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Conserved domains on  [gi|296278229|ref|NP_078781|]
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NADPH oxidase 5 isoform 1 [Homo sapiens]

Protein Classification

ferric reductase family protein( domain architecture ID 13419158)

ferric reductase family protein functions as an oxidoreductase, such as human NADPH oxidase 1, a voltage-gated proton channel that mediates the H(+) currents of resting phagocytes and other tissues

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 448-765 1.05e-43

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: 156.70  E-value: 1.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 448 IMEVNLLP-SKVTHLLIKRPPFFHYRPGDYLYLNIPTIAR-YEWHPFTISSAPEQ-KDTIWLHIRSQGQWTNRLYEsfka 524
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLLSfWQSHPFTIASSPEDeQDTLSLIIRAKKGFTTRLLR---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 525 sdplgrgskrlsrsvtmrksqrsskgsEILLEKHKFCNIKCYIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIM 604
Cdd:cd06186   77 ---------------------------KALKSPGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 605 YRHQKRkhtcpscqhswiegvqdnMKLHKVDFIWINRDQRSFEWFVSLLTK-LEMDQAEeaqygrflELHMYMTsalgkn 683
Cdd:cd06186  130 RRSSKT------------------SRTRRVKLVWVVRDREDLEWFLDELRAaQELEVDG--------EIEIYVT------ 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 684 dmkaiglqmaldllankekkdsitglqtrtqpgrpdwskvfqkvaaekkgkvQVFFCGSPALAKVLKGHC---EKFGFRF 760
Cdd:cd06186  178 ----------------------------------------------------RVVVCGPPGLVDDVRNAVakkGGTGVEF 205


                 ....*
gi 296278229 761 FQENF 765
Cdd:cd06186  206 HEESF 210
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
42-197 3.49e-16

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 75.98  E-value: 3.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  42 DGEISLQEFKAALHvkesFFAERFFALFDSDRSGTITLQELQEALTLLIHGSPMDKLKFLFQVYDIDvcarqgasagtew 121
Cdd:COG5126   19 DGVLERDDFEALFR----RLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTD------------- 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296278229 122 gagagphwassplgtGSGSIDPDELRTVLqsclreSAISLPDEKLDqltlALFESADADGNGAITFEELRDELQRF 197
Cdd:COG5126   82 ---------------GDGKISADEFRRLL------TALGVSEEEAD----ELFARLDTDGDGKISFEEFVAAVRDY 132
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 296-402 5.75e-08

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: 51.89  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  296 LRATWLAQV--LPLDQNIQFHQLMGYVVVGLSLVHTVAHTVNFVlqaqaeasPFQFWELLLTtrpgigWVHGSASPTGVA 373
Cdd:pfam01794  17 LRNNPLEWLtgLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWL--------RFSLEGILDL------LLKRPYNILGII 82

                          90       100
                  ....*....|....*....|....*....
gi 296278229  374 LLLLLLLMFICSSSCIRRSGhFEVFYWTH 402
Cdd:pfam01794  83 ALVLLVLLAITSLPPFRRLS-YELFLYLH 110
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 448-765 1.05e-43

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: 156.70  E-value: 1.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 448 IMEVNLLP-SKVTHLLIKRPPFFHYRPGDYLYLNIPTIAR-YEWHPFTISSAPEQ-KDTIWLHIRSQGQWTNRLYEsfka 524
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLLSfWQSHPFTIASSPEDeQDTLSLIIRAKKGFTTRLLR---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 525 sdplgrgskrlsrsvtmrksqrsskgsEILLEKHKFCNIKCYIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIM 604
Cdd:cd06186   77 ---------------------------KALKSPGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 605 YRHQKRkhtcpscqhswiegvqdnMKLHKVDFIWINRDQRSFEWFVSLLTK-LEMDQAEeaqygrflELHMYMTsalgkn 683
Cdd:cd06186  130 RRSSKT------------------SRTRRVKLVWVVRDREDLEWFLDELRAaQELEVDG--------EIEIYVT------ 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 684 dmkaiglqmaldllankekkdsitglqtrtqpgrpdwskvfqkvaaekkgkvQVFFCGSPALAKVLKGHC---EKFGFRF 760
Cdd:cd06186  178 ----------------------------------------------------RVVVCGPPGLVDDVRNAVakkGGTGVEF 205


                 ....*
gi 296278229 761 FQENF 765
Cdd:cd06186  206 HEESF 210
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 381-610 4.16e-29

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 123.80  E-value: 4.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 381 MFICSSSCIRRSgHFEVFYWTHLSYLLVWLLLIFHGPNFWKWLLVPGI-LFFLEKAIGLAVSRmAAVCIMEVNLLPSKVT 459
Cdd:PLN02844 250 IWITSLPQIRRK-RFEIFYYTHHLYIVFLIFFLFHAGDRHFYMVFPGIfLFGLDKLLRIVQSR-PETCILSARLFPCKAI 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 460 HLLIKRPPFFHYRPGDYLYLNIPTIARYEWHPFTI-SSAPEQKDTIWLHIRSQGQWTNRLYESFKAsdplgrgskrlsrs 538
Cdd:PLN02844 328 ELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFSItSSSNIDDHTMSVIIKCEGGWTNSLYNKIQA-------------- 393

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296278229 539 vtmrksqrsskgsEILLEKHKFCNIKCYIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMYRHQKR 610
Cdd:PLN02844 394 -------------ELDSETNQMNCIPVAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSR 452
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
582-750 1.11e-26

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 106.27  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  582 EHAVLIGAGIGITPFASILQSIMYRHQKRKHTcpscqhswiegvqdnmklhKVDFIWINRDQRSFEWFvslltKLEMDQA 661
Cdd:pfam08030   2 ENVLLVAGGIGITPFISILKDLGNKSKKLKTK-------------------KIKFYWVVRDLSSLEWF-----KDVLNEL 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  662 EEaQYGRFLELHMYMTSALGKNDMKAIGLQMALDLLANKEKKDSITGLQTRTQPGRPDWSKVFQKVA-AEKKGKVQVFFC 740
Cdd:pfam08030  58 EE-LKELNIEIHIYLTGEYEAEDASDQSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAkQHPNGSIGVFSC 136

                         170
                  ....*....|
gi 296278229  741 GSPALAKVLK 750
Cdd:pfam08030 137 GPPSLVDELR 146
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
282-759 7.39e-21

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 96.12  E-value: 7.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 282 SFIAVLMLRrcLTWLRATWLaqvlPLDQNIQFHQLMGYVVVGLSLVHTVAHTVNFVLQAqaEASPFQFWELLLTTrpgig 361
Cdd:COG4097   55 SLQFLLAAR--PPWLERPFG----GLDRLYRLHKWLGILALVLALAHPLLLLGPKWLVG--WGGLPARLAALLTL----- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 362 wVHGSASPTG-VALLLLLLLMFIcssSCIRRSGHFEVFYWTHLSYLLVWLLLIFH---GPNFWKWLLVPGILFFLEKAIG 437
Cdd:COG4097  122 -LRGLAELLGeWAFYLLLALVVL---SLLRRRLPYELWRLTHRLLAVAYLLLAFHhllLGGPFYWSPPAGVLWAALAAAG 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 438 LA---VSRMAAVCIM--------EVNLLPSKVTHLLIK--RPPFFHYRPGDYLYLNIPTIA-RYEWHPFTISSAPEQKDT 503
Cdd:COG4097  198 LAaavYSRLGRPLRSrrhpyrveSVEPEAGDVVELTLRpeGGRWLGHRAGQFAFLRFDGSPfWEEAHPFSISSAPGGDGR 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 504 IWLHIRSQGQWTNRLyesfkasdplgrgskrlsrsvtmrksQRSSKGSEIllekhkfcnikcYIDGPYGTPT-RRIFASE 582
Cdd:COG4097  278 LRFTIKALGDFTRRL--------------------------GRLKPGTRV------------YVEGPYGRFTfDRRDTAP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 583 HAVLIGAGIGITPFASILQSimyrHQKRKHTCPscqhswiegvqdnmklhKVDFIWINRDQRSFEwFVSLLTKLemdqae 662
Cdd:COG4097  320 RQVWIAGGIGITPFLALLRA----LAARPGDQR-----------------PVDLFYCVRDEEDAP-FLEELRAL------ 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 663 eAQYGRFLELHMYMTSALGKNDMKAIglqmaldllankekkdsitglqTRTQPGRPDWSkvfqkvaaekkgkvqVFFCGS 742
Cdd:COG4097  372 -AARLAGLRLHLVVSDEDGRLTAERL----------------------RRLVPDLAEAD---------------VFFCGP 413

                        490       500
                 ....*....|....*....|....*....
gi 296278229 743 PALAKVLKG------------HCEKFGFR 759
Cdd:COG4097  414 PGMMDALRRdlralgvparriHQERFEFR 442
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
42-197 3.49e-16

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 75.98  E-value: 3.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  42 DGEISLQEFKAALHvkesFFAERFFALFDSDRSGTITLQELQEALTLLIHGSPMDKLKFLFQVYDIDvcarqgasagtew 121
Cdd:COG5126   19 DGVLERDDFEALFR----RLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTD------------- 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296278229 122 gagagphwassplgtGSGSIDPDELRTVLqsclreSAISLPDEKLDqltlALFESADADGNGAITFEELRDELQRF 197
Cdd:COG5126   82 ---------------GDGKISADEFRRLL------TALGVSEEEAD----ELFARLDTDGDGKISFEEFVAAVRDY 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 97-192 3.72e-09

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: 53.32  E-value: 3.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  97 KLKFLFQVYDIDvcarqgasagtewgagagphwassplgtGSGSIDPDELRTVLQSCLResaiSLPDEKLDQLtlalFES 176
Cdd:cd00051    1 ELREAFRLFDKD----------------------------GDGTISADELKAALKSLGE----GLSEEEIDEM----IRE 44

                         90
                 ....*....|....*.
gi 296278229 177 ADADGNGAITFEELRD 192
Cdd:cd00051   45 VDKDGDGKIDFEEFLE 60
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 296-402 5.75e-08

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: 51.89  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  296 LRATWLAQV--LPLDQNIQFHQLMGYVVVGLSLVHTVAHTVNFVlqaqaeasPFQFWELLLTtrpgigWVHGSASPTGVA 373
Cdd:pfam01794  17 LRNNPLEWLtgLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWL--------RFSLEGILDL------LLKRPYNILGII 82

                          90       100
                  ....*....|....*....|....*....
gi 296278229  374 LLLLLLLMFICSSSCIRRSGhFEVFYWTH 402
Cdd:pfam01794  83 ALVLLVLLAITSLPPFRRLS-YELFLYLH 110
EF-hand_7 pfam13499
EF-hand domain pair;
95-189 2.70e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229   95 MDKLKFLFQVYDIDvcarqgasagtewgagagphwassplgtGSGSIDPDELRTVLQSCLResAISLPDEKLDQLtlalF 174
Cdd:pfam13499   1 EEKLKEAFKLLDSD----------------------------GDGYLDVEELKKLLRKLEE--GEPLSDEEVEEL----F 46

                          90
                  ....*....|....*
gi 296278229  175 ESADADGNGAITFEE 189
Cdd:pfam13499  47 KEFDLDKDGRISFEE 61
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 63-89 2.29e-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: 35.82  E-value: 2.29e-03
                           10        20
                   ....*....|....*....|....*..
gi 296278229    63 ERFFALFDSDRSGTITLQELQEALTLL 89
Cdd:smart00054   3 KEAFRLFDKDGDGKIDFEEFKDLLKAL 29
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
42-87 3.98e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 39.66  E-value: 3.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 296278229  42 DGEISLQEFKAALHVKESFF-AERFFALFDSDRSGTITLQELQEALT 87
Cdd:NF041410 117 DGSISSDELSAGLTSAGSSAdSSQLFSALDSDGDGSVSSDELAAALQ 163
 
Name Accession Description Interval E-value
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 448-765 1.05e-43

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: 156.70  E-value: 1.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 448 IMEVNLLP-SKVTHLLIKRPPFFHYRPGDYLYLNIPTIAR-YEWHPFTISSAPEQ-KDTIWLHIRSQGQWTNRLYEsfka 524
Cdd:cd06186    1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLLSfWQSHPFTIASSPEDeQDTLSLIIRAKKGFTTRLLR---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 525 sdplgrgskrlsrsvtmrksqrsskgsEILLEKHKFCNIKCYIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIM 604
Cdd:cd06186   77 ---------------------------KALKSPGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 605 YRHQKRkhtcpscqhswiegvqdnMKLHKVDFIWINRDQRSFEWFVSLLTK-LEMDQAEeaqygrflELHMYMTsalgkn 683
Cdd:cd06186  130 RRSSKT------------------SRTRRVKLVWVVRDREDLEWFLDELRAaQELEVDG--------EIEIYVT------ 177

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 684 dmkaiglqmaldllankekkdsitglqtrtqpgrpdwskvfqkvaaekkgkvQVFFCGSPALAKVLKGHC---EKFGFRF 760
Cdd:cd06186  178 ----------------------------------------------------RVVVCGPPGLVDDVRNAVakkGGTGVEF 205


                 ....*
gi 296278229 761 FQENF 765
Cdd:cd06186  206 HEESF 210
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 381-610 4.16e-29

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 123.80  E-value: 4.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 381 MFICSSSCIRRSgHFEVFYWTHLSYLLVWLLLIFHGPNFWKWLLVPGI-LFFLEKAIGLAVSRmAAVCIMEVNLLPSKVT 459
Cdd:PLN02844 250 IWITSLPQIRRK-RFEIFYYTHHLYIVFLIFFLFHAGDRHFYMVFPGIfLFGLDKLLRIVQSR-PETCILSARLFPCKAI 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 460 HLLIKRPPFFHYRPGDYLYLNIPTIARYEWHPFTI-SSAPEQKDTIWLHIRSQGQWTNRLYESFKAsdplgrgskrlsrs 538
Cdd:PLN02844 328 ELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFSItSSSNIDDHTMSVIIKCEGGWTNSLYNKIQA-------------- 393

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296278229 539 vtmrksqrsskgsEILLEKHKFCNIKCYIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMYRHQKR 610
Cdd:PLN02844 394 -------------ELDSETNQMNCIPVAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSSR 452
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
582-750 1.11e-26

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 106.27  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  582 EHAVLIGAGIGITPFASILQSIMYRHQKRKHTcpscqhswiegvqdnmklhKVDFIWINRDQRSFEWFvslltKLEMDQA 661
Cdd:pfam08030   2 ENVLLVAGGIGITPFISILKDLGNKSKKLKTK-------------------KIKFYWVVRDLSSLEWF-----KDVLNEL 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  662 EEaQYGRFLELHMYMTSALGKNDMKAIGLQMALDLLANKEKKDSITGLQTRTQPGRPDWSKVFQKVA-AEKKGKVQVFFC 740
Cdd:pfam08030  58 EE-LKELNIEIHIYLTGEYEAEDASDQSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAkQHPNGSIGVFSC 136

                         170
                  ....*....|
gi 296278229  741 GSPALAKVLK 750
Cdd:pfam08030 137 GPPSLVDELR 146
PLN02631 PLN02631
ferric-chelate reductase
 299-616 1.90e-23

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 105.89  E-value: 1.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 299 TWLAQVLPL-----DQNIQFHQLMGYVVVGLSLVHTVAHTVnfvlqaqaeaspfqFWELLLTTRPGIGWvhgsaSPT--- 370
Cdd:PLN02631 172 TRASTILPLvgltsESSIKYHIWLGHVSNFLFLVHTVVFLI--------------YWAMINKLMETFAW-----NPTyvp 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 371 ---GVALLLLLLLMFICSSSCIRRSgHFEVFYWTHLSYLLVWLLLIFHGPNFWKWLLVPGI-LFFLEKAIGLAVSRMAAV 446
Cdd:PLN02631 233 nlaGTIAMVIGIAMWVTSLPSFRRK-KFELFFYTHHLYGLYIVFYVIHVGDSWFCMILPNIfLFFIDRYLRFLQSTKRSR 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 447 cIMEVNLLPSKVTHLLIKRPPFFHYRPGDYLYLNIPTIARYEWHPFTISSAPE-QKDTIWLHIRSQGQWTNRLYesfkas 525
Cdd:PLN02631 312 -LVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNlEKDTLSVVIRRQGSWTQKLY------ 384

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 526 dplgrgsKRLSRSVTmrksqrsskgseillekhkfcNIKCYIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMY 605
Cdd:PLN02631 385 -------THLSSSID---------------------SLEVSTEGPYGPNSFDVSRHNSLILVSGGSGITPFISVIRELIF 436

                        330
                 ....*....|.
gi 296278229 606 RHQKRKHTCPS 616
Cdd:PLN02631 437 QSQNPSTKLPD 447
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 458-763 3.68e-22

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: 95.59  E-value: 3.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 458 VTHLLIKRPPFFHYRPGDYLYLNIPTIARYEWHPFTISSAPEQKDTIWLHIRSqgqwtnrlyesfkasDPLGRGSKRLSR 537
Cdd:cd00322   10 VRLFRLQLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEEGELELTVKI---------------VPGGPFSAWLHD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 538 SvtmrksqrsSKGSEILlekhkfcnikcyIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMYRHQKRKHTcpsc 617
Cdd:cd00322   75 L---------KPGDEVE------------VSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEIT---- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 618 qhswiegvqdnmklhkvdFIWINRDQRSFeWFVSLLTKLemdqaeeAQYGRFLELHMYMTSalgkndmkaiglqmaldll 697
Cdd:cd00322  130 ------------------LLYGARTPADL-LFLDELEEL-------AKEGPNFRLVLALSR------------------- 164

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296278229 698 ankekkDSITGLQTRTQPGRPDwskvFQKVAAEKKGKVQVFFCGSPALAKVLKGHCEKFG---FRFFQE 763
Cdd:cd00322  165 ------ESEAKLGPGGRIDREA----EILALLPDDSGALVYICGPPAMAKAVREALVSLGvpeERIHTE 223
PLN02292 PLN02292
ferric-chelate reductase
 305-615 2.25e-21

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 99.56  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 305 LPLDQNIQFHQLMGYVVVGLSLVHTVAHTVNFvlqaqaeASPFQFWELLLTTRPGIGWVHGSASptgvalLLLLLLMFIC 384
Cdd:PLN02292 200 LTSESSIKYHIWLGHLVMTLFTSHGLCYIIYW-------ISMNQVSQMLEWDRTGVSNLAGEIA------LVAGLVMWAT 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 385 SSSCIRRSgHFEVFYWTHLSYLLVWLLLIFHGPNFWKWLLVPGILFFLEKAIGLAVSRMAAVCIMEVNLLPSKVTHLLIK 464
Cdd:PLN02292 267 TYPKIRRR-FFEVFFYTHYLYIVFMLFFVFHVGISFALISFPGFYIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNFS 345

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 465 RPPFFHYRPGDYLYLNIPTIARYEWHPFTI-SSAPEQKDTIWLHIRSQGQWTNRLYESFKASDPLgrgsKRLSRSVtmrk 543
Cdd:PLN02292 346 KNPMLMYSPTSIMFVNIPSISKLQWHPFTItSSSKLEPEKLSVMIKSQGKWSTKLYHMLSSSDQI----DRLAVSV---- 417

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296278229 544 sqrsskgseillekhkfcnikcyiDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMYRHQKRKHTCP 615
Cdd:PLN02292 418 ------------------------EGPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLIYTSSTETCKIP 465
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
282-759 7.39e-21

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 96.12  E-value: 7.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 282 SFIAVLMLRrcLTWLRATWLaqvlPLDQNIQFHQLMGYVVVGLSLVHTVAHTVNFVLQAqaEASPFQFWELLLTTrpgig 361
Cdd:COG4097   55 SLQFLLAAR--PPWLERPFG----GLDRLYRLHKWLGILALVLALAHPLLLLGPKWLVG--WGGLPARLAALLTL----- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 362 wVHGSASPTG-VALLLLLLLMFIcssSCIRRSGHFEVFYWTHLSYLLVWLLLIFH---GPNFWKWLLVPGILFFLEKAIG 437
Cdd:COG4097  122 -LRGLAELLGeWAFYLLLALVVL---SLLRRRLPYELWRLTHRLLAVAYLLLAFHhllLGGPFYWSPPAGVLWAALAAAG 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 438 LA---VSRMAAVCIM--------EVNLLPSKVTHLLIK--RPPFFHYRPGDYLYLNIPTIA-RYEWHPFTISSAPEQKDT 503
Cdd:COG4097  198 LAaavYSRLGRPLRSrrhpyrveSVEPEAGDVVELTLRpeGGRWLGHRAGQFAFLRFDGSPfWEEAHPFSISSAPGGDGR 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 504 IWLHIRSQGQWTNRLyesfkasdplgrgskrlsrsvtmrksQRSSKGSEIllekhkfcnikcYIDGPYGTPT-RRIFASE 582
Cdd:COG4097  278 LRFTIKALGDFTRRL--------------------------GRLKPGTRV------------YVEGPYGRFTfDRRDTAP 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 583 HAVLIGAGIGITPFASILQSimyrHQKRKHTCPscqhswiegvqdnmklhKVDFIWINRDQRSFEwFVSLLTKLemdqae 662
Cdd:COG4097  320 RQVWIAGGIGITPFLALLRA----LAARPGDQR-----------------PVDLFYCVRDEEDAP-FLEELRAL------ 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 663 eAQYGRFLELHMYMTSALGKNDMKAIglqmaldllankekkdsitglqTRTQPGRPDWSkvfqkvaaekkgkvqVFFCGS 742
Cdd:COG4097  372 -AARLAGLRLHLVVSDEDGRLTAERL----------------------RRLVPDLAEAD---------------VFFCGP 413

                        490       500
                 ....*....|....*....|....*....
gi 296278229 743 PALAKVLKG------------HCEKFGFR 759
Cdd:COG4097  414 PGMMDALRRdlralgvparriHQERFEFR 442
FAD_binding_8 pfam08022
FAD-binding domain;
451-575 1.89e-18

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 81.23  E-value: 1.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  451 VNLLPSKVTHLLIKRPP-FFHYRPGDYLYLNI-PTIARYEWHPFTISSAPEQkDTIWLHIRSQGQWTNRLYesfkasdpl 528
Cdd:pfam08022   9 VALLPDNVLKLRVSKPKkPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSD-DKLSLHIKVKGGWTRKLA--------- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 296278229  529 grgsKRLSRSvtmrksqrSSKGSEILLEKhkfcnIKCYIDGPYGTPT 575
Cdd:pfam08022  79 ----NYLSSS--------CPKSPENGKDK-----PRVLIEGPYGPPS 108
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 467-765 2.45e-17

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: 81.53  E-value: 2.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 467 PFFHYRPGDYLYLNIPTIARYEWHPFTISSAPEQKDTIWLHIRSQGQWTNRLYESFKASDPLgrgskrlsrsvtmrksqr 546
Cdd:cd06198   19 PALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGRLRFTIKALGDYTRRLAERLKPGTRV------------------ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 547 sskgseillekhkfcnikcYIDGPYGTPTRRIfASEHAVLIGAGIGITPFASILQSimyrHQKRKHTCPscqhswiegvq 626
Cdd:cd06198   81 -------------------TVEGPYGRFTFDD-RRARQIWIAGGIGITPFLALLEA----LAARGDARP----------- 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 627 dnmklhkVDFIWINRDQRSFeWFVSLLTKLemdqAEEAQYgrflELHMYMTSalgkndmkaiglqmaldllanKEKKDSI 706
Cdd:cd06198  126 -------VTLFYCVRDPEDA-VFLDELRAL----AAAAGV----VLHVIDSP---------------------SDGRLTL 168

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296278229 707 TGLQTRTQPGRPDWSkvfqkvaaekkgkvqVFFCGSPALAKVLKGHCEKFGF---RFFQENF 765
Cdd:cd06198  169 EQLVRALVPDLADAD---------------VWFCGPPGMADALEKGLRALGVparRFHYERF 215
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
42-197 3.49e-16

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 75.98  E-value: 3.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  42 DGEISLQEFKAALHvkesFFAERFFALFDSDRSGTITLQELQEALTLLIHGSPMDKLKFLFQVYDIDvcarqgasagtew 121
Cdd:COG5126   19 DGVLERDDFEALFR----RLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTD------------- 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296278229 122 gagagphwassplgtGSGSIDPDELRTVLqsclreSAISLPDEKLDqltlALFESADADGNGAITFEELRDELQRF 197
Cdd:COG5126   82 ---------------GDGKISADEFRRLL------TALGVSEEEAD----ELFARLDTDGDGKISFEEFVAAVRDY 132
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 448-609 2.82e-11

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


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 64.50  E-value: 2.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 448 IMEVNLLPSKVTHLLIKRPPF-FHYRPGDYLYLNIPtiARYEWHPFTISSAPEQKDTIWLHIRSqgqwtnrlyesfkasd 526
Cdd:COG0543    2 VVSVERLAPDVYLLRLEAPLIaLKFKPGQFVMLRVP--GDGLRRPFSIASAPREDGTIELHIRV---------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 527 pLGRGSKRLSRsvtMRKsqrsskGSEILLEkhkfcnikcyidGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMYR 606
Cdd:COG0543   64 -VGKGTRALAE---LKP------GDELDVR------------GPLGNGFPLEDSGRPVLLVAGGTGLAPLRSLAEALLAR 121


                 ...
gi 296278229 607 HQK 609
Cdd:COG0543  122 GRR 124
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
458-763 2.09e-09

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


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 58.65  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 458 VTHLLIKRP---PFFHYRPGDYLYLNIPTIARYEWHPFTISSAPEQkDTIWLHIRsqgqwtnRlyesfkasDPLGRGSKR 534
Cdd:COG1018   18 VVSFTLEPPdgaPLPRFRPGQFVTLRLPIDGKPLRRAYSLSSAPGD-GRLEITVK-------R--------VPGGGGSNW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 535 LSRSVTmrksqrssKGSEILlekhkfcnikcyIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMYRHQKRkhtc 614
Cdd:COG1018   82 LHDHLK--------VGDTLE------------VSGPRGDFVLDPEPARPLLLIAGGIGITPFLSMLRTLLARGPFR---- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 615 pscqhswiegvqdnmklhKVDFIWINRDQRSFeWFVSLLTKLemdqaeEAQYGRFlELHMYMTSAlgkndmkaiglqmal 694
Cdd:COG1018  138 ------------------PVTLVYGARSPADL-AFRDELEAL------AARHPRL-RLHPVLSRE--------------- 176

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296278229 695 dllankekkdsitglqTRTQPGRPDWSKVfQKVAAEKKGkVQVFFCGSPALAKVLKGHCEKFGF---RFFQE 763
Cdd:COG1018  177 ----------------PAGLQGRLDAELL-AALLPDPAD-AHVYLCGPPPMMEAVRAALAELGVpeeRIHFE 230
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
17-158 2.37e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.34  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  17 GTMSAEE-DARWLRWVTQQFKTI-AGEDGEISLQEFKAALHVKESF----FAERFFALFDSDRSGTITLQELQEALTLLi 90
Cdd:COG5126   20 GVLERDDfEALFRRLWATLFSEAdTDGDGRISREEFVAGMESLFEAtvepFARAAFDLLDTDGDGKISADEFRRLLTAL- 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296278229  91 hGSPMDKLKFLFQVYDIDvcarqgasagtewgagagphwassplgtGSGSIDPDELRTVLQSCLRESA 158
Cdd:COG5126   99 -GVSEEEADELFARLDTD----------------------------GDGKISFEEFVAAVRDYYTPDA 137
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 97-192 3.72e-09

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: 53.32  E-value: 3.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  97 KLKFLFQVYDIDvcarqgasagtewgagagphwassplgtGSGSIDPDELRTVLQSCLResaiSLPDEKLDQLtlalFES 176
Cdd:cd00051    1 ELREAFRLFDKD----------------------------GDGTISADELKAALKSLGE----GLSEEEIDEM----IRE 44

                         90
                 ....*....|....*.
gi 296278229 177 ADADGNGAITFEELRD 192
Cdd:cd00051   45 VDKDGDGKIDFEEFLE 60
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 296-402 5.75e-08

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: 51.89  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  296 LRATWLAQV--LPLDQNIQFHQLMGYVVVGLSLVHTVAHTVNFVlqaqaeasPFQFWELLLTtrpgigWVHGSASPTGVA 373
Cdd:pfam01794  17 LRNNPLEWLtgLSYDRLLLFHRWLGRLAFLLALLHVILYLIYWL--------RFSLEGILDL------LLKRPYNILGII 82

                          90       100
                  ....*....|....*....|....*....
gi 296278229  374 LLLLLLLMFICSSSCIRRSGhFEVFYWTH 402
Cdd:pfam01794  83 ALVLLVLLAITSLPPFRRLS-YELFLYLH 110
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 62-151 3.02e-07

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: 47.93  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  62 AERFFALFDSDRSGTITLQELQEALTLLIHGSPMDKLKFLFQVYDIDvcarqgasagtewgagagphwassplgtGSGSI 141
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKD----------------------------GDGKI 53

                         90
                 ....*....|
gi 296278229 142 DPDELRTVLQ 151
Cdd:cd00051   54 DFEEFLELMA 63
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 42-87 1.00e-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: 43.69  E-value: 1.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 296278229  42 DGEISLQEFKAALHVKESFF----AERFFALFDSDRSGTITLQELQEALT 87
Cdd:cd00051   14 DGTISADELKAALKSLGEGLseeeIDEMIREVDKDGDGKIDFEEFLELMA 63
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 451-611 2.12e-05

NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron transfer from iron complexes or iron proteins. Structurally similar to ferredoxin reductases, but with only 15% sequence identity, flavin reductases reduce FAD, FMN, or riboflavin via NAD(P)H. Flavin is used as a substrate, rather than a tightly bound prosthetic group as in flavoenzymes; weaker binding is due to the absence of a binding site for the AMP moeity of FAD.


Pssm-ID: 99786 [Multi-domain]  Cd Length: 224  Bit Score: 46.39  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 451 VNLLPSKVTHLLIKRPPFFHYRPGDYLYLNIPTIARYewhPFTISSAPEQKDTIWLHIR--SQGQWTNRLYESFKASDpl 528
Cdd:cd06189    6 IEPLNDDVYRVRLKPPAPLDFLAGQYLDLLLDDGDKR---PFSIASAPHEDGEIELHIRavPGGSFSDYVFEELKENG-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 529 grgskrlsrsvTMRksqrsskgseillekhkfcnikcyIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMYRHQ 608
Cdd:cd06189   81 -----------LVR------------------------IEGPLGDFFLREDSDRPLILIAGGTGFAPIKSILEHLLAQGS 125


                 ...
gi 296278229 609 KRK 611
Cdd:cd06189  126 KRP 128
EF-hand_7 pfam13499
EF-hand domain pair;
95-189 2.70e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229   95 MDKLKFLFQVYDIDvcarqgasagtewgagagphwassplgtGSGSIDPDELRTVLQSCLResAISLPDEKLDQLtlalF 174
Cdd:pfam13499   1 EEKLKEAFKLLDSD----------------------------GDGYLDVEELKKLLRKLEE--GEPLSDEEVEEL----F 46

                          90
                  ....*....|....*
gi 296278229  175 ESADADGNGAITFEE 189
Cdd:pfam13499  47 KEFDLDKDGRISFEE 61
EF-hand_7 pfam13499
EF-hand domain pair;
62-108 3.81e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.24  E-value: 3.81e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 296278229   62 AERFFALFDSDRSGTITLQELQEALTLLIHGSPMDK--LKFLFQVYDID 108
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDeeVEELFKEFDLD 52
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 68-106 3.91e-05

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 44.57  E-value: 3.91e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 296278229  68 LFDSDRSGTITLQELQEALTLLIHGSPMDKLKFLFQVYD 106
Cdd:cd15901   62 LYDRNRTGCIRLLSVKIALITLCAASLLDKYRYLFGQLA 100
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 448-610 5.75e-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: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 448 IMEVNLLPSKVTHLLIKRPPFFHYRPGDYLYLNIPTiARYEWHPFTISSAPEQKDTIWLHIR--SQGQWTNRLYESFKAS 525
Cdd:cd06187    1 VVSVERLTHDIAVVRLQLDQPLPFWAGQYVNVTVPG-RPRTWRAYSPANPPNEDGEIEFHVRavPGGRVSNALHDELKVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 526 DPLgrgskrlsrsvtmrksqrsskgseillekhkfcnikcYIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMY 605
Cdd:cd06187   80 DRV-------------------------------------RLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDALR 122


                 ....*
gi 296278229 606 RHQKR 610
Cdd:cd06187  123 RGEPR 127
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 30-190 6.53e-05

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 44.14  E-value: 6.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  30 WVTQQFKTIAGEDGEISLQEFKAAL--HVKESFFAERFF---------ALFDSDRSGTItlqELQEALTLLIHgspMDKL 98
Cdd:cd16182    1 QVRELFEKLAGEDEEIDAVELQKLLnaSLLKDMPKFDGFsletcrsliALMDTNGSGRL---DLEEFKTLWSD---LKKW 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  99 KFLFQVYDIDvcarqgasagtewgagagphwassplgtGSGSIDPDELRTVLQSClresAISLPDEKLDQLTLALfesad 178
Cdd:cd16182   75 QAIFKKFDTD----------------------------RSGTLSSYELRKALESA----GFHLSNKVLQALVLRY----- 117

                        170
                 ....*....|..
gi 296278229 179 ADGNGAITFEEL 190
Cdd:cd16182  118 ADSTGRITFEDF 129
FNR1 cd06195
Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible ...
 463-601 2.41e-04

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


Pssm-ID: 99792 [Multi-domain]  Cd Length: 241  Bit Score: 43.32  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 463 IKRPPFFHYRPGDYLYLNIPT-----IARyewhPFTISSAPEQKdtiWLHIRS----QGQWTNRLYesfkasdplgrgsk 533
Cdd:cd06195   17 VTRDIPFRFQAGQFTKLGLPNddgklVRR----AYSIASAPYEE---NLEFYIilvpDGPLTPRLF-------------- 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296278229 534 RLSRsvtmrksqrsskGSEILLEKhkfcnikcyidGPYGTPT-RRIFASEHAVLIGAGIGITPFASILQ 601
Cdd:cd06195   76 KLKP------------GDTIYVGK-----------KPTGFLTlDEVPPGKRLWLLATGTGIAPFLSMLR 121
EF-hand_6 pfam13405
EF-hand domain;
63-89 3.33e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 38.31  E-value: 3.33e-04
                          10        20
                  ....*....|....*....|....*..
gi 296278229   63 ERFFALFDSDRSGTITLQELQEALTLL 89
Cdd:pfam13405   3 REAFKLFDKDGDGKISLEELRKALRSL 29
phenol_2-monooxygenase_like cd06211
Phenol 2-monooxygenase (phenol hydroxylase) is a flavoprotein monooxygenase, able to use ...
 457-611 3.52e-04

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


Pssm-ID: 99807  Cd Length: 238  Bit Score: 42.70  E-value: 3.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 457 KVTHLLIKRPPFFHYRPGDYLYLNIPTIARYEwhPFTISSAPEQKDTIWLHIR--SQGQWTNRLYESFKASDPLGrgskr 534
Cdd:cd06211   22 KGVRLKLDEPEEIEFQAGQYVNLQAPGYEGTR--AFSIASSPSDAGEIELHIRlvPGGIATTYVHKQLKEGDELE----- 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296278229 535 lsrsvtmrksqrsskgseillekhkfcnikcyIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMYRHQKRK 611
Cdd:cd06211   95 --------------------------------ISGPYGDFFVRDSDQRPIIFIAGGSGLSSPRSMILDLLERGDTRK 139
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 63-89 4.68e-04

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: 37.77  E-value: 4.68e-04
                          10        20
                  ....*....|....*....|....*..
gi 296278229   63 ERFFALFDSDRSGTITLQELQEALTLL 89
Cdd:pfam00036   3 KEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 42-106 7.42e-04

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 41.05  E-value: 7.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  42 DGEISLQEFkAALH-----VKESFFAerffalFDSDRSGTITLQELQEALTLLIHGSPMDKLKFLFQVYD 106
Cdd:cd16185   50 NGTIDFEEF-AALHqflsnMQNGFEQ------RDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFD 112
flavohem_like_fad_nad_binding cd06184
FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain ...
 585-632 7.74e-04

FAD_NAD(P)H binding domain of flavohemoglobin. Flavohemoglobins have a globin domain containing a B-type heme fused with a ferredoxin reductase-like FAD/NAD-binding domain. Flavohemoglobins detoxify nitric oxide (NO) via an NO dioxygenase reaction. The hemoglobin domain adopts a globin fold with an embedded heme molecule. Flavohemoglobins also have a C-terminal reductase domain with bindiing sites for FAD and NAD(P)H. This domain catalyzes the conversion of NO + O2 + NAD(P)H to NO3- + NAD(P)+. Instead of the oxygen transport function of hemoglobins, flavohemoglobins seem to act in NO dioxygenation and NO signalling.


Pssm-ID: 99781  Cd Length: 247  Bit Score: 41.77  E-value: 7.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 296278229 585 VLIGAGIGITPFASILQSIMYRHQKRK----HTCPSCQH-------SWIEGVQDNMKLH 632
Cdd:cd06184  117 VLISAGVGITPMLSMLEALAAEGPGRPvtfiHAARNSAVhafrdelEELAARLPNLKLH 175
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 62-197 1.08e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 40.59  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  62 AERFFALFDSDRSGTITLQELQEALTLLIHGSP-MDKLKFLFQVYDIDvcarqgasagtewgagagphwassplgtGSGS 140
Cdd:cd16180    2 LRRIFQAVDRDRSGRISAKELQRALSNGDWTPFsIETVRLMINMFDRD----------------------------RSGT 53

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296278229 141 IDPDELrTVLQSCLRESAislpdekldqltlALFESADADGNGAITFEELRDELQRF 197
Cdd:cd16180   54 INFDEF-VGLWKYIQDWR-------------RLFRRFDRDRSGSIDFNELQNALSSF 96
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 63-89 2.29e-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: 35.82  E-value: 2.29e-03
                           10        20
                   ....*....|....*....|....*..
gi 296278229    63 ERFFALFDSDRSGTITLQELQEALTLL 89
Cdd:smart00054   3 KEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 35-152 2.49e-03

Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), calpain-B (CalpB), and similar proteins; The family contains two calpains that have been found in Drosophila, CalpA and CalpB. CalpA, also termed calcium-activated neutral proteinase A (CANP A), or calpain-A catalytic subunit, is a Drosophila calpain homolog specifically expressed in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. CalpB, also termed calcium-activated neutral proteinase B (CANP B), contains calpain-B catalytic subunit 1 and calpain-B catalytic subunit 2. Both CalpA and CalpB are closely related to that of vertebrate calpains, and they share similar domain architecture, which consists of four domains: the N-terminal domain I, the catalytic domain II carrying the three active site residues, Cys, His and Asn, the Ca2+-regulated phospholipid-binding domain III, and penta-EF-hand Ca2+-binding domain IV. Besides, CalpA and CalpB display some distinguishing structural features that are not found in mammalian typical calpains. CalpA harbors a 76 amino acid long hydrophobic stretch inserted in domain IV, which may be involved in membrane attachment of this enzyme. CalpB has an unusually long N-terminal tail of 224 amino acids, which belongs to the class of intrinsically unstructured proteins (IUP) and may become ordered upon binding to target protein(s). Moreover, they do not need small regulatory subunits for their catalytic activity, and their proteolytic function is not regulated by an intrinsic inhibitor as the Drosophila genome contains neither regulatory subunit nor calpastatin orthologs. As a result, they may exist as a monomer or perhaps as a homo- or heterodimer together with a second large subunit. Furthermore, both CalpA and CalpB are dispensable for viability and fertility and do not share vital functions during Drosophila development. Phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol, and phosphatidic acid can stimulate the activity and the rate of activation of CalpA, but not CalpB. Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis. CalpB directly interacts with talin, an important component of the focal adhesion complex, and functions as an important modulator in border cell migration within egg chambers, which may act via the digestion of talin. CalpB can be phosphorylated by cAMP-dependent protein kinase (protein kinase A, PKA; EC 2.7.11.11) at Ser240 and Ser845, as well as by mitogen-activated protein kinase (ERK1 and ERK2; EC 2.7.11.24) at Thr747. The activation of the ERK pathway by extracellular signals results in the phosphorylation and activation of calpain B. In Schneider cells (S2), calpain B was mainly in the cytoplasm and upon a rise in Ca2+ the enzyme adhered to intracellular membranes.


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 39.49  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229  35 FKTIAGEDGEISLQEFKAAL--HVKESFFAERF--------FALFDSDRSGTITLQELQEALTLLihgspmDKLKFLFQV 104
Cdd:cd16196    6 FDKIAGEDMEIDAYELQDILntAFKKDFPFDGFsldacrsmVAMMDVDRSGKLGFEEFKKLWEDL------RSWKRVFKL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 296278229 105 YDIDvcarqgasagtewgagagphwassplgtGSGSIDPDELRTVLQS 152
Cdd:cd16196   80 FDTD----------------------------GSGSFSSFELRNALNS 99
PA_degradation_oxidoreductase_like cd06214
NAD(P) binding domain of ferredoxin reductase like phenylacetic acid (PA) degradation ...
 569-613 2.81e-03

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


Pssm-ID: 99810 [Multi-domain]  Cd Length: 241  Bit Score: 40.22  E-value: 2.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 296278229 569 GPYGTPTRRifASEHAVLIGAGIGITPFASILQSIMYRHQKRKHT 613
Cdd:cd06214   98 GRFTLPPLP--GARHYVLFAAGSGITPVLSILKTALAREPASRVT 140
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 469-601 3.56e-03

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: 40.00  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296278229 469 FHYRPGDYLYLNIPTIARYEWHPFTISSAPEQKDTIWLHIrsqgqwtnrlyesfkasDPLGRGSKRLSRSvtmrksqrsS 548
Cdd:cd06192   23 RLFRPGQFVFLRNFESPGLERIPLSLAGVDPEEGTISLLV-----------------EIRGPKTKLIAEL---------K 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 296278229 549 KGSEIllekhkfcnikcYIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQ 601
Cdd:cd06192   77 PGEKL------------DVMGPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAK 117
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 43-87 3.91e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 38.66  E-value: 3.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 296278229  43 GEISLQEFKAALHVKESFfaERFFALFDSDRSGTITLQELQEALT 87
Cdd:cd16180   52 GTINFDEFVGLWKYIQDW--RRLFRRFDRDRSGSIDFNELQNALS 94
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
42-87 3.98e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 39.66  E-value: 3.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 296278229  42 DGEISLQEFKAALHVKESFF-AERFFALFDSDRSGTITLQELQEALT 87
Cdd:NF041410 117 DGSISSDELSAGLTSAGSSAdSSQLFSALDSDGDGSVSSDELAAALQ 163
EFh_PEF_sorcin cd16187
Penta-EF hand, calcium binding motifs, found in sorcin; Sorcin, also termed 22 kDa Ca2 ...
 43-87 4.93e-03

Penta-EF hand, calcium binding motifs, found in sorcin; Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. The up-regulation of sorcin is correlated with a number of cancer types, including colorectal, gastric and breast cancer. It may represent a therapeutic target for reversing tumor multidrug resistance (MDR). Sorcin participates in the regulation of calcium homeostasis in cells and is necessary for the activation of mitosis and cytokinesis. It enhances metastasis and promotes epithelial-to-mesenchymal transition of colorectal cancer. Moreover, sorcin has been implicated in the regulation of intracellular Ca2+ cycling and cardiac excitation-contraction coupling. It displays the anti-apoptotic properties via the modulation of mitochondrial Ca2+ handling in cardiac myocytes. It can target and activate the sarcolemmal Na+/Ca2+ exchanger (NCX1) in cardiac muscle. Meanwhile, sorcin modulates cardiac L-type Ca2+ current by functional interaction with the alpha1C subunit. It also associates with calcium/calmodulin-dependent protein kinase IIdeltaC (CaMKIIdelta(C)) and further modulates ryanodine receptor (RyR) function in cardiac myocytes. Furthermore, sorcin may act as a Ca2+ sensor for glucose-induced nuclear translocation and the activation of carbohydrate-responsive element-binding protein (ChREBP)-dependent genes. As a mitochondrial chaperone TRAP1 interactor, sorcin involves in mitochondrial metabolism through the TRAP1 pathway. In addition, sorcin may regulate the inhibition of type I interferon response in cells through interacting with foot-and-mouth disease virus (FMDV) VP1. Sorcin contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH.


Pssm-ID: 320062 [Multi-domain]  Cd Length: 165  Bit Score: 38.73  E-value: 4.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 296278229  43 GEISLQEFKAALHVKESFfaERFFALFDSDRSGTITLQELQEALT 87
Cdd:cd16187   55 GTMGFNEFKELWAVLNGW--RQHFISFDSDRSGTVDPQELQKALT 97
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 137-203 9.38e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 38.49  E-value: 9.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296278229 137 GSGSIDPDELRTVLQSCLRESAISLPDEKLDQLTLALFESADADGNGAITFeelrDELQRFPGVMEN 203
Cdd:cd15902  103 GSGFIEAKELKGFLKDLLLKNKKHVSPPKLDEYTKLILKEFDANKDGKLEL----DEMAKLLPVQEN 165
 
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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