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Conserved domains on  [gi|17933592|ref|NP_525084|]
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rhomboid-4, isoform B [Drosophila melanogaster]

Protein Classification

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 ...
226-374 5.99e-36

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: 128.88  E-value: 5.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   226 PYKRYEGWRFVSYMFVHVGIMHLMMNLIIQIFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSPR-IFLAGASGGVYA 304
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLsTPSVGASGAIFG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   305 LITAHIATIIMNYSEMEYAIVQLLAFLVFCFTDLGTSVYRHLtdqhdQIGYVAHLSGAVAGLLVGIGVLR 374
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLLPGN-----GVSNLAHLGGLLVGLLLGFILLR 145
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
49-131 8.94e-12

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.50  E-value: 8.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  49 RQDTIDMEEIPLNQTNSQEPEDRRKMHEIFDKHDSDRDGLINTHELKELISDgycRDIPAYIADQILKRSDQDNDGHLDF 128
Cdd:COG5126  46 GDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTA---LGVSEEEADELFARLDTDGDGKISF 122

                ...
gi 17933592 129 EEF 131
Cdd:COG5126 123 EEF 125
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
226-374 5.99e-36

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: 128.88  E-value: 5.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   226 PYKRYEGWRFVSYMFVHVGIMHLMMNLIIQIFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSPR-IFLAGASGGVYA 304
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLsTPSVGASGAIFG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   305 LITAHIATIIMNYSEMEYAIVQLLAFLVFCFTDLGTSVYRHLtdqhdQIGYVAHLSGAVAGLLVGIGVLR 374
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLLPGN-----GVSNLAHLGGLLVGLLLGFILLR 145
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
178-380 2.84e-27

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


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 107.25  E-value: 2.84e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592 178 PPLTMVLFsIIEIIMFLVDVIhfqddpnyqdrigesTSGPAATLFIYNPYKRYEG--WRFVSYMFVHVGIMHLMMNLIIQ 255
Cdd:COG0705   3 PPVTLALI-ALNVLVFLLQLL---------------LGGELLNWLALVPARLLLGelWRLLTSMFLHGGFLHLLFNMLAL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592 256 IFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSP--RIFLAGASGGVYALITAHIATIIMNYSEMEYAIVQLLAFLVF 333
Cdd:COG0705  67 WVFGPLLERRLGSKRFLLLYLLSGLGGGLLQLLFSPgsGYPLVGASGAIFGLLGALLVLGPRRRVLLLFIPIPALLFLLV 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17933592 334 CFtdlGTSVYRHLTDQhDQIGYVAHLSGAVAGLLVGIgVLRNLEVRR 380
Cdd:COG0705 147 WL---LLGLLFGLLGG-GGIAWEAHLGGLLAGLLLAL-LLRKLRRRR 188
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
49-131 8.94e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.50  E-value: 8.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  49 RQDTIDMEEIPLNQTNSQEPEDRRKMHEIFDKHDSDRDGLINTHELKELISDgycRDIPAYIADQILKRSDQDNDGHLDF 128
Cdd:COG5126  46 GDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTA---LGVSEEEADELFARLDTDGDGKISF 122

                ...
gi 17933592 129 EEF 131
Cdd:COG5126 123 EEF 125
rhom_GG_sort TIGR03902
rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like ...
219-370 2.15e-11

rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like intramembrane serine protease. Its species distribution closely matches model TIGR03501, GlyGly-CTERM, which describes a protein targeting domain analogous to LPXTG and PEP-CTERM. In a number of species (Ralstonia eutropha ,R. metallidurans, R. solanacearum, Marinobacter aquaeolei, etc) with just one GlyGly-CTERM protein (i.e., a dedicated system), the rhombosortase and GlyGly-CTERM genes are adjacent.


Pssm-ID: 274845  Cd Length: 154  Bit Score: 61.82  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   219 ATLFIYNPY--KRYEGWRFVSYMFVHVGIMHLMMNLIIQIFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSPRI-FL 295
Cdd:TIGR03902   1 SDLLAYDRAaiLDGEWWRLLTGHFVHLNWWHLLMNLAGLLLLWALFGRHLRARRLLLLLLLLSLLISLGLLLFLPSLqWY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17933592   296 AGASGGVYALITAHIATIIMNYSEMEYAIVQLLAF-LVFCFTDLGTSVYRHLTDQHdqIGYVAHLSGAVAGLLVGI 370
Cdd:TIGR03902  81 VGLSGVLHGLFAWGALRDIRYGRRSGWLLLLGVIAkLAWEQLFGASAFTAALIGAP--VATEAHLAGAISGLLIAL 154
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
73-134 1.27e-10

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: 56.79  E-value: 1.27e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17933592  73 KMHEIFDKHDSDRDGLINTHELKELISdGYCRDIPAYIADQILKRSDQDNDGHLDFEEFYAM 134
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALK-SLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
71-134 6.92e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.95  E-value: 6.92e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17933592    71 RRKMHEIFDKHDSDRDGLINTHELKELISdGYCRDIPA--YIADQILKRSDQDNDGHLDFEEFYAM 134
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLR-KLEEGEPLsdEEVEELFKEFDLDKDGRISFEEFLEL 65
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
67-137 6.88e-08

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 49.97  E-value: 6.88e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17933592     67 EPEDRRKMHEIFDKHDSDRDGLINTHELKELIsdgYCRDIPAYIADQILKRSDQDNDGHLDFEEFY-AMSLR 137
Cdd:smart00027   5 SPEDKAKYEQIFRSLDKNQDGTVTGAQAKPIL---LKSGLPQTLLAKIWNLADIDNDGELDKDEFAlAMHLI 73
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
182-402 2.72e-06

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 48.69  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  182 MVLFSIIEIIMFLVDVIHFQDDPnyqdrigestSGPAATLFI-----YNP-YKRYEGWRFVSYMFVHVGIMHLMMNLIIQ 255
Cdd:PTZ00101  56 IMAISIIQIIVFIISVSIKPADF----------LTPSDSLLVtlganVASrIKQGEIHRLILPIFLHANIFHTFFNVFFQ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  256 IFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSPRIFLAGASGGVYALITAHIATIIMNYSEMEYAIVQLLAFLVFCF 335
Cdd:PTZ00101 126 LRMGFTLEKNYGIVKIIILYFLTGIYGNILSSSVTYCPIKVGASTSGMGLLGIVTSELILLWHVIRHRERVVFNIIFFSL 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17933592  336 tdlgTSVYRHLTDQHDQIGYVAHLSGAVAGllVGIGVLRNLEVRRWERILWWVAVIVYFALMTTGII 402
Cdd:PTZ00101 206 ----ISFFYYFTFNGSNIDHVGHLGGLLSG--ISMGILYNSQMENKPSWYDHMKMASYACLALLAIV 266
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
61-167 3.51e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 47.75  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   61 NQTNSQEPEDrrkmhEIFDKHDSDRDGLINTHELKELISDGyCRDIPAYIADQILKRSDQDNDGHLDFEEFYAMSlrhkw 140
Cdd:NF041410  21 SSARSQQFQK-----QLFAKLDSDGDGSVSQDELSSALSSK-SDDGSLIDLSELFSDLDSDGDGSLSSDELAAAA----- 89
                         90       100
                 ....*....|....*....|....*..
gi 17933592  141 mvrnmltrycryvvPPPKPLEGDEPDG 167
Cdd:NF041410  90 --------------PPPPPPPDQAPST 102
CCC1_like cd01059
CCC1-related family of proteins; CCC1_like: This protein family includes the proteins related ...
272-406 3.30e-04

CCC1-related family of proteins; CCC1_like: This protein family includes the proteins related to CCC1, a yeast vacuole transmembrane protein responsible for the iron and manganese transport from the cytosol into vacuole. It also includes the proteins similar to nodulin-21, a plant nodule-specific protein that may be involved in symbiotic nitrogen fixation.


Pssm-ID: 153121  Cd Length: 143  Bit Score: 40.67  E-value: 3.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592 272 GLVYLAGVLAGSMGTSLTSPRIFLAGASGGVYA----LITAHIATiimnYSEMEY-AIVQLLAFLVFCFTDLGTSVYrhL 346
Cdd:cd01059  11 GLVSTFALVAGVAAAGDSTKAILLAGLAGLVAGaismAAGEYVSV----KSQRDKaALASGLSFILGGLLPLLPYLL--L 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592 347 TDQHDQIGYVAHLSGAVAGLLVGIGVLRNLEVRRWERILwWVAVIVYFALMTTGIIIHVF 406
Cdd:cd01059  85 PAGSLALAVSVALVVALALFLLGAFVAKLGGAKKIRAAL-RMVVLGLLAAALTYLLGRLF 143
PTZ00184 PTZ00184
calmodulin; Provisional
52-134 8.31e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 39.74  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   52 TIDMEE-IPLNQTNSQEPEDRRKMHEIFDKHDSDRDGLINTHELKE-LISDGycRDIPAYIADQILKRSDQDNDGHLDFE 129
Cdd:PTZ00184  63 TIDFPEfLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHvMTNLG--EKLTDEEVDEMIREADVDGDGQINYE 140

                 ....*
gi 17933592  130 EFYAM 134
Cdd:PTZ00184 141 EFVKM 145
 
Name Accession Description Interval E-value
Rhomboid pfam01694
Rhomboid family; This family contains integral membrane proteins that are related to ...
226-374 5.99e-36

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: 128.88  E-value: 5.99e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   226 PYKRYEGWRFVSYMFVHVGIMHLMMNLIIQIFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSPR-IFLAGASGGVYA 304
Cdd:pfam01694   1 PVQPGQLWRLITSMFLHAGWLHLLFNMLALLFFGGPLERILGSVRFLLLYLLSGIAGSLLSYLFSPLsTPSVGASGAIFG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   305 LITAHIATIIMNYSEMEYAIVQLLAFLVFCFTDLGTSVYRHLtdqhdQIGYVAHLSGAVAGLLVGIGVLR 374
Cdd:pfam01694  81 LLGALLVLGPRNRILLFGLIGALLALLLFILLNLVLGLLPGN-----GVSNLAHLGGLLVGLLLGFILLR 145
GlpG COG0705
Membrane-associated serine protease, rhomboid family [Posttranslational modification, protein ...
178-380 2.84e-27

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


Pssm-ID: 440469 [Multi-domain]  Cd Length: 189  Bit Score: 107.25  E-value: 2.84e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592 178 PPLTMVLFsIIEIIMFLVDVIhfqddpnyqdrigesTSGPAATLFIYNPYKRYEG--WRFVSYMFVHVGIMHLMMNLIIQ 255
Cdd:COG0705   3 PPVTLALI-ALNVLVFLLQLL---------------LGGELLNWLALVPARLLLGelWRLLTSMFLHGGFLHLLFNMLAL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592 256 IFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSP--RIFLAGASGGVYALITAHIATIIMNYSEMEYAIVQLLAFLVF 333
Cdd:COG0705  67 WVFGPLLERRLGSKRFLLLYLLSGLGGGLLQLLFSPgsGYPLVGASGAIFGLLGALLVLGPRRRVLLLFIPIPALLFLLV 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 17933592 334 CFtdlGTSVYRHLTDQhDQIGYVAHLSGAVAGLLVGIgVLRNLEVRR 380
Cdd:COG0705 147 WL---LLGLLFGLLGG-GGIAWEAHLGGLLAGLLLAL-LLRKLRRRR 188
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
49-131 8.94e-12

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 62.50  E-value: 8.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  49 RQDTIDMEEIPLNQTNSQEPEDRRKMHEIFDKHDSDRDGLINTHELKELISDgycRDIPAYIADQILKRSDQDNDGHLDF 128
Cdd:COG5126  46 GDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTA---LGVSEEEADELFARLDTDGDGKISF 122

                ...
gi 17933592 129 EEF 131
Cdd:COG5126 123 EEF 125
rhom_GG_sort TIGR03902
rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like ...
219-370 2.15e-11

rhomboid family GlyGly-CTERM serine protease; This model describes a rhomboid-like intramembrane serine protease. Its species distribution closely matches model TIGR03501, GlyGly-CTERM, which describes a protein targeting domain analogous to LPXTG and PEP-CTERM. In a number of species (Ralstonia eutropha ,R. metallidurans, R. solanacearum, Marinobacter aquaeolei, etc) with just one GlyGly-CTERM protein (i.e., a dedicated system), the rhombosortase and GlyGly-CTERM genes are adjacent.


Pssm-ID: 274845  Cd Length: 154  Bit Score: 61.82  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   219 ATLFIYNPY--KRYEGWRFVSYMFVHVGIMHLMMNLIIQIFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSPRI-FL 295
Cdd:TIGR03902   1 SDLLAYDRAaiLDGEWWRLLTGHFVHLNWWHLLMNLAGLLLLWALFGRHLRARRLLLLLLLLSLLISLGLLLFLPSLqWY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17933592   296 AGASGGVYALITAHIATIIMNYSEMEYAIVQLLAF-LVFCFTDLGTSVYRHLTDQHdqIGYVAHLSGAVAGLLVGI 370
Cdd:TIGR03902  81 VGLSGVLHGLFAWGALRDIRYGRRSGWLLLLGVIAkLAWEQLFGASAFTAALIGAP--VATEAHLAGAISGLLIAL 154
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
73-134 1.27e-10

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: 56.79  E-value: 1.27e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17933592  73 KMHEIFDKHDSDRDGLINTHELKELISdGYCRDIPAYIADQILKRSDQDNDGHLDFEEFYAM 134
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALK-SLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
71-134 6.92e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 54.95  E-value: 6.92e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17933592    71 RRKMHEIFDKHDSDRDGLINTHELKELISdGYCRDIPA--YIADQILKRSDQDNDGHLDFEEFYAM 134
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLR-KLEEGEPLsdEEVEELFKEFDLDKDGRISFEEFLEL 65
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
67-137 6.88e-08

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 49.97  E-value: 6.88e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17933592     67 EPEDRRKMHEIFDKHDSDRDGLINTHELKELIsdgYCRDIPAYIADQILKRSDQDNDGHLDFEEFY-AMSLR 137
Cdd:smart00027   5 SPEDKAKYEQIFRSLDKNQDGTVTGAQAKPIL---LKSGLPQTLLAKIWNLADIDNDGELDKDEFAlAMHLI 73
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
76-136 1.80e-07

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: 47.98  E-value: 1.80e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17933592  76 EIFDKHDSDRDGLINTHELKE-LISDGycrdIPAYIADQILKRSDQDNDGHLDFEEFY-AMSL 136
Cdd:cd00052   3 QIFRSLDPDGDGLISGDEARPfLGKSG----LPRSVLAQIWDLADTDKDGKLDKEEFAiAMHL 61
EF-hand_8 pfam13833
EF-hand domain pair;
86-137 9.60e-07

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 45.38  E-value: 9.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 17933592    86 DGLINTHELKELISDGYCRDIPAYIADQILKRSDQDNDGHLDFEEFYAMSLR 137
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLLER 53
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
73-152 1.66e-06

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: 47.28  E-value: 1.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  73 KMHEIFDKHDSDRDGLINTHELKELIS-DGYCRDiPAYIAdQILKRSDQDNDGHLDFEEFYAM--SLRHKWMVRNMLTRY 149
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKrLNIRVS-EKELK-KLFKEVDTNGDGTLTFDEFEELykSLTERPELEPIFKKY 78

                ...
gi 17933592 150 CRY 152
Cdd:cd15898  79 AGT 81
PTZ00101 PTZ00101
rhomboid-1 protease; Provisional
182-402 2.72e-06

rhomboid-1 protease; Provisional


Pssm-ID: 185445  Cd Length: 278  Bit Score: 48.69  E-value: 2.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  182 MVLFSIIEIIMFLVDVIHFQDDPnyqdrigestSGPAATLFI-----YNP-YKRYEGWRFVSYMFVHVGIMHLMMNLIIQ 255
Cdd:PTZ00101  56 IMAISIIQIIVFIISVSIKPADF----------LTPSDSLLVtlganVASrIKQGEIHRLILPIFLHANIFHTFFNVFFQ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  256 IFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSPRIFLAGASGGVYALITAHIATIIMNYSEMEYAIVQLLAFLVFCF 335
Cdd:PTZ00101 126 LRMGFTLEKNYGIVKIIILYFLTGIYGNILSSSVTYCPIKVGASTSGMGLLGIVTSELILLWHVIRHRERVVFNIIFFSL 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17933592  336 tdlgTSVYRHLTDQHDQIGYVAHLSGAVAGllVGIGVLRNLEVRRWERILWWVAVIVYFALMTTGII 402
Cdd:PTZ00101 206 ----ISFFYYFTFNGSNIDHVGHLGGLLSG--ISMGILYNSQMENKPSWYDHMKMASYACLALLAIV 266
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
61-167 3.51e-06

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 47.75  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   61 NQTNSQEPEDrrkmhEIFDKHDSDRDGLINTHELKELISDGyCRDIPAYIADQILKRSDQDNDGHLDFEEFYAMSlrhkw 140
Cdd:NF041410  21 SSARSQQFQK-----QLFAKLDSDGDGSVSQDELSSALSSK-SDDGSLIDLSELFSDLDSDGDGSLSSDELAAAA----- 89
                         90       100
                 ....*....|....*....|....*..
gi 17933592  141 mvrnmltrycryvvPPPKPLEGDEPDG 167
Cdd:NF041410  90 --------------PPPPPPPDQAPST 102
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
54-139 1.45e-05

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: 46.52  E-value: 1.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  54 DMEEIPlnqtnsqEPEDRRKMHEIFDKHDSDRDGLINTHELKELISDGYCRDIPAYIAD--QILKRSDQDNDGHLDFEEF 131
Cdd:cd16225  23 EFEEDS-------EPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIMEKTQEHFQEAVEEneQIFKAVDTDKDGNVSWEEY 95

                ....*...
gi 17933592 132 YAMSLRHK 139
Cdd:cd16225  96 RVHFLLSK 103
PRK10907 PRK10907
intramembrane serine protease GlpG; Provisional
224-306 1.57e-05

intramembrane serine protease GlpG; Provisional


Pssm-ID: 182828 [Multi-domain]  Cd Length: 276  Bit Score: 46.15  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  224 YNPYKRYEGWRFVSYMFVHVGIMHLMMNLIIQIFLGIALELVHHWWRVGLVYLAGVLAGSMGTSLTSPrIFLAGASGGVY 303
Cdd:PRK10907 127 FDPSLKFELWRYFTHALLHFSLLHILFNLLWWWYLGGAVEKRLGSGKLIVITLISALLSGWVQSKFSG-PWFGGLSGVVY 205

                 ...
gi 17933592  304 ALI 306
Cdd:PRK10907 206 ALM 208
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
62-134 3.62e-05

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 42.52  E-value: 3.62e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17933592  62 QTNSQEPEDRRKMHEIFDKhdsDRDGLINTHELKELIS----DGYCRDIPAYIADQILKRSDQDNDGHLDFEEFYAM 134
Cdd:cd16252  30 QTSEQQEEAIRKAFQMLDK---DKSGFIEWNEIKYILStvpsSMPVAPLSDEEAEAMIQAADTDGDGRIDFQEFSDM 103
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
68-131 4.11e-05

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: 44.88  E-value: 4.11e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17933592  68 PED-RRKMHEIFDKHDSDRDGLINTHELKELISdgYCRDipAYI---ADQILKRSDQDNDGHLDFEEF 131
Cdd:cd16226  30 PEEsKERLGIIVDKIDKNGDGFVTEEELKDWIK--YVQK--KYIredVDRQWKEYDPNKDGKLSWEEY 93
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
50-131 4.16e-05

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 45.00  E-value: 4.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  50 QDTIDMEEIPLNQTNSQEPEDRRKM----HEIFDKHDSDRDGLINTHELKELISDGYCRDIPAYIADQILKRSDQDNDGH 125
Cdd:cd16227  96 ADSFGYDDEDNEEMIKDSTEDDLKLleddKEMFEAADLNKDGKLDKTEFSAFQHPEEYPHMHPVLIEQTLRDKDKDNDGF 175

                ....*.
gi 17933592 126 LDFEEF 131
Cdd:cd16227 176 ISFQEF 181
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
76-131 4.67e-05

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: 41.71  E-value: 4.67e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17933592  76 EIFDKHdSDRDG---LINTHELKELISD------GYCRDIPAYiaDQILKRSDQDNDGHLDFEEF 131
Cdd:cd00213  12 DVFHKY-SGKEGdkdTLSKKELKELLETelpnflKNQKDPEAV--DKIMKDLDVNKDGKVDFQEF 73
EFh_HEF_SCGN cd16178
EF-hand, calcium binding motif, found in secretagogin (SCGN); SCGN is a six EF-hand ...
57-197 5.10e-05

EF-hand, calcium binding motif, found in secretagogin (SCGN); 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 calcium sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. It also serves as a calcium buffer in neurons. Thus, SCGN may be linked to the pathogenesis of neurological diseases such as Alzheimer's, and also acts as a serum marker of neuronal damage, or as a tumor biomarker. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. All six EF hand motifs of SCGN in some eukaryotes, including D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, could potentially bind six calcium ions. In contrast, SCGNs from higher eukaryotes have at least one non-functional EF-hand motif due to the mutation(s) or deletions. For instance, the EF1 loop does not coordinate calcium ion due to the key residue asparagine replaced by lysine in SCGNs of many mammalian species. Moreover, the EF2 loop seems to be competent for calcium-binding in most mammalian SCGNs except for human and chimpanzee orthologs.


Pssm-ID: 320078 [Multi-domain]  Cd Length: 257  Bit Score: 44.70  E-value: 5.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  57 EIPLnqTNSQEpedrrkMHEIFDKHDSDRDGLINTHELKELISD---GYCRDIPA-----YiADQILKRSDQDNDGHLDF 128
Cdd:cd16178  85 EEPL--DSSVE------FMRIWRKYDADSSGYISAAELKNFLRDlflQHKKVITEdkldeY-TDTMMKIFDKNKDGRLDL 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592 129 EE----------------FYAMSLRHKwmVRNMLTRYCRYVVPPPKPLEGDEPDGAYEKQMSICPPPLTMV-LFSIIEII 191
Cdd:cd16178 156 NDmarilalqenfllqfkMDAMSEEER--KRDFEKIFAHYDVSKTGALEGPEVDGFVKDMMELVKPSISGVqLDKFKEII 233

                ....*.
gi 17933592 192 MFLVDV 197
Cdd:cd16178 234 LNHCDV 239
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
74-149 7.45e-05

EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes represent a class of neuron-specific metazoan PI-PLCs that are most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. They are phosphatidylinositol 4,5-bisphosphate-hydrolyzing enzymes that are more sensitive to Ca2+ than other PI-PLC isozymes. They function as calcium sensors activated by small increases in intracellular calcium concentrations. They are also activated through G-protein-coupled receptor (GPCR) stimulation, and further mediate GPCR signalling pathways. PI-PLC-eta isozymes contain an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases. There are two PI-PLC-eta isozymes (1-2). Aside from the PI-PLC-eta isozymes identified in mammals, their eukaryotic homologs are also present in this family.


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 42.37  E-value: 7.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  74 MHEIFDKHDSDRDGLINTHELKELISDgYCRDIPAYIADQILKRSDQD-NDGHLDFEEFYA----MSLRHKwmVRNMLTR 148
Cdd:cd16205   2 LKQTFEEADKNGDGLLSIGEILQLMHK-LNVNLPRRKVRQMFKEADTDdNQGTLDFEEFCAfykmMSTRRE--LYLLLLS 78

                .
gi 17933592 149 Y 149
Cdd:cd16205  79 Y 79
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
62-130 1.04e-04

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 43.58  E-value: 1.04e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17933592  62 QTNSQEPE----DRRKMHEIFDKhdsDRDGLINTHELKELIsDGYCRDIPAYIADQILKRSDQDNDGHLDFEE 130
Cdd:cd15899 190 DENEEEPEwvkvEKERFVELRDK---DKDGKLDGEELLSWV-DPSNQEIALEEAKHLIAESDENKDGKLSPEE 258
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
68-130 1.42e-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: 43.34  E-value: 1.42e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17933592  68 PEDRRKMHEI-----FDKHDSDRDGLInthELKELISDGYcRDI-----PAYIAD---QILKRSDQDNDGHLDFEE 130
Cdd:cd16226 147 PEEFPHMRDIvvqetLEDIDKNKDGFI---SLEEYIGDMY-RDDdeeedPDWVKSereQFKEFRDKNKDGKMDREE 218
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
75-131 1.44e-04

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain 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 C-terminal C2 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. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 41.44  E-value: 1.44e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17933592  75 HEIFDKHDSDRDGLINTHELKEL-------ISDGYCRDIpayiadqiLKRSDQDNDGHLDFEEF 131
Cdd:cd16202   3 KDQFRKADKNGDGKLSFKECKKLlkklnvkVDKDYAKKL--------FQEADTSGEDVLDEEEF 58
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
74-143 2.27e-04

The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five EF-hand calcium-binding proteins, including several classical calpain large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14), two calpain small subunits (CAPNS1 and CAPNS2), as well as non-calpain PEF proteins, ALG-2 (apoptosis-linked gene 2, also termed programmed cell death protein 6, PDCD6), peflin, sorcin, and grancalcin. Based on the sequence similarity of EF1 hand, ALG-2 and peflin have been classified into group I PEF proteins. Calcium-dependent protease calpain subfamily members, sorcin and grancalcin, are group II PEF proteins. Calpains (EC 3.4.22.17) are calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates. They have been implicated in a number of physiological processes such as cell cycle progression, remodeling of cytoskeletal-cell membrane attachments, signal transduction, gene expression and apoptosis. ALG-2 is a pro-apoptotic factor that forms a homodimer in the cell or a heterodimer with its closest paralog peflin through their EF5s. Peflin is a 30-kD PEF protein with a longer N-terminal hydrophobic domain than any other member of the PEF family, and it contains nine nonapeptide (A/PPGGPYGGP) repeats. It exists only as a heterodimer with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. ALG-2 interacts with various proteins in a Ca2+-dependent manner. Sorcin (for soluble resistance-related calcium binding protein) is a soluble resistance-related calcium-binding protein that participates in the regulation of calcium homeostasis in cells. Grancalcin is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It plays a key role in leukocyte-specific functions that are responsible for host defense. Grancalcin can form a heterodimer together with sorcin. Members in this family contain five EF-hand motifs attached to an N-terminal region of variable length containing one or more short Gly/Pro-rich sequences. These proteins form homodimers or heterodimers through pairing between the 5th EF-hands from the two molecules. Unlike calmodulin, the PEF domains do not undergo major conformational changes upon binding Ca2+.


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 41.65  E-value: 2.27e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17933592  74 MHEIFDKHDSDRDGLINTHELKELISD-GYcrDIPAYIADQILKRSDQDNdGHLDFEEFYAMSLRHKWMVR 143
Cdd:cd15897  72 WQEIFRTYDTDGSGTIDSNELRQALSGaGY--RLSEQTYDIIIRRYDRGR-GNIDFDDFIQCCVRLQRLTD 139
CCC1_like cd01059
CCC1-related family of proteins; CCC1_like: This protein family includes the proteins related ...
272-406 3.30e-04

CCC1-related family of proteins; CCC1_like: This protein family includes the proteins related to CCC1, a yeast vacuole transmembrane protein responsible for the iron and manganese transport from the cytosol into vacuole. It also includes the proteins similar to nodulin-21, a plant nodule-specific protein that may be involved in symbiotic nitrogen fixation.


Pssm-ID: 153121  Cd Length: 143  Bit Score: 40.67  E-value: 3.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592 272 GLVYLAGVLAGSMGTSLTSPRIFLAGASGGVYA----LITAHIATiimnYSEMEY-AIVQLLAFLVFCFTDLGTSVYrhL 346
Cdd:cd01059  11 GLVSTFALVAGVAAAGDSTKAILLAGLAGLVAGaismAAGEYVSV----KSQRDKaALASGLSFILGGLLPLLPYLL--L 84
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592 347 TDQHDQIGYVAHLSGAVAGLLVGIGVLRNLEVRRWERILwWVAVIVYFALMTTGIIIHVF 406
Cdd:cd01059  85 PAGSLALAVSVALVVALALFLLGAFVAKLGGAKKIRAAL-RMVVLGLLAAALTYLLGRLF 143
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
71-131 3.37e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 3.37e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17933592  71 RRKMHEIFDKHDSDRDGLINTHELKELISDGYCRDIPAyIADQILKRSDQDNDGHLDFEEF 131
Cdd:COG5126  32 RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEP-FARAAFDLLDTDGDGKISADEF 91
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
61-131 5.96e-04

EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic reticulum resident low-affinity Ca2+-binding protein with six EF-hand motifs and a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It is expressed at the cell surface. RCN-1 acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signaling cascade. It also plays a key role in the development of doxorubicin-associated resistance.


Pssm-ID: 320027 [Multi-domain]  Cd Length: 267  Bit Score: 41.40  E-value: 5.96e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17933592  61 NQTNSQEPEDRrkMHEIFDKHDSDRDGLINTHELKELISDGYCRDIPAYIAdQILKRSDQDNDGHLDFEEF 131
Cdd:cd16229  26 DQLTPEESKER--LGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIYENVA-KVWKDYDLNKDNKISWEEY 93
PTZ00184 PTZ00184
calmodulin; Provisional
52-134 8.31e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 39.74  E-value: 8.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   52 TIDMEE-IPLNQTNSQEPEDRRKMHEIFDKHDSDRDGLINTHELKE-LISDGycRDIPAYIADQILKRSDQDNDGHLDFE 129
Cdd:PTZ00184  63 TIDFPEfLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHvMTNLG--EKLTDEEVDEMIREADVDGDGQINYE 140

                 ....*
gi 17933592  130 EFYAM 134
Cdd:PTZ00184 141 EFVKM 145
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
72-131 9.31e-04

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 39.82  E-value: 9.31e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17933592  72 RKMHEIFDKHDSDRDGLINTHELKE-LISDGYcrDIPAYIADQILKRSDQDNDGHLDFEEF 131
Cdd:cd16180  67 QDWRRLFRRFDRDRSGSIDFNELQNaLSSFGY--RLSPQFVQLLVRKFDRRRRGSISFDDF 125
EF-hand_6 pfam13405
EF-hand domain;
73-98 1.10e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.39  E-value: 1.10e-03
                          10        20
                  ....*....|....*....|....*.
gi 17933592    73 KMHEIFDKHDSDRDGLINTHELKELI 98
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKAL 26
PTZ00183 PTZ00183
centrin; Provisional
51-132 1.17e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 39.29  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592   51 DTIDMEEIPLNQTNS-QEPEDRRKMHEIFDKHDSDRDGLINTHELKELisdgyCRDIPAYIADQILK----RSDQDNDGH 125
Cdd:PTZ00183  68 GKIDFEEFLDIMTKKlGERDPREEILKAFRLFDDDKTGKISLKNLKRV-----AKELGETITDEELQemidEADRNGDGE 142

                 ....*..
gi 17933592  126 LDFEEFY 132
Cdd:PTZ00183 143 ISEEEFY 149
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
78-140 1.24e-03

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


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 39.51  E-value: 1.24e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17933592  78 FDKHDSDRDGLINTHELKELISDGycrdIPAY---IADQILKRSDQDNDGHLDFEEFYAMslrHKW 140
Cdd:cd16185   6 FRAVDRDRSGSIDVNELQKALAGG----GLLFslaTAEKLIRMFDRDGNGTIDFEEFAAL---HQF 64
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
71-134 1.48e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.62  E-value: 1.48e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17933592  71 RRKMHEIFDKHDSDRDGLINTHELKELisdgycrdiPAYIADQILKRSDQDNDGHLDFEEFYAM 134
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEAL---------FRRLWATLFSEADTDGDGRISREEFVAG 58
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
65-134 1.74e-03

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 37.51  E-value: 1.74e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17933592  65 SQEPEDRRKMHEIFDKhdsDRDGLINTHELKELI----SDGycRDIPAYIADQILKRSDQDNDGHLDFEEFYAM 134
Cdd:cd16251  30 QKSEDQIKKVFQILDK---DKSGFIEEEELKYILkgfsIAG--RDLTDEETKALLAAGDTDGDGKIGVEEFATL 98
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
49-144 2.47e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed calcium-binding protein ERC-55, or E6-binding protein (E6BP), or TCBP-49, is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. It is associated with tumorigenesis, in particular with transformation of cells of the cervix induced by human papillomavirus (HPV), through binding to human papillomavirus (HPV) E6 oncogenic protein. It specifically interacts with vitamin D receptor among nuclear receptors. RCN2 contains an N-terminal signal sequence followed by six copies of the EF-hand Ca2+-binding motif, and a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 39.34  E-value: 2.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17933592  49 RQDTIDMEEIP-LNQTNS---QEPEDRRKM-----HEIFDKHDSDRDGLINTHE-LKELISDGYCRDIPAYI---ADQIL 115
Cdd:cd16224 129 RFDKANTDGGPgLNLTEFiafEHPEEVDYMtefviQEALEEHDKDGDGFISLEEfLGDYRKDPTANEDPEWIiveKDRFV 208
                        90       100
                ....*....|....*....|....*....
gi 17933592 116 KRSDQDNDGHLDFEEFYAmslrhkWMVRN 144
Cdd:cd16224 209 NDYDKDNDGKLDPQELLP------WVVPN 231
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
73-100 4.08e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 34.68  E-value: 4.08e-03
                          10        20
                  ....*....|....*....|....*...
gi 17933592    73 KMHEIFDKHDSDRDGLINTHELKELISD 100
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
74-149 4.14e-03

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


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 37.96  E-value: 4.14e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17933592  74 MHEIFDKHDSDRDGLINTHELKE-LISDGYCRDIPAYIAdqILKRSDQDNDGHLDFEEFYAMSLrHKWMVRNMLTRY 149
Cdd:cd16185  68 MQNGFEQRDTSRSGRLDANEVHEaLAASGFQLDPPAFQA--LFRKFDPDRGGSLGFDDYIELCI-FLASARNLFQAF 141
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
73-99 4.71e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 34.28  E-value: 4.71e-03
                           10        20
                   ....*....|....*....|....*..
gi 17933592     73 KMHEIFDKHDSDRDGLINTHELKELIS 99
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLK 27
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
65-134 4.83e-03

EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319996 [Multi-domain]  Cd Length: 101  Bit Score: 36.38  E-value: 4.83e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17933592  65 SQEPEDRRKMHEIFDKhdsDRDGLINTHELKELI---SDGyCRDIPAYIADQILKRSDQDNDGHLDFEEFYAM 134
Cdd:cd16253  30 KKSPADIKKVFNILDQ---DKSGFIEEEELKLFLknfSDG-ARVLSDKETKNFLAAGDSDGDGKIGVDEFKSM 98
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
76-131 6.43e-03

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


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 38.10  E-value: 6.43e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17933592  76 EIFDKHDSDRDGLINTHELKELISD--------GYCRDIPAYIADQILKRSDQDNDGHLDFEEF 131
Cdd:cd15902   3 EVWMHFDADGNGYIEGKELDSFLREllkalngkDKTDDEVAEKKKEFMEKYDENEDGKIEIREL 66
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
74-141 8.62e-03

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


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 36.82  E-value: 8.62e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17933592  74 MHEIFDKHdSDRDGLINTHELKELISDGYCRDIPAY------IADQILKRSDQDNDGHLDFEEFYAMSLR-HKWM 141
Cdd:cd16182   2 VRELFEKL-AGEDEEIDAVELQKLLNASLLKDMPKFdgfsleTCRSLIALMDTNGSGRLDLEEFKTLWSDlKKWQ 75
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
69-131 8.63e-03

EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This family corresponds to a group of uncharacterized RCN2-like proteins, which are mainly found in protostomes. Although their biological function remains unclear, they show high sequence similarity with RCN2 (also known as E6BP or TCBP-49), which is an endoplasmic reticulum resident low-affinity Ca2+-binding protein that has been implicated in immunity, redox homeostasis, cell cycle regulation and coagulation. Members in this family contain six copies of the EF-hand Ca2+-binding motif, but may lack a C-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide that is required for retention of RCN2 in the endoplasmic reticulum (ER).


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 37.68  E-value: 8.63e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17933592  69 EDRRKMHEIFDKHDSDRDGLINTHELKELISDGYcRDIPAYIADQILKRSDQDNDGHLDFEEF 131
Cdd:cd16227  33 EAKRRLAVLAKKMDLNDDGFIDRKELKAWILRSF-KMLDEEEANERFEEADEDGDGKVTWEEY 94
PTZ00184 PTZ00184
calmodulin; Provisional
69-145 9.15e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 36.66  E-value: 9.15e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17933592   69 EDRRKMHEIFDKHDSDRDGLINTHELKELISDGYCRDIPAYIADQIlKRSDQDNDGHLDFEEFYAMslrhkwMVRNM 145
Cdd:PTZ00184   8 EQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMI-NEVDADGNGTIDFPEFLTL------MARKM 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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