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Conserved domains on  [gi|489192247|ref|WP_003101595|]
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MULTISPECIES: ferric reductase-like transmembrane domain-containing protein [Pseudomonas]

Protein Classification

ferredoxin reductase family protein( domain architecture ID 11467864)

ferredoxin reductase family protein; ferredoxin reductase family protein may transfer electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH; contains a ferric reductase-like transmembrane domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
23-434 1.34e-153

Predicted ferric reductase [Inorganic ion transport and metabolism];


:

Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 442.41  E-value: 1.34e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247  23 PPASLDIWVVRKQAILLTGVASFALMSLIMLLAVRPVWLEKPLDGLDRMYRLHKWAGILAIVLGLLHYLLELAGPWLAGI 102
Cdd:COG4097   29 LPAPAGGRGLRTALGQLTGLLALALMSLQFLLAARPPWLERPFGGLDRLYRLHKWLGILALVLALAHPLLLLGPKWLVGW 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 103 VGKPvkgPRVETFLDVFRGSAKELGEWSAWILGGMLLVTLW-QRFPYHLWRYVHKALALVYLVLAFHSVVLAPASYWSQP 181
Cdd:COG4097  109 GGLP---ARLAALLTLLRGLAELLGEWAFYLLLALVVLSLLrRRLPYELWRLTHRLLAVAYLLLAFHHLLLGGPFYWSPP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 182 AGWLVAACALLGSACALLSLSGRIGRTRRHAGVVTAVERHGESLLEVTCRLQGD--WSHRAGQFAFLTCDR---LEGAHP 256
Cdd:COG4097  186 AGVLWAALAAAGLAAAVYSRLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDGspfWEEAHP 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 257 FTIASADRGCGEVRFSIKALGDYTRRLQdNLEVGARVEVEGPYGCFDF-RRGLAGRQVWVAAGIGVTPFIAWLESLQAAP 335
Cdd:COG4097  266 FSISSAPGGDGRLRFTIKALGDFTRRLG-RLKPGTRVYVEGPYGRFTFdRRDTAPRQVWIAGGIGITPFLALLRALAARP 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 336 ESAPSVELHYCVRNSQEALFAGRLRELCEHLPSVTLHIRYSDEQGKPQAAQLGVLKSAEGRWpSVWFCGPQGLADSLRRD 415
Cdd:COG4097  345 GDQRPVDLFYCVRDEEDAPFLEELRALAARLAGLRLHLVVSDEDGRLTAERLRRLVPDLAEA-DVFFCGPPGMMDALRRD 423

                        410
                 ....*....|....*....
gi 489192247 416 LRRQGMPLRLFHQEAFRMR 434
Cdd:COG4097  424 LRALGVPARRIHQERFEFR 442
 
Name Accession Description Interval E-value
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
23-434 1.34e-153

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 442.41  E-value: 1.34e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247  23 PPASLDIWVVRKQAILLTGVASFALMSLIMLLAVRPVWLEKPLDGLDRMYRLHKWAGILAIVLGLLHYLLELAGPWLAGI 102
Cdd:COG4097   29 LPAPAGGRGLRTALGQLTGLLALALMSLQFLLAARPPWLERPFGGLDRLYRLHKWLGILALVLALAHPLLLLGPKWLVGW 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 103 VGKPvkgPRVETFLDVFRGSAKELGEWSAWILGGMLLVTLW-QRFPYHLWRYVHKALALVYLVLAFHSVVLAPASYWSQP 181
Cdd:COG4097  109 GGLP---ARLAALLTLLRGLAELLGEWAFYLLLALVVLSLLrRRLPYELWRLTHRLLAVAYLLLAFHHLLLGGPFYWSPP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 182 AGWLVAACALLGSACALLSLSGRIGRTRRHAGVVTAVERHGESLLEVTCRLQGD--WSHRAGQFAFLTCDR---LEGAHP 256
Cdd:COG4097  186 AGVLWAALAAAGLAAAVYSRLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDGspfWEEAHP 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 257 FTIASADRGCGEVRFSIKALGDYTRRLQdNLEVGARVEVEGPYGCFDF-RRGLAGRQVWVAAGIGVTPFIAWLESLQAAP 335
Cdd:COG4097  266 FSISSAPGGDGRLRFTIKALGDFTRRLG-RLKPGTRVYVEGPYGRFTFdRRDTAPRQVWIAGGIGITPFLALLRALAARP 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 336 ESAPSVELHYCVRNSQEALFAGRLRELCEHLPSVTLHIRYSDEQGKPQAAQLGVLKSAEGRWpSVWFCGPQGLADSLRRD 415
Cdd:COG4097  345 GDQRPVDLFYCVRDEEDAPFLEELRALAARLAGLRLHLVVSDEDGRLTAERLRRLVPDLAEA-DVFFCGPPGMMDALRRD 423

                        410
                 ....*....|....*....
gi 489192247 416 LRRQGMPLRLFHQEAFRMR 434
Cdd:COG4097  424 LRALGVPARRIHQERFEFR 442
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 223-432 2.28e-89

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: 270.28  E-value: 2.28e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 223 ESLLEVTCRLQGDWS---HRAGQFAFLTCDR--LEGAHPFTIASADRGCGEVRFSIKALGDYTRRLQDNLEVGARVEVEG 297
Cdd:cd06198    5 EVRPTTTLTLEPRGPalgHRAGQFAFLRFDAsgWEEPHPFTISSAPDPDGRLRFTIKALGDYTRRLAERLKPGTRVTVEG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 298 PYGCFDFRRGlAGRQVWVAAGIGVTPFIAWLESLQAAPESAPsVELHYCVRNSQEALFAGRLRELCEHLpSVTLHIRYSD 377
Cdd:cd06198   85 PYGRFTFDDR-RARQIWIAGGIGITPFLALLEALAARGDARP-VTLFYCVRDPEDAVFLDELRALAAAA-GVVLHVIDSP 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489192247 378 EQGKPQAAQLGVLKSAEGRWPSVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAFR 432
Cdd:cd06198  162 SDGRLTLEQLVRALVPDLADADVWFCGPPGMADALEKGLRALGVPARRFHYERFE 216
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 40-166 7.04e-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: 68.06  E-value: 7.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247   40 TGVASFALMSLIMLLAVRPVWLEKPLD-GLDRMYRLHKWAGILAIVlgllhylleLAGPWLAGIVGKPVKGPRVETFLDV 118
Cdd:pfam01794   1 LGILALALLPLLLLLALRNNPLEWLTGlSYDRLLLFHRWLGRLAFL---------LALLHVILYLIYWLRFSLEGILDLL 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489192247  119 FRGSAKELGEWSAWILGGMLLVTL--WQRFPYHLWRYVHKALALVYLVLA 166
Cdd:pfam01794  72 LKRPYNILGIIALVLLVLLAITSLppFRRLSYELFLYLHILLAVAFLLLV 121
PRK13289 PRK13289
NO-inducible flavohemoprotein;
270-431 1.04e-12

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 69.06  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 270 RFSIK--ALGDYTRRLQDNLEVGARVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESLQAAPESAPSVELHYCv 347
Cdd:PRK13289 220 RISVKreAGGKVSNYLHDHVNVGDVLELAAPAGDFFLDVASDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAA- 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 348 RNSQEALFAGRLRELCEHLPSVTLHIRYS------------DEQGKPQAAQL-GVLKSAEGrwpSVWFCGPQGLADSLRR 414
Cdd:PRK13289 299 RNGGVHAFRDEVEALAARHPNLKAHTWYRepteqdragedfDSEGLMDLEWLeAWLPDPDA---DFYFCGPVPFMQFVAK 375

                        170
                 ....*....|....*..
gi 489192247 415 DLRRQGMPLRLFHQEAF 431
Cdd:PRK13289 376 QLLELGVPEERIHYEFF 392
 
Name Accession Description Interval E-value
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
23-434 1.34e-153

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 442.41  E-value: 1.34e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247  23 PPASLDIWVVRKQAILLTGVASFALMSLIMLLAVRPVWLEKPLDGLDRMYRLHKWAGILAIVLGLLHYLLELAGPWLAGI 102
Cdd:COG4097   29 LPAPAGGRGLRTALGQLTGLLALALMSLQFLLAARPPWLERPFGGLDRLYRLHKWLGILALVLALAHPLLLLGPKWLVGW 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 103 VGKPvkgPRVETFLDVFRGSAKELGEWSAWILGGMLLVTLW-QRFPYHLWRYVHKALALVYLVLAFHSVVLAPASYWSQP 181
Cdd:COG4097  109 GGLP---ARLAALLTLLRGLAELLGEWAFYLLLALVVLSLLrRRLPYELWRLTHRLLAVAYLLLAFHHLLLGGPFYWSPP 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 182 AGWLVAACALLGSACALLSLSGRIGRTRRHAGVVTAVERHGESLLEVTCRLQGD--WSHRAGQFAFLTCDR---LEGAHP 256
Cdd:COG4097  186 AGVLWAALAAAGLAAAVYSRLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDGspfWEEAHP 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 257 FTIASADRGCGEVRFSIKALGDYTRRLQdNLEVGARVEVEGPYGCFDF-RRGLAGRQVWVAAGIGVTPFIAWLESLQAAP 335
Cdd:COG4097  266 FSISSAPGGDGRLRFTIKALGDFTRRLG-RLKPGTRVYVEGPYGRFTFdRRDTAPRQVWIAGGIGITPFLALLRALAARP 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 336 ESAPSVELHYCVRNSQEALFAGRLRELCEHLPSVTLHIRYSDEQGKPQAAQLGVLKSAEGRWpSVWFCGPQGLADSLRRD 415
Cdd:COG4097  345 GDQRPVDLFYCVRDEEDAPFLEELRALAARLAGLRLHLVVSDEDGRLTAERLRRLVPDLAEA-DVFFCGPPGMMDALRRD 423

                        410
                 ....*....|....*....
gi 489192247 416 LRRQGMPLRLFHQEAFRMR 434
Cdd:COG4097  424 LRALGVPARRIHQERFEFR 442
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 223-432 2.28e-89

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: 270.28  E-value: 2.28e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 223 ESLLEVTCRLQGDWS---HRAGQFAFLTCDR--LEGAHPFTIASADRGCGEVRFSIKALGDYTRRLQDNLEVGARVEVEG 297
Cdd:cd06198    5 EVRPTTTLTLEPRGPalgHRAGQFAFLRFDAsgWEEPHPFTISSAPDPDGRLRFTIKALGDYTRRLAERLKPGTRVTVEG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 298 PYGCFDFRRGlAGRQVWVAAGIGVTPFIAWLESLQAAPESAPsVELHYCVRNSQEALFAGRLRELCEHLpSVTLHIRYSD 377
Cdd:cd06198   85 PYGRFTFDDR-RARQIWIAGGIGITPFLALLEALAARGDARP-VTLFYCVRDPEDAVFLDELRALAAAA-GVVLHVIDSP 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489192247 378 EQGKPQAAQLGVLKSAEGRWPSVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAFR 432
Cdd:cd06198  162 SDGRLTLEQLVRALVPDLADADVWFCGPPGMADALEKGLRALGVPARRFHYERFE 216
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
208-429 3.97e-40

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 143.39  E-value: 3.97e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 208 TRRHAGVVTAVERHGESLLEVTCRLQGDW---SHRAGQFA--FLTCDRLEGAHPFTIASADRGcGEVRFSIKAL--GDYT 280
Cdd:COG1018    1 AGFRPLRVVEVRRETPDVVSFTLEPPDGAplpRFRPGQFVtlRLPIDGKPLRRAYSLSSAPGD-GRLEITVKRVpgGGGS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 281 RRLQDNLEVGARVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESLQAApESAPSVELHYCVRNSQEALFAGRLR 360
Cdd:COG1018   80 NWLHDHLKVGDTLEVSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLAR-GPFRPVTLVYGARSPADLAFRDELE 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489192247 361 ELCEHLPSVTLHIRYSDE----QGKPQAAQLG-VLKSAEGRwpSVWFCGPQGLADSLRRDLRRQGMPLRLFHQE 429
Cdd:COG1018  159 ALAARHPRLRLHPVLSREpaglQGRLDAELLAaLLPDPADA--HVYLCGPPPMMEAVRAALAELGVPEERIHFE 230
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 216-429 4.99e-36

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: 132.19  E-value: 4.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 216 TAVERHGESLLEVTCRLQGDWSHRAGQFAFLTC--DRLEGAHPFTIASADRGCGEVRFSIKA--LGDYTRRLQdNLEVGA 291
Cdd:cd00322    1 VATEDVTDDVRLFRLQLPNGFSFKPGQYVDLHLpgDGRGLRRAYSIASSPDEEGELELTVKIvpGGPFSAWLH-DLKPGD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 292 RVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESLQAAPESAPsVELHYCVRNSQEALFAGRLRELCEHLPSVTL 371
Cdd:cd00322   80 EVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGE-ITLLYGARTPADLLFLDELEELAKEGPNFRL 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489192247 372 HIRYSDEQGKPQAAQLGVLKSAEGRW-------PSVWFCGPQGLADSLRRDLRRQGMPLRLFHQE 429
Cdd:cd00322  159 VLALSRESEAKLGPGGRIDREAEILAllpddsgALVYICGPPAMAKAVREALVSLGVPEERIHTE 223
FNR_iron_sulfur_binding_2 cd06216
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 207-431 1.75e-30

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99812 [Multi-domain]  Cd Length: 243  Bit Score: 117.71  E-value: 1.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 207 RTRRHAGVVTAVERHGESLLEVTCRLQGDW-SHRAGQFAFLTCDrLEGAH---PFTIASAD-RGCGEVRFSIKAL--GDY 279
Cdd:cd06216   14 SARELRARVVAVRPETADMVTLTLRPNRGWpGHRAGQHVRLGVE-IDGVRhwrSYSLSSSPtQEDGTITLTVKAQpdGLV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 280 TRRLQDNLEVGARVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESLQAAPESAPsVELHYCVRNSQEALFAGRL 359
Cdd:cd06216   93 SNWLVNHLAPGDVVELSQPQGDFVLPDPLPPRLLLIAAGSGITPVMSMLRTLLARGPTAD-VVLLYYARTREDVIFADEL 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489192247 360 RELCEHLPSVTLHIRYSDE--QGKPQAAQLGVLKSAEGRWPsVWFCGPQGLADSLRRDLRRQGMPLRLfHQEAF 431
Cdd:cd06216  172 RALAAQHPNLRLHLLYTREelDGRLSAAHLDAVVPDLADRQ-VYACGPPGFLDAAEELLEAAGLADRL-HTERF 243
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 218-431 1.61e-24

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: 100.46  E-value: 1.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 218 VERHGES-LLEVTCRLQGDWSHRAGQFAFLTCDRLEG---AHPFTIASA-DRGCGEVRFSIKAL-GDyTRRLQDNLEVGA 291
Cdd:cd06186    4 VELLPDSdVIRLTIPKPKPFKWKPGQHVYLNFPSLLSfwqSHPFTIASSpEDEQDTLSLIIRAKkGF-TTRLLRKALKSP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 292 ------RVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESL---QAAPESAPSVELHYCVRNSQEAL-FAGRLRE 361
Cdd:cd06186   83 gggvslKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLlrrSSKTSRTRRVKLVWVVRDREDLEwFLDELRA 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 362 LCEHLPSVTLHIRYSdeqgkpqaaqlgvlksaegrwpSVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06186  163 AQELEVDGEIEIYVT----------------------RVVVCGPPGLVDDVRNAVAKKGGTGVEFHEESF 210
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 215-427 4.53e-22

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 94.54  E-value: 4.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 215 VTAVERHGESLLEVTCRL-QGDWSHRAGQFAFLTCDRLEGAHPFTIASADRGCGEVRFSIKALGDYTRRLqDNLEVGARV 293
Cdd:COG0543    2 VVSVERLAPDVYLLRLEApLIALKFKPGQFVMLRVPGDGLRRPFSIASAPREDGTIELHIRVVGKGTRAL-AELKPGDEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 294 EVEGPYG-CFDFRRGlaGRQVW-VAAGIGVTPFIAWLESLQAAPesaPSVELHYCVRNSQEALFAGRLRELCEHLPSVTL 371
Cdd:COG0543   81 DVRGPLGnGFPLEDS--GRPVLlVAGGTGLAPLRSLAEALLARG---RRVTLYLGARTPEDLYLLDELEALADFRVVVTT 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489192247 372 HIRYSDEQGKPQAAQLGVLKSAEGRWpsVWFCGPQGLADSLRRDLRRQGMPLRLFH 427
Cdd:COG0543  156 DDGWYGRKGFVTDALKELLAEDSGDD--VYACGPPPMMKAVAELLLERGVPPERIY 209
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 228-431 3.66e-21

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 91.56  E-value: 3.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 228 VTCRLQG-DWS---HRAGQFAFLTCDRLEGAH---PFTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEVGARVEVEGP 298
Cdd:cd06217   17 KTFRLAVpDGVpppFLAGQHVDLRLTAIDGYTaqrSYSIASSPTQRGRVELTVKRVpgGEVSPYLHDEVKVGDLLEVRGP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 299 YGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESLQAApESAPSVELHYCVRNSQEALFAGRLRELCEHLPSVTLHIRYSDE 378
Cdd:cd06217   97 IGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDL-GWPVPFRLLYSARTAEDVIFRDELEQLARRHPNLHVTEALTRA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 379 QGKPQAAQLGVLKSA-------EGRWPSVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06217  176 APADWLGPAGRITADliaelvpPLAGRRVYVCGPPAFVEAATRLLLELGVPRDRIRTEAF 235
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 233-431 2.54e-20

Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR 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 methnae assimilation in a variety of 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: 99788 [Multi-domain]  Cd Length: 231  Bit Score: 89.12  E-value: 2.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 233 QGDWS-HRAGQFAFL--TCDRLEGAHPFTIASADRGcGEVRFSIKAL--GDYTRRLQDNLEVGARVEVEGPYGCFDFRRG 307
Cdd:cd06191   22 GPLQYgFRPGQHVTLklDFDGEELRRCYSLCSSPAP-DEISITVKRVpgGRVSNYLREHIQPGMTVEVMGPQGHFVYQPQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 308 LAGRQVWVAAGIGVTPFIAWLES-LQAAPESapSVELHYCVRNSQEALFAGRLRELCEHLPSVTLHIRYSDEQGK---PQ 383
Cdd:cd06191  101 PPGRYLLVAAGSGITPLMAMIRAtLQTAPES--DFTLIHSARTPADMIFAQELRELADKPQRLRLLCIFTRETLDsdlLH 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489192247 384 AAQLGVLKSAEGRWP-----SVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06191  179 GRIDGEQSLGAALIPdrlerEAFICGPAGMMDAVETALKELGMPPERIHTERF 231
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 270-431 7.79e-20

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: 88.38  E-value: 7.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 270 RFSIK--ALGDYTRRLQDNLEVGARVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESLqAAPESAPSVELHYCV 347
Cdd:cd06184   72 RISVKrePGGLVSNYLHDNVKVGDVLEVSAPAGDFVLDEASDRPLVLISAGVGITPMLSMLEAL-AAEGPGRPVTFIHAA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 348 RNSQEALFAGRLRELCEHLPSVTLHIRYSDeqgkPQAAQLGVLKSAEGR----W---------PSVWFCGPQGLADSLRR 414
Cdd:cd06184  151 RNSAVHAFRDELEELAARLPNLKLHVFYSE----PEAGDREEDYDHAGRidlaLlrelllpadADFYLCGPVPFMQAVRE 226

                        170
                 ....*....|....*..
gi 489192247 415 DLRRQGMPLRLFHQEAF 431
Cdd:cd06184  227 GLKALGVPAERIHYEVF 243
PDR_like cd06185
Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron ...
 281-431 9.71e-20

Phthalate dioxygenase reductase (PDR) is an FMN-dependent reductase that mediates electron transfer from NADH to FMN to an iron sulfur cluster. PDR has an an N-terminal ferrredoxin reductase (FNR)-like NAD(H) binding domain and a C-terminal iron-sulfur [2Fe-2S] cluster domain. Although structurally homologous to FNR, PDR binds FMN rather than FAD in it's FNR-like domain. Electron transfer between pyrimidines and iron-sulfur clusters (Rieske center [2Fe-2S]) or heme groups is mediated by flavins in respiration, photosynthesis, and oxygenase systems. Type I dioxygenase systems, including the hydroxylate phthalate system, have 2 components, a monomeric reductase consisting of a flavin and a 2Fe-2S center and a multimeric oxygenase. In contrast to other Rieske dioxygenases the ferredoxin like domain is C-, not N-terminal.


Pssm-ID: 99782 [Multi-domain]  Cd Length: 211  Bit Score: 87.15  E-value: 9.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 281 RRLQDNLEVGARVEVEGPYGCFDFRRGlAGRQVWVAAGIGVTPFIAWLESLQAAPEsapSVELHYCVRNSQEALFAGRLR 360
Cdd:cd06185   71 RYMHELLRVGDELEVSAPRNLFPLDEA-ARRHLLIAGGIGITPILSMARALAARGA---DFELHYAGRSREDAAFLDELA 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489192247 361 ELCEHlpsvTLHIRYSDEQGKPQAAQLgvLKSAEGRWpSVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06185  147 ALPGD----RVHLHFDDEGGRLDLAAL--LAAPPAGT-HVYVCGPEGMMDAVRAAAAALGWPEARLHFERF 210
FNR_iron_sulfur_binding_1 cd06215
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 239-431 2.82e-19

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal portion of the FAD/NAD binding domain contains most of the NADP(H) binding residues and the N-terminal sub-domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. In this ferredoxin like sub-group, the FAD/NAD sub-domains is typically fused to a C-terminal iron-sulfur binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins which act as electron carriers in photosynthesis and ferredoxins which participate in redox chains from bacteria to mammals. Ferredoxin reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99811 [Multi-domain]  Cd Length: 231  Bit Score: 86.10  E-value: 2.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 239 RAGQFAFLTCDRLEGAH--PFTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEVGARVEVEGPYGCFDFRRGLAGRQVW 314
Cdd:cd06215   29 KPGQFLTLELEIDGETVyrAYTLSSSPSRPDSLSITVKRVpgGLVSNWLHDNLKVGDELWASGPAGEFTLIDHPADKLLL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 315 VAAGIGVTPFIAWLESLqAAPESAPSVELHYCVRNSQEALFAGRLRELCEHLPSVTLHI--------RYSDEQGKPQAAQ 386
Cdd:cd06215  109 LSAGSGITPMMSMARWL-LDTRPDADIVFIHSARSPADIIFADELEELARRHPNFRLHLileqpapgAWGGYRGRLNAEL 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489192247 387 LGVLKS-AEGRWpsVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06215  188 LALLVPdLKERT--VFVCGPAGFMKAVKSLLAELGFPMSRFHQESF 231
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 215-431 3.33e-17

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons using oxygen as the oxidant. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate, while mono-oxygenases (aka mixed oxygenases) add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99784 [Multi-domain]  Cd Length: 224  Bit Score: 80.33  E-value: 3.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 215 VTAVERHGESLLEVTCRLQGDWSHRAGQFAFLTCDRLEG-AHPFTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEVGA 291
Cdd:cd06187    1 VVSVERLTHDIAVVRLQLDQPLPFWAGQYVNVTVPGRPRtWRAYSPANPPNEDGEIEFHVRAVpgGRVSNALHDELKVGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 292 RVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESLQAAPESAPsVELHYCVRNSQEALFAGRLRELCEHLPSVTL 371
Cdd:cd06187   81 RVRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDALRRGEPRP-VHLFFGARTERDLYDLEGLLALAARHPWLRV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489192247 372 HIRYSDEQGKPQAAQLGVLKSAEGRWPS-----VWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06187  160 VPVVSHEEGAWTGRRGLVTDVVGRDGPDwadhdIYICGPPAMVDATVDALLARGAPPERIHFDKF 224
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 226-431 2.71e-16

NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation oxidoreductase. PA oxidoreductases of E. coli hydroxylate PA-CoA in the second step of PA degradation. Members of this group typically fuse a ferredoxin reductase-like domain with an iron-sulfur binding cluster domain. Ferredoxins 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 portion may contain a flavin prosthetic group, as in flavoenzymes, or use flavin as a substrate. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria and participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99810 [Multi-domain]  Cd Length: 241  Bit Score: 77.97  E-value: 2.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 226 LEVTCRLQGDWSHRAGQFafLTCDRLEGAH----PFTIASAdRGCGEVRFSIKAL--GDYTRRLQDNLEVGARVEVEGPY 299
Cdd:cd06214   21 FDVPEELRDAFRYRPGQF--LTLRVPIDGEevrrSYSICSS-PGDDELRITVKRVpgGRFSNWANDELKAGDTLEVMPPA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 300 GCFDFRRGLAGRQ-VWVAAGIGVTPFIAWLESLQAApESAPSVELHYCVRNSQEALFAGRLRELC-EHLPSVTLHIRYSD 377
Cdd:cd06214   98 GRFTLPPLPGARHyVLFAAGSGITPVLSILKTALAR-EPASRVTLVYGNRTEASVIFREELADLKaRYPDRLTVIHVLSR 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489192247 378 EQGKPQ-------AAQLGVLKSAEGRWPSV--WF-CGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06214  177 EQGDPDllrgrldAAKLNALLKNLLDATEFdeAFlCGPEPMMDAVEAALLELGVPAERIHRELF 240
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 40-166 7.04e-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: 68.06  E-value: 7.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247   40 TGVASFALMSLIMLLAVRPVWLEKPLD-GLDRMYRLHKWAGILAIVlgllhylleLAGPWLAGIVGKPVKGPRVETFLDV 118
Cdd:pfam01794   1 LGILALALLPLLLLLALRNNPLEWLTGlSYDRLLLFHRWLGRLAFL---------LALLHVILYLIYWLRFSLEGILDLL 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489192247  119 FRGSAKELGEWSAWILGGMLLVTL--WQRFPYHLWRYVHKALALVYLVLA 166
Cdd:pfam01794  72 LKRPYNILGIIALVLLVLLAITSLppFRRLSYELFLYLHILLAVAFLLLV 121
oxygenase_e_transfer_subunit cd06213
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 212-431 8.02e-14

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. Electron transfer is from NADH via FAD (in the oxygenase reductase) and an [2FE-2S] ferredoxin center (fused to the FAD/NADH domain and/or discrete) to the oxygenase. Dioxygenases add both atoms of oxygen to the substrate while mono-oxygenases add one atom to the substrate and one atom to water. In dioxygenases, Class I enzymes are 2 component, containing a reductase with Rieske type [2Fe-2S] redox centers and an oxygenase. Class II are 3 component, having discrete flavin and ferredoxin proteins and an oxygenase. Class III have 2 [2Fe-2S] centers, one fused to the flavin domain and the other separate.


Pssm-ID: 99809  Cd Length: 227  Bit Score: 70.42  E-value: 8.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 212 AGVVTAVERHGESLLEVTCRLQGDWSHRAGQFAFLTCDRLEGAHPFTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEV 289
Cdd:cd06213    2 RGTIVAQERLTHDIVRLTVQLDRPIAYKAGQYAELTLPGLPAARSYSFANAPQGDGQLSFHIRKVpgGAFSGWLFGADRT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 290 GARVEVEGPYGCFDFRRGLAgRQVWVAAGIGVTPFIAWLESLQAAPESAPsVELHYCVRnSQEALFA------------G 357
Cdd:cd06213   82 GERLTVRGPFGDFWLRPGDA-PILCIAGGSGLAPILAILEQARAAGTKRD-VTLLFGAR-TQRDLYAldeiaaiaarwrG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 358 RLR--ELCEHLPS----------VTLHIRysdeQGKPQAAQlgvlksaegrwpsVWFCGPQGLADSLRRDLRRQGMPLRL 425
Cdd:cd06213  159 RFRfiPVLSEEPAdsswkgarglVTEHIA----EVLLAATE-------------AYLCGPPAMIDAAIAVLRALGIAREH 221


                 ....*.
gi 489192247 426 FHQEAF 431
Cdd:cd06213  222 IHADRF 227
T4MO_e_transfer_like cd06190
Toluene-4-monoxygenase electron transfer component of Pseudomonas mendocina hydroxylates ...
 215-422 3.71e-13

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: 68.43  E-value: 3.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 215 VTAVERHGESLLEVTCRLQGDWSHRAGQFAFLTCDRLEGAHPFTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEVGAR 292
Cdd:cd06190    1 LVDVRELTHDVAEFRFALDGPADFLPGQYALLALPGVEGARAYSMANLANASGEWEFIIKRKpgGAASNALFDNLEPGDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 293 VEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLE-SLQAAPESAPSVELHYCVRNSQEALFAGRLRELCEHLPSVTL 371
Cdd:cd06190   81 LELDGPYGLAYLRPDEDRDIVCIAGGSGLAPMLSILRgAARSPYLSDRPVDLFYGGRTPSDLCALDELSALVALGARLRV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489192247 372 HIRYSDEQGKPQAAQLG--------VLKSAEGRWPS--VWFCGPQGLADSLRRDLRRQGMP 422
Cdd:cd06190  161 TPAVSDAGSGSAAGWDGptgfvhevVEATLGDRLAEfeFYFAGPPPMVDAVQRMLMIEGVV 221
monooxygenase_like cd06212
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 240-431 3.79e-13

The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial oxygenases which oxidize hydrocarbons. These flavoprotein monooxygenases use molecular oxygen as a substrate and require reduced FAD. One atom of oxygen is incorportated into the aromatic compond, while the other is used to form a molecule of water. In contrast dioxygenases add both atoms of oxygen to the substrate.


Pssm-ID: 99808 [Multi-domain]  Cd Length: 232  Bit Score: 68.51  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 240 AGQFAFLTCDRLEGAHPFTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEVGARVEVEGPYGCFDFRRGLAGRQVWVAA 317
Cdd:cd06212   32 AGQYVDITVPGTEETRSFSMANTPADPGRLEFIIKKYpgGLFSSFLDDGLAVGDPVTVTGPYGTCTLRESRDRPIVLIGG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 318 GIGVTPFIAWLESLQAAPESAPsVELHYCVRNSQEALFAGRLRELCEHLPSVTLHIRYSDEQgkPQAA---QLGVLKSAE 394
Cdd:cd06212  112 GSGMAPLLSLLRDMAASGSDRP-VRFFYGARTARDLFYLEEIAALGEKIPDFTFIPALSESP--DDEGwsgETGLVTEVV 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489192247 395 GRWPS------VWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06212  189 QRNEAtlagcdVYLCGPPPMIDAALPVLEMSGVPPDQIFYDKF 231
MMO_FAD_NAD_binding cd06210
Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent ...
 240-431 4.65e-13

Methane monooxygenase (MMO) reductase of methanotrophs catalyzes the NADH-dependent hydroxylation of methane to methanol. This multicomponent enzyme mediates electron transfer via a hydroxylase (MMOH), a coupling protein, and a reductase which is comprised of an N-terminal [2Fe-2S] ferredoxin domain, an FAD binding subdomain, and an NADH binding subdomain. Oxygenases oxidize hydrocarbons using dioxygen as the oxidant. Dioxygenases add both atom of oxygen to the substrate, while mono-oxygenases add one atom to the substrate and one atom to water.


Pssm-ID: 99806  Cd Length: 236  Bit Score: 68.52  E-value: 4.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 240 AGQFAFLTCDRLEGAHPFTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEVGARVEVEGPYGCFDFR-RGLAGRqVWVA 316
Cdd:cd06210   37 PGQFVEIEIPGTDTRRSYSLANTPNWDGRLEFLIRLLpgGAFSTYLETRAKVGQRLNLRGPLGAFGLReNGLRPR-WFVA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 317 AGIGVTPFIAWLESLQAAPESAPSVeLHYCVRNSQEALFAGRLRELCEHLPSVTLHI-------RYSDEQGKPQAAQLGV 389
Cdd:cd06210  116 GGTGLAPLLSMLRRMAEWGEPQEAR-LFFGVNTEAELFYLDELKRLADSLPNLTVRIcvwrpggEWEGYRGTVVDALRED 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489192247 390 LKSAEGRwPSVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06210  195 LASSDAK-PDIYLCGPPGMVDAAFAAAREAGVPDEQVYLEKF 235
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 215-431 4.76e-13

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: 67.96  E-value: 4.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 215 VTAVERHGESLLEVTCRLQGDWSHRAGQFAFLTcdrLEGAH--PFTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEVG 290
Cdd:cd06189    3 VESIEPLNDDVYRVRLKPPAPLDFLAGQYLDLL---LDDGDkrPFSIASAPHEDGEIELHIRAVpgGSFSDYVFEELKEN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 291 ARVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESLQAAPESAPsVELHYCVRNsQEALFA-GRLRELCEHLPSV 369
Cdd:cd06189   80 GLVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGSKRP-IHLYWGART-EEDLYLdELLEAWAEAHPNF 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489192247 370 TLHIRYSDEQGKPQAAQLGVLKSAEGRWPS-----VWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06189  158 TYVPVLSEPEEGWQGRTGLVHEAVLEDFPDlsdfdVYACGSPEMVYAARDDFVEKGLPEENFFSDAF 224
PRK13289 PRK13289
NO-inducible flavohemoprotein;
270-431 1.04e-12

NO-inducible flavohemoprotein;


Pssm-ID: 237337 [Multi-domain]  Cd Length: 399  Bit Score: 69.06  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 270 RFSIK--ALGDYTRRLQDNLEVGARVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESLQAAPESAPSVELHYCv 347
Cdd:PRK13289 220 RISVKreAGGKVSNYLHDHVNVGDVLELAAPAGDFFLDVASDTPVVLISGGVGITPMLSMLETLAAQQPKRPVHFIHAA- 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 348 RNSQEALFAGRLRELCEHLPSVTLHIRYS------------DEQGKPQAAQL-GVLKSAEGrwpSVWFCGPQGLADSLRR 414
Cdd:PRK13289 299 RNGGVHAFRDEVEALAARHPNLKAHTWYRepteqdragedfDSEGLMDLEWLeAWLPDPDA---DFYFCGPVPFMQFVAK 375

                        170
                 ....*....|....*..
gi 489192247 415 DLRRQGMPLRLFHQEAF 431
Cdd:PRK13289 376 QLLELGVPEERIHYEFF 392
antC PRK11872
anthranilate 1,2-dioxygenase electron transfer component AntC;
206-428 2.56e-09

anthranilate 1,2-dioxygenase electron transfer component AntC;


Pssm-ID: 183350 [Multi-domain]  Cd Length: 340  Bit Score: 58.60  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 206 GRTRRHAGVVTAVERHGESllevTCRLQGDWSHRA-------GQFAFLTCDRLEGAHPFTIASADRGCGEVRFSIKAL-- 276
Cdd:PRK11872 102 GDTLKISGVVTAVELVSET----TAILHLDASAHGrqldflpGQYARLQIPGTDDWRSYSFANRPNATNQLQFLIRLLpd 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 277 GDYTRRLQDNLEVGARVEVEGPYGCFDFR---RGLagrqVWVAAGIGVTPFIAWLESLQAAPeSAPSVELHYCVRNSQEA 353
Cdd:PRK11872 178 GVMSNYLRERCQVGDEILFEAPLGAFYLReveRPL----VFVAGGTGLSAFLGMLDELAEQG-CSPPVHLYYGVRHAADL 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 354 LFAGRLRELCEHLPSVTLHIRYSDE----QGK----PQAAQLGVLKSAEGrwpSVWFCGPQGLADSLRRDLRRQGMP-LR 424
Cdd:PRK11872 253 CELQRLAAYAERLPNFRYHPVVSKAsadwQGKrgyiHEHFDKAQLRDQAF---DMYLCGPPPMVEAVKQWLDEQALEnYR 329


                 ....
gi 489192247 425 LFHQ 428
Cdd:PRK11872 330 LYYE 333
FNR_like_2 cd06197
FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) ...
 257-417 5.67e-09

FAD/NAD(P) binding domain of ferredoxin reductase-like proteins. Ferredoxin reductase (FNR) 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 have a variety of physiological functions in a variety of organisms including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which varies 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 two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99794  Cd Length: 220  Bit Score: 56.25  E-value: 5.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 257 FTIASA---DRGCGEVRFSIKALGDYTRRLQDNLE--VGARVEVE-----GPYGCFDFRRGLAGRQVWVAAGIGVTPFIA 326
Cdd:cd06197   63 FTVSSApphDPATDEFEITVRKKGPVTGFLFQVARrlREQGLEVPvlgvgGEFTLSLPGEGAERKMVWIAGGVGITPFLA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 327 WLESLQAAPESAPSVELhycvrnsqeaLFAGRLRElcehLPSVTLHIRYSdeQGKPQAAQLGVLKsaegrwpSVWFCGPQ 406
Cdd:cd06197  143 MLRAILSSRNTTWDITL----------LWSLREDD----LPLVMDTLVRF--PGLPVSTTLFITS-------EVYLCGPP 199

                        170
                 ....*....|.
gi 489192247 407 GLADSLRRDLR 417
Cdd:cd06197  200 ALEKAVLEWLE 210
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 235-364 1.21e-08

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: 55.33  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 235 DWSHRA--GQFAFLTcDRLEGAHPFTIASADrgcGEVRFSIKALGDYTRRLQDnLEVGARVEVEGPYG-CFDFRrglAGR 311
Cdd:cd06220   19 DWDFDFkpGQFVMVW-VPGVDEIPMSLSYID---GPNSITVKKVGEATSALHD-LKEGDKLGIRGPYGnGFELV---GGK 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489192247 312 QVWVAAGIGVTPFIAWLESLQAAPEsapsVELHYCVRNSQEALFAGRLRELCE 364
Cdd:cd06220   91 VLLIGGGIGIAPLAPLAERLKKAAD----VTVLLGARTKEELLFLDRLRKSDE 139
FAD_binding_8 pfam08022
FAD-binding domain;
222-300 2.57e-08

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 51.57  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247  222 GESLLEVTC-RLQGDWSHRAGQFAFLTCDR----LEgAHPFTIASAdRGCGEVRFSIKALGDYTRRLQ-----------D 285
Cdd:pfam08022  13 PDNVLKLRVsKPKKPFKYKPGQYMFINFLPplsfLQ-SHPFTITSA-PSDDKLSLHIKVKGGWTRKLAnylssscpkspE 90

                          90
                  ....*....|....*
gi 489192247  286 NLEVGARVEVEGPYG 300
Cdd:pfam08022  91 NGKDKPRVLIEGPYG 105
sulfite_reductase_like cd06221
Anaerobic sulfite reductase contains an FAD and NADPH binding module with structural ...
 226-362 2.61e-08

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: 54.54  E-value: 2.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 226 LEVTCRLQGDWSHRAGQFAFLTCdrlegahpftiasadRGCGEVRFS--------------IKALGDYTRRLQDnLEVGA 291
Cdd:cd06221   16 LRLEDDDEELFTFKPGQFVMLSL---------------PGVGEAPISissdptrrgpleltIRRVGRVTEALHE-LKPGD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489192247 292 RVEVEGPYGC-FDFRRgLAGRQV-WVAAGIGVTPFIAWLESLQAAPESAPSVELHYCVRNSQEALFAGRLREL 362
Cdd:cd06221   80 TVGLRGPFGNgFPVEE-MKGKDLlLVAGGLGLAPLRSLINYILDNREDYGKVTLLYGARTPEDLLFKEELKEW 151
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 267-408 1.39e-07

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: 52.18  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 267 GEVRFSIKAL--GDYTRRLqDNLEVGARVEVEGPYGCFDFRRGLAGRQV-WVAAGIGVTPFIAWLESLQAAPESAPSVEL 343
Cdd:cd06183   60 GYFDLLIKIYpgGKMSQYL-HSLKPGDTVEIRGPFGKFEYKPNGKVKHIgMIAGGTGITPMLQLIRAILKDPEDKTKISL 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489192247 344 HYCVRNSQEALFAGRLRELCEHLP---SVTLHIrysDEQGKPQAAQLG-----VLKSAEGRWPS----VWFCGPQGL 408
Cdd:cd06183  139 LYANRTEEDILLREELDELAKKHPdrfKVHYVL---SRPPEGWKGGVGfitkeMIKEHLPPPPSedtlVLVCGPPPM 212
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 215-431 1.48e-07

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an N-terminal Iron-Sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 51.89  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 215 VTAVERHGESLLEVTCRLQGDWSHRAGQFAFLTcdRLEG-AHPFTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEVGA 291
Cdd:cd06194    1 VVSLQRLSPDVLRVRLEPDRPLPYLPGQYVNLR--RAGGlARSYSPTSLPDGDNELEFHIRRKpnGAFSGWLGEEARPGH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 292 RVEVEGPYG-CFDFRRGLAGRQVWVAAGIGVTPFIAwleSLQAAPESAPSVELHYCV--RNSQEALFAGRLRELCEHLPS 368
Cdd:cd06194   79 ALRLQGPFGqAFYRPEYGEGPLLLVGAGTGLAPLWG---IARAALRQGHQGEIRLVHgaRDPDDLYLHPALLWLAREHPN 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489192247 369 VTLHIRYSDEQGKPQAAQLGVLKSAEGRWPS---VWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06194  156 FRYIPCVSEGSQGDPRVRAGRIAAHLPPLTRddvVYLCGAPSMVNAVRRRAFLAGAPMKRIYADPF 221
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 239-431 7.72e-07

Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use molecular oxygen as a substrate in the microbial degredation of phenol. This protein is encoded by a single gene and uses a tightly bound FAD cofactor in the NAD(P)H dependent conversion of phenol and O2 to catechol and H2O. This group is related to the NAD binding ferredoxin reductases.


Pssm-ID: 99807  Cd Length: 238  Bit Score: 50.02  E-value: 7.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 239 RAGQFAFLTCDRLEGAHPFTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEVGARVEVEGPYGCFDFRRGLAGRQVWVA 316
Cdd:cd06211   37 QAGQYVNLQAPGYEGTRAFSIASSPSDAGEIELHIRLVpgGIATTYVHKQLKEGDELEISGPYGDFFVRDSDQRPIIFIA 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 317 AGIGVTPFIAWLESLQAAPESAPsVELHYCVRNSQEALFAGRLRELCEHLPSVTLHIRYSDEQGKPQAA--------QLG 388
Cdd:cd06211  117 GGSGLSSPRSMILDLLERGDTRK-ITLFFGARTRAELYYLDEFEALEKDHPNFKYVPALSREPPESNWKgftgfvhdAAK 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 489192247 389 VLKSAEGRWPSVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:cd06211  196 KHFKNDFRGHKAYLCGPPPMIDACIKTLMQGRLFERDIYYEKF 238
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 214-367 2.04e-06

Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 48.72  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 214 VVTAVERHGESLLEVTCRLQGDWSHRAGQFA--FLTCDrlEG---AHPFTIASA--DRgcgEVRFSIKAL--GDYTRRLQ 284
Cdd:cd06195    1 TVLKRRDWTDDLFSFRVTRDIPFRFQAGQFTklGLPND--DGklvRRAYSIASApyEE---NLEFYIILVpdGPLTPRLF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 285 dNLEVGARVEVE-GPYGCFDFRRGLAGRQVW-VAAGIGVTPFIAWLESlqaaPESAP---SVELHYCVRNSQEALFAGRL 359
Cdd:cd06195   76 -KLKPGDTIYVGkKPTGFLTLDEVPPGKRLWlLATGTGIAPFLSMLRD----LEIWErfdKIVLVHGVRYAEELAYQDEI 150


                 ....*...
gi 489192247 360 RELCEHLP 367
Cdd:cd06195  151 EALAKQYN 158
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 236-432 4.76e-06

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 48.17  E-value: 4.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 236 WSHRAGQFAFLTCDRL-EGAHPFTIASADrgcGEVRF---SIKAL--GDYTRRLQDNLEVGARVEVEGPYGCFDFRRGLA 309
Cdd:PRK10684  35 YPYRAGQYALVSIRNSaETLRAYTLSSTP---GVSEFitlTVRRIddGVGSQWLTRDVKRGDYLWLSDAMGEFTCDDKAE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 310 GRQVWVAAGIGVTPFIA---WLesLQAAPESapSVELHYCVRNSQEALFAGRLRELCEHLPSVTLHIRYSdeqgkpQAAQ 386
Cdd:PRK10684 112 DKYLLLAAGCGVTPIMSmrrWL--LKNRPQA--DVQVIFNVRTPQDVIFADEWRQLKQRYPQLNLTLVAE------NNAT 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489192247 387 LGVLK---SAE---GRWP-----SVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAFR 432
Cdd:PRK10684 182 EGFIAgrlTREllqQAVPdlasrTVMTCGPAPYMDWVEQEVKALGVTADRFFKEKFF 238
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 250-333 1.70e-05

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 varies in orientation with respect to the NAD(P) binding domain. The N-terminal region 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: 99793 [Multi-domain]  Cd Length: 218  Bit Score: 45.69  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 250 RLEGaHPFTIAS--ADRgcgEVRFSIKALGDY---TRRLqDNLEVGARVEVEGPYGCFDFRrglaGRQVWVAAGIGVTPF 324
Cdd:cd06196   44 RDEK-RPFTFTSlpEDD---VLEFVIKSYPDHdgvTEQL-GRLQPGDTLLIEDPWGAIEYK----GPGVFIAGGAGITPF 114


                 ....*....
gi 489192247 325 IAWLESLQA 333
Cdd:cd06196  115 IAILRDLAA 123
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 255-352 4.11e-05

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 45.99  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 255 HPFTIASA----DRGCGEVrfsIKALGDYTRRLQDNLEVGAR----------VEVEGPYG--CFDFRRglAGRQVWVAAG 318
Cdd:PLN02844 358 HPFSITSSsnidDHTMSVI---IKCEGGWTNSLYNKIQAELDsetnqmncipVAIEGPYGpaSVDFLR--YDSLLLVAGG 432

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489192247 319 IGVTPFIAWLESLQAAPES----APSVELHYCVRNSQE 352
Cdd:PLN02844 433 IGITPFLSILKEIASQSSSryrfPKRVQLIYVVKKSQD 470
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 237-366 5.09e-05

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 45.70  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247  237 SHRAGQFAFLtcdRL-EGAH--PFTIASADRGCGEVRFSIKALGDYTRRLQDNLEVG-ARVEVEGPYGcFDFRRGLAGRQ 312
Cdd:PRK12775   27 SAEPGHFVML---RLyEGAEriPLTVADFDRKKGTITMVVQALGKTTREMMTKFKAGdTFEDFVGPLG-LPQHIDKAGHV 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489192247  313 VWVAAGIGVTPFIAWLESLQAAPESAPSVelhYCVRNSQEALFAGRLRELCEHL 366
Cdd:PRK12775  103 VLVGGGLGVAPVYPQLRAFKEAGARTTGI---IGFRNKDLVFWEDKFGKYCDDL 153
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 215-323 1.29e-04

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: 43.47  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 215 VTAVERHGESLLEVTCR-LQGDWSHRAGQFAFLTC---DRLEGAhPFTIASADRGCGEVRFSIKALGDYTRRLQdNLEVG 290
Cdd:cd06192    1 IVKKEQLEPNLVLLTIKaPLAARLFRPGQFVFLRNfesPGLERI-PLSLAGVDPEEGTISLLVEIRGPKTKLIA-ELKPG 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 489192247 291 ARVEVEGPYGcfdfrRGLAGRQ-----VWVAAGIGVTP 323
Cdd:cd06192   79 EKLDVMGPLG-----NGFEGPKkggtvLLVAGGIGLAP 111
NADH_quinone_reductase cd06188
Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) ...
 286-379 9.28e-04

Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) FAD/NADH binding domain. (Na+-NQR) provides a means of storing redox reaction energy via the transmembrane translocation of Na2+ ions. The C-terminal domain resembles ferredoxin:NADP+ oxidoreductase, and has NADH and FAD binding sites. (Na+-NQR) is distinct from H+-translocating NADH:quinone oxidoreductases and noncoupled NADH:quinone oxidoreductases. The 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 of this group typically contains an iron-sulfur cluster binding domain.


Pssm-ID: 99785 [Multi-domain]  Cd Length: 283  Bit Score: 40.75  E-value: 9.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 286 NLEVGARVEVEGPYGCFdFRRGLAGRQVWVAAGIGVTPFIAWLESLQAAPESAPSVELHYCVRNSQEALFAGRLRELCEH 365
Cdd:cd06188  128 NLKPGDKVTASGPFGEF-FIKDTDREMVFIGGGAGMAPLRSHIFHLLKTLKSKRKISFWYGARSLKELFYQEEFEALEKE 206

                         90
                 ....*....|....
gi 489192247 366 LPSVTLHIRYSDEQ 379
Cdd:cd06188  207 FPNFKYHPVLSEPQ 220
PLN02292 PLN02292
ferric-chelate reductase
 255-331 1.25e-03

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 41.01  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 255 HPFTIASADRGCGE-VRFSIKALGDYTRRLQDNLEVGAR-----VEVEGPYG--CFDFRRGLAgrQVWVAAGIGVTPFIA 326
Cdd:PLN02292 371 HPFTITSSSKLEPEkLSVMIKSQGKWSTKLYHMLSSSDQidrlaVSVEGPYGpaSTDFLRHES--LVMVSGGSGITPFIS 448


                 ....*
gi 489192247 327 WLESL 331
Cdd:PLN02292 449 IIRDL 453
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 315-414 1.87e-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: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247  315 VAAGIGVTPFIAWLESLQAAPESAPSVELHYCVRNSQEALFAGRLRELCEHLPSvTLHIRY--SDEQGKPQAA----QLG 388
Cdd:pfam00175   2 IAGGTGIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDELAEKHPG-RLTVVYvvSRPEAGWTGGkgrvQDA 80

                          90       100
                  ....*....|....*....|....*....
gi 489192247  389 VLKSAEGRWPS---VWFCGPQGLADSLRR 414
Cdd:pfam00175  81 LLEDHLSLPDEethVYVCGPPGMIKAVRK 109
PLN02631 PLN02631
ferric-chelate reductase
 255-343 2.84e-03

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 40.03  E-value: 2.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 255 HPFTI-ASADRGCGEVRFSIKALGDYTRRLQDNLEVGA---RVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLES 330
Cdd:PLN02631 354 HPFTItSSSNLEKDTLSVVIRRQGSWTQKLYTHLSSSIdslEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRE 433

                         90
                 ....*....|...
gi 489192247 331 LQAAPESaPSVEL 343
Cdd:PLN02631 434 LIFQSQN-PSTKL 445
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
240-302 7.17e-03

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 36.02  E-value: 7.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489192247  240 AGQ--FAFLTCDRLEGAHPFTIASADRGCGEVRFSIKAL--GDYTRRLqDNLEVGARVEVEGPYGCF 302
Cdd:pfam00970  32 VGQhlFLRLPIDGELVIRSYTPISSDDDKGYLELLVKVYpgGKMSQYL-DELKIGDTIDFKGPLGRF 97
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 257-431 7.96e-03

CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 38.31  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 257 FTIASADRGCGEVRFSIKAL--GDYTRRLQDNLEVGARVEVEGPYGCFDFRRGLAGRQVWVAAGIGVTPFIAWLESLQAA 334
Cdd:PRK07609 150 YSIANAPHSGGPLELHIRHMpgGVFTDHVFGALKERDILRIEGPLGTFFLREDSDKPIVLLASGTGFAPIKSIVEHLRAK 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489192247 335 PESAPsVELHYCVRNSQEaLFagrLRELCE----HLPSVTLHIRYSDEQGKP----------QA--AQLGVLKSAEgrwp 398
Cdd:PRK07609 230 GIQRP-VTLYWGARRPED-LY---LSALAEqwaeELPNFRYVPVVSDALDDDawtgrtgfvhQAvlEDFPDLSGHQ---- 300

                        170       180       190
                 ....*....|....*....|....*....|...
gi 489192247 399 sVWFCGPQGLADSLRRDLRRQGMPLRLFHQEAF 431
Cdd:PRK07609 301 -VYACGSPVMVYAARDDFVAAGLPAEEFFADAF 332
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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