEPARPL---LLIAGGIGITPFLSMLRTLL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 468 dDWKPYklRRLYFIWVCRDIQSFrWFADLLCMLHNKfwqenrpdYVNIQLYLSQTDGiqkiigekyhalnSRLFIGRPRW 547
Cdd:COG1018 132 -ARGPF--RPVTLVYGARSPADL-AFRDELEALAAR--------HPRLRLHPVLSRE-------------PAGLQGRLDA 186
|
250 260
....*....|....*....|...
gi 221042164 548 KLLFDEIAKYNRGKtvgVFCCGP 570
Cdd:COG1018 187 ELLAALLPDPADAH---VYLCGP 206
|
|
| DHOD_e_trans_like2 |
cd06220 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
330-472 |
2.64e-06 |
|
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.
Pssm-ID: 99816 [Multi-domain] Cd Length: 233 Bit Score: 48.78 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 330 VTIISVIshpsdvMEIRMVK-----ENFKARPGQYITLHCPSVSALenhPFTLTMCPTEtkatFGVHLKIVGDWTERFRD 404
Cdd:cd06220 1 VTIKEVI------DETPTVKtfvfdWDFDFKPGQFVMVWVPGVDEI---PMSLSYIDGP----NSITVKKVGEATSALHD 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221042164 405 LllppssqdseilpfiqsRNYPKLYIDGPFGSPFEesLNYEVSLCVAGGIGVTPfasiLNTLLDDWKP 472
Cdd:cd06220 68 L-----------------KEGDKLGIRGPYGNGFE--LVGGKVLLIGGGIGIAP----LAPLAERLKK 112
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
330-462 |
2.88e-06 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 49.10 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 330 VTIISVISHPSDVMEIRM-VKENFKARPGQYITLHCPSVSALENHPFTLTMCPTEtKATFGVhlKIVGDWTERFRDLllp 408
Cdd:PRK00054 7 MKIVENKEIAPNIYTLVLdGEKVFDMKPGQFVMVWVPGVEPLLERPISISDIDKN-EITILY--RKVGEGTKKLSKL--- 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 221042164 409 pSSQDSeilpfiqsrnypkLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASI 462
Cdd:PRK00054 81 -KEGDE-------------LDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYEL 120
|
|
| cyt_b5_reduct_like |
cd06183 |
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ... |
427-570 |
2.00e-05 |
|
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.
Pssm-ID: 99780 [Multi-domain] Cd Length: 234 Bit Score: 46.41 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 427 KLYIDGPFGS-PFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkPYKLRRLYFIWVCRDIQsfrwfaDLLCMLHNKFW 505
Cdd:cd06183 86 TVEIRGPFGKfEYKPNGKVKHIGMIAGGTGITPMLQLIRAILKD--PEDKTKISLLYANRTEE------DILLREELDEL 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221042164 506 QENRPDYVNIQLYLSQTDGIQKIigekyhalnsrlFIGRPRWKLLFDEIAKYNRGKTVgVFCCGP 570
Cdd:cd06183 158 AKKHPDRFKVHYVLSRPPEGWKG------------GVGFITKEMIKEHLPPPPSEDTL-VLVCGP 209
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
342-463 |
3.10e-05 |
|
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.
Pssm-ID: 99789 [Multi-domain] Cd Length: 243 Bit Score: 45.78 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 342 VMEIRMVKENFKARPGQYITLHCPSVSALENHPFTLtMCPTETKATFGVHLKIVGDWTERFrdLLLPPSSqdseilpfiq 421
Cdd:cd06192 13 LLTIKAPLAARLFRPGQFVFLRNFESPGLERIPLSL-AGVDPEEGTISLLVEIRGPKTKLI--AELKPGE---------- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 221042164 422 srnypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASIL 463
Cdd:cd06192 80 -----KLDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIA 116
|
|
| flavohem_like_fad_nad_binding |
cd06184 |
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ... |
450-496 |
6.00e-04 |
|
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.
Pssm-ID: 99781 Cd Length: 247 Bit Score: 41.77 E-value: 6.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 221042164 450 VAGGIGVTPFASILNTLLDDWKPyklRRLYFIWVCRDIQS--FR-WFADL 496
Cdd:cd06184 119 ISAGVGITPMLSMLEALAAEGPG---RPVTFIHAARNSAVhaFRdELEEL 165
|
|
| sulfite_reductase_like |
cd06221 |
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ... |
427-570 |
7.72e-04 |
|
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural similarity to ferredoxin reductase and sequence similarity to dihydroorotate dehydrogenases. Clostridium pasteurianum inducible dissimilatory type sulfite reductase is linked to ferredoxin and reduces NH2OH and SeO3 at a lesser rate than it's normal substate SO3(2-). Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+.
Pssm-ID: 99817 [Multi-domain] Cd Length: 253 Bit Score: 41.44 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 427 KLYIDGPFGSPF--EESLNYEVsLCVAGGIGVTPFASILNTLLDDWKPYKlrRLYFiwvcrdIQSFRWFADLLCMLHNKF 504
Cdd:cd06221 80 TVGLRGPFGNGFpvEEMKGKDL-LLVAGGLGLAPLRSLINYILDNREDYG--KVTL------LYGARTPEDLLFKEELKE 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221042164 505 WQenrpDYVNIQLYLSQTDGiqkIIGEKYHalnsrlfIGRPrwKLLFDEIAkYNRGKTVgVFCCGP 570
Cdd:cd06221 151 WA----KRSDVEVILTVDRA---EEGWTGN-------VGLV--TDLLPELT-LDPDNTV-AIVCGP 198
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
330-513 |
2.02e-03 |
|
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.
Pssm-ID: 99786 [Multi-domain] Cd Length: 224 Bit Score: 39.84 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 330 VTIISVISHpsDVMEIR-MVKENFKARPGQYITLHCPSVSALenhPFTLTMCPTETkATFGVHLKIVGDWteRFRDlllp 408
Cdd:cd06189 3 VESIEPLND--DVYRVRlKPPAPLDFLAGQYLDLLLDDGDKR---PFSIASAPHED-GEIELHIRAVPGG--SFSD---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 409 pssqdsEILPFIQSRNypKLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDwkpyKLRR-LYFIWVCRDI 487
Cdd:cd06189 71 ------YVFEELKENG--LVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQ----GSKRpIHLYWGARTE 138
|
170 180
....*....|....*....|....*...
gi 221042164 488 QSFrwFADLLCmlhnKFWQENRP--DYV 513
Cdd:cd06189 139 EDL--YLDELL----EAWAEAHPnfTYV 160
|
|
| NAD_binding_1 |
pfam00175 |
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ... |
450-524 |
2.76e-03 |
|
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.
Pssm-ID: 425503 [Multi-domain] Cd Length: 109 Bit Score: 37.62 E-value: 2.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 221042164 450 VAGGIGVTPFASILNTLLDDWKPykLRRLYFIWVCRDiqsfrwFADLLCMLHNKFWQENRPDYVNIQLYLSQTDG 524
Cdd:pfam00175 2 IAGGTGIAPVRSMLRAILEDPKD--PTQVVLVFGNRN------EDDILYREELDELAEKHPGRLTVVYVVSRPEA 68
|
|
| T4MO_e_transfer_like |
cd06190 |
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ... |
427-486 |
5.83e-03 |
|
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates toluene and forms p-cresol as part of a three component toluene-4-monoxygenase system. Electron transfer is from NADH to an NADH:ferredoxin oxidoreductase (TmoF in P. mendocina) to ferredoxin to an iron-containing oxygenase. TmoF is homologous to other mono- and dioxygenase systems within the ferredoxin reductase family.
Pssm-ID: 99787 Cd Length: 232 Bit Score: 38.77 E-value: 5.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 221042164 427 KLYIDGPFGSPFEESLNYEVSLCVAGGIGVTPFASILNTLLDDWKPYKlRRLYFIWVCRD 486
Cdd:cd06190 80 ELELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRGAARSPYLSD-RPVDLFYGGRT 138
|
|
| |
