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Conserved domains on  [gi|1054314513|ref|NP_001317110|]
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rhomboid-related protein 3 isoform 2 [Homo sapiens]

Protein Classification

rhomboid family intramembrane serine protease( domain architecture ID 12145414)

rhomboid family intramembrane serine protease is a membrane-bound protein that catalyzes regulated intramembrane proteolysis, resulting in the release of functional polypeptides from their membrane anchor; contains an EF-hand calcium binding domain

CATH:  1.20.1540.10
EC:  3.4.21.-
Gene Ontology:  GO:0004252|GO:0005509
MEROPS:  S54
PubMed:  22035660|24099005|28707401
SCOP:  4000471

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 197-351 3.79e-29

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


:

Pssm-ID: 426384  Cd Length: 147  Bit Score: 110.39  E-value: 3.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 197 PQLRAQVWRYLTYIFMHAGIEHLGLNVVLQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADM-TAPVVGSSGGVYA 275
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPlSTPSVGASGAIFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054314513 276 LVSAHLANIVMNWSGMKcqFKLLRMAVALICMSMEFGRAVWLRFhpsayppcpHPSFVAHLGGVAVGITLGVVVLR 351
Cdd:pfam01694  81 LLGALLVLGPRNRILLF--GLIGALLALLLFILLNLVLGLLPGN---------GVSNLAHLGGLLVGLLLGFILLR 145
EF-hand_7 pfam13499
EF-hand domain pair;
38-92 2.86e-07

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 2.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054314513  38 FDPGNTGYISTGKFRSLLESH--SSKLDPHKREVLLALADSHADGQIGYQDFVSLMS 92
Cdd:pfam13499  11 LDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 197-351 3.79e-29

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 110.39  E-value: 3.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 197 PQLRAQVWRYLTYIFMHAGIEHLGLNVVLQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADM-TAPVVGSSGGVYA 275
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPlSTPSVGASGAIFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054314513 276 LVSAHLANIVMNWSGMKcqFKLLRMAVALICMSMEFGRAVWLRFhpsayppcpHPSFVAHLGGVAVGITLGVVVLR 351
Cdd:pfam01694  81 LLGALLVLGPRNRILLF--GLIGALLALLLFILLNLVLGLLPGN---------GVSNLAHLGGLLVGLLLGFILLR 145
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 179-356 2.81e-19

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 84.91  E-value: 2.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 179 FVLQVTHPRYLKNSLVYHPQ--LRAQVWRYLTYIFMHAGIEHLGLNVVLQLLVGVPLEMVHGATRIGLVYVAGVVAGSLA 256
Cdd:COG0705    17 FLLQLLLGGELLNWLALVPArlLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPLLERRLGSKRFLLLYLLSGLGGGLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 257 VSVADMT--APVVGSSGGVYALVSAHLA-NIVMNWSGMKCQFKLLRMAVALICMSMEFGRAVWlrfhpsayppcPHPSFV 333
Cdd:COG0705    97 QLLFSPGsgYPLVGASGAIFGLLGALLVlGPRRRVLLLFIPIPALLFLLVWLLLGLLFGLLGG-----------GGIAWE 165

                         170       180
                  ....*....|....*....|...
gi 1054314513 334 AHLGGVAVGITLGVVVLRNYEQR 356
Cdd:COG0705   166 AHLGGLLAGLLLALLLRKLRRRR 188
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
 200-386 1.52e-10

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 61.41  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 200 RAQVWRYLTYIFMHAGIEHLGLNVVLQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADMTAPVVGSSGGVYALVSA 279
Cdd:PTZ00101   99 QGEIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVKIIILYFLTGIYGNILSSSVTYCPIKVGASTSGMGLLGI 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 280 HLANIVMNWSGMKCQFKLLRMAVALICMSMEFgravWLRFHPSAYppcphpSFVAHLGGVAVGITLGVVvlrnYEQRLQD 359
Cdd:PTZ00101  179 VTSELILLWHVIRHRERVVFNIIFFSLISFFY----YFTFNGSNI------DHVGHLGGLLSGISMGIL----YNSQMEN 244

                         170       180
                  ....*....|....*....|....*....
gi 1054314513 360 QSLW--WIFVAMYTVFVLFAVFWNIFAYT 386
Cdd:PTZ00101  245 KPSWydHMKMASYACLALLAIVPPIVLFA 273
EF-hand_7 pfam13499
EF-hand domain pair;
38-92 2.86e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 2.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054314513  38 FDPGNTGYISTGKFRSLLESH--SSKLDPHKREVLLALADSHADGQIGYQDFVSLMS 92
Cdd:pfam13499  11 LDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 38-94 1.82e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.45  E-value: 1.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054314513  38 FDPGNTGYISTGKFRSLLESHSSKLDPHKREVLLALADSHADGQIGYQDFVSLMSNK 94
Cdd:PTZ00184   93 FDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMSK 149
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 38-91 1.74e-03

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


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 38.72  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054314513  38 FDPGNTGYISTGKFRSLLESHSSKLDPHkreVLLALAD--SHADGQIGYQDFVSLM 91
Cdd:cd16196    80 FDTDGSGSFSSFELRNALNSAGFRLSNA---TLNALVLrySNKDGRISFDDFIMCA 132
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
38-91 6.13e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.69  E-value: 6.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054314513  38 FDPGNTGYISTGKFRSLLESHssKLDPHKREVLLALADSHADGQIGYQDFVSLM 91
Cdd:COG5126    78 LDTDGDGKISADEFRRLLTAL--GVSEEEADELFARLDTDGDGKISFEEFVAAV 129
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 197-351 3.79e-29

Rhomboid family; This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.


Pssm-ID: 426384  Cd Length: 147  Bit Score: 110.39  E-value: 3.79e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 197 PQLRAQVWRYLTYIFMHAGIEHLGLNVVLQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADM-TAPVVGSSGGVYA 275
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPlSTPSVGASGAIFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1054314513 276 LVSAHLANIVMNWSGMKcqFKLLRMAVALICMSMEFGRAVWLRFhpsayppcpHPSFVAHLGGVAVGITLGVVVLR 351
Cdd:pfam01694  81 LLGALLVLGPRNRILLF--GLIGALLALLLFILLNLVLGLLPGN---------GVSNLAHLGGLLVGLLLGFILLR 145
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 179-356 2.81e-19

Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 84.91  E-value: 2.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 179 FVLQVTHPRYLKNSLVYHPQ--LRAQVWRYLTYIFMHAGIEHLGLNVVLQLLVGVPLEMVHGATRIGLVYVAGVVAGSLA 256
Cdd:COG0705    17 FLLQLLLGGELLNWLALVPArlLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPLLERRLGSKRFLLLYLLSGLGGGLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 257 VSVADMT--APVVGSSGGVYALVSAHLA-NIVMNWSGMKCQFKLLRMAVALICMSMEFGRAVWlrfhpsayppcPHPSFV 333
Cdd:COG0705    97 QLLFSPGsgYPLVGASGAIFGLLGALLVlGPRRRVLLLFIPIPALLFLLVWLLLGLLFGLLGG-----------GGIAWE 165

                         170       180
                  ....*....|....*....|...
gi 1054314513 334 AHLGGVAVGITLGVVVLRNYEQR 356
Cdd:COG0705   166 AHLGGLLAGLLLALLLRKLRRRR 188
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
 200-386 1.52e-10

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 61.41  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 200 RAQVWRYLTYIFMHAGIEHLGLNVVLQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADMTAPVVGSSGGVYALVSA 279
Cdd:PTZ00101   99 QGEIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVKIIILYFLTGIYGNILSSSVTYCPIKVGASTSGMGLLGI 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1054314513 280 HLANIVMNWSGMKCQFKLLRMAVALICMSMEFgravWLRFHPSAYppcphpSFVAHLGGVAVGITLGVVvlrnYEQRLQD 359
Cdd:PTZ00101  179 VTSELILLWHVIRHRERVVFNIIFFSLISFFY----YFTFNGSNI------DHVGHLGGLLSGISMGIL----YNSQMEN 244

                         170       180
                  ....*....|....*....|....*....
gi 1054314513 360 QSLW--WIFVAMYTVFVLFAVFWNIFAYT 386
Cdd:PTZ00101  245 KPSWydHMKMASYACLALLAIVPPIVLFA 273
EF-hand_7 pfam13499
EF-hand domain pair;
38-92 2.86e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 2.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054314513  38 FDPGNTGYISTGKFRSLLESH--SSKLDPHKREVLLALADSHADGQIGYQDFVSLMS 92
Cdd:pfam13499  11 LDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 38-94 1.82e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.45  E-value: 1.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054314513  38 FDPGNTGYISTGKFRSLLESHSSKLDPHKREVLLALADSHADGQIGYQDFVSLMSNK 94
Cdd:PTZ00184   93 FDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMSK 149
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 38-91 1.74e-03

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


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 38.72  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1054314513  38 FDPGNTGYISTGKFRSLLESHSSKLDPHkreVLLALAD--SHADGQIGYQDFVSLM 91
Cdd:cd16196    80 FDTDGSGSFSSFELRNALNSAGFRLSNA---TLNALVLrySNKDGRISFDDFIMCA 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 36-92 2.99e-03

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: 35.99  E-value: 2.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1054314513  36 EDFDPGNTGYISTGKFRSLLESHSSKLDPHKREVLLALADSHADGQIGYQDFVSLMS 92
Cdd:cd00051     7 RLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 36-91 4.01e-03

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 35.66  E-value: 4.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1054314513  36 EDFDPGNTGYISTGKFRSLLEShsSKLDphkREVL---LALADSHADGQIGYQDFVSLM 91
Cdd:cd00052     6 RSLDPDGDGLISGDEARPFLGK--SGLP---RSVLaqiWDLADTDKDGKLDKEEFAIAM 59
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
38-91 6.13e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 36.69  E-value: 6.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1054314513  38 FDPGNTGYISTGKFRSLLESHssKLDPHKREVLLALADSHADGQIGYQDFVSLM 91
Cdd:COG5126    78 LDTDGDGKISADEFRRLLTAL--GVSEEEADELFARLDTDGDGKISFEEFVAAV 129
 
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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