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Conserved domains on  [gi|21218408|ref|NP_631974|]
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rhomboid-related protein 3 [Mus musculus]

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 ...
 205-359 1.08e-27

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: 106.54  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408   205 PQLRAQAWRYVTYIFMHAGVEQLGLNVALQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADM-TAPVVGSSGGVYA 283
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPlSTPSVGASGAIFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21218408   284 LVSAHLANIVMNWSGMKcqFKLLRMAVALICMSMEFGRAVWLRFhpsayppcpHPSFVAHLGGVAVGITLGVVVLR 359
Cdd:pfam01694  81 LLGALLVLGPRNRILLF--GLIGALLALLLFILLNLVLGLLPGN---------GVSNLAHLGGLLVGLLLGFILLR 145
EF-hand_7 pfam13499
EF-hand domain pair;
36-100 6.46e-08

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.17  E-value: 6.46e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21218408    36 EDHWKVLFEKFDPGSTGYISTGKFRSLLESHSSKLDPHKKEV--LLALADSHADGQICYQDFVNLMS 100
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVeeLFKEFDLDKDGRISFEEFLELYS 67
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 205-359 1.08e-27

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: 106.54  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408   205 PQLRAQAWRYVTYIFMHAGVEQLGLNVALQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADM-TAPVVGSSGGVYA 283
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPlSTPSVGASGAIFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21218408   284 LVSAHLANIVMNWSGMKcqFKLLRMAVALICMSMEFGRAVWLRFhpsayppcpHPSFVAHLGGVAVGITLGVVVLR 359
Cdd:pfam01694  81 LLGALLVLGPRNRILLF--GLIGALLALLLFILLNLVLGLLPGN---------GVSNLAHLGGLLVGLLLGFILLR 145
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 163-364 6.46e-18

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


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 81.06  E-value: 6.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408 163 PWFMITITLLEVALFLYNGVLLDQFVlqvthprylkNSLVYHPQ--LRAQAWRYVTYIFMHAGVEQLGLNVALQLLVGVP 240
Cdd:COG0705   3 PPVTLALIALNVLVFLLQLLLGGELL----------NWLALVPArlLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408 241 LEMVHGATRIGLVYVAGVVAGSLAVSVADMT--APVVGSSGGVYALVSAHLA-NIVMNWSGMKCQFKLLRMAVALICMSM 317
Cdd:COG0705  73 LERRLGSKRFLLLYLLSGLGGGLLQLLFSPGsgYPLVGASGAIFGLLGALLVlGPRRRVLLLFIPIPALLFLLVWLLLGL 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21218408 318 EFGRAVWlrfhpsayppcPHPSFVAHLGGVAVGITLGVVVLRNYEQR 364
Cdd:COG0705 153 LFGLLGG-----------GGIAWEAHLGGLLAGLLLALLLRKLRRRR 188
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
 208-395 3.85e-08

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 54.09  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408  208 RAQAWRYVTYIFMHAGVEQLGLNVALQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADMTAPVVGSSGGVYALVSA 287
Cdd:PTZ00101  99 QGEIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVKIIILYFLTGIYGNILSSSVTYCPIKVGASTSGMGLLGI 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408  288 HLANIVMNWSGMKCQFKLLRMAVALICMSMEFgravWLRFHPSAYppcphpSFVAHLGGVAVGITLGVVvlrnYEQRLQD 367
Cdd:PTZ00101 179 VTSELILLWHVIRHRERVVFNIIFFSLISFFY----YFTFNGSNI------DHVGHLGGLLSGISMGIL----YNSQMEN 244

                        170       180       190
                 ....*....|....*....|....*....|
gi 21218408  368 QSLW--WIFVTMYTIFVLFAVFWNIFAYTL 395
Cdd:PTZ00101 245 KPSWydHMKMASYACLALLAIVPPIVLFAV 274
EF-hand_7 pfam13499
EF-hand domain pair;
36-100 6.46e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.17  E-value: 6.46e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21218408    36 EDHWKVLFEKFDPGSTGYISTGKFRSLLESHSSKLDPHKKEV--LLALADSHADGQICYQDFVNLMS 100
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVeeLFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 36-102 3.70e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 49.37  E-value: 3.70e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21218408   36 EDHWKVLFEKFDPGSTGYISTGKFRSLLESHSSKLDPHKKEVLLALADSHADGQICYQDFVNLMSNK 102
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMSK 149
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 38-99 1.80e-06

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: 47.58  E-value: 1.80e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21218408  38 HWKVLFEKFDPGSTGYISTGKFRSLLESHSSKLDPHkkeVLLALAD--SHADGQICYQDFVNLM 99
Cdd:cd16196  72 SWKRVFKLFDTDGSGSFSSFELRNALNSAGFRLSNA---TLNALVLrySNKDGRISFDDFIMCA 132
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
42-99 7.60e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 7.60e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21218408  42 LFEKFDPGSTGYISTGKFRSLLESHssKLDPHKKEVLLALADSHADGQICYQDFVNLM 99
Cdd:COG5126  74 AFDLLDTDGDGKISADEFRRLLTAL--GVSEEEADELFARLDTDGDGKISFEEFVAAV 129
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
 205-359 1.08e-27

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: 106.54  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408   205 PQLRAQAWRYVTYIFMHAGVEQLGLNVALQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADM-TAPVVGSSGGVYA 283
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPlSTPSVGASGAIFG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21218408   284 LVSAHLANIVMNWSGMKcqFKLLRMAVALICMSMEFGRAVWLRFhpsayppcpHPSFVAHLGGVAVGITLGVVVLR 359
Cdd:pfam01694  81 LLGALLVLGPRNRILLF--GLIGALLALLLFILLNLVLGLLPGN---------GVSNLAHLGGLLVGLLLGFILLR 145
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
 163-364 6.46e-18

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


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 81.06  E-value: 6.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408 163 PWFMITITLLEVALFLYNGVLLDQFVlqvthprylkNSLVYHPQ--LRAQAWRYVTYIFMHAGVEQLGLNVALQLLVGVP 240
Cdd:COG0705   3 PPVTLALIALNVLVFLLQLLLGGELL----------NWLALVPArlLLGELWRLLTSMFLHGGFLHLLFNMLALWVFGPL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408 241 LEMVHGATRIGLVYVAGVVAGSLAVSVADMT--APVVGSSGGVYALVSAHLA-NIVMNWSGMKCQFKLLRMAVALICMSM 317
Cdd:COG0705  73 LERRLGSKRFLLLYLLSGLGGGLLQLLFSPGsgYPLVGASGAIFGLLGALLVlGPRRRVLLLFIPIPALLFLLVWLLLGL 152

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21218408 318 EFGRAVWlrfhpsayppcPHPSFVAHLGGVAVGITLGVVVLRNYEQR 364
Cdd:COG0705 153 LFGLLGG-----------GGIAWEAHLGGLLAGLLLALLLRKLRRRR 188
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
 208-395 3.85e-08

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 54.09  E-value: 3.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408  208 RAQAWRYVTYIFMHAGVEQLGLNVALQLLVGVPLEMVHGATRIGLVYVAGVVAGSLAVSVADMTAPVVGSSGGVYALVSA 287
Cdd:PTZ00101  99 QGEIHRLILPIFLHANIFHTFFNVFFQLRMGFTLEKNYGIVKIIILYFLTGIYGNILSSSVTYCPIKVGASTSGMGLLGI 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408  288 HLANIVMNWSGMKCQFKLLRMAVALICMSMEFgravWLRFHPSAYppcphpSFVAHLGGVAVGITLGVVvlrnYEQRLQD 367
Cdd:PTZ00101 179 VTSELILLWHVIRHRERVVFNIIFFSLISFFY----YFTFNGSNI------DHVGHLGGLLSGISMGIL----YNSQMEN 244

                        170       180       190
                 ....*....|....*....|....*....|
gi 21218408  368 QSLW--WIFVTMYTIFVLFAVFWNIFAYTL 395
Cdd:PTZ00101 245 KPSWydHMKMASYACLALLAIVPPIVLFAV 274
EF-hand_7 pfam13499
EF-hand domain pair;
36-100 6.46e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.17  E-value: 6.46e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21218408    36 EDHWKVLFEKFDPGSTGYISTGKFRSLLESHSSKLDPHKKEV--LLALADSHADGQICYQDFVNLMS 100
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVeeLFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 36-102 3.70e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 49.37  E-value: 3.70e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21218408   36 EDHWKVLFEKFDPGSTGYISTGKFRSLLESHSSKLDPHKKEVLLALADSHADGQICYQDFVNLMSNK 102
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMMSK 149
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 38-99 1.80e-06

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: 47.58  E-value: 1.80e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21218408  38 HWKVLFEKFDPGSTGYISTGKFRSLLESHSSKLDPHkkeVLLALAD--SHADGQICYQDFVNLM 99
Cdd:cd16196  72 SWKRVFKLFDTDGSGSFSSFELRNALNSAGFRLSNA---TLNALVLrySNKDGRISFDDFIMCA 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 40-100 1.42e-04

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: 39.45  E-value: 1.42e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21218408  40 KVLFEKFDPGSTGYISTGKFRSLLESHSSKLDphKKEV--LLALADSHADGQICYQDFVNLMS 100
Cdd:cd00051   3 REAFRLFDKDGDGTISADELKAALKSLGEGLS--EEEIdeMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
42-99 7.60e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 7.60e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 21218408  42 LFEKFDPGSTGYISTGKFRSLLESHssKLDPHKKEVLLALADSHADGQICYQDFVNLM 99
Cdd:COG5126  74 AFDLLDTDGDGKISADEFRRLLTAL--GVSEEEADELFARLDTDGDGKISFEEFVAAV 129
EF-hand_11 pfam08976
EF-hand domain; This domain is found predominantly in DJ binding proteins.
 30-106 1.55e-03

EF-hand domain; This domain is found predominantly in DJ binding proteins.


Pssm-ID: 401068  Cd Length: 105  Bit Score: 37.77  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21218408    30 RLPAAPEDHWKVL---FEKFDPGSTGYISTGKFRSLLESHSSKLDPHKKEVLLALADSHADGQICYQDFVNLMSNKRSNS 106
Cdd:pfam08976  10 RLHKAVASHYHAItqeFENFDTLKSNTISRDEFRAICNRHIQILTDEQFDRLWNELPVNAKGRLKYPDFLSKFSIERTAA 89
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 42-99 3.05e-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: 36.04  E-value: 3.05e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21218408  42 LFEKFDPGSTGYISTGKFRSLLEShsSKLDphkKEVL---LALADSHADGQICYQDFVNLM 99
Cdd:cd00052   4 IFRSLDPDGDGLISGDEARPFLGK--SGLP---RSVLaqiWDLADTDKDGKLDKEEFAIAM 59
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 49-99 9.50e-03

S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins.


Pssm-ID: 238131 [Multi-domain]  Cd Length: 88  Bit Score: 35.16  E-value: 9.50e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21218408  49 GSTGYISTGKFRSLLESH-----SSKLDPHKKEVLLALADSHADGQICYQDFVNLM 99
Cdd:cd00213  22 GDKDTLSKKELKELLETElpnflKNQKDPEAVDKIMKDLDVNKDGKVDFQEFLVLI 77
 
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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