|
Name |
Accession |
Description |
Interval |
E-value |
| NADPH_Ox |
pfam08414 |
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ... |
145-245 |
2.60e-57 |
|
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: 191.64 E-value: 2.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 145 YDRTKSAATHALKGLKFISKTDG--AAAWAALEKRFDELTATttGLLPRALFGECIGMnKDSKEFAGELFDALSRRRNIT 222
Cdd:pfam08414 1 LDRTKSGAARALKGLRFISKTDGgeGAGWKAVEKRFDKLAVD--GLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77
|
90 100
....*....|....*....|...
gi 1340525132 223 GDLINKAQLKEFWDQIADQSFDS 245
Cdd:pfam08414 78 GDSITKEELKEFWEQISDQSFDS 100
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
723-901 |
5.64e-49 |
|
Ferric reductase NAD binding domain;
:
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 170.21 E-value: 5.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 723 YDVVLLVGLGIGATPMISIVKDIVNNMKTkkeedealenggnsplppaspmskkstsnFNTTRAYFYWVTREQGSFDWFK 802
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKK-----------------------------LKTKKIKFYWVVRDLSSLEWFK 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 803 GVMNEVAETDQNgVIEMHNYCTSVYEEGDARSALITMLQSLNHAKNGVDVVSGTRVKSHFAKPNWRSVFKRIALTHSGQR 882
Cdd:pfam08030 52 DVLNELEELKEL-NIEIHIYLTGEYEAEDASDQSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGS 130
|
170
....*....|....*....
gi 1340525132 883 IGVFYCGAPAPVKELKQLA 901
Cdd:pfam08030 131 IGVFSCGPPSLVDELRNLV 149
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
602-717 |
7.64e-47 |
|
FAD-binding domain;
:
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 162.50 E-value: 7.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 602 KPVKMLKVAVYPGNVLALHMSKPQG-FKYKSGQYMFVNC-AAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRQLKTVF 679
Cdd:pfam08022 2 FGVPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYL 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 1340525132 680 SQVCQppangksgllrAEFQNNPNFPKVLIDGPYGAPA 717
Cdd:pfam08022 82 SSSCP-----------KSPENGKDKPRVLIEGPYGPPS 108
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
411-560 |
5.12e-14 |
|
Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.
:
Pssm-ID: 426438 [Multi-domain] Cd Length: 121 Bit Score: 69.22 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 411 LNMALILLPVCRNT-ITWLRNktklgvvVPFDDNLNFHKVIAVGITIGVGLHAISHLACDFPRllsateeeyepmqrffg 489
Cdd:pfam01794 7 ALLPLLLLLALRNNpLEWLTG-------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF----------------- 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340525132 490 DQPDTYWHFVKEAAGYTGIIMVVLMAIAFTLATPWLRRGrlnlpkplkkltGFNAFWYSHHLFVIVYTMLI 560
Cdd:pfam01794 63 SLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHILLAVAFLLLV 121
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
244-306 |
1.28e-05 |
|
EF-hand domain pair;
:
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 43.78 E-value: 1.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340525132 244 DSRLQTFFDMVDKDADGRINEAEVREIISLSASANKLSniqkqaDEYAALIMEELDPDNLGYI 306
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLS------DEEVEELFKEFDLDKDGRI 57
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NADPH_Ox |
pfam08414 |
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ... |
145-245 |
2.60e-57 |
|
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: 191.64 E-value: 2.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 145 YDRTKSAATHALKGLKFISKTDG--AAAWAALEKRFDELTATttGLLPRALFGECIGMnKDSKEFAGELFDALSRRRNIT 222
Cdd:pfam08414 1 LDRTKSGAARALKGLRFISKTDGgeGAGWKAVEKRFDKLAVD--GLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77
|
90 100
....*....|....*....|...
gi 1340525132 223 GDLINKAQLKEFWDQIADQSFDS 245
Cdd:pfam08414 78 GDSITKEELKEFWEQISDQSFDS 100
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
723-901 |
5.64e-49 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 170.21 E-value: 5.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 723 YDVVLLVGLGIGATPMISIVKDIVNNMKTkkeedealenggnsplppaspmskkstsnFNTTRAYFYWVTREQGSFDWFK 802
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKK-----------------------------LKTKKIKFYWVVRDLSSLEWFK 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 803 GVMNEVAETDQNgVIEMHNYCTSVYEEGDARSALITMLQSLNHAKNGVDVVSGTRVKSHFAKPNWRSVFKRIALTHSGQR 882
Cdd:pfam08030 52 DVLNELEELKEL-NIEIHIYLTGEYEAEDASDQSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGS 130
|
170
....*....|....*....
gi 1340525132 883 IGVFYCGAPAPVKELKQLA 901
Cdd:pfam08030 131 IGVFSCGPPSLVDELRNLV 149
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
602-717 |
7.64e-47 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 162.50 E-value: 7.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 602 KPVKMLKVAVYPGNVLALHMSKPQG-FKYKSGQYMFVNC-AAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRQLKTVF 679
Cdd:pfam08022 2 FGVPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYL 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 1340525132 680 SQVCQppangksgllrAEFQNNPNFPKVLIDGPYGAPA 717
Cdd:pfam08022 82 SSSCP-----------KSPENGKDKPRVLIEGPYGPPS 108
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
608-832 |
1.08e-46 |
|
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: 165.94 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 608 KVAVYP-GNVLALHMSKPQGFKYKSGQYMFVNCAAV-SPFEWHPFSITSAPGD--DYLSVHIRTL-GDWTRQLKTVFSQv 682
Cdd:cd06186 3 TVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALKS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 683 cqppangksgllraefQNNPNFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDIVNNMKTKkeedealeng 762
Cdd:cd06186 82 ----------------PGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKT---------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 763 gnsplppaspmskkstsnFNTTRAYFYWVTREQGSFDWFKGVMNEVAETDQNGVIemHNYCTSVYEEGDA 832
Cdd:cd06186 136 ------------------SRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEI--EIYVTRVVVCGPP 185
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
524-752 |
1.48e-23 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 106.86 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 524 WLRRGRLNLPKPLKKLTG---------------FNAFWYSHHLFVIVYTMLIVHGIKIYLtkewykkttwmYLAVP-ILL 587
Cdd:PLN02844 230 WQKTGRIYLAGEIALVTGlviwitslpqirrkrFEIFYYTHHLYIVFLIFFLFHAGDRHF-----------YMVFPgIFL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 588 YMGERLTRALRSSVKPVkMLKVAVYPGNVLALHMSKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPG--DDYLSVHI 665
Cdd:PLN02844 299 FGLDKLLRIVQSRPETC-ILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNidDHTMSVII 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 666 RTLGDWTRQLktvfSQVCQPPANGKSGLLRaefqnnpNFPkVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDI 745
Cdd:PLN02844 378 KCEGGWTNSL----YNKIQAELDSETNQMN-------CIP-VAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEI 445
|
....*..
gi 1340525132 746 VNNMKTK 752
Cdd:PLN02844 446 ASQSSSR 452
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
491-744 |
1.48e-21 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 98.81 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 491 QPDTYWHFVKEAAGYTGIIMVVLMAIAFTLAT--PWLRR----------------------------------------- 527
Cdd:COG4097 31 APAGGRGLRTALGQLTGLLALALMSLQFLLAArpPWLERpfggldrlyrlhkwlgilalvlalahpllllgpkwlvgwgg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 528 ------GRLNLPKPLKKLTGFNAFW---------------------YSHHLFVIVYTMLIVHGIkiyLTKEWYKKTTWMY 580
Cdd:COG4097 111 lparlaALLTLLRGLAELLGEWAFYlllalvvlsllrrrlpyelwrLTHRLLAVAYLLLAFHHL---LLGGPFYWSPPAG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 581 LAVPILLYMGerLTRALRSSV-KPVKMLKVA------VYPGN---VLALHMSKPQGFKYKSGQYMFVNCAAvSPF--EWH 648
Cdd:COG4097 188 VLWAALAAAG--LAAAVYSRLgRPLRSRRHPyrvesvEPEAGdvvELTLRPEGGRWLGHRAGQFAFLRFDG-SPFweEAH 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 649 PFSITSAP-GDDYLSVHIRTLGDWTRQLKTVfsqvcQPpanGKsgllraefqnnpnfpKVLIDGPYGA-PAQDYKKYDVV 726
Cdd:COG4097 265 PFSISSAPgGDGRLRFTIKALGDFTRRLGRL-----KP---GT---------------RVYVEGPYGRfTFDRRDTAPRQ 321
|
330
....*....|....*...
gi 1340525132 727 LLVGLGIGATPMISIVKD 744
Cdd:COG4097 322 VWIAGGIGITPFLALLRA 339
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
508-752 |
5.87e-19 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 92.03 E-value: 5.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 508 IIMVVLMAIAFTlATPWLRRGRlnlpkplkkltgFNAFWYSHHLFVIVYTMLIVHgikiyltkewyKKTTWMYLAVP-IL 586
Cdd:PLN02631 238 IAMVIGIAMWVT-SLPSFRRKK------------FELFFYTHHLYGLYIVFYVIH-----------VGDSWFCMILPnIF 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 587 LYMGERLTRALRSSvKPVKMLKVAVYPGNVLALHMSKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPG--DDYLSVH 664
Cdd:PLN02631 294 LFFIDRYLRFLQST-KRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNleKDTLSVV 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 665 IRTLGDWTRQLKTVFSqvcqppangksgllraefqNNPNFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKD 744
Cdd:PLN02631 373 IRRQGSWTQKLYTHLS-------------------SSIDSLEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRE 433
|
....*...
gi 1340525132 745 IVNNMKTK 752
Cdd:PLN02631 434 LIFQSQNP 441
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
411-560 |
5.12e-14 |
|
Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.
Pssm-ID: 426438 [Multi-domain] Cd Length: 121 Bit Score: 69.22 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 411 LNMALILLPVCRNT-ITWLRNktklgvvVPFDDNLNFHKVIAVGITIGVGLHAISHLACDFPRllsateeeyepmqrffg 489
Cdd:pfam01794 7 ALLPLLLLLALRNNpLEWLTG-------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF----------------- 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340525132 490 DQPDTYWHFVKEAAGYTGIIMVVLMAIAFTLATPWLRRGrlnlpkplkkltGFNAFWYSHHLFVIVYTMLI 560
Cdd:pfam01794 63 SLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHILLAVAFLLLV 121
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
244-306 |
1.28e-05 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 43.78 E-value: 1.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340525132 244 DSRLQTFFDMVDKDADGRINEAEVREIISLSASANKLSniqkqaDEYAALIMEELDPDNLGYI 306
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLS------DEEVEELFKEFDLDKDGRI 57
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
226-272 |
2.92e-05 |
|
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: 42.53 E-value: 2.92e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1340525132 226 INKAQLKEFWDQIADQSFDSRLQTFFDMVDKDADGRINEAEVREIIS 272
Cdd:cd00051 17 ISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NADPH_Ox |
pfam08414 |
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ... |
145-245 |
2.60e-57 |
|
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: 191.64 E-value: 2.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 145 YDRTKSAATHALKGLKFISKTDG--AAAWAALEKRFDELTATttGLLPRALFGECIGMnKDSKEFAGELFDALSRRRNIT 222
Cdd:pfam08414 1 LDRTKSGAARALKGLRFISKTDGgeGAGWKAVEKRFDKLAVD--GLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77
|
90 100
....*....|....*....|...
gi 1340525132 223 GDLINKAQLKEFWDQIADQSFDS 245
Cdd:pfam08414 78 GDSITKEELKEFWEQISDQSFDS 100
|
|
| NAD_binding_6 |
pfam08030 |
Ferric reductase NAD binding domain; |
723-901 |
5.64e-49 |
|
Ferric reductase NAD binding domain;
Pssm-ID: 429792 [Multi-domain] Cd Length: 149 Bit Score: 170.21 E-value: 5.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 723 YDVVLLVGLGIGATPMISIVKDIVNNMKTkkeedealenggnsplppaspmskkstsnFNTTRAYFYWVTREQGSFDWFK 802
Cdd:pfam08030 1 YENVLLVAGGIGITPFISILKDLGNKSKK-----------------------------LKTKKIKFYWVVRDLSSLEWFK 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 803 GVMNEVAETDQNgVIEMHNYCTSVYEEGDARSALITMLQSLNHAKNGVDVVSGTRVKSHFAKPNWRSVFKRIALTHSGQR 882
Cdd:pfam08030 52 DVLNELEELKEL-NIEIHIYLTGEYEAEDASDQSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGS 130
|
170
....*....|....*....
gi 1340525132 883 IGVFYCGAPAPVKELKQLA 901
Cdd:pfam08030 131 IGVFSCGPPSLVDELRNLV 149
|
|
| FAD_binding_8 |
pfam08022 |
FAD-binding domain; |
602-717 |
7.64e-47 |
|
FAD-binding domain;
Pssm-ID: 285293 [Multi-domain] Cd Length: 108 Bit Score: 162.50 E-value: 7.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 602 KPVKMLKVAVYPGNVLALHMSKPQG-FKYKSGQYMFVNC-AAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRQLKTVF 679
Cdd:pfam08022 2 FGVPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANYL 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 1340525132 680 SQVCQppangksgllrAEFQNNPNFPKVLIDGPYGAPA 717
Cdd:pfam08022 82 SSSCP-----------KSPENGKDKPRVLIEGPYGPPS 108
|
|
| NOX_Duox_like_FAD_NADP |
cd06186 |
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ... |
608-832 |
1.08e-46 |
|
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: 165.94 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 608 KVAVYP-GNVLALHMSKPQGFKYKSGQYMFVNCAAV-SPFEWHPFSITSAPGD--DYLSVHIRTL-GDWTRQLKTVFSQv 682
Cdd:cd06186 3 TVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALKS- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 683 cqppangksgllraefQNNPNFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDIVNNMKTKkeedealeng 762
Cdd:cd06186 82 ----------------PGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRSSKT---------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 763 gnsplppaspmskkstsnFNTTRAYFYWVTREQGSFDWFKGVMNEVAETDQNGVIemHNYCTSVYEEGDA 832
Cdd:cd06186 136 ------------------SRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEI--EIYVTRVVVCGPP 185
|
|
| PLN02844 |
PLN02844 |
oxidoreductase/ferric-chelate reductase |
524-752 |
1.48e-23 |
|
oxidoreductase/ferric-chelate reductase
Pssm-ID: 215453 [Multi-domain] Cd Length: 722 Bit Score: 106.86 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 524 WLRRGRLNLPKPLKKLTG---------------FNAFWYSHHLFVIVYTMLIVHGIKIYLtkewykkttwmYLAVP-ILL 587
Cdd:PLN02844 230 WQKTGRIYLAGEIALVTGlviwitslpqirrkrFEIFYYTHHLYIVFLIFFLFHAGDRHF-----------YMVFPgIFL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 588 YMGERLTRALRSSVKPVkMLKVAVYPGNVLALHMSKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPG--DDYLSVHI 665
Cdd:PLN02844 299 FGLDKLLRIVQSRPETC-ILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNidDHTMSVII 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 666 RTLGDWTRQLktvfSQVCQPPANGKSGLLRaefqnnpNFPkVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDI 745
Cdd:PLN02844 378 KCEGGWTNSL----YNKIQAELDSETNQMN-------CIP-VAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEI 445
|
....*..
gi 1340525132 746 VNNMKTK 752
Cdd:PLN02844 446 ASQSSSR 452
|
|
| COG4097 |
COG4097 |
Predicted ferric reductase [Inorganic ion transport and metabolism]; |
491-744 |
1.48e-21 |
|
Predicted ferric reductase [Inorganic ion transport and metabolism];
Pssm-ID: 443273 [Multi-domain] Cd Length: 442 Bit Score: 98.81 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 491 QPDTYWHFVKEAAGYTGIIMVVLMAIAFTLAT--PWLRR----------------------------------------- 527
Cdd:COG4097 31 APAGGRGLRTALGQLTGLLALALMSLQFLLAArpPWLERpfggldrlyrlhkwlgilalvlalahpllllgpkwlvgwgg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 528 ------GRLNLPKPLKKLTGFNAFW---------------------YSHHLFVIVYTMLIVHGIkiyLTKEWYKKTTWMY 580
Cdd:COG4097 111 lparlaALLTLLRGLAELLGEWAFYlllalvvlsllrrrlpyelwrLTHRLLAVAYLLLAFHHL---LLGGPFYWSPPAG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 581 LAVPILLYMGerLTRALRSSV-KPVKMLKVA------VYPGN---VLALHMSKPQGFKYKSGQYMFVNCAAvSPF--EWH 648
Cdd:COG4097 188 VLWAALAAAG--LAAAVYSRLgRPLRSRRHPyrvesvEPEAGdvvELTLRPEGGRWLGHRAGQFAFLRFDG-SPFweEAH 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 649 PFSITSAP-GDDYLSVHIRTLGDWTRQLKTVfsqvcQPpanGKsgllraefqnnpnfpKVLIDGPYGA-PAQDYKKYDVV 726
Cdd:COG4097 265 PFSISSAPgGDGRLRFTIKALGDFTRRLGRL-----KP---GT---------------RVYVEGPYGRfTFDRRDTAPRQ 321
|
330
....*....|....*...
gi 1340525132 727 LLVGLGIGATPMISIVKD 744
Cdd:COG4097 322 VWIAGGIGITPFLALLRA 339
|
|
| PLN02292 |
PLN02292 |
ferric-chelate reductase |
542-753 |
3.97e-19 |
|
ferric-chelate reductase
Pssm-ID: 215165 [Multi-domain] Cd Length: 702 Bit Score: 92.62 E-value: 3.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 542 FNAFWYSHHLFVIVYTMLIVH-GIkiyltkewykktTWMYLAVP-ILLYMGERLTRALRSSvKPVKMLKVAVYPGNVLAL 619
Cdd:PLN02292 276 FEVFFYTHYLYIVFMLFFVFHvGI------------SFALISFPgFYIFLVDRFLRFLQSR-NNVKLVSARVLPCDTVEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 620 HMSKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPG--DDYLSVHIRTLGDWTRQLKTVFSQvcqppangksgllrae 697
Cdd:PLN02292 343 NFSKNPMLMYSPTSIMFVNIPSISKLQWHPFTITSSSKlePEKLSVMIKSQGKWSTKLYHMLSS---------------- 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1340525132 698 fQNNPNFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDIVNNMKTKK 753
Cdd:PLN02292 407 -SDQIDRLAVSVEGPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLIYTSSTET 461
|
|
| PLN02631 |
PLN02631 |
ferric-chelate reductase |
508-752 |
5.87e-19 |
|
ferric-chelate reductase
Pssm-ID: 178238 [Multi-domain] Cd Length: 699 Bit Score: 92.03 E-value: 5.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 508 IIMVVLMAIAFTlATPWLRRGRlnlpkplkkltgFNAFWYSHHLFVIVYTMLIVHgikiyltkewyKKTTWMYLAVP-IL 586
Cdd:PLN02631 238 IAMVIGIAMWVT-SLPSFRRKK------------FELFFYTHHLYGLYIVFYVIH-----------VGDSWFCMILPnIF 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 587 LYMGERLTRALRSSvKPVKMLKVAVYPGNVLALHMSKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPG--DDYLSVH 664
Cdd:PLN02631 294 LFFIDRYLRFLQST-KRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNleKDTLSVV 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 665 IRTLGDWTRQLKTVFSqvcqppangksgllraefqNNPNFPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKD 744
Cdd:PLN02631 373 IRRQGSWTQKLYTHLS-------------------SSIDSLEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRE 433
|
....*...
gi 1340525132 745 IVNNMKTK 752
Cdd:PLN02631 434 LIFQSQNP 441
|
|
| FNR_like_3 |
cd06198 |
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ... |
611-744 |
5.06e-15 |
|
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: 74.99 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 611 VYPGNVLALHMSKPQgFKYKSGQYMFVNCAAVSPFEWHPFSITSAPGDDY-LSVHIRTLGDWTRQLKTvfsQVcQPpanG 689
Cdd:cd06198 6 VRPTTTLTLEPRGPA-LGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALGDYTRRLAE---RL-KP---G 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1340525132 690 KsgllraefqnnpnfpKVLIDGPYGAPAQDYKKYDVVLLVGlGIGATPMISIVKD 744
Cdd:cd06198 78 T---------------RVTVEGPYGRFTFDDRRARQIWIAG-GIGITPFLALLEA 116
|
|
| Ferric_reduct |
pfam01794 |
Ferric reductase like transmembrane component; This family includes a common region in the ... |
411-560 |
5.12e-14 |
|
Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.
Pssm-ID: 426438 [Multi-domain] Cd Length: 121 Bit Score: 69.22 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 411 LNMALILLPVCRNT-ITWLRNktklgvvVPFDDNLNFHKVIAVGITIGVGLHAISHLACDFPRllsateeeyepmqrffg 489
Cdd:pfam01794 7 ALLPLLLLLALRNNpLEWLTG-------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF----------------- 62
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340525132 490 DQPDTYWHFVKEAAGYTGIIMVVLMAIAFTLATPWLRRGrlnlpkplkkltGFNAFWYSHHLFVIVYTMLI 560
Cdd:pfam01794 63 SLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHILLAVAFLLLV 121
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
622-745 |
7.86e-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: 71.71 E-value: 7.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 622 SKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPGD-DYLSVHIRTLgdwtrqlktvfsqvcqpPANGKSGLLRAEFQN 700
Cdd:cd00322 16 QLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEeGELELTVKIV-----------------PGGPFSAWLHDLKPG 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1340525132 701 NpnfpKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDI 745
Cdd:cd00322 79 D----EVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHL 119
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
174-306 |
1.10e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 49.02 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 174 LEKRFDELTATTTGLLPRAlfgecigmnkDSKEFAGELFDALSRRRNITGD-LINKAQLKEFWDQIADQSFDSRLQTFFD 252
Cdd:COG5126 7 LDRRFDLLDADGDGVLERD----------DFEALFRRLWATLFSEADTDGDgRISREEFVAGMESLFEATVEPFARAAFD 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1340525132 253 MVDKDADGRINEAEVREIIslsaSANKLSniqkqaDEYAALIMEELDPDNLGYI 306
Cdd:COG5126 77 LLDTDGDGKISADEFRRLL----TALGVS------EEEADELFARLDTDGDGKI 120
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
244-306 |
1.28e-05 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 43.78 E-value: 1.28e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340525132 244 DSRLQTFFDMVDKDADGRINEAEVREIISLSASANKLSniqkqaDEYAALIMEELDPDNLGYI 306
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLS------DEEVEELFKEFDLDKDGRI 57
|
|
| DHOD_e_trans_like |
cd06192 |
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ... |
632-743 |
2.69e-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: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 632 GQYMFVNCAAVSPFEWHPFSITSA-PGDDYLSVHIRTLGdwtrqlktvfsqvcqppanGKSGLLraeFQNNPNFPKVLId 710
Cdd:cd06192 28 GQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRG-------------------PKTKLI---AELKPGEKLDVM- 84
|
90 100 110
....*....|....*....|....*....|...
gi 1340525132 711 GPYGAPAQDYKKYDVVLLVGLGIGATPMISIVK 743
Cdd:cd06192 85 GPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAK 117
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
226-272 |
2.92e-05 |
|
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: 42.53 E-value: 2.92e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1340525132 226 INKAQLKEFWDQIADQSFDSRLQTFFDMVDKDADGRINEAEVREIIS 272
Cdd:cd00051 17 ISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| flavin_oxioreductase |
cd06189 |
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ... |
614-748 |
2.75e-04 |
|
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: 43.31 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 614 GNVLALHMSKPQGFKYKSGQYMFVNcaaVSPFEWHPFSITSAP-GDDYLSVHIRtlgdwtRQLKTVFSQvcqppangksg 692
Cdd:cd06189 11 DDVYRVRLKPPAPLDFLAGQYLDLL---LDDGDKRPFSIASAPhEDGEIELHIR------AVPGGSFSD----------- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1340525132 693 LLRAEFQNNpnfPKVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDIVNN 748
Cdd:cd06189 71 YVFEELKEN---GLVRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQ 123
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
246-306 |
3.84e-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: 39.45 E-value: 3.84e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340525132 246 RLQTFFDMVDKDADGRINEAEVREIISlSASANKLsniQKQADEyaalIMEELDPDNLGYI 306
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALK-SLGEGLS---EEEIDE----MIREVDKDGDGKI 53
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
161-271 |
4.57e-03 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 38.23 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340525132 161 FISKTDGAAAWAAL-EKRFDELTATTTGLLPRALFGECI--GMNKDSKEFAGELFDALSRrrniTGD-LINKAQLKEFWD 236
Cdd:COG5126 21 VLERDDFEALFRRLwATLFSEADTDGDGRISREEFVAGMesLFEATVEPFARAAFDLLDT----DGDgKISADEFRRLLT 96
|
90 100 110
....*....|....*....|....*....|....*
gi 1340525132 237 QIADQsfDSRLQTFFDMVDKDADGRINEAEVREII 271
Cdd:COG5126 97 ALGVS--EEEADELFARLDTDGDGKISFEEFVAAV 129
|
|
| |
