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Conserved domains on  [gi|1002267452|ref|XP_015638046|]
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putative respiratory burst oxidase homolog protein H isoform X2 [Oryza sativa Japonica Group]

Protein Classification

ferric reductase family protein( domain architecture ID 12091675)

ferric reductase family protein similar to Saccharomyces cerevisiae AIM14, a probable cell surface metalloreductase that may be involved in iron or copper homeostasis, and ferric reductase transmembrane component 6, a metalloreductase responsible for reducing vacuolar iron and copper prior to transport into the cytosol

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 ...
 48-147 9.57e-52

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: 175.46  E-value: 9.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452  48 LKRTHSSAQPALRGLRFLDKTSAG-KDGWKNVEKRFDEMSADGRLPQESFAKCIGMADSKEFASEVFVALARRRSIKpED 126
Cdd:pfam08414   1 LDRTKSGAARALKGLRFISKTDGGeGAGWKAVEKRFDKLAVDGLLPRSKFGECIGMKDSKEFAGELFDALARRRGIT-GD 79

                          90       100
                  ....*....|....*....|.
gi 1002267452 127 GITKEQLKEFWEELTDQNFDS 147
Cdd:pfam08414  80 SITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
646-801 2.67e-41

Ferric reductase NAD binding domain;


:

Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 148.26  E-value: 2.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 646 ATPFISILKDLLNNIKSNGDVqsthdaelgctfksngpgRAYFYWVTREQGSFEWFKGVMNDVAESDHDNvIEMHNYLTS 725
Cdd:pfam08030  13 ITPFISILKDLGNKSKKLKTK------------------KIKFYWVVRDLSSLEWFKDVLNELEELKELN-IEIHIYLTG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 726 VYEEGDARSALI-----AMVQSLQHAKNGVDIVsgskiRTHFARPNWRKVFSDLANAHQNSRIGVFYCGSPTLTKMLRDL 800
Cdd:pfam08030  74 EYEAEDASDQSDssirsENFDSLMNEVIGVDFV-----EFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNL 148


                  .
gi 1002267452 801 S 801
Cdd:pfam08030 149 V 149
FAD_binding_8 pfam08022
FAD-binding domain;
504-628 4.91e-38

FAD-binding domain;


:

Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 137.08  E-value: 4.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 504 SYGVTVIKAAIYPGNVLSIHMNKPS-SFKYKSGMYMFVKC-PDVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTTELRNL 581
Cdd:pfam08022   1 IFGVPKAKVALLPDNVLKLRVSKPKkPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1002267452 582 FGKACEAQVSSKKAtlarlettiiadglkeetcFPKVFIDGPFGAPA 628
Cdd:pfam08022  81 LSSSCPKSPENGKD-------------------KPRVLIEGPYGPPS 108
COG4097 super family cl34712
Predicted ferric reductase [Inorganic ion transport and metabolism];
343-656 2.76e-14

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: 76.09  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 343 DDNINFHKVIALTIAIGAATHTLAHVTCDFPRLVSCPRDKFEATLGPyfnyvqptySSLVASTPGWTG-ILMILIMSFSF 421
Cdd:COG4097    75 DRLYRLHKWLGILALVLALAHPLLLLGPKWLVGWGGLPARLAALLTL---------LRGLAELLGEWAfYLLLALVVLSL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 422 tlathsFRRsvvKLPsplhhlagFNAFWYAHHLLVIAYILLVLHSyfIFLTKQWYNRT-------TWMFLAVPVLFYSce 494
Cdd:COG4097   146 ------LRR---RLP--------YELWRLTHRLLAVAYLLLAFHH--LLLGGPFYWSPpagvlwaALAAAGLAAAVYS-- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 495 RTIRRVRESSYGVTVIKAAIYPGNVLSIHMNKPSS--FKYKSGMYMFVKCPDvSPF--EWHPFSITSAP-GDDYLSVHIR 569
Cdd:COG4097   205 RLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDG-SPFweEAHPFSISSAPgGDGRLRFTIK 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 570 TLGDWTTELRNLfgkaceaqvsskkatlarlettiiadglKEETcfpKVFIDGPFGApaqnykkYDILLLIGLGIGA--- 646
Cdd:COG4097   284 ALGDFTRRLGRL----------------------------KPGT---RVYVEGPYGR-------FTFDRRDTAPRQVwia 325

                         330
                  ....*....|....*
gi 1002267452 647 -----TPFISILKDL 656
Cdd:COG4097   326 ggigiTPFLALLRAL 340
EF-hand_7 pfam13499
EF-hand domain pair;
146-218 4.77e-06

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.94  E-value: 4.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002267452 146 DSRLRIFFDMCDKNGDGQLTEDEVKEVIVLSAAANKLAKlkshaaTYASLIMEELDPDHRGYIEIWQLETLLR 218
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSD------EEVEELFKEFDLDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
NADPH_Ox pfam08414
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ...
 48-147 9.57e-52

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: 175.46  E-value: 9.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452  48 LKRTHSSAQPALRGLRFLDKTSAG-KDGWKNVEKRFDEMSADGRLPQESFAKCIGMADSKEFASEVFVALARRRSIKpED 126
Cdd:pfam08414   1 LDRTKSGAARALKGLRFISKTDGGeGAGWKAVEKRFDKLAVDGLLPRSKFGECIGMKDSKEFAGELFDALARRRGIT-GD 79

                          90       100
                  ....*....|....*....|.
gi 1002267452 127 GITKEQLKEFWEELTDQNFDS 147
Cdd:pfam08414  80 SITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
646-801 2.67e-41

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 148.26  E-value: 2.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 646 ATPFISILKDLLNNIKSNGDVqsthdaelgctfksngpgRAYFYWVTREQGSFEWFKGVMNDVAESDHDNvIEMHNYLTS 725
Cdd:pfam08030  13 ITPFISILKDLGNKSKKLKTK------------------KIKFYWVVRDLSSLEWFKDVLNELEELKELN-IEIHIYLTG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 726 VYEEGDARSALI-----AMVQSLQHAKNGVDIVsgskiRTHFARPNWRKVFSDLANAHQNSRIGVFYCGSPTLTKMLRDL 800
Cdd:pfam08030  74 EYEAEDASDQSDssirsENFDSLMNEVIGVDFV-----EFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNL 148


                  .
gi 1002267452 801 S 801
Cdd:pfam08030 149 V 149
FAD_binding_8 pfam08022
FAD-binding domain;
504-628 4.91e-38

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 137.08  E-value: 4.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 504 SYGVTVIKAAIYPGNVLSIHMNKPS-SFKYKSGMYMFVKC-PDVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTTELRNL 581
Cdd:pfam08022   1 IFGVPKAKVALLPDNVLKLRVSKPKkPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1002267452 582 FGKACEAQVSSKKAtlarlettiiadglkeetcFPKVFIDGPFGAPA 628
Cdd:pfam08022  81 LSSSCPKSPENGKD-------------------KPRVLIEGPYGPPS 108
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 509-819 1.65e-32

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: 125.11  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 509 VIKAAIYP-GNVLSIHMNKPSSFKYKSGMYMFVKCPDV-SPFEWHPFSITSAPGD--DYLSVHIRTLGDWTTELRNLfgk 584
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKKGFTTRLLRK--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 585 aceaqvsskkatlarlettiiADGLKEETCFPKVFIDGPFGAPAQNYKKYDillliglgigATPFISILKDLLNNIKsng 664
Cdd:cd06186    78 ---------------------ALKSPGGGVSLKVLVEGPYGSSSEDLLSYDnvllvaggsgITFVLPILRDLLRRSS--- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 665 dvqsthdaelgctfKSNGPGRAYFYWVTREQGSFEWFKGVMNdvAESDHDNVIEMHNYLTsvyeegdarsaliamvqslq 744
Cdd:cd06186   134 --------------KTSRTRRVKLVWVVRDREDLEWFLDELR--AAQELEVDGEIEIYVT-------------------- 177

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002267452 745 hakngvdivsgskirthfarpnwrkvfsdlanahqnsriGVFYCGSPTltkMLRDLSLEFSQTTTTRFHFHKENF 819
Cdd:cd06186   178 ---------------------------------------RVVVCGPPG---LVDDVRNAVAKKGGTGVEFHEESF 210
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 445-662 3.59e-18

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 89.52  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 445 FNAFWYAHHLLVIAYILLVLHSYfiflTKQWYnrttWMFlavPVLFYSCERTIRRVRESSYGVTVIKAAIYPGNVLSIHM 524
Cdd:PLN02844  263 FEIFYYTHHLYIVFLIFFLFHAG----DRHFY----MVF---PGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVL 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 525 NKPSSFKYKSGMYMFVKCPDVSPFEWHPFSITSAPG--DDYLSVHIRTLGDWTTELRNLFgkacEAQVSSkkatlarlet 602
Cdd:PLN02844  332 PKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNidDHTMSVIIKCEGGWTNSLYNKI----QAELDS---------- 397

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 603 tiiadGLKEETCFPkVFIDGPFGAPAQNYKKYDILLLIGLGIGATPFISILKDLLNNIKS 662
Cdd:PLN02844  398 -----ETNQMNCIP-VAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSS 451
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
343-656 2.76e-14

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 76.09  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 343 DDNINFHKVIALTIAIGAATHTLAHVTCDFPRLVSCPRDKFEATLGPyfnyvqptySSLVASTPGWTG-ILMILIMSFSF 421
Cdd:COG4097    75 DRLYRLHKWLGILALVLALAHPLLLLGPKWLVGWGGLPARLAALLTL---------LRGLAELLGEWAfYLLLALVVLSL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 422 tlathsFRRsvvKLPsplhhlagFNAFWYAHHLLVIAYILLVLHSyfIFLTKQWYNRT-------TWMFLAVPVLFYSce 494
Cdd:COG4097   146 ------LRR---RLP--------YELWRLTHRLLAVAYLLLAFHH--LLLGGPFYWSPpagvlwaALAAAGLAAAVYS-- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 495 RTIRRVRESSYGVTVIKAAIYPGNVLSIHMNKPSS--FKYKSGMYMFVKCPDvSPF--EWHPFSITSAP-GDDYLSVHIR 569
Cdd:COG4097   205 RLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDG-SPFweEAHPFSISSAPgGDGRLRFTIK 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 570 TLGDWTTELRNLfgkaceaqvsskkatlarlettiiadglKEETcfpKVFIDGPFGApaqnykkYDILLLIGLGIGA--- 646
Cdd:COG4097   284 ALGDFTRRLGRL----------------------------KPGT---RVYVEGPYGR-------FTFDRRDTAPRQVwia 325

                         330
                  ....*....|....*
gi 1002267452 647 -----TPFISILKDL 656
Cdd:COG4097   326 ggigiTPFLALLRAL 340
PLN02631 PLN02631
ferric-chelate reductase
 396-679 8.92e-13

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 72.00  E-value: 8.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 396 PTYSSLVASTpgwtgILMILIMSFSFTlATHSFRRSvvklpsplhhlaGFNAFWYAHHLLVIAYILLVLHSyfifltkqw 475
Cdd:PLN02631  228 PTYVPNLAGT-----IAMVIGIAMWVT-SLPSFRRK------------KFELFFYTHHLYGLYIVFYVIHV--------- 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 476 ynRTTWMFLAVPVLFYSCERTIRRVRESSYGVTVIKAAIYPGNVLSIHMNKPSSFKYKSGMYMFVKCPDVSPFEWHPFSI 555
Cdd:PLN02631  281 --GDSWFCMILPNIFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTI 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 556 TSAPG--DDYLSVHIRTLGDWTTELrnlfgkaceaqvsskkatLARLETTIiaDGLKEETcfpkvfiDGPFGAPAQNYKK 633
Cdd:PLN02631  359 TSSSNleKDTLSVVIRRQGSWTQKL------------------YTHLSSSI--DSLEVST-------EGPYGPNSFDVSR 411

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1002267452 634 YDILLLIGLGIGATPFISILKDLLNniKSNGDVQSTHDAELGCTFK 679
Cdd:PLN02631  412 HNSLILVSGGSGITPFISVIRELIF--QSQNPSTKLPDVLLVCSFK 455
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 314-463 8.53e-12

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: 62.67  E-value: 8.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 314 LNMAVILLPVCRNT-LTRLRStalskvVPFDDNINFHKVIALTIAIGAATHTLAHVTCDFPRLVScprdkfeatlgpyfn 392
Cdd:pfam01794   7 ALLPLLLLLALRNNpLEWLTG------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLE--------------- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002267452 393 yvqPTYSSLVASTPGWTGILMILIMSFSFTLATHSFRRSvvklpsplhhlaGFNAFWYAHHLLVIAYILLV 463
Cdd:pfam01794  66 ---GILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHILLAVAFLLLV 121
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
76-208 5.70e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.18  E-value: 5.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452  76 KNVEKRFDEMSA--DGRLPQESFAKcIGMADSKEFASEVFValarrrsikPEDG-ITKEQLKEFWEELTDQNFDSRLRIF 152
Cdd:COG5126     5 RKLDRRFDLLDAdgDGVLERDDFEA-LFRRLWATLFSEADT---------DGDGrISREEFVAGMESLFEATVEPFARAA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002267452 153 FDMCDKNGDGQLTEDEVKEVivlsaaankLAKLKSHAATyASLIMEELDPDHRGYI 208
Cdd:COG5126    75 FDLLDTDGDGKISADEFRRL---------LTALGVSEEE-ADELFARLDTDGDGKI 120
EF-hand_7 pfam13499
EF-hand domain pair;
146-218 4.77e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.94  E-value: 4.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002267452 146 DSRLRIFFDMCDKNGDGQLTEDEVKEVIVLSAAANKLAKlkshaaTYASLIMEELDPDHRGYIEIWQLETLLR 218
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSD------EEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 62-226 6.22e-06

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: 48.50  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452  62 LRFLDKTSAGKDGWK-NVEKRFDE-MSA-----DGRL----------PQESFAKCIgMADSKEFASEVFVALARRRSIKP 124
Cdd:cd15902    25 LRELLKALNGKDKTDdEVAEKKKEfMEKydeneDGKIeirelanilpTEENFLLLF-RREQPLISSVEFMKIWRKYDTDG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 125 EDGITKEQLKEFWEELTDQN----FDSRLRIFFDMC----DKNGDGQLTEDE------VKEVIVLSAAANKLAKLKShaA 190
Cdd:cd15902   104 SGFIEAKELKGFLKDLLLKNkkhvSPPKLDEYTKLIlkefDANKDGKLELDEmakllpVQENFLLKFQILGAMDLTK--E 181

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1002267452 191 TYASlIMEELDPDHRGYIEIWQLETLLRGMVTAQGP 226
Cdd:cd15902   182 DFEK-VFEHYDKDNNGVIEGNELDALLKDLLEKNKA 216
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 126-173 2.60e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 42.53  E-value: 2.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002267452 126 DG-ITKEQLKEFWEELTDQNFDSRLRIFFDMCDKNGDGQLTEDEVKEVI 173
Cdd:cd00051    14 DGtISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
 
Name Accession Description Interval E-value
NADPH_Ox pfam08414
Respiratory burst NADPH oxidase; This domain is found in plant proteins such as respiratory ...
 48-147 9.57e-52

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: 175.46  E-value: 9.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452  48 LKRTHSSAQPALRGLRFLDKTSAG-KDGWKNVEKRFDEMSADGRLPQESFAKCIGMADSKEFASEVFVALARRRSIKpED 126
Cdd:pfam08414   1 LDRTKSGAARALKGLRFISKTDGGeGAGWKAVEKRFDKLAVDGLLPRSKFGECIGMKDSKEFAGELFDALARRRGIT-GD 79

                          90       100
                  ....*....|....*....|.
gi 1002267452 127 GITKEQLKEFWEELTDQNFDS 147
Cdd:pfam08414  80 SITKEELKEFWEQISDQSFDS 100
NAD_binding_6 pfam08030
Ferric reductase NAD binding domain;
646-801 2.67e-41

Ferric reductase NAD binding domain;


Pssm-ID: 429792 [Multi-domain]  Cd Length: 149  Bit Score: 148.26  E-value: 2.67e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 646 ATPFISILKDLLNNIKSNGDVqsthdaelgctfksngpgRAYFYWVTREQGSFEWFKGVMNDVAESDHDNvIEMHNYLTS 725
Cdd:pfam08030  13 ITPFISILKDLGNKSKKLKTK------------------KIKFYWVVRDLSSLEWFKDVLNELEELKELN-IEIHIYLTG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 726 VYEEGDARSALI-----AMVQSLQHAKNGVDIVsgskiRTHFARPNWRKVFSDLANAHQNSRIGVFYCGSPTLTKMLRDL 800
Cdd:pfam08030  74 EYEAEDASDQSDssirsENFDSLMNEVIGVDFV-----EFHFGRPNWKEVLKDIAKQHPNGSIGVFSCGPPSLVDELRNL 148


                  .
gi 1002267452 801 S 801
Cdd:pfam08030 149 V 149
FAD_binding_8 pfam08022
FAD-binding domain;
504-628 4.91e-38

FAD-binding domain;


Pssm-ID: 285293 [Multi-domain]  Cd Length: 108  Bit Score: 137.08  E-value: 4.91e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 504 SYGVTVIKAAIYPGNVLSIHMNKPS-SFKYKSGMYMFVKC-PDVSPFEWHPFSITSAPGDDYLSVHIRTLGDWTTELRNL 581
Cdd:pfam08022   1 IFGVPKAKVALLPDNVLKLRVSKPKkPFKYKPGQYMFINFlPPLSFLQSHPFTITSAPSDDKLSLHIKVKGGWTRKLANY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1002267452 582 FGKACEAQVSSKKAtlarlettiiadglkeetcFPKVFIDGPFGAPA 628
Cdd:pfam08022  81 LSSSCPKSPENGKD-------------------KPRVLIEGPYGPPS 108
NOX_Duox_like_FAD_NADP cd06186
NADPH oxidase (NOX) catalyzes the generation of reactive oxygen species (ROS) such as ...
 509-819 1.65e-32

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: 125.11  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 509 VIKAAIYP-GNVLSIHMNKPSSFKYKSGMYMFVKCPDV-SPFEWHPFSITSAPGD--DYLSVHIRTLGDWTTELRNLfgk 584
Cdd:cd06186     1 IATVELLPdSDVIRLTIPKPKPFKWKPGQHVYLNFPSLlSFWQSHPFTIASSPEDeqDTLSLIIRAKKGFTTRLLRK--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 585 aceaqvsskkatlarlettiiADGLKEETCFPKVFIDGPFGAPAQNYKKYDillliglgigATPFISILKDLLNNIKsng 664
Cdd:cd06186    78 ---------------------ALKSPGGGVSLKVLVEGPYGSSSEDLLSYDnvllvaggsgITFVLPILRDLLRRSS--- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 665 dvqsthdaelgctfKSNGPGRAYFYWVTREQGSFEWFKGVMNdvAESDHDNVIEMHNYLTsvyeegdarsaliamvqslq 744
Cdd:cd06186   134 --------------KTSRTRRVKLVWVVRDREDLEWFLDELR--AAQELEVDGEIEIYVT-------------------- 177

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002267452 745 hakngvdivsgskirthfarpnwrkvfsdlanahqnsriGVFYCGSPTltkMLRDLSLEFSQTTTTRFHFHKENF 819
Cdd:cd06186   178 ---------------------------------------RVVVCGPPG---LVDDVRNAVAKKGGTGVEFHEESF 210
PLN02844 PLN02844
oxidoreductase/ferric-chelate reductase
 445-662 3.59e-18

oxidoreductase/ferric-chelate reductase


Pssm-ID: 215453 [Multi-domain]  Cd Length: 722  Bit Score: 89.52  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 445 FNAFWYAHHLLVIAYILLVLHSYfiflTKQWYnrttWMFlavPVLFYSCERTIRRVRESSYGVTVIKAAIYPGNVLSIHM 524
Cdd:PLN02844  263 FEIFYYTHHLYIVFLIFFLFHAG----DRHFY----MVF---PGIFLFGLDKLLRIVQSRPETCILSARLFPCKAIELVL 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 525 NKPSSFKYKSGMYMFVKCPDVSPFEWHPFSITSAPG--DDYLSVHIRTLGDWTTELRNLFgkacEAQVSSkkatlarlet 602
Cdd:PLN02844  332 PKDPGLKYAPTSVIFMKIPSISRFQWHPFSITSSSNidDHTMSVIIKCEGGWTNSLYNKI----QAELDS---------- 397

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 603 tiiadGLKEETCFPkVFIDGPFGAPAQNYKKYDILLLIGLGIGATPFISILKDLLNNIKS 662
Cdd:PLN02844  398 -----ETNQMNCIP-VAIEGPYGPASVDFLRYDSLLLVAGGIGITPFLSILKEIASQSSS 451
COG4097 COG4097
Predicted ferric reductase [Inorganic ion transport and metabolism];
343-656 2.76e-14

Predicted ferric reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443273 [Multi-domain]  Cd Length: 442  Bit Score: 76.09  E-value: 2.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 343 DDNINFHKVIALTIAIGAATHTLAHVTCDFPRLVSCPRDKFEATLGPyfnyvqptySSLVASTPGWTG-ILMILIMSFSF 421
Cdd:COG4097    75 DRLYRLHKWLGILALVLALAHPLLLLGPKWLVGWGGLPARLAALLTL---------LRGLAELLGEWAfYLLLALVVLSL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 422 tlathsFRRsvvKLPsplhhlagFNAFWYAHHLLVIAYILLVLHSyfIFLTKQWYNRT-------TWMFLAVPVLFYSce 494
Cdd:COG4097   146 ------LRR---RLP--------YELWRLTHRLLAVAYLLLAFHH--LLLGGPFYWSPpagvlwaALAAAGLAAAVYS-- 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 495 RTIRRVRESSYGVTVIKAAIYPGNVLSIHMNKPSS--FKYKSGMYMFVKCPDvSPF--EWHPFSITSAP-GDDYLSVHIR 569
Cdd:COG4097   205 RLGRPLRSRRHPYRVESVEPEAGDVVELTLRPEGGrwLGHRAGQFAFLRFDG-SPFweEAHPFSISSAPgGDGRLRFTIK 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 570 TLGDWTTELRNLfgkaceaqvsskkatlarlettiiadglKEETcfpKVFIDGPFGApaqnykkYDILLLIGLGIGA--- 646
Cdd:COG4097   284 ALGDFTRRLGRL----------------------------KPGT---RVYVEGPYGR-------FTFDRRDTAPRQVwia 325

                         330
                  ....*....|....*
gi 1002267452 647 -----TPFISILKDL 656
Cdd:COG4097   326 ggigiTPFLALLRAL 340
PLN02292 PLN02292
ferric-chelate reductase
 445-680 3.11e-13

ferric-chelate reductase


Pssm-ID: 215165 [Multi-domain]  Cd Length: 702  Bit Score: 73.36  E-value: 3.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 445 FNAFWYAHHLLVIAYILLVLHSYFIFltkqwynrttwMFLAVPVLFYSCERTIRRVRESSYGVTVIKAAIYPGNVLSIHM 524
Cdd:PLN02292  276 FEVFFYTHYLYIVFMLFFVFHVGISF-----------ALISFPGFYIFLVDRFLRFLQSRNNVKLVSARVLPCDTVELNF 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 525 NKPSSFKYKSGMYMFVKCPDVSPFEWHPFSITSAPG--DDYLSVHIRTLGDWTTELRNLFGKaceaqvSSKKATLArlet 602
Cdd:PLN02292  345 SKNPMLMYSPTSIMFVNIPSISKLQWHPFTITSSSKlePEKLSVMIKSQGKWSTKLYHMLSS------SDQIDRLA---- 414

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 603 tiiadglkeetcfpkVFIDGPFGAPAQNYKKYDILLLIGLGIGATPFISILKDLLNniksngdVQSTHDAE-----LGCT 677
Cdd:PLN02292  415 ---------------VSVEGPYGPASTDFLRHESLVMVSGGSGITPFISIIRDLIY-------TSSTETCKipkitLICA 472


                  ...
gi 1002267452 678 FKS 680
Cdd:PLN02292  473 FKN 475
PLN02631 PLN02631
ferric-chelate reductase
 396-679 8.92e-13

ferric-chelate reductase


Pssm-ID: 178238 [Multi-domain]  Cd Length: 699  Bit Score: 72.00  E-value: 8.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 396 PTYSSLVASTpgwtgILMILIMSFSFTlATHSFRRSvvklpsplhhlaGFNAFWYAHHLLVIAYILLVLHSyfifltkqw 475
Cdd:PLN02631  228 PTYVPNLAGT-----IAMVIGIAMWVT-SLPSFRRK------------KFELFFYTHHLYGLYIVFYVIHV--------- 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 476 ynRTTWMFLAVPVLFYSCERTIRRVRESSYGVTVIKAAIYPGNVLSIHMNKPSSFKYKSGMYMFVKCPDVSPFEWHPFSI 555
Cdd:PLN02631  281 --GDSWFCMILPNIFLFFIDRYLRFLQSTKRSRLVSARILPSDNLELTFSKTPGLHYTPTSILFLHVPSISKLQWHPFTI 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 556 TSAPG--DDYLSVHIRTLGDWTTELrnlfgkaceaqvsskkatLARLETTIiaDGLKEETcfpkvfiDGPFGAPAQNYKK 633
Cdd:PLN02631  359 TSSSNleKDTLSVVIRRQGSWTQKL------------------YTHLSSSI--DSLEVST-------EGPYGPNSFDVSR 411

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1002267452 634 YDILLLIGLGIGATPFISILKDLLNniKSNGDVQSTHDAELGCTFK 679
Cdd:PLN02631  412 HNSLILVSGGSGITPFISVIRELIF--QSQNPSTKLPDVLLVCSFK 455
Ferric_reduct pfam01794
Ferric reductase like transmembrane component; This family includes a common region in the ...
 314-463 8.53e-12

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: 62.67  E-value: 8.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 314 LNMAVILLPVCRNT-LTRLRStalskvVPFDDNINFHKVIALTIAIGAATHTLAHVTCDFPRLVScprdkfeatlgpyfn 392
Cdd:pfam01794   7 ALLPLLLLLALRNNpLEWLTG------LSYDRLLLFHRWLGRLAFLLALLHVILYLIYWLRFSLE--------------- 65

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002267452 393 yvqPTYSSLVASTPGWTGILMILIMSFSFTLATHSFRRSvvklpsplhhlaGFNAFWYAHHLLVIAYILLV 463
Cdd:pfam01794  66 ---GILDLLLKRPYNILGIIALVLLVLLAITSLPPFRRL------------SYELFLYLHILLAVAFLLLV 121
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
76-208 5.70e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.18  E-value: 5.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452  76 KNVEKRFDEMSA--DGRLPQESFAKcIGMADSKEFASEVFValarrrsikPEDG-ITKEQLKEFWEELTDQNFDSRLRIF 152
Cdd:COG5126     5 RKLDRRFDLLDAdgDGVLERDDFEA-LFRRLWATLFSEADT---------DGDGrISREEFVAGMESLFEATVEPFARAA 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002267452 153 FDMCDKNGDGQLTEDEVKEVivlsaaankLAKLKSHAATyASLIMEELDPDHRGYI 208
Cdd:COG5126    75 FDLLDTDGDGKISADEFRRL---------LTALGVSEEE-ADELFARLDTDGDGKI 120
FNR_like_3 cd06198
NAD(P) binding domain of ferredoxin reductase-like proteins catalyze electron transfer ...
 516-580 1.27e-06

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: 49.95  E-value: 1.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002267452 516 PGNVLSIHMNKPS-SFKYKSGMYMFVKCPDVSPFEWHPFSITSAPGDDY-LSVHIRTLGDWTTELRN 580
Cdd:cd06198     6 VRPTTTLTLEPRGpALGHRAGQFAFLRFDASGWEEPHPFTISSAPDPDGrLRFTIKALGDYTRRLAE 72
EF-hand_7 pfam13499
EF-hand domain pair;
146-218 4.77e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 44.94  E-value: 4.77e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002267452 146 DSRLRIFFDMCDKNGDGQLTEDEVKEVIVLSAAANKLAKlkshaaTYASLIMEELDPDHRGYIEIWQLETLLR 218
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSD------EEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 62-226 6.22e-06

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: 48.50  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452  62 LRFLDKTSAGKDGWK-NVEKRFDE-MSA-----DGRL----------PQESFAKCIgMADSKEFASEVFVALARRRSIKP 124
Cdd:cd15902    25 LRELLKALNGKDKTDdEVAEKKKEfMEKydeneDGKIeirelanilpTEENFLLLF-RREQPLISSVEFMKIWRKYDTDG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 125 EDGITKEQLKEFWEELTDQN----FDSRLRIFFDMC----DKNGDGQLTEDE------VKEVIVLSAAANKLAKLKShaA 190
Cdd:cd15902   104 SGFIEAKELKGFLKDLLLKNkkhvSPPKLDEYTKLIlkefDANKDGKLELDEmakllpVQENFLLKFQILGAMDLTK--E 181

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1002267452 191 TYASlIMEELDPDHRGYIEIWQLETLLRGMVTAQGP 226
Cdd:cd15902   182 DFEK-VFEHYDKDNNGVIEGNELDALLKDLLEKNKA 216
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 126-173 2.60e-05

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 42.53  E-value: 2.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002267452 126 DG-ITKEQLKEFWEELTDQNFDSRLRIFFDMCDKNGDGQLTEDEVKEVI 173
Cdd:cd00051    14 DGtISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 148-220 9.14e-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: 40.99  E-value: 9.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002267452 148 RLRIFFDMCDKNGDGQLTEDEVKEVIVLSAAANKLAKLKShaatyaslIMEELDPDHRGYIeiwQLETLLRGM 220
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDE--------MIREVDKDGDGKI---DFEEFLELM 62
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 527-581 1.03e-04

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: 44.36  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1002267452 527 PSSFKYKSGMYMFVKCPDVSPFEWHPFSITSAPGD-DYLSVHIRT--LGDWTTELRNL 581
Cdd:cd00322    18 PNGFSFKPGQYVDLHLPGDGRGLRRAYSIASSPDEeGELELTVKIvpGGPFSAWLHDL 75
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 106-212 2.22e-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: 43.83  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452 106 KEFASEVFVAlarrrsikpedgitkEQLKEFwEELTDQNFDSRLRIFFDMCDKNGDGQLTEDEVKEVIvlsaaankLAKL 185
Cdd:cd16225     9 KEFHKEVFLG---------------NEKEEF-EEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWI--------MEKT 64

                          90       100       110
                  ....*....|....*....|....*....|
gi 1002267452 186 KSH---AATYASLIMEELDPDHRGYIEiWQ 212
Cdd:cd16225    65 QEHfqeAVEENEQIFKAVDTDKDGNVS-WE 93
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 130-173 4.21e-04

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


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 42.96  E-value: 4.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1002267452 130 KEQLKEFwEELTDQNFDSRLRIFFDMCDKNGDGQLTEDEVKEVI 173
Cdd:cd16226    19 KEEAKEF-DQLTPEESKERLGIIVDKIDKNGDGFVTEEELKDWI 61
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 148-218 2.31e-03

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 39.19  E-value: 2.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002267452 148 RLRIFFDMCDKNGDGQLTEDEVKEVIvlsaaaNKLAKLKSHAatYASLIMEELDPDHRGYIEIWQLETLLR 218
Cdd:cd15898     1 WLRRQWIKADKDGDGKLSLKEIKKLL------KRLNIRVSEK--ELKKLFKEVDTNGDGTLTFDEFEELYK 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
75-171 2.89e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.62  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002267452  75 WKNVEKRFDEmSADGRLPQESFAKCIG---MADSKEFASEVFVALARrrsikpeDG---ITKEQLKEFWEELTDQnfDSR 148
Cdd:COG5126    35 WATLFSEADT-DGDGRISREEFVAGMEslfEATVEPFARAAFDLLDT-------DGdgkISADEFRRLLTALGVS--EEE 104

                          90       100
                  ....*....|....*....|...
gi 1002267452 149 LRIFFDMCDKNGDGQLTEDEVKE 171
Cdd:COG5126   105 ADELFARLDTDGDGKISFEEFVA 127
EF-hand_6 pfam13405
EF-hand domain;
148-173 7.14e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 7.14e-03
                          10        20
                  ....*....|....*....|....*.
gi 1002267452 148 RLRIFFDMCDKNGDGQLTEDEVKEVI 173
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKAL 26
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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