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Conserved domains on  [gi|1270980525|gb|PHT29300|]
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Respiratory burst oxidase -like protein D [Capsicum baccatum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NADPH_Ox pfam08414
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ...
 143-243 2.80e-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: 2.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 143 FDRNKSAAAHALKGLKFISKTDGG--AGWAAVEKRFDEITAStsGLLPRAKFGECIGMnKESKDFAGELYDALARRRNIT 220
Cdd:pfam08414   1 LDRTKSGAARALKGLRFISKTDGGegAGWKAVEKRFDKLAVD--GLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77

                          90       100
                  ....*....|....*....|...
gi 1270980525 221 TDSINKAQLKEFWDQVADQSFDT 243
Cdd:pfam08414  78 GDSITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
726-912 2.17e-47

Ferric reductase NAD binding domain;


:

Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 165.59  E-value: 2.17e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 726 YEVVLLVGLGIGATPMISIVKDIVNNMKAmdeeqnslenghggsnaasnaspniaqkrgksgsasgrnnFNTRRAYFYWV 805
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK----------------------------------------LKTKKIKFYWV 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 806 TREQGSFDWFKGIMNEAAEMDHKgVIEMHNYCTSVYEEGDARSALI-----TMLQSLHHAKNGVDIVsgtrvKSHFAKPN 880
Cdd:pfam08030  41 VRDLSSLEWFKDVLNELEELKEL-NIEIHIYLTGEYEAEDASDQSDssirsENFDSLMNEVIGVDFV-----EFHFGRPN 114

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270980525 881 WRNVYKRIALNHPEAKVGVFYCGAPALTKELR 912
Cdd:pfam08030 115 WKEVLKDIAKQHPNGSIGVFSCGPPSLVDELR 146
FAD_binding_8 pfam08022
FAD-binding domain;
601-720 4.18e-47

FAD-binding domain;


:

Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 163.28  E-value: 4.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 601 IKAVKILKVAVYPGNVLALHMSKPQG-YKYKSGQYMFVNC-AAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRQLKTV 678
Cdd:pfam08022   1 IFGVPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1270980525 679 FSEVCQpppngksgllradyLQGENNPDFPRVLIDGPYGAPA 720
Cdd:pfam08022  81 LSSSCP--------------KSPENGKDKPRVLIEGPYGPPS 108
PLN02844 super family cl33578
oxidoreductase/ferric-chelate reductase
 413-748 2.03e-23

oxidoreductase/ferric-chelate reductase


The actual alignment was detected with superfamily member PLN02844:

Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 106.47  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 413 MAIILFPVCRNTITWlrnktRLgVAVPFDDNLNFHKVIAVAIALGVGVHGLAHLTcdfprVLNASEDEEETIeyyFREQP 492
Cdd:PLN02844  167 LALLLLPVLRGLALF-----RL-LGIQFEASVRYHVWLGTSMIFFATVHGASTLF-----IWGISHHIQDEI---WKWQK 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 493 TNYWWFIKGVEGVTGIIMVVLmaiaftlATPWFRRGRvsfpkpfhkltgFNAFWYSHHLFVIVYTLLIVHGEKLYitktw 572
Cdd:PLN02844  233 TGRIYLAGEIALVTGLVIWIT-------SLPQIRRKR------------FEIFYYTHHLYIVFLIFFLFHAGDRH----- 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 573 ykrttwMYLTVP-LVLYAGERLLRAFRSSIKAVkILKVAVYPGNVLALHMSKPQGYKYKSGQYMFVNCAAVSPFEWHPFS 651
Cdd:PLN02844  289 ------FYMVFPgIFLFGLDKLLRIVQSRPETC-ILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFS 361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 652 ITSAPG--DDYLSVHIRTLGDWTRQLKTVFSEVcqpppngksglLRADYLQGENNPdfprVLIDGPYGAPAQDYKNYEVV 729
Cdd:PLN02844  362 ITSSSNidDHTMSVIIKCEGGWTNSLYNKIQAE-----------LDSETNQMNCIP----VAIEGPYGPASVDFLRYDSL 426

                         330
                  ....*....|....*....
gi 1270980525 730 LLVGLGIGATPMISIVKDI 748
Cdd:PLN02844  427 LLVAGGIGITPFLSILKEI 445
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 244-312 7.52e-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: 7.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270980525 244 RLQTFFDMVDKDADGRITEEEVREIIGlsasanrlSTIQKQADEYAAMIMEELDPNNLGYIMIEnlEML 312
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALK--------SLGEGLSEEEIDEMIREVDKDGDGKIDFE--EFL 59
 
Name Accession Description Interval E-value
NADPH_Ox pfam08414
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ...
 143-243 2.80e-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: 2.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 143 FDRNKSAAAHALKGLKFISKTDGG--AGWAAVEKRFDEITAStsGLLPRAKFGECIGMnKESKDFAGELYDALARRRNIT 220
Cdd:pfam08414   1 LDRTKSGAARALKGLRFISKTDGGegAGWKAVEKRFDKLAVD--GLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77

                          90       100
                  ....*....|....*....|...
gi 1270980525 221 TDSINKAQLKEFWDQVADQSFDT 243
Cdd:pfam08414  78 GDSITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
726-912 2.17e-47

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 165.59  E-value: 2.17e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 726 YEVVLLVGLGIGATPMISIVKDIVNNMKAmdeeqnslenghggsnaasnaspniaqkrgksgsasgrnnFNTRRAYFYWV 805
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK----------------------------------------LKTKKIKFYWV 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 806 TREQGSFDWFKGIMNEAAEMDHKgVIEMHNYCTSVYEEGDARSALI-----TMLQSLHHAKNGVDIVsgtrvKSHFAKPN 880
Cdd:pfam08030  41 VRDLSSLEWFKDVLNELEELKEL-NIEIHIYLTGEYEAEDASDQSDssirsENFDSLMNEVIGVDFV-----EFHFGRPN 114

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270980525 881 WRNVYKRIALNHPEAKVGVFYCGAPALTKELR 912
Cdd:pfam08030 115 WKEVLKDIAKQHPNGSIGVFSCGPPSLVDELR 146
FAD_binding_8 pfam08022
FAD-binding domain;
601-720 4.18e-47

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 163.28  E-value: 4.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 601 IKAVKILKVAVYPGNVLALHMSKPQG-YKYKSGQYMFVNC-AAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRQLKTV 678
Cdd:pfam08022   1 IFGVPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1270980525 679 FSEVCQpppngksgllradyLQGENNPDFPRVLIDGPYGAPA 720
Cdd:pfam08022  81 LSSSCP--------------KSPENGKDKPRVLIEGPYGPPS 108
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 606-933 6.86e-47

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: 166.71  E-value: 6.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 606 ILKVAVYP-GNVLALHMSKPQGYKYKSGQYMFVNCAAV-SPFEWHPFSITSAPGD--DYLSVHIRTL-GDWTRqlktvfs 680
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTR------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 681 evcqpppngksglLRADYLQGENNPDFPRVLIDGPYGAPAQDYKNYEVVLLVGLGIGATPMISIVKDIVNNMkamdeeqn 760
Cdd:cd06186    74 -------------LLRKALKSPGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS-------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 761 slenghggsnaasnaspniaqkrgksgsasgRNNFNTRRAYFYWVTREQGSFDWFKGIMNEAAEMDHKGVIemHNYCTsv 840
Cdd:cd06186   133 -------------------------------SKTSRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEI--EIYVT-- 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 841 yeegdarsalitmlqslhhakngvdivsgtrvkshfakpnwrnvykrialnhpeakvGVFYCGAPALTKELRQHAldfSH 920
Cdd:cd06186   178 ---------------------------------------------------------RVVVCGPPGLVDDVRNAV---AK 197

                         330
                  ....*....|...
gi 1270980525 921 KTSTKFDFHKENF 933
Cdd:cd06186   198 KGGTGVEFHEESF 210
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 413-748 2.03e-23

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 106.47  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 413 MAIILFPVCRNTITWlrnktRLgVAVPFDDNLNFHKVIAVAIALGVGVHGLAHLTcdfprVLNASEDEEETIeyyFREQP 492
Cdd:PLN02844  167 LALLLLPVLRGLALF-----RL-LGIQFEASVRYHVWLGTSMIFFATVHGASTLF-----IWGISHHIQDEI---WKWQK 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 493 TNYWWFIKGVEGVTGIIMVVLmaiaftlATPWFRRGRvsfpkpfhkltgFNAFWYSHHLFVIVYTLLIVHGEKLYitktw 572
Cdd:PLN02844  233 TGRIYLAGEIALVTGLVIWIT-------SLPQIRRKR------------FEIFYYTHHLYIVFLIFFLFHAGDRH----- 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 573 ykrttwMYLTVP-LVLYAGERLLRAFRSSIKAVkILKVAVYPGNVLALHMSKPQGYKYKSGQYMFVNCAAVSPFEWHPFS 651
Cdd:PLN02844  289 ------FYMVFPgIFLFGLDKLLRIVQSRPETC-ILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFS 361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 652 ITSAPG--DDYLSVHIRTLGDWTRQLKTVFSEVcqpppngksglLRADYLQGENNPdfprVLIDGPYGAPAQDYKNYEVV 729
Cdd:PLN02844  362 ITSSSNidDHTMSVIIKCEGGWTNSLYNKIQAE-----------LDSETNQMNCIP----VAIEGPYGPASVDFLRYDSL 426

                         330
                  ....*....|....*....
gi 1270980525 730 LLVGLGIGATPMISIVKDI 748
Cdd:PLN02844  427 LLVAGGIGITPFLSILKEI 445
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
508-747 2.90e-19

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 91.49  E-value: 2.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 508 IIMVVLMAIAFtlatpwFRRGrvsFP-KPFHKLtgfnafwysHHLFVIVYTLLIVHGekLYITKTWY----KRTTW---M 579
Cdd:COG4097   135 YLLLALVVLSL------LRRR---LPyELWRLT---------HRLLAVAYLLLAFHH--LLLGGPFYwsppAGVLWaalA 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 580 YLTVPLVLYAgeRLLRAFRSSIKAVKILKVAVYPGNVLALHMSKPQG--YKYKSGQYMFVNCAAvSPF--EWHPFSITSA 655
Cdd:COG4097   195 AAGLAAAVYS--RLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDG-SPFweEAHPFSISSA 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 656 P-GDDYLSVHIRTLGDWTRQLKTVfsevcQPppnGKsgllradylqgennpdfpRVLIDGPYGA-PAQDYKNYEVVLLVG 733
Cdd:COG4097   272 PgGDGRLRFTIKALGDFTRRLGRL-----KP---GT------------------RVYVEGPYGRfTFDRRDTAPRQVWIA 325

                         250
                  ....*....|....
gi 1270980525 734 LGIGATPMISIVKD 747
Cdd:COG4097   326 GGIGITPFLALLRA 339
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 411-560 8.54e-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: 68.83  E-value: 8.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 411 LNMAIILFPVCRNT-ITWLRNktrlgvaVPFDDNLNFHKVIAVAIALGVGVHGLAHLTCDFPRvlnasedeeeTIEYYFR 489
Cdd:pfam01794   7 ALLPLLLLLALRNNpLEWLTG-------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF----------SLEGILD 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270980525 490 EQPTNYWWFikgvegvTGIIMVVLMAIAFTLATPWFRRGrvsfpkpfhkltGFNAFWYSHHLFVIVYTLLI 560
Cdd:pfam01794  70 LLLKRPYNI-------LGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHILLAVAFLLLV 121
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
172-304 4.44e-07

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 172 VEKRFDEITASTSGLLPRAKFGEcigmnkeskdFAGELYDALARRRNITTD-SINKAQLKEFWDQVADQSFDTRLQTFFD 250
Cdd:COG5126     7 LDRRFDLLDADGDGVLERDDFEA----------LFRRLWATLFSEADTDGDgRISREEFVAGMESLFEATVEPFARAAFD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1270980525 251 MVDKDADGRITEEEVREIIglsaSANRLStiqkqaDEYAAMIMEELDPNNLGYI 304
Cdd:COG5126    77 LLDTDGDGKISADEFRRLL----TALGVS------EEEADELFARLDTDGDGKI 120
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 244-312 7.52e-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: 7.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270980525 244 RLQTFFDMVDKDADGRITEEEVREIIGlsasanrlSTIQKQADEYAAMIMEELDPNNLGYIMIEnlEML 312
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALK--------SLGEGLSEEEIDEMIREVDKDGDGKIDFE--EFL 59
EF-hand_7 pfam13499
EF-hand domain pair;
242-304 1.68e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.40  E-value: 1.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270980525 242 DTRLQTFFDMVDKDADGRITEEEVREIIglsasaNRLSTIQKQADEYAAMIMEELDPNNLGYI 304
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLL------RKLEEGEPLSDEEVEELFKEFDLDKDGRI 57
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 249-269 9.34e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 34.66  E-value: 9.34e-03
                           10        20
                   ....*....|....*....|.
gi 1270980525  249 FDMVDKDADGRITEEEVREII 269
Cdd:smart00054   6 FRLFDKDGDGKIDFEEFKDLL 26
 
Name Accession Description Interval E-value
NADPH_Ox pfam08414
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ...
 143-243 2.80e-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: 2.80e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 143 FDRNKSAAAHALKGLKFISKTDGG--AGWAAVEKRFDEITAStsGLLPRAKFGECIGMnKESKDFAGELYDALARRRNIT 220
Cdd:pfam08414   1 LDRTKSGAARALKGLRFISKTDGGegAGWKAVEKRFDKLAVD--GLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77

                          90       100
                  ....*....|....*....|...
gi 1270980525 221 TDSINKAQLKEFWDQVADQSFDT 243
Cdd:pfam08414  78 GDSITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
726-912 2.17e-47

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 165.59  E-value: 2.17e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 726 YEVVLLVGLGIGATPMISIVKDIVNNMKAmdeeqnslenghggsnaasnaspniaqkrgksgsasgrnnFNTRRAYFYWV 805
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK----------------------------------------LKTKKIKFYWV 40

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 806 TREQGSFDWFKGIMNEAAEMDHKgVIEMHNYCTSVYEEGDARSALI-----TMLQSLHHAKNGVDIVsgtrvKSHFAKPN 880
Cdd:pfam08030  41 VRDLSSLEWFKDVLNELEELKEL-NIEIHIYLTGEYEAEDASDQSDssirsENFDSLMNEVIGVDFV-----EFHFGRPN 114

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1270980525 881 WRNVYKRIALNHPEAKVGVFYCGAPALTKELR 912
Cdd:pfam08030 115 WKEVLKDIAKQHPNGSIGVFSCGPPSLVDELR 146
FAD_binding_8 pfam08022
FAD-binding domain;
601-720 4.18e-47

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 163.28  E-value: 4.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 601 IKAVKILKVAVYPGNVLALHMSKPQG-YKYKSGQYMFVNC-AAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRQLKTV 678
Cdd:pfam08022   1 IFGVPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1270980525 679 FSEVCQpppngksgllradyLQGENNPDFPRVLIDGPYGAPA 720
Cdd:pfam08022  81 LSSSCP--------------KSPENGKDKPRVLIEGPYGPPS 108
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 606-933 6.86e-47

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: 166.71  E-value: 6.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 606 ILKVAVYP-GNVLALHMSKPQGYKYKSGQYMFVNCAAV-SPFEWHPFSITSAPGD--DYLSVHIRTL-GDWTRqlktvfs 680
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTR------- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 681 evcqpppngksglLRADYLQGENNPDFPRVLIDGPYGAPAQDYKNYEVVLLVGLGIGATPMISIVKDIVNNMkamdeeqn 760
Cdd:cd06186    74 -------------LLRKALKSPGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLLRRS-------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 761 slenghggsnaasnaspniaqkrgksgsasgRNNFNTRRAYFYWVTREQGSFDWFKGIMNEAAEMDHKGVIemHNYCTsv 840
Cdd:cd06186   133 -------------------------------SKTSRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEI--EIYVT-- 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 841 yeegdarsalitmlqslhhakngvdivsgtrvkshfakpnwrnvykrialnhpeakvGVFYCGAPALTKELRQHAldfSH 920
Cdd:cd06186   178 ---------------------------------------------------------RVVVCGPPGLVDDVRNAV---AK 197

                         330
                  ....*....|...
gi 1270980525 921 KTSTKFDFHKENF 933
Cdd:cd06186   198 KGGTGVEFHEESF 210
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 413-748 2.03e-23

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 106.47  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 413 MAIILFPVCRNTITWlrnktRLgVAVPFDDNLNFHKVIAVAIALGVGVHGLAHLTcdfprVLNASEDEEETIeyyFREQP 492
Cdd:PLN02844  167 LALLLLPVLRGLALF-----RL-LGIQFEASVRYHVWLGTSMIFFATVHGASTLF-----IWGISHHIQDEI---WKWQK 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 493 TNYWWFIKGVEGVTGIIMVVLmaiaftlATPWFRRGRvsfpkpfhkltgFNAFWYSHHLFVIVYTLLIVHGEKLYitktw 572
Cdd:PLN02844  233 TGRIYLAGEIALVTGLVIWIT-------SLPQIRRKR------------FEIFYYTHHLYIVFLIFFLFHAGDRH----- 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 573 ykrttwMYLTVP-LVLYAGERLLRAFRSSIKAVkILKVAVYPGNVLALHMSKPQGYKYKSGQYMFVNCAAVSPFEWHPFS 651
Cdd:PLN02844  289 ------FYMVFPgIFLFGLDKLLRIVQSRPETC-ILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFS 361

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 652 ITSAPG--DDYLSVHIRTLGDWTRQLKTVFSEVcqpppngksglLRADYLQGENNPdfprVLIDGPYGAPAQDYKNYEVV 729
Cdd:PLN02844  362 ITSSSNidDHTMSVIIKCEGGWTNSLYNKIQAE-----------LDSETNQMNCIP----VAIEGPYGPASVDFLRYDSL 426

                         330
                  ....*....|....*....
gi 1270980525 730 LLVGLGIGATPMISIVKDI 748
Cdd:PLN02844  427 LLVAGGIGITPFLSILKEI 445
PLN02631 PLN02631
ferric-chelate reductase
 495-749 2.75e-19

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 93.18  E-value: 2.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 495 YWWFIKGVEGVTGIIMVVLMAIAFTLATPWFRRGRvsfpkpfhkltgFNAFWYSHHLFVIVYTLLIVH-GEklyitktwy 573
Cdd:PLN02631  224 FAWNPTYVPNLAGTIAMVIGIAMWVTSLPSFRRKK------------FELFFYTHHLYGLYIVFYVIHvGD--------- 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 574 krtTWMYLTVP-LVLYAGERLLRaFRSSIKAVKILKVAVYPGNVLALHMSKPQGYKYKSGQYMFVNCAAVSPFEWHPFSI 652
Cdd:PLN02631  283 ---SWFCMILPnIFLFFIDRYLR-FLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTI 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 653 TSAPG--DDYLSVHIRTLGDWTRQLKTVFSevcqpppngksgllradylqgeNNPDFPRVLIDGPYGAPAQDYKNYEVVL 730
Cdd:PLN02631  359 TSSSNleKDTLSVVIRRQGSWTQKLYTHLS----------------------SSIDSLEVSTEGPYGPNSFDVSRHNSLI 416

                         250
                  ....*....|....*....
gi 1270980525 731 LVGLGIGATPMISIVKDIV 749
Cdd:PLN02631  417 LVSGGSGITPFISVIRELI 435
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
508-747 2.90e-19

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 91.49  E-value: 2.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 508 IIMVVLMAIAFtlatpwFRRGrvsFP-KPFHKLtgfnafwysHHLFVIVYTLLIVHGekLYITKTWY----KRTTW---M 579
Cdd:COG4097   135 YLLLALVVLSL------LRRR---LPyELWRLT---------HRLLAVAYLLLAFHH--LLLGGPFYwsppAGVLWaalA 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 580 YLTVPLVLYAgeRLLRAFRSSIKAVKILKVAVYPGNVLALHMSKPQG--YKYKSGQYMFVNCAAvSPF--EWHPFSITSA 655
Cdd:COG4097   195 AAGLAAAVYS--RLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDG-SPFweEAHPFSISSA 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 656 P-GDDYLSVHIRTLGDWTRQLKTVfsevcQPppnGKsgllradylqgennpdfpRVLIDGPYGA-PAQDYKNYEVVLLVG 733
Cdd:COG4097   272 PgGDGRLRFTIKALGDFTRRLGRL-----KP---GT------------------RVYVEGPYGRfTFDRRDTAPRQVWIA 325

                         250
                  ....*....|....
gi 1270980525 734 LGIGATPMISIVKD 747
Cdd:COG4097   326 GGIGITPFLALLRA 339
PLN02292 PLN02292
ferric-chelate reductase
 497-749 1.62e-18

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 90.70  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 497 WFIKGVEGVTGIIMVVLMAIAFTLATPWFRRgrvsfpkpfhklTGFNAFWYSHHLFvIVYTLLIVhgeklyitktWYKRT 576
Cdd:PLN02292  243 WDRTGVSNLAGEIALVAGLVMWATTYPKIRR------------RFFEVFFYTHYLY-IVFMLFFV----------FHVGI 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 577 TWMYLTVP-LVLYAGERLLRaFRSSIKAVKILKVAVYPGNVLALHMSKPQGYKYKSGQYMFVNCAAVSPFEWHPFSITSA 655
Cdd:PLN02292  300 SFALISFPgFYIFLVDRFLR-FLQSRNNVKLVSARVLPCDTVELNFSKNPMLMYSPTSIMFVNIPSISKLQWHPFTITSS 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 656 PG--DDYLSVHIRTLGDWTRQLKtvfsevcqpppngksgllraDYLQGENNPDFPRVLIDGPYGAPAQDYKNYEVVLLVG 733
Cdd:PLN02292  379 SKlePEKLSVMIKSQGKWSTKLY--------------------HMLSSSDQIDRLAVSVEGPYGPASTDFLRHESLVMVS 438

                         250
                  ....*....|....*.
gi 1270980525 734 LGIGATPMISIVKDIV 749
Cdd:PLN02292  439 GGSGITPFISIIRDLI 454
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 611-747 2.96e-14

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: 72.67  E-value: 2.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 611 VYPGNVLALHMSKPQgYKYKSGQYMFVNCAAVSPFEWHPFSITSAPGDDY-LSVHIRTLGDWTRQLKTvfsevcqpppng 689
Cdd:cd06198     6 VRPTTTLTLEPRGPA-LGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALGDYTRRLAE------------ 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1270980525 690 ksgLLRAdylqGEnnpdfpRVLIDGPYGAPAQDYKNYEVVLLVGlGIGATPMISIVKD 747
Cdd:cd06198    73 ---RLKP----GT------RVTVEGPYGRFTFDDRRARQIWIAG-GIGITPFLALLEA 116
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 411-560 8.54e-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: 68.83  E-value: 8.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 411 LNMAIILFPVCRNT-ITWLRNktrlgvaVPFDDNLNFHKVIAVAIALGVGVHGLAHLTCDFPRvlnasedeeeTIEYYFR 489
Cdd:pfam01794   7 ALLPLLLLLALRNNpLEWLTG-------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF----------SLEGILD 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270980525 490 EQPTNYWWFikgvegvTGIIMVVLMAIAFTLATPWFRRGrvsfpkpfhkltGFNAFWYSHHLFVIVYTLLI 560
Cdd:pfam01794  70 LLLKRPYNI-------LGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHILLAVAFLLLV 121
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 622-748 9.43e-13

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: 68.63  E-value: 9.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 622 SKPQGYKYKSGQYMFVNCAAVSPFEWHPFSITSAPGD-DYLSVHIRTLgdwtrqlktvfsevcqpPPNGKSGLLRADYLq 700
Cdd:cd00322    16 QLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEeGELELTVKIV-----------------PGGPFSAWLHDLKP- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1270980525 701 GEnnpdfpRVLIDGPYGAPAQDYKNYEVVLLVGLGIGATPMISIVKDI 748
Cdd:cd00322    78 GD------EVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHL 119
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
172-304 4.44e-07

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 172 VEKRFDEITASTSGLLPRAKFGEcigmnkeskdFAGELYDALARRRNITTD-SINKAQLKEFWDQVADQSFDTRLQTFFD 250
Cdd:COG5126     7 LDRRFDLLDADGDGVLERDDFEA----------LFRRLWATLFSEADTDGDgRISREEFVAGMESLFEATVEPFARAAFD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1270980525 251 MVDKDADGRITEEEVREIIglsaSANRLStiqkqaDEYAAMIMEELDPNNLGYI 304
Cdd:COG5126    77 LLDTDGDGKISADEFRRLL----TALGVS------EEEADELFARLDTDGDGKI 120
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 244-312 7.52e-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: 7.52e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270980525 244 RLQTFFDMVDKDADGRITEEEVREIIGlsasanrlSTIQKQADEYAAMIMEELDPNNLGYIMIEnlEML 312
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALK--------SLGEGLSEEEIDEMIREVDKDGDGKIDFE--EFL 59
EF-hand_7 pfam13499
EF-hand domain pair;
242-304 1.68e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.40  E-value: 1.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270980525 242 DTRLQTFFDMVDKDADGRITEEEVREIIglsasaNRLSTIQKQADEYAAMIMEELDPNNLGYI 304
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLL------RKLEEGEPLSDEEVEELFKEFDLDKDGRI 57
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 223-269 4.03e-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: 42.15  E-value: 4.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1270980525 223 SINKAQLKEFWDQVADQSFDTRLQTFFDMVDKDADGRITEEEVREII 269
Cdd:cd00051    16 TISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 624-748 6.27e-05

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: 45.28  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 624 PQGYKYKSGQYMFVNcAAVSPFEWHPFSITSAPGDD-YLSVHIRTlgdwtrqlktvfsevcqpPPNGK-SGLLRADYLQG 701
Cdd:cd06187    19 DQPLPFWAGQYVNVT-VPGRPRTWRAYSPANPPNEDgEIEFHVRA------------------VPGGRvSNALHDELKVG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1270980525 702 EnnpdfpRVLIDGPYGAPAQDYKNYEVVLLVGLGIGATPMISIVKDI 748
Cdd:cd06187    80 D------RVRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDA 120
FNR_like_1 cd06196
Ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain ...
 604-747 1.52e-04

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: 44.15  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 604 VKILKVAVYPGNVLALHMSKPQGYKYKSGQYMFVncaAVSPFEW----HPFSITSAPGDDYLSVHIRTlgdwtrqlktvf 679
Cdd:cd06196     3 VTLLSIEPVTHDVKRLRFDKPEGYDFTPGQATEV---AIDKPGWrdekRPFTFTSLPEDDVLEFVIKS------------ 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270980525 680 sevcQPPPNGKSGLLRaDYLQGEnnpdfpRVLIDGPYGapAQDYKNYEVVLLVGLGIgaTPMISIVKD 747
Cdd:cd06196    68 ----YPDHDGVTEQLG-RLQPGD------TLLIEDPWG--AIEYKGPGVFIAGGAGI--TPFIAILRD 120
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 627-746 5.40e-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: 42.70  E-value: 5.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 627 YKYKSGQYMFVNCAAVSPFEWHPFSITSA-PGDDYLSVHIRTLGdwtrqlktvfsevcqpppnGKSGLLrADYLQGENnp 705
Cdd:cd06192    23 RLFRPGQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRG-------------------PKTKLI-AELKPGEK-- 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1270980525 706 dfprVLIDGPYGAPAQDYKNYEVVLLVGLGIGATPMISIVK 746
Cdd:cd06192    81 ----LDVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAK 117
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 605-751 7.83e-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: 42.15  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 605 KILKVAVYPGNVLALHMSKPQGYKYKSGQYMFVNcaaVSPFEWHPFSITSAP-GDDYLSVHIRtlgdwtRQlktvfsevc 683
Cdd:cd06189     2 KVESIEPLNDDVYRVRLKPPAPLDFLAGQYLDLL---LDDGDKRPFSIASAPhEDGEIELHIR------AV--------- 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270980525 684 qppPNGKSGLLRADYLQgENNPdfprVLIDGPYGAPAQDYKNYEVVLLVGLGIGATPMISIVKDIVNN 751
Cdd:cd06189    64 ---PGGSFSDYVFEELK-ENGL----VRIEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQ 123
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 230-304 4.26e-03

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 39.87  E-value: 4.26e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270980525 230 KEFwDQVADQSFDTRLQTFFDMVDKDADGRITEEEVREIIglsasanrlSTIQKQA-DEYAAMIMEELDPNNLGYI 304
Cdd:cd16226    23 KEF-DQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWI---------KYVQKKYiREDVDRQWKEYDPNKDGKL 88
DHOD_e_trans_like1 cd06219
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 667-771 5.25e-03

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 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, and then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99815 [Multi-domain]  Cd Length: 248  Bit Score: 39.48  E-value: 5.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270980525 667 TLGDWTRQLKT---VFSEVcqpppnGKSGLLRADYLQGENNPDFprvliDGPYGAPAqDYKNYEVVLLVGLGIGATPMIS 743
Cdd:cd06219    47 TIADWDPEKGTitiVVQVV------GKSTRELATLEEGDKIHDV-----VGPLGKPS-EIENYGTVVFVGGGVGIAPIYP 114

                          90       100
                  ....*....|....*....|....*...
gi 1270980525 744 IvkdivnnMKAMDEEQNSLENGHGGSNA 771
Cdd:cd06219   115 I-------AKALKEAGNRVITIIGARTK 135
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 249-269 9.34e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 34.66  E-value: 9.34e-03
                           10        20
                   ....*....|....*....|.
gi 1270980525  249 FDMVDKDADGRITEEEVREII 269
Cdd:smart00054   6 FRLFDKDGDGKIDFEEFKDLL 26
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 244-269 9.95e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.30  E-value: 9.95e-03
                          10        20
                  ....*....|....*....|....*.
gi 1270980525 244 RLQTFFDMVDKDADGRITEEEVREII 269
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELL 26
 
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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