|
Name |
Accession |
Description |
Interval |
E-value |
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
736-903 |
1.50e-55 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 188.70 E-value: 1.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 736 YDVVLLVGLGIGATPMISILKDIINNMKGpdrdsdiennnsnnnskgFKTRKAYFYWVTREQGSFEWFKGIMDEISELDE 815
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKK------------------LKTKKIKFYWVVRDLSSLEWFKDVLNELEELKE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 816 EgIIELHNYCTSVYEEGDARVALI-----AMLQSLQHAKNGVDVVsgtrvKSHFAKPNWRQVYKKIAVQHPGKRIGVFYC 890
Cdd:pfam08030 63 L-NIEIHIYLTGEYEAEDASDQSDssirsENFDSLMNEVIGVDFV-----EFHFGRPNWKEVLKDIAKQHPNGSIGVFSC 136
|
170
....*....|...
gi 15238842 891 GMPGMIKELKNLA 903
Cdd:pfam08030 137 GPPSLVDELRNLV 149
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
619-921 |
1.68e-51 |
|
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: 179.81 E-value: 1.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 619 IKVAVYP-GNVLSLHMTKPQGFKYKSGQFMLVNCRAV-SPFEWHPFSITSAPGD--DYLSVHIRTL-GDWTRKLRtvfse 693
Cdd:cd06186 2 ATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 694 vckpptagksgllRADGGDGNLPFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISILKDIINNMKgpdrdsdien 773
Cdd:cd06186 77 -------------KALKSPGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSS---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 774 nnsnnnsKGFKTRKAYFYWVTREQGSFEWFKGIMDEISELDEEGIIELhnYCTsvyeegdarvaliamlqslqhakngvd 853
Cdd:cd06186 134 -------KTSRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEIEI--YVT--------------------------- 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15238842 854 vvsgtrvkshfakpnwrqvykkiavqhpgkriGVFYCGMPGMIKELKNLAldfSRKTTTKFDFHKENF 921
Cdd:cd06186 178 --------------------------------RVVVCGPPGLVDDVRNAV---AKKGGTGVEFHEESF 210
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
613-730 |
1.80e-45 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 158.65 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 613 IKPVKMIKVAVYPGNVLSLHMTKPQG-FKYKSGQFMLVNC-RAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRKLRTV 690
Cdd:pfam08022 1 IFGVPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANY 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15238842 691 FSEVCKpptagksgllraDGGDGNLPFPKVLIDGPYGAPA 730
Cdd:pfam08022 81 LSSSCP------------KSPENGKDKPRVLIEGPYGPPS 108
|
|
| NADPH_Ox |
pfam08414 |
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ... |
158-256 |
7.82e-45 |
|
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory burst NADPH oxidase proteins which produce reactive oxygen species as a defence mechanism. It tends to occur to the N-terminus of an EF-hand (pfam00036), which suggests a direct regulatory effect of Ca2+ on the activity of the NADPH oxidase in plants.
Pssm-ID: 462469 Cd Length: 100 Bit Score: 156.59 E-value: 7.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 158 FDRTSSAAIHALKGLKFIATKT----AAWPAVDQRFDKLSADsnGLLLSAKFWECLGMnKESKDFADQLFRALARRNNVS 233
Cdd:pfam08414 1 LDRTKSGAARALKGLRFISKTDggegAGWKAVEKRFDKLAVD--GLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77
|
90 100
....*....|....*....|...
gi 15238842 234 GDAITKEQLRIFWEQISDESFDA 256
Cdd:pfam08414 78 GDSITKEELKEFWEQISDQSFDS 100
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
453-921 |
1.99e-26 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 113.45 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 453 DDSLNFHKVIASGIVVGVLLHAGAHLtcdFPRLIAADEDTYEPMEKYFgdQPTSYWWFVKGVegWTGIVMVVLMAIAFtl 532
Cdd:COG4097 75 DRLYRLHKWLGILALVLALAHPLLLL---GPKWLVGWGGLPARLAALL--TLLRGLAELLGE--WAFYLLLALVVLSL-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 533 atpwFRRNklnLPnflkkltgFNAFWYTHHLFIIVYALLIVHGI---KLYLTKIWYQKTTWMYLAVPILLYASERLLRAF 609
Cdd:COG4097 146 ----LRRR---LP--------YELWRLTHRLLAVAYLLLAFHHLllgGPFYWSPPAGVLWAALAAAGLAAAVYSRLGRPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 610 RSSIKPVKMIKVAVYPGNVLSLHMTKPQG--FKYKSGQFMLVNC-RAVSPFEWHPFSITSAP-GDDYLSVHIRTLGDWTR 685
Cdd:COG4097 211 RSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFdGSPFWEEAHPFSISSAPgGDGRLRFTIKALGDFTR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 686 KLRTVfsevcKPptagksgllradgGDgnlpfpKVLIDGPYGA-PAQDYKKYDVVLLVGLGIGATPMISILKDIinnmkg 764
Cdd:COG4097 291 RLGRL-----KP-------------GT------RVYVEGPYGRfTFDRRDTAPRQVWIAGGIGITPFLALLRAL------ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 765 PDRDSDiennnsnnnskgfkTRKAYFYWVTREQGSFEwFKgimDEISEL-DEEGIIELHNYCTSvyEEGdarvaliamlq 843
Cdd:COG4097 341 AARPGD--------------QRPVDLFYCVRDEEDAP-FL---EELRALaARLAGLRLHLVVSD--EDG----------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 844 slqhakngvdVVSGTRVKSHFakPNWRQVYkkiavqhpgkrigVFYCGMPGMIKELKN--LALDFSRKtttkfDFHKENF 921
Cdd:COG4097 390 ----------RLTAERLRRLV--PDLAEAD-------------VFFCGPPGMMDALRRdlRALGVPAR-----RIHQERF 439
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
425-758 |
1.22e-24 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 110.32 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 425 MALILLPVCRN-TITWLRNktklgtvVPFDDSLNFHKVIASGIVVGVLLHAGAHLTcdfprLIAADEDTYEPMEKYfgdQ 503
Cdd:PLN02844 167 LALLLLPVLRGlALFRLLG-------IQFEASVRYHVWLGTSMIFFATVHGASTLF-----IWGISHHIQDEIWKW---Q 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 504 PTSYWWFVKGVEGWTGIVMVVLmaiaftlATPWFRRNKlnlpnflkkltgFNAFWYTHHLFIIVYALLIVHGIKLYLtki 583
Cdd:PLN02844 232 KTGRIYLAGEIALVTGLVIWIT-------SLPQIRRKR------------FEIFYYTHHLYIVFLIFFLFHAGDRHF--- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 584 wyqkttwmYLAVP-ILLYASERLLRAFRSsiKPVKMIKVA-VYPGNVLSLHMTKPQGFKYKSGQFMLVNCRAVSPFEWHP 661
Cdd:PLN02844 290 --------YMVFPgIFLFGLDKLLRIVQS--RPETCILSArLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHP 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 662 FSITSAPG--DDYLSVHIRTLGDWTRKLRTVFSEvckpptagksgllRADGGDGNLPFPKVLIDGPYGAPAQDYKKYDVV 739
Cdd:PLN02844 360 FSITSSSNidDHTMSVIIKCEGGWTNSLYNKIQA-------------ELDSETNQMNCIPVAIEGPYGPASVDFLRYDSL 426
|
330
....*....|....*....
gi 15238842 740 LLVGLGIGATPMISILKDI 758
Cdd:PLN02844 427 LLVAGGIGITPFLSILKEI 445
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
506-765 |
5.53e-21 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 98.58 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 506 SYWWFVKGVEGWTGIVMVVLMAIAFTLATPWFRRNKlnlpnflkkltgFNAFWYTHHLFIIVYALLIVHgiklyltkiwy 585
Cdd:PLN02631 223 TFAWNPTYVPNLAGTIAMVIGIAMWVTSLPSFRRKK------------FELFFYTHHLYGLYIVFYVIH----------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 586 QKTTWMYLAVP-ILLYASERLLRaFRSSIKPVKMIKVAVYPGNVLSLHMTKPQGFKYKSGQFMLVNCRAVSPFEWHPFSI 664
Cdd:PLN02631 280 VGDSWFCMILPnIFLFFIDRYLR-FLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTI 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 665 TSAPG--DDYLSVHIRTLGDWTRKLRTVFSEvckpptagksgllradggdgNLPFPKVLIDGPYGAPAQDYKKYDVVLLV 742
Cdd:PLN02631 359 TSSSNleKDTLSVVIRRQGSWTQKLYTHLSS--------------------SIDSLEVSTEGPYGPNSFDVSRHNSLILV 418
|
250 260
....*....|....*....|...
gi 15238842 743 GLGIGATPMISILKDIINNMKGP 765
Cdd:PLN02631 419 SGGSGITPFISVIRELIFQSQNP 441
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
625-921 |
7.46e-18 |
|
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: 83.08 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 625 PGNVLSLHMTKPQ-GFKYKSGQFMLVNCRAVSPFEWHPFSITSAPGDDY-LSVHIRTLGDWTRKLRTvfsevckpptagk 702
Cdd:cd06198 6 VRPTTTLTLEPRGpALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALGDYTRRLAE------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 703 sgLLRAdgGDgnlpfpKVLIDGPYGAPAQDYKKYDVVLLVGlGIGATPMISILKDiinnmkGPDRDSDiennnsnnnskg 782
Cdd:cd06198 73 --RLKP--GT------RVTVEGPYGRFTFDDRRARQIWIAG-GIGITPFLALLEA------LAARGDA------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 783 fktRKAYFYWVTREQGSFeWFkgiMDEISELDEEGIIELHnyctsVYEEGDARVALIAMLQSLQHakngvdvvsgtrvks 862
Cdd:cd06198 124 ---RPVTLFYCVRDPEDA-VF---LDELRALAAAAGVVLH-----VIDSPSDGRLTLEQLVRALV--------------- 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15238842 863 hfakPNWRQVykkiavqhpgkriGVFYCGMPGMIKELKNlalDFSRKTTTKFDFHKENF 921
Cdd:cd06198 177 ----PDLADA-------------DVWFCGPPGMADALEK---GLRALGVPARRFHYERF 215
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
424-572 |
1.37e-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: 71.15 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 424 NMALILLPVCRNT-ITWLRNktklgtvVPFDDSLNFHKVIASGIVVGVLLHAGAHLTCDFPRliaadedtyepmekyfgD 502
Cdd:pfam01794 8 LLPLLLLLALRNNpLEWLTG-------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF-----------------S 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 503 QPTSYWWFVKGVEGWTGIVMVVLMAIAFTLATPWFRRNklnlpnflkkltGFNAFWYTHHLFIIVYALLI 572
Cdd:pfam01794 64 LEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHILLAVAFLLLV 121
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
185-317 |
9.36e-09 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 54.80 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 185 VDQRFDKLSADSNGLLLSAKFweclgmnkesKDFADQLFRALARRNNVSGD-AITKEQLRIFWEQISDESFDAKLQVFFD 263
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDF----------EALFRRLWATLFSEADTDGDgRISREEFVAGMESLFEATVEPFARAAFD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15238842 264 MVDKDEDGRVTEEEVAEIIslsaSANKLSNIQkqakeyAALIMEELDPDNAGFI 317
Cdd:COG5126 77 LLDTDGDGKISADEFRRLL----TALGVSEEE------ADELFARLDTDGDGKI 120
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
237-283 |
8.43e-06 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 44.08 E-value: 8.43e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15238842 237 ITKEQLRIFWEQISDESFDAKLQVFFDMVDKDEDGRVTEEEVAEIIS 283
Cdd:cd00051 17 ISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
255-317 |
1.68e-04 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 40.70 E-value: 1.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15238842 255 DAKLQVFFDMVDKDEDGRVTEEEVAEIISLSASANKLSniqkqaKEYAALIMEELDPDNAGFI 317
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLS------DEEVEELFKEFDLDKDGRI 57
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
736-903 |
1.50e-55 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 188.70 E-value: 1.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 736 YDVVLLVGLGIGATPMISILKDIINNMKGpdrdsdiennnsnnnskgFKTRKAYFYWVTREQGSFEWFKGIMDEISELDE 815
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKK------------------LKTKKIKFYWVVRDLSSLEWFKDVLNELEELKE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 816 EgIIELHNYCTSVYEEGDARVALI-----AMLQSLQHAKNGVDVVsgtrvKSHFAKPNWRQVYKKIAVQHPGKRIGVFYC 890
Cdd:pfam08030 63 L-NIEIHIYLTGEYEAEDASDQSDssirsENFDSLMNEVIGVDFV-----EFHFGRPNWKEVLKDIAKQHPNGSIGVFSC 136
|
170
....*....|...
gi 15238842 891 GMPGMIKELKNLA 903
Cdd:pfam08030 137 GPPSLVDELRNLV 149
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
619-921 |
1.68e-51 |
|
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: 179.81 E-value: 1.68e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 619 IKVAVYP-GNVLSLHMTKPQGFKYKSGQFMLVNCRAV-SPFEWHPFSITSAPGD--DYLSVHIRTL-GDWTRKLRtvfse 693
Cdd:cd06186 2 ATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLR----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 694 vckpptagksgllRADGGDGNLPFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISILKDIINNMKgpdrdsdien 773
Cdd:cd06186 77 -------------KALKSPGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSS---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 774 nnsnnnsKGFKTRKAYFYWVTREQGSFEWFKGIMDEISELDEEGIIELhnYCTsvyeegdarvaliamlqslqhakngvd 853
Cdd:cd06186 134 -------KTSRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEIEI--YVT--------------------------- 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15238842 854 vvsgtrvkshfakpnwrqvykkiavqhpgkriGVFYCGMPGMIKELKNLAldfSRKTTTKFDFHKENF 921
Cdd:cd06186 178 --------------------------------RVVVCGPPGLVDDVRNAV---AKKGGTGVEFHEESF 210
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
613-730 |
1.80e-45 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 158.65 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 613 IKPVKMIKVAVYPGNVLSLHMTKPQG-FKYKSGQFMLVNC-RAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRKLRTV 690
Cdd:pfam08022 1 IFGVPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANY 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15238842 691 FSEVCKpptagksgllraDGGDGNLPFPKVLIDGPYGAPA 730
Cdd:pfam08022 81 LSSSCP------------KSPENGKDKPRVLIEGPYGPPS 108
|
|
| NADPH_Ox |
pfam08414 |
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ... |
158-256 |
7.82e-45 |
|
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory burst NADPH oxidase proteins which produce reactive oxygen species as a defence mechanism. It tends to occur to the N-terminus of an EF-hand (pfam00036), which suggests a direct regulatory effect of Ca2+ on the activity of the NADPH oxidase in plants.
Pssm-ID: 462469 Cd Length: 100 Bit Score: 156.59 E-value: 7.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 158 FDRTSSAAIHALKGLKFIATKT----AAWPAVDQRFDKLSADsnGLLLSAKFWECLGMnKESKDFADQLFRALARRNNVS 233
Cdd:pfam08414 1 LDRTKSGAARALKGLRFISKTDggegAGWKAVEKRFDKLAVD--GLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77
|
90 100
....*....|....*....|...
gi 15238842 234 GDAITKEQLRIFWEQISDESFDA 256
Cdd:pfam08414 78 GDSITKEELKEFWEQISDQSFDS 100
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
453-921 |
1.99e-26 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 113.45 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 453 DDSLNFHKVIASGIVVGVLLHAGAHLtcdFPRLIAADEDTYEPMEKYFgdQPTSYWWFVKGVegWTGIVMVVLMAIAFtl 532
Cdd:COG4097 75 DRLYRLHKWLGILALVLALAHPLLLL---GPKWLVGWGGLPARLAALL--TLLRGLAELLGE--WAFYLLLALVVLSL-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 533 atpwFRRNklnLPnflkkltgFNAFWYTHHLFIIVYALLIVHGI---KLYLTKIWYQKTTWMYLAVPILLYASERLLRAF 609
Cdd:COG4097 146 ----LRRR---LP--------YELWRLTHRLLAVAYLLLAFHHLllgGPFYWSPPAGVLWAALAAAGLAAAVYSRLGRPL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 610 RSSIKPVKMIKVAVYPGNVLSLHMTKPQG--FKYKSGQFMLVNC-RAVSPFEWHPFSITSAP-GDDYLSVHIRTLGDWTR 685
Cdd:COG4097 211 RSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFdGSPFWEEAHPFSISSAPgGDGRLRFTIKALGDFTR 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 686 KLRTVfsevcKPptagksgllradgGDgnlpfpKVLIDGPYGA-PAQDYKKYDVVLLVGLGIGATPMISILKDIinnmkg 764
Cdd:COG4097 291 RLGRL-----KP-------------GT------RVYVEGPYGRfTFDRRDTAPRQVWIAGGIGITPFLALLRAL------ 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 765 PDRDSDiennnsnnnskgfkTRKAYFYWVTREQGSFEwFKgimDEISEL-DEEGIIELHNYCTSvyEEGdarvaliamlq 843
Cdd:COG4097 341 AARPGD--------------QRPVDLFYCVRDEEDAP-FL---EELRALaARLAGLRLHLVVSD--EDG----------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 844 slqhakngvdVVSGTRVKSHFakPNWRQVYkkiavqhpgkrigVFYCGMPGMIKELKN--LALDFSRKtttkfDFHKENF 921
Cdd:COG4097 390 ----------RLTAERLRRLV--PDLAEAD-------------VFFCGPPGMMDALRRdlRALGVPAR-----RIHQERF 439
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
425-758 |
1.22e-24 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 110.32 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 425 MALILLPVCRN-TITWLRNktklgtvVPFDDSLNFHKVIASGIVVGVLLHAGAHLTcdfprLIAADEDTYEPMEKYfgdQ 503
Cdd:PLN02844 167 LALLLLPVLRGlALFRLLG-------IQFEASVRYHVWLGTSMIFFATVHGASTLF-----IWGISHHIQDEIWKW---Q 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 504 PTSYWWFVKGVEGWTGIVMVVLmaiaftlATPWFRRNKlnlpnflkkltgFNAFWYTHHLFIIVYALLIVHGIKLYLtki 583
Cdd:PLN02844 232 KTGRIYLAGEIALVTGLVIWIT-------SLPQIRRKR------------FEIFYYTHHLYIVFLIFFLFHAGDRHF--- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 584 wyqkttwmYLAVP-ILLYASERLLRAFRSsiKPVKMIKVA-VYPGNVLSLHMTKPQGFKYKSGQFMLVNCRAVSPFEWHP 661
Cdd:PLN02844 290 --------YMVFPgIFLFGLDKLLRIVQS--RPETCILSArLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHP 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 662 FSITSAPG--DDYLSVHIRTLGDWTRKLRTVFSEvckpptagksgllRADGGDGNLPFPKVLIDGPYGAPAQDYKKYDVV 739
Cdd:PLN02844 360 FSITSSSNidDHTMSVIIKCEGGWTNSLYNKIQA-------------ELDSETNQMNCIPVAIEGPYGPASVDFLRYDSL 426
|
330
....*....|....*....
gi 15238842 740 LLVGLGIGATPMISILKDI 758
Cdd:PLN02844 427 LLVAGGIGITPFLSILKEI 445
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
506-765 |
5.53e-21 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 98.58 E-value: 5.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 506 SYWWFVKGVEGWTGIVMVVLMAIAFTLATPWFRRNKlnlpnflkkltgFNAFWYTHHLFIIVYALLIVHgiklyltkiwy 585
Cdd:PLN02631 223 TFAWNPTYVPNLAGTIAMVIGIAMWVTSLPSFRRKK------------FELFFYTHHLYGLYIVFYVIH----------- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 586 QKTTWMYLAVP-ILLYASERLLRaFRSSIKPVKMIKVAVYPGNVLSLHMTKPQGFKYKSGQFMLVNCRAVSPFEWHPFSI 664
Cdd:PLN02631 280 VGDSWFCMILPnIFLFFIDRYLR-FLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTI 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 665 TSAPG--DDYLSVHIRTLGDWTRKLRTVFSEvckpptagksgllradggdgNLPFPKVLIDGPYGAPAQDYKKYDVVLLV 742
Cdd:PLN02631 359 TSSSNleKDTLSVVIRRQGSWTQKLYTHLSS--------------------SIDSLEVSTEGPYGPNSFDVSRHNSLILV 418
|
250 260
....*....|....*....|...
gi 15238842 743 GLGIGATPMISILKDIINNMKGP 765
Cdd:PLN02631 419 SGGSGITPFISVIRELIFQSQNP 441
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
625-921 |
7.46e-18 |
|
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: 83.08 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 625 PGNVLSLHMTKPQ-GFKYKSGQFMLVNCRAVSPFEWHPFSITSAPGDDY-LSVHIRTLGDWTRKLRTvfsevckpptagk 702
Cdd:cd06198 6 VRPTTTLTLEPRGpALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALGDYTRRLAE------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 703 sgLLRAdgGDgnlpfpKVLIDGPYGAPAQDYKKYDVVLLVGlGIGATPMISILKDiinnmkGPDRDSDiennnsnnnskg 782
Cdd:cd06198 73 --RLKP--GT------RVTVEGPYGRFTFDDRRARQIWIAG-GIGITPFLALLEA------LAARGDA------------ 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 783 fktRKAYFYWVTREQGSFeWFkgiMDEISELDEEGIIELHnyctsVYEEGDARVALIAMLQSLQHakngvdvvsgtrvks 862
Cdd:cd06198 124 ---RPVTLFYCVRDPEDA-VF---LDELRALAAAAGVVLH-----VIDSPSDGRLTLEQLVRALV--------------- 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 15238842 863 hfakPNWRQVykkiavqhpgkriGVFYCGMPGMIKELKNlalDFSRKTTTKFDFHKENF 921
Cdd:cd06198 177 ----PDLADA-------------DVWFCGPPGMADALEK---GLRALGVPARRFHYERF 215
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
554-759 |
9.80e-18 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 88.39 E-value: 9.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 554 FNAFWYTHHLFIIVYALLIVH-GIklyltkiwyqktTWMYLAVP-ILLYASERLLRaFRSSIKPVKMIKVAVYPGNVLSL 631
Cdd:PLN02292 276 FEVFFYTHYLYIVFMLFFVFHvGI------------SFALISFPgFYIFLVDRFLR-FLQSRNNVKLVSARVLPCDTVEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 632 HMTKPQGFKYKSGQFMLVNCRAVSPFEWHPFSITSAPG--DDYLSVHIRTLGDWTRKLRTVFSEvckpptagksgllrad 709
Cdd:PLN02292 343 NFSKNPMLMYSPTSIMFVNIPSISKLQWHPFTITSSSKlePEKLSVMIKSQGKWSTKLYHMLSS---------------- 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15238842 710 ggDGNLPFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISILKDII 759
Cdd:PLN02292 407 --SDQIDRLAVSVEGPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
424-572 |
1.37e-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: 71.15 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 424 NMALILLPVCRNT-ITWLRNktklgtvVPFDDSLNFHKVIASGIVVGVLLHAGAHLTCDFPRliaadedtyepmekyfgD 502
Cdd:pfam01794 8 LLPLLLLLALRNNpLEWLTG-------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF-----------------S 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 503 QPTSYWWFVKGVEGWTGIVMVVLMAIAFTLATPWFRRNklnlpnflkkltGFNAFWYTHHLFIIVYALLI 572
Cdd:pfam01794 64 LEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHILLAVAFLLLV 121
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
634-837 |
2.41e-14 |
|
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: 73.25 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 634 TKPQGFKYKSGQFMLVNCRAVSPFEWHPFSITSAPGD-DYLSVHIRT--LGDWTRKLRtvfsevckpptagksgllRADG 710
Cdd:cd00322 16 QLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEeGELELTVKIvpGGPFSAWLH------------------DLKP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 711 GDgnlpfpKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISILKDIINNmkgpdrdsdiennnsnnnskgFKTRKAYF 790
Cdd:cd00322 78 GD------EVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAAD---------------------KPGGEITL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 15238842 791 YWVTREQGSFeWFKgimDEISELDEEGIIELHNYCTSVYEEGDARVA 837
Cdd:cd00322 131 LYGARTPADL-LFL---DELEELAKEGPNFRLVLALSRESEAKLGPG 173
|
|
| Mcr1 |
COG0543 |
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ... |
636-761 |
9.16e-11 |
|
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];
Pssm-ID: 440309 [Multi-domain] Cd Length: 247 Bit Score: 62.96 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 636 PQGFKYKSGQFMLVncRAVSPFEWHPFSITSAPGDD-YLSVHIRTLGDWTRKLRTvfsevckpptagksglLRAdgGDgn 714
Cdd:COG0543 21 LIALKFKPGQFVML--RVPGDGLRRPFSIASAPREDgTIELHIRVVGKGTRALAE----------------LKP--GD-- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 15238842 715 lpfpKVLIDGPYGAP---AQDYKKydvVLLVGLGIGATPMISILKDIINN 761
Cdd:COG0543 79 ----ELDVRGPLGNGfplEDSGRP---VLLVAGGTGLAPLRSLAEALLAR 121
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
185-317 |
9.36e-09 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 54.80 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 185 VDQRFDKLSADSNGLLLSAKFweclgmnkesKDFADQLFRALARRNNVSGD-AITKEQLRIFWEQISDESFDAKLQVFFD 263
Cdd:COG5126 7 LDRRFDLLDADGDGVLERDDF----------EALFRRLWATLFSEADTDGDgRISREEFVAGMESLFEATVEPFARAAFD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15238842 264 MVDKDEDGRVTEEEVAEIIslsaSANKLSNIQkqakeyAALIMEELDPDNAGFI 317
Cdd:COG5126 77 LLDTDGDGKISADEFRRLL----TALGVSEEE------ADELFARLDTDGDGKI 120
|
|
| Fpr |
COG1018 |
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion]; |
627-768 |
1.91e-08 |
|
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
Pssm-ID: 440641 [Multi-domain] Cd Length: 231 Bit Score: 55.95 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 627 NVLSLHMTKPQG---FKYKSGQFMLVNCRAVSPFEWHPFSITSAPGDDYLSVHIRTLGDwtRKLRTVFSEVCKPptagks 703
Cdd:COG1018 17 DVVSFTLEPPDGaplPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGDGRLEITVKRVPG--GGGSNWLHDHLKV------ 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15238842 704 gllradgGDgnlpfpKVLIDGPYGA---PAQDYKKYdvvLLVGLGIGATPMISILKDIINNmkGPDRD 768
Cdd:COG1018 89 -------GD------TLEVSGPRGDfvlDPEPARPL---LLIAGGIGITPFLSMLRTLLAR--GPFRP 138
|
|
| PRK00054 |
PRK00054 |
dihydroorotate dehydrogenase electron transfer subunit; Reviewed |
638-816 |
3.06e-07 |
|
dihydroorotate dehydrogenase electron transfer subunit; Reviewed
Pssm-ID: 234601 [Multi-domain] Cd Length: 250 Bit Score: 52.57 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 638 GFKYKSGQFMLVNCRAVSPFEWHPFSItSAPGDDYLSVHIRTLGDWTRKLRTvfsevckpptagksglLRAdgGDgnlpf 717
Cdd:PRK00054 29 VFDMKPGQFVMVWVPGVEPLLERPISI-SDIDKNEITILYRKVGEGTKKLSK----------------LKE--GD----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 718 pKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISILKDIINnmKGPDRDSDIennnsnnnskGFKTRKAYFY------ 791
Cdd:PRK00054 85 -ELDIRGPLGNGFDLEEIGGKVLLVGGGIGVAPLYELAKELKK--KGVEVTTVL----------GARTKDEVIFeeefak 151
|
170 180 190
....*....|....*....|....*....|
gi 15238842 792 ----WVTREQGSFEwFKG-IMDEISELDEE 816
Cdd:PRK00054 152 vgdvYVTTDDGSYG-FKGfVTDVLDELDSE 180
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
237-283 |
8.43e-06 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 44.08 E-value: 8.43e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15238842 237 ITKEQLRIFWEQISDESFDAKLQVFFDMVDKDEDGRVTEEEVAEIIS 283
Cdd:cd00051 17 ISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
644-756 |
2.63e-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: 46.55 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 644 GQFMLVNCRAVSPFEWHPFSITSA-PGDDYLSVHIRTLGDWTRKLrtvfsevckpptagksGLLRAdgGDgnlpfpKVLI 722
Cdd:cd06192 28 GQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRGPKTKLI----------------AELKP--GE------KLDV 83
|
90 100 110
....*....|....*....|....*....|....
gi 15238842 723 DGPYGAPAQDYKKYDVVLLVGLGIGATPMISILK 756
Cdd:cd06192 84 MGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAK 117
|
|
| FNR_like_1 |
cd06196 |
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ... |
627-757 |
2.68e-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: 46.46 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 627 NVLSLHMTKPQGFKYKSGQFMLVncrAVSPFEW----HPFSITSAPGDDYLSVHIRTLGD---WTRKLRTVfsevcKPpt 699
Cdd:cd06196 14 DVKRLRFDKPEGYDFTPGQATEV---AIDKPGWrdekRPFTFTSLPEDDVLEFVIKSYPDhdgVTEQLGRL-----QP-- 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15238842 700 agksgllradgGDgnlpfpKVLIDGPYGapAQDYKKYDVVLLVGLGIgaTPMISILKD 757
Cdd:cd06196 84 -----------GD------TLLIEDPWG--AIEYKGPGVFIAGGAGI--TPFIAILRD 120
|
|
| monooxygenase_like |
cd06212 |
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ... |
629-767 |
3.73e-05 |
|
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: 46.17 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 629 LSLHMTKPQGFKYKSGQFmlVNCRAVSPFEWHPFSITSAPGDDylsvhirtlgdwtrklrTVFSEVCKPPTAGK-SGLLR 707
Cdd:cd06212 18 LRLRLEEPEPIKFFAGQY--VDITVPGTEETRSFSMANTPADP-----------------GRLEFIIKKYPGGLfSSFLD 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 708 adggDGNLPFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISILKDIINnmKGPDR 767
Cdd:cd06212 79 ----DGLAVGDPVTVTGPYGTCTLRESRDRPIVLIGGGSGMAPLLSLLRDMAA--SGSDR 132
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
626-800 |
8.86e-05 |
|
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: 44.85 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 626 GNVLSLHMTKPQGFKYKSGQFMLVNcraVSPFEWHPFSITSAP-GDDYLSVHIRTLGDWTRKLRtVFSEvckpptagksg 704
Cdd:cd06189 11 DDVYRVRLKPPAPLDFLAGQYLDLL---LDDGDKRPFSIASAPhEDGEIELHIRAVPGGSFSDY-VFEE----------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 705 lLRADGgdgnlpfpKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISILKDIINNmkgpdrdsdiennnsnnnskGFK 784
Cdd:cd06189 76 -LKENG--------LVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQ--------------------GSK 126
|
170
....*....|....*.
gi 15238842 785 tRKAYFYWVTREQGSF 800
Cdd:cd06189 127 -RPIHLYWGARTEEDL 141
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
255-317 |
1.68e-04 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 40.70 E-value: 1.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15238842 255 DAKLQVFFDMVDKDEDGRVTEEEVAEIISLSASANKLSniqkqaKEYAALIMEELDPDNAGFI 317
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLS------DEEVEELFKEFDLDKDGRI 57
|
|
| DHOD_e_trans_like2 |
cd06220 |
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ... |
639-816 |
3.48e-04 |
|
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: 43.01 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 639 FKYKSGQFMLVNCRAVSPFewhPFSITSAPGDDYLSVHIRtlGDWTRKLRTVfsevcKPptagksgllradgGDgnlpfp 718
Cdd:cd06220 22 FDFKPGQFVMVWVPGVDEI---PMSLSYIDGPNSITVKKV--GEATSALHDL-----KE-------------GD------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 719 KVLIDGPYGAPAQ-DYKKydvVLLVGLGIGATPMISILKDiinNMKGPDRDSDIennnsnnnskGFKTRKAYFY------ 791
Cdd:cd06220 73 KLGIRGPYGNGFElVGGK---VLLIGGGIGIAPLAPLAER---LKKAADVTVLL----------GARTKEELLFldrlrk 136
|
170 180 190
....*....|....*....|....*....|
gi 15238842 792 ----WVTREQGSFEwFKG-IMDEISELDEE 816
Cdd:cd06220 137 sdelIVTTDDGSYG-FKGfVTDLLKELDLE 165
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
257-325 |
4.59e-04 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 39.07 E-value: 4.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15238842 257 KLQVFFDMVDKDEDGRVTEEEVAEIIslsasaNKLSniQKQAKEYAALIMEELDPDNAGFIMIEnlEML 325
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAAL------KSLG--EGLSEEEIDEMIREVDKDGDGKIDFE--EFL 59
|
|
| EFh_CREC_cab45 |
cd16225 |
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ... |
247-317 |
1.34e-03 |
|
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.
Pssm-ID: 320023 [Multi-domain] Cd Length: 278 Bit Score: 41.52 E-value: 1.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15238842 247 EQISDESFDAKLQVFFDMVDKDEDGRVTEEEVAEIIslsasankLSNIQ---KQAKEYAALIMEELDPDNAGFI 317
Cdd:cd16225 25 EEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWI--------MEKTQehfQEAVEENEQIFKAVDTDKDGNV 90
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
186-282 |
1.75e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 39.78 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 186 DQRFDKLSADSNGLLLSAKFWECL--GMNKESKDFADQLFRALARrnnvSGD-AITKEQLRIFWEQIsdESFDAKLQVFF 262
Cdd:COG5126 36 ATLFSEADTDGDGRISREEFVAGMesLFEATVEPFARAAFDLLDT----DGDgKISADEFRRLLTAL--GVSEEEADELF 109
|
90 100
....*....|....*....|
gi 15238842 263 DMVDKDEDGRVTEEEVAEII 282
Cdd:COG5126 110 ARLDTDGDGKISFEEFVAAV 129
|
|
| FNR_N-term_Iron_sulfur_binding |
cd06194 |
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ... |
627-757 |
2.30e-03 |
|
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: 40.33 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238842 627 NVLSLHMTKPQGFKYKSGQFmlVNCRaVSPFEWHPFSITSAP-GDDYLSVHIRtlgdwtrklrtvfsevCKPPTAgKSGL 705
Cdd:cd06194 10 DVLRVRLEPDRPLPYLPGQY--VNLR-RAGGLARSYSPTSLPdGDNELEFHIR----------------RKPNGA-FSGW 69
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 15238842 706 LRADGGDGNlpfpKVLIDGPYG-APAQDYKKYDVVLLVGLGIGATPMISILKD 757
Cdd:cd06194 70 LGEEARPGH----ALRLQGPFGqAFYRPEYGEGPLLLVGAGTGLAPLWGIARA 118
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
221-283 |
3.06e-03 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 36.85 E-value: 3.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15238842 221 QLFRALARRNNvsgDAITKEQLRIF--WEQISDESFDAKLQVFFDMVDKDEDGRVTEEEVAEIIS 283
Cdd:pfam13499 6 EAFKLLDSDGD---GYLDVEELKKLlrKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
|
|
| |
