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Conserved domains on  [gi|1585682695|ref|XP_028115410|]
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LOW QUALITY PROTEIN: respiratory burst oxidase homolog protein C-like [Camellia sinensis]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 13750575)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

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 ...
 150-250 2.65e-58

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: 194.33  E-value: 2.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 150 FDRNKSAAAHALKGLKFISKTDGG--AGWAAVEKRFNNLTSstNGLLHRSLFGECIGMnKESKEFAGELFDALGRRRNIT 227
Cdd:pfam08414   1 LDRTKSGAARALKGLRFISKTDGGegAGWKAVEKRFDKLAV--DGLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77

                          90       100
                  ....*....|....*....|...
gi 1585682695 228 GDMINLAELKEFWEQISDQSFDS 250
Cdd:pfam08414  78 GDSITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
732-904 2.84e-50

Ferric reductase NAD binding domain;


:

Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 173.68  E-value: 2.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 732 YDVVLLVGLGIGATPMISIVKDIVDNMKAndeeenaleggdgatatkrsgnsFKTTRAYFYWVTREQGSFDWFKGIMNEV 811
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK-----------------------LKTKKIKFYWVVRDLSSLEWFKDVLNEL 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 812 AETDKNgVIEMHNYCTSVYEEGDARSALITMLQSLNHAKHGVDVVSGTRVKSHFAKPNWRNVYKRIALNHTNGRVGVFYC 891
Cdd:pfam08030  58 EELKEL-NIEIHIYLTGEYEAEDASDQSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSC 136

                         170
                  ....*....|...
gi 1585682695 892 GAPALTKELKQLA 904
Cdd:pfam08030 137 GPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 612-835 2.81e-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: 167.87  E-value: 2.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 612 ILKVAVYP-GNVLAIHMSKPQGFKYKSGQYMFVNCAAV-SPFEWHPFSITSAPGD--DYLSVHIRTL-GDWTRQLKTVFS 686
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 687 EvcqppptgksgllradymqgENNPNFPRVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDIVdnmkandeeen 766
Cdd:cd06186    81 S--------------------PGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLL----------- 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1585682695 767 aleggdgatatKRSGNSFKTTRAYFYWVTREQGSFDWFKGIMNEVAETDKNGVIemHNYCTSVYEEGDA 835
Cdd:cd06186   130 -----------RRSSKTSRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEI--EIYVTRVVVCGPP 185
COG4097 super family cl34712
Predicted ferric reductase [Inorganic ion transport and metabolism];
452-757 1.17e-22

Predicted ferric reductase [Inorganic ion transport and metabolism];


The actual alignment was detected with superfamily member COG4097:

Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 101.89  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 452 FHKLIAVAIALGVGIH-AIYHLvcdfPRLIQASPEKYAPMEPYFGEQAHSYwhfvKSFEGISGIIMVVLMAIAFtlaspw 530
Cdd:COG4097    80 LHKWLGILALVLALAHpLLLLG----PKWLVGWGGLPARLAALLTLLRGLA----ELLGEWAFYLLLALVVLSL------ 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 531 FRRNrvnLPkalkklsgFNAFWYSHHLFVIVYGLLIAHGI---KLYLTHKWYKKTVWMYLAVPIILYACERLIRLFRSSI 607
Cdd:COG4097   146 LRRR---LP--------YELWRLTHRLLAVAYLLLAFHHLllgGPFYWSPPAGVLWAALAAAGLAAAVYSRLGRPLRSRR 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 608 KPVKILKVAVYPGNVLAIHMS--KPQGFKYKSGQYMFVNCAAvSPF--EWHPFSITSAP-GDDYLSVHIRTLGDWTRQLK 682
Cdd:COG4097   215 HPYRVESVEPEAGDVVELTLRpeGGRWLGHRAGQFAFLRFDG-SPFweEAHPFSISSAPgGDGRLRFTIKALGDFTRRLG 293

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1585682695 683 TVfsevcqppPTGKsgllradymqgennpnfpRVLIDGPYGA-PAQDYKKYDVVLLVGLGIGATPMISIVKDIVDN 757
Cdd:COG4097   294 RL--------KPGT------------------RVYVEGPYGRfTFDRRDTAPRQVWIAGGIGITPFLALLRALAAR 343
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 231-277 3.21e-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: 3.21e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1585682695 231 INLAELKEFWEQISDQSFDSRLQTFFDMVDKDADGRITGEEVKEIIT 277
Cdd:cd00051    17 ISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
249-311 1.88e-06

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.09  E-value: 1.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1585682695 249 DSRLQTFFDMVDKDADGRITGEEVKEIITLSASANKLSniqkqaDEYAALIMEELDPDNAGYI 311
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLS------DEEVEELFKEFDLDKDGRI 57
 
Name Accession Description Interval E-value
NADPH_Ox pfam08414
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ...
 150-250 2.65e-58

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: 194.33  E-value: 2.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 150 FDRNKSAAAHALKGLKFISKTDGG--AGWAAVEKRFNNLTSstNGLLHRSLFGECIGMnKESKEFAGELFDALGRRRNIT 227
Cdd:pfam08414   1 LDRTKSGAARALKGLRFISKTDGGegAGWKAVEKRFDKLAV--DGLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77

                          90       100
                  ....*....|....*....|...
gi 1585682695 228 GDMINLAELKEFWEQISDQSFDS 250
Cdd:pfam08414  78 GDSITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
732-904 2.84e-50

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 173.68  E-value: 2.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 732 YDVVLLVGLGIGATPMISIVKDIVDNMKAndeeenaleggdgatatkrsgnsFKTTRAYFYWVTREQGSFDWFKGIMNEV 811
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK-----------------------LKTKKIKFYWVVRDLSSLEWFKDVLNEL 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 812 AETDKNgVIEMHNYCTSVYEEGDARSALITMLQSLNHAKHGVDVVSGTRVKSHFAKPNWRNVYKRIALNHTNGRVGVFYC 891
Cdd:pfam08030  58 EELKEL-NIEIHIYLTGEYEAEDASDQSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSC 136

                         170
                  ....*....|...
gi 1585682695 892 GAPALTKELKQLA 904
Cdd:pfam08030 137 GPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 612-835 2.81e-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: 167.87  E-value: 2.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 612 ILKVAVYP-GNVLAIHMSKPQGFKYKSGQYMFVNCAAV-SPFEWHPFSITSAPGD--DYLSVHIRTL-GDWTRQLKTVFS 686
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 687 EvcqppptgksgllradymqgENNPNFPRVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDIVdnmkandeeen 766
Cdd:cd06186    81 S--------------------PGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLL----------- 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1585682695 767 aleggdgatatKRSGNSFKTTRAYFYWVTREQGSFDWFKGIMNEVAETDKNGVIemHNYCTSVYEEGDA 835
Cdd:cd06186   130 -----------RRSSKTSRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEI--EIYVTRVVVCGPP 185
FAD_binding_8 pfam08022
FAD-binding domain;
607-726 4.97e-47

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 162.89  E-value: 4.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 607 IKPVKILKVAVYPGNVLAIHMSKPQG-FKYKSGQYMFVNC-AAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRQLKTV 684
Cdd:pfam08022   1 IFGVPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1585682695 685 FSEVCQPPPtgksgllradymqgENNPNFPRVLIDGPYGAPA 726
Cdd:pfam08022  81 LSSSCPKSP--------------ENGKDKPRVLIEGPYGPPS 108
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 511-754 3.02e-23

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 106.08  E-value: 3.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 511 ISGIIMVVLMAIAFTLASPWFRRNRvnlpkalkklsgFNAFWYSHHLFVIvygLLIAhgiklYLTHKWYKKTVWMYLAvp 590
Cdd:PLN02844  238 LAGEIALVTGLVIWITSLPQIRRKR------------FEIFYYTHHLYIV---FLIF-----FLFHAGDRHFYMVFPG-- 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 591 IILYACERLIRLFRSSIKPVkILKVAVYPGNVLAIHMSKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPG--DDYLS 668
Cdd:PLN02844  296 IFLFGLDKLLRIVQSRPETC-ILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNidDHTMS 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 669 VHIRTLGDWTRQLKTVFSEVcqppptgksglLRADYMQGENNPnfprVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMI 748
Cdd:PLN02844  375 VIIKCEGGWTNSLYNKIQAE-----------LDSETNQMNCIP----VAIEGPYGPASVDFLRYDSLLLVAGGIGITPFL 439


                  ....*.
gi 1585682695 749 SIVKDI 754
Cdd:PLN02844  440 SILKEI 445
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
452-757 1.17e-22

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 101.89  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 452 FHKLIAVAIALGVGIH-AIYHLvcdfPRLIQASPEKYAPMEPYFGEQAHSYwhfvKSFEGISGIIMVVLMAIAFtlaspw 530
Cdd:COG4097    80 LHKWLGILALVLALAHpLLLLG----PKWLVGWGGLPARLAALLTLLRGLA----ELLGEWAFYLLLALVVLSL------ 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 531 FRRNrvnLPkalkklsgFNAFWYSHHLFVIVYGLLIAHGI---KLYLTHKWYKKTVWMYLAVPIILYACERLIRLFRSSI 607
Cdd:COG4097   146 LRRR---LP--------YELWRLTHRLLAVAYLLLAFHHLllgGPFYWSPPAGVLWAALAAAGLAAAVYSRLGRPLRSRR 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 608 KPVKILKVAVYPGNVLAIHMS--KPQGFKYKSGQYMFVNCAAvSPF--EWHPFSITSAP-GDDYLSVHIRTLGDWTRQLK 682
Cdd:COG4097   215 HPYRVESVEPEAGDVVELTLRpeGGRWLGHRAGQFAFLRFDG-SPFweEAHPFSISSAPgGDGRLRFTIKALGDFTRRLG 293

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1585682695 683 TVfsevcqppPTGKsgllradymqgennpnfpRVLIDGPYGA-PAQDYKKYDVVLLVGLGIGATPMISIVKDIVDN 757
Cdd:COG4097   294 RL--------KPGT------------------RVYVEGPYGRfTFDRRDTAPRQVWIAGGIGITPFLALLRALAAR 343
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 417-566 6.53e-14

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 69.22  E-value: 6.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 417 LNMAIILLPVCRNT-ITWLRNktklgvaVPFDDNLNFHKLIAVAIALGVGIHAIYHLVCDFPRliqaspekyapmepyfg 495
Cdd:pfam01794   7 ALLPLLLLLALRNNpLEWLTG-------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF----------------- 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1585682695 496 EQAHSYWHFVKSFEGISGIIMVVLMAIAFTLASPWFRRnrvnlpkalkklSGFNAFWYSHHLFVIVYGLLI 566
Cdd:pfam01794  63 SLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRR------------LSYELFLYLHILLAVAFLLLV 121
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 231-277 3.21e-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: 3.21e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1585682695 231 INLAELKEFWEQISDQSFDSRLQTFFDMVDKDADGRITGEEVKEIIT 277
Cdd:cd00051    17 ISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
212-311 6.12e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.41  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 212 FAGELFDALGRRRNITGD-MINLAELKEFWEQISDQSFDSRLQTFFDMVDKDADGRITGEEVKEIITlsasANKLSniqk 290
Cdd:COG5126    30 LFRRLWATLFSEADTDGDgRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT----ALGVS---- 101

                          90       100
                  ....*....|....*....|.
gi 1585682695 291 qaDEYAALIMEELDPDNAGYI 311
Cdd:COG5126   102 --EEEADELFARLDTDGDGKI 120
EF-hand_7 pfam13499
EF-hand domain pair;
249-311 1.88e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.09  E-value: 1.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1585682695 249 DSRLQTFFDMVDKDADGRITGEEVKEIITLSASANKLSniqkqaDEYAALIMEELDPDNAGYI 311
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLS------DEEVEELFKEFDLDKDGRI 57
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 210-311 5.06e-04

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 43.06  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 210 KEFAGELFdaLGRrrnitgdminlaELKEFwEQISDQSFDSRLQTFFDMVDKDADGRITGEEVKEIItlsasankLSNIQ 289
Cdd:cd16225     9 KEFHKEVF--LGN------------EKEEF-EEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWI--------MEKTQ 65

                          90       100
                  ....*....|....*....|....*
gi 1585682695 290 ---KQADEYAALIMEELDPDNAGYI 311
Cdd:cd16225    66 ehfQEAVEENEQIFKAVDTDKDGNV 90
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 256-277 9.85e-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: 34.28  E-value: 9.85e-03
                           10        20
                   ....*....|....*....|..
gi 1585682695  256 FDMVDKDADGRITGEEVKEIIT 277
Cdd:smart00054   6 FRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
NADPH_Ox pfam08414
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ...
 150-250 2.65e-58

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: 194.33  E-value: 2.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 150 FDRNKSAAAHALKGLKFISKTDGG--AGWAAVEKRFNNLTSstNGLLHRSLFGECIGMnKESKEFAGELFDALGRRRNIT 227
Cdd:pfam08414   1 LDRTKSGAARALKGLRFISKTDGGegAGWKAVEKRFDKLAV--DGLLPRSKFGECIGM-KDSKEFAGELFDALARRRGIT 77

                          90       100
                  ....*....|....*....|...
gi 1585682695 228 GDMINLAELKEFWEQISDQSFDS 250
Cdd:pfam08414  78 GDSITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
732-904 2.84e-50

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 173.68  E-value: 2.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 732 YDVVLLVGLGIGATPMISIVKDIVDNMKAndeeenaleggdgatatkrsgnsFKTTRAYFYWVTREQGSFDWFKGIMNEV 811
Cdd:pfam08030   1 YENVLLVAGGIGITPFISILKDLGNKSKK-----------------------LKTKKIKFYWVVRDLSSLEWFKDVLNEL 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 812 AETDKNgVIEMHNYCTSVYEEGDARSALITMLQSLNHAKHGVDVVSGTRVKSHFAKPNWRNVYKRIALNHTNGRVGVFYC 891
Cdd:pfam08030  58 EELKEL-NIEIHIYLTGEYEAEDASDQSDSSIRSENFDSLMNEVIGVDFVEFHFGRPNWKEVLKDIAKQHPNGSIGVFSC 136

                         170
                  ....*....|...
gi 1585682695 892 GAPALTKELKQLA 904
Cdd:pfam08030 137 GPPSLVDELRNLV 149
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 612-835 2.81e-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: 167.87  E-value: 2.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 612 ILKVAVYP-GNVLAIHMSKPQGFKYKSGQYMFVNCAAV-SPFEWHPFSITSAPGD--DYLSVHIRTL-GDWTRQLKTVFS 686
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKkGFTTRLLRKALK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 687 EvcqppptgksgllradymqgENNPNFPRVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDIVdnmkandeeen 766
Cdd:cd06186    81 S--------------------PGGGVSLKVLVEGPYGSSSEDLLSYDNVLLVAGGSGITFVLPILRDLL----------- 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1585682695 767 aleggdgatatKRSGNSFKTTRAYFYWVTREQGSFDWFKGIMNEVAETDKNGVIemHNYCTSVYEEGDA 835
Cdd:cd06186   130 -----------RRSSKTSRTRRVKLVWVVRDREDLEWFLDELRAAQELEVDGEI--EIYVTRVVVCGPP 185
FAD_binding_8 pfam08022
FAD-binding domain;
607-726 4.97e-47

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 162.89  E-value: 4.97e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 607 IKPVKILKVAVYPGNVLAIHMSKPQG-FKYKSGQYMFVNC-AAVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTRQLKTV 684
Cdd:pfam08022   1 IFGVPKAKVALLPDNVLKLRVSKPKKpFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1585682695 685 FSEVCQPPPtgksgllradymqgENNPNFPRVLIDGPYGAPA 726
Cdd:pfam08022  81 LSSSCPKSP--------------ENGKDKPRVLIEGPYGPPS 108
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 511-754 3.02e-23

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 106.08  E-value: 3.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 511 ISGIIMVVLMAIAFTLASPWFRRNRvnlpkalkklsgFNAFWYSHHLFVIvygLLIAhgiklYLTHKWYKKTVWMYLAvp 590
Cdd:PLN02844  238 LAGEIALVTGLVIWITSLPQIRRKR------------FEIFYYTHHLYIV---FLIF-----FLFHAGDRHFYMVFPG-- 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 591 IILYACERLIRLFRSSIKPVkILKVAVYPGNVLAIHMSKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPG--DDYLS 668
Cdd:PLN02844  296 IFLFGLDKLLRIVQSRPETC-ILSARLFPCKAIELVLPKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNidDHTMS 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 669 VHIRTLGDWTRQLKTVFSEVcqppptgksglLRADYMQGENNPnfprVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMI 748
Cdd:PLN02844  375 VIIKCEGGWTNSLYNKIQAE-----------LDSETNQMNCIP----VAIEGPYGPASVDFLRYDSLLLVAGGIGITPFL 439


                  ....*.
gi 1585682695 749 SIVKDI 754
Cdd:PLN02844  440 SILKEI 445
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
452-757 1.17e-22

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 101.89  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 452 FHKLIAVAIALGVGIH-AIYHLvcdfPRLIQASPEKYAPMEPYFGEQAHSYwhfvKSFEGISGIIMVVLMAIAFtlaspw 530
Cdd:COG4097    80 LHKWLGILALVLALAHpLLLLG----PKWLVGWGGLPARLAALLTLLRGLA----ELLGEWAFYLLLALVVLSL------ 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 531 FRRNrvnLPkalkklsgFNAFWYSHHLFVIVYGLLIAHGI---KLYLTHKWYKKTVWMYLAVPIILYACERLIRLFRSSI 607
Cdd:COG4097   146 LRRR---LP--------YELWRLTHRLLAVAYLLLAFHHLllgGPFYWSPPAGVLWAALAAAGLAAAVYSRLGRPLRSRR 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 608 KPVKILKVAVYPGNVLAIHMS--KPQGFKYKSGQYMFVNCAAvSPF--EWHPFSITSAP-GDDYLSVHIRTLGDWTRQLK 682
Cdd:COG4097   215 HPYRVESVEPEAGDVVELTLRpeGGRWLGHRAGQFAFLRFDG-SPFweEAHPFSISSAPgGDGRLRFTIKALGDFTRRLG 293

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1585682695 683 TVfsevcqppPTGKsgllradymqgennpnfpRVLIDGPYGA-PAQDYKKYDVVLLVGLGIGATPMISIVKDIVDN 757
Cdd:COG4097   294 RL--------KPGT------------------RVYVEGPYGRfTFDRRDTAPRQVWIAGGIGITPFLALLRALAAR 343
PLN02631 PLN02631
ferric-chelate reductase
 511-755 4.41e-19

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 92.41  E-value: 4.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 511 ISGIIMVVLMAIAFTLASPWFRRNRvnlpkalkklsgFNAFWYSHHLfvivYGLLIAhgikLYLTHKwykKTVWMYLAVP 590
Cdd:PLN02631  234 LAGTIAMVIGIAMWVTSLPSFRRKK------------FELFFYTHHL----YGLYIV----FYVIHV---GDSWFCMILP 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 591 -IILYACERLIRlFRSSIKPVKILKVAVYPGNVLAIHMSKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPG--DDYL 667
Cdd:PLN02631  291 nIFLFFIDRYLR-FLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTITSSSNleKDTL 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 668 SVHIRTLGDWTRQLKTVFSEvcqppptgksgllRADYMQgennpnfprVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPM 747
Cdd:PLN02631  370 SVVIRRQGSWTQKLYTHLSS-------------SIDSLE---------VSTEGPYGPNSFDVSRHNSLILVSGGSGITPF 427


                  ....*...
gi 1585682695 748 ISIVKDIV 755
Cdd:PLN02631  428 ISVIRELI 435
PLN02292 PLN02292
ferric-chelate reductase
 548-755 7.31e-17

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 85.30  E-value: 7.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 548 FNAFWYSHHLFVIVYGLLIAH-GIKLYLthkwykktvwmyLAVP-IILYACERLIRlFRSSIKPVKILKVAVYPGNVLAI 625
Cdd:PLN02292  276 FEVFFYTHYLYIVFMLFFVFHvGISFAL------------ISFPgFYIFLVDRFLR-FLQSRNNVKLVSARVLPCDTVEL 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 626 HMSKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPG--DDYLSVHIRTLGDWTRQLKtvfsevcqppptgksgllraD 703
Cdd:PLN02292  343 NFSKNPMLMYSPTSIMFVNIPSISKLQWHPFTITSSSKlePEKLSVMIKSQGKWSTKLY--------------------H 402

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1585682695 704 YMQGENNPNFPRVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDIV 755
Cdd:PLN02292  403 MLSSSDQIDRLAVSVEGPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLI 454
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 617-753 2.20e-15

NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) domain, which varies in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99795 [Multi-domain]  Cd Length: 216  Bit Score: 76.14  E-value: 2.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 617 VYPGNVLAIHMSKPQgFKYKSGQYMFVNCAAVSPFEWHPFSITSAPGDDY-LSVHIRTLGDWTRQLKTvfsevcqppptg 695
Cdd:cd06198     6 VRPTTTLTLEPRGPA-LGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALGDYTRRLAE------------ 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1585682695 696 ksgLLRAdymqGEnnpnfpRVLIDGPYGAPAQDYKKYDVVLLVGlGIGATPMISIVKD 753
Cdd:cd06198    73 ---RLKP----GT------RVTVEGPYGRFTFDDRRARQIWIAG-GIGITPFLALLEA 116
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 417-566 6.53e-14

Ferric reductase like transmembrane component; This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane. The Frp1 protein from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake. Cytochrome B-245 heavy chain is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterized by the absence of a functional plasma membrane associated NADPH oxidase. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease.


Pssm-ID: 426438 [Multi-domain]  Cd Length: 121  Bit Score: 69.22  E-value: 6.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 417 LNMAIILLPVCRNT-ITWLRNktklgvaVPFDDNLNFHKLIAVAIALGVGIHAIYHLVCDFPRliqaspekyapmepyfg 495
Cdd:pfam01794   7 ALLPLLLLLALRNNpLEWLTG-------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRF----------------- 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1585682695 496 EQAHSYWHFVKSFEGISGIIMVVLMAIAFTLASPWFRRnrvnlpkalkklSGFNAFWYSHHLFVIVYGLLI 566
Cdd:pfam01794  63 SLEGILDLLLKRPYNILGIIALVLLVLLAITSLPPFRR------------LSYELFLYLHILLAVAFLLLV 121
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 628-754 5.57e-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: 69.40  E-value: 5.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 628 SKPQGFKYKSGQYMFVNCAAVSPFEWHPFSITSAPGD-DYLSVHIRTLgdwtrqlktvfsevcqpPPTGKSGLLRADYMq 706
Cdd:cd00322    16 QLPNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEeGELELTVKIV-----------------PGGPFSAWLHDLKP- 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1585682695 707 GEnnpnfpRVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDI 754
Cdd:cd00322    78 GD------EVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHL 119
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 231-277 3.21e-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: 3.21e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1585682695 231 INLAELKEFWEQISDQSFDSRLQTFFDMVDKDADGRITGEEVKEIIT 277
Cdd:cd00051    17 ISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
212-311 6.12e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.41  E-value: 6.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 212 FAGELFDALGRRRNITGD-MINLAELKEFWEQISDQSFDSRLQTFFDMVDKDADGRITGEEVKEIITlsasANKLSniqk 290
Cdd:COG5126    30 LFRRLWATLFSEADTDGDgRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLT----ALGVS---- 101

                          90       100
                  ....*....|....*....|.
gi 1585682695 291 qaDEYAALIMEELDPDNAGYI 311
Cdd:COG5126   102 --EEEADELFARLDTDGDGKI 120
EF-hand_7 pfam13499
EF-hand domain pair;
249-311 1.88e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.09  E-value: 1.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1585682695 249 DSRLQTFFDMVDKDADGRITGEEVKEIITLSASANKLSniqkqaDEYAALIMEELDPDNAGYI 311
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLS------DEEVEELFKEFDLDKDGRI 57
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 251-319 2.01e-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: 42.92  E-value: 2.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1585682695 251 RLQTFFDMVDKDADGRITGEEVKEIItlsasaNKLSniQKQADEYAALIMEELDPDNAGYIMIEnlEML 319
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAAL------KSLG--EGLSEEEIDEMIREVDKDGDGKIDFE--EFL 59
O2ase_reductase_like cd06187
The oxygenase reductase FAD/NADH binding domain acts as part of the multi-component bacterial ...
 630-754 8.19e-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: 44.89  E-value: 8.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 630 PQGFKYKSGQYMFVNcAAVSPFEWHPFSITSAPGDD-YLSVHIRTL-GDWTrqlktvfsevcqppptgkSGLLRADYMQG 707
Cdd:cd06187    19 DQPLPFWAGQYVNVT-VPGRPRTWRAYSPANPPNEDgEIEFHVRAVpGGRV------------------SNALHDELKVG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1585682695 708 EnnpnfpRVLIDGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVKDI 754
Cdd:cd06187    80 D------RVRLSGPYGTFYLRRDHDRPVLCIAGGTGLAPLRAIVEDA 120
DHOD_e_trans_like cd06192
FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like ...
 638-752 8.62e-05

FAD/NAD binding domain (electron transfer subunit) of dihydroorotate dehydrogenase-like proteins. Dihydroorotate dehydrogenases (DHODs) catalyze the only redox reaction in pyrimidine de novo biosynthesis. They catalyze the oxidation of (S)-dihydroorotate to orotate coupled with the reduction of NAD+. In L. lactis, DHOD B (encoded by pyrDa) is co-expressed with pyrK and both gene products are required for full activity, as well as NAD binding. NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer between an NAD(P)-binding domain of the alpha/beta class and a discrete (usually N-terminal) domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal domain may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Ferredoxin is reduced in the final stage of photosystem I. The flavoprotein Ferredoxin-NADP+ reductase transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) which then transfers a hydride ion to convert NADP+ to NADPH.


Pssm-ID: 99789 [Multi-domain]  Cd Length: 243  Bit Score: 45.01  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 638 GQYMFVNCAAVSPFEWHPFSITSA-PGDDYLSVHIRTLGdwtrqlktvfsevcqppptGKSGLLradymqGENNPNFPRV 716
Cdd:cd06192    28 GQFVFLRNFESPGLERIPLSLAGVdPEEGTISLLVEIRG-------------------PKTKLI------AELKPGEKLD 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1585682695 717 LIdGPYGAPAQDYKKYDVVLLVGLGIGATPMISIVK 752
Cdd:cd06192    83 VM-GPLGNGFEGPKKGGTVLLVAGGIGLAPLLPIAK 117
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 210-311 5.06e-04

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 43.06  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 210 KEFAGELFdaLGRrrnitgdminlaELKEFwEQISDQSFDSRLQTFFDMVDKDADGRITGEEVKEIItlsasankLSNIQ 289
Cdd:cd16225     9 KEFHKEVF--LGN------------EKEEF-EEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWI--------MEKTQ 65

                          90       100
                  ....*....|....*....|....*
gi 1585682695 290 ---KQADEYAALIMEELDPDNAGYI 311
Cdd:cd16225    66 ehfQEAVEENEQIFKAVDTDKDGNV 90
flavin_oxioreductase cd06189
NAD(P)H dependent flavin oxidoreductases use flavin as a substrate in mediating electron ...
 611-672 6.36e-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: 6.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1585682695 611 KILKVAVYPGNVLAIHMSKPQGFKYKSGQYMFVNcaaVSPFEWHPFSITSAP-GDDYLSVHIR 672
Cdd:cd06189     2 KVESIEPLNDDVYRVRLKPPAPLDFLAGQYLDLL---LDDGDKRPFSIASAPhEDGEIELHIR 61
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
149-277 1.01e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.16  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 149 RFDRNKSAaahalkglkFISKTDGGAGWAA-VEKRFNNLTSSTNGLLHRSLFGECI--GMNKESKEFAGELFDALGRrrn 225
Cdd:COG5126    13 LLDADGDG---------VLERDDFEALFRRlWATLFSEADTDGDGRISREEFVAGMesLFEATVEPFARAAFDLLDT--- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1585682695 226 iTGD-MINLAELKEFWEQISDQsfDSRLQTFFDMVDKDADGRITGEEVKEIIT 277
Cdd:COG5126    81 -DGDgKISADEFRRLLTALGVS--EEEADELFARLDTDGDGKISFEEFVAAVR 130
EF-hand_7 pfam13499
EF-hand domain pair;
215-277 2.23e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 2.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1585682695 215 ELFDALGRRRNitgDMINLAELKEFWEQIS-DQSF-DSRLQTFFDMVDKDADGRITGEEVKEIIT 277
Cdd:pfam13499   6 EAFKLLDSDGD---GYLDVEELKKLLRKLEeGEPLsDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FNR_N-term_Iron_sulfur_binding cd06194
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 623-753 4.75e-03

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


Pssm-ID: 99791 [Multi-domain]  Cd Length: 222  Bit Score: 39.56  E-value: 4.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 623 LAIHMSKPqgFKYKSGQYMFVncaAVSPFEWHPFSITSAP-GDDYLSVHIRtlgdwtRQlktvfsevcqpPPTGKSGLLR 701
Cdd:cd06194    14 VRLEPDRP--LPYLPGQYVNL---RRAGGLARSYSPTSLPdGDNELEFHIR------RK-----------PNGAFSGWLG 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1585682695 702 ADYMQGEnnpnfpRVLIDGPYG-APAQDYKKYDVVLLVGLGIGATPMISIVKD 753
Cdd:cd06194    72 EEARPGH------ALRLQGPFGqAFYRPEYGEGPLLLVGAGTGLAPLWGIARA 118
DHOD_e_trans_like2 cd06220
FAD/NAD binding domain in the electron transfer subunit of dihydroorotate dehydrogenase-like ...
 633-753 9.42e-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 3 cofactors: FMN, FAD, and an [2Fe-2S] cluster.


Pssm-ID: 99816 [Multi-domain]  Cd Length: 233  Bit Score: 38.77  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1585682695 633 FKYKSGQYMFVNCAAVSPFewhPFSITSAPGDDYLSVHIRtlGDWTRQLktvfsevcqppptgksgllrADYMQGEnnpn 712
Cdd:cd06220    22 FDFKPGQFVMVWVPGVDEI---PMSLSYIDGPNSITVKKV--GEATSAL--------------------HDLKEGD---- 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1585682695 713 fpRVLIDGPYGAPAQ-DYKKydvVLLVGLGIGATPMISIVKD 753
Cdd:cd06220    73 --KLGIRGPYGNGFElVGGK---VLLIGGGIGIAPLAPLAER 109
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 256-277 9.85e-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: 34.28  E-value: 9.85e-03
                           10        20
                   ....*....|....*....|..
gi 1585682695  256 FDMVDKDADGRITGEEVKEIIT 277
Cdd:smart00054   6 FRLFDKDGDGKIDFEEFKDLLK 27
 
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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