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Conserved domains on  [gi|45552009|ref|NP_733366|]
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aralar1, isoform B [Drosophila melanogaster]

Protein Classification

calcium-binding mitochondrial carrier protein( domain architecture ID 11473923)

calcium-binding mitochondrial carrier protein transfers molecules across the membranes of organelles, usually mitochondria, in a calcium-dependent manner

Gene Ontology:  GO:0016020|GO:1990542|GO:0005509
PubMed:  31787485|32783608|23266187|28707401|2479149
TCDB:  2.A.29

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
322-420 1.03e-28

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 110.05  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   322 QVLESSYRFTLGSFAGAVGATVVYPIDLVKTRMQNQRAGSYIGevaYRNSWDCFKKVVRHEGFMGLYRGLLPQLMGVAPE 401
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSK---GRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPA 77

                          90
                  ....*....|....*....
gi 45552009   402 KAIKLTVNDLVRDKLTDKK 420
Cdd:pfam00153  78 AAIYFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
516-605 8.49e-28

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 107.36  E-value: 8.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   516 HPLTLLAAGAIAGVPAASLVTPADVIKTRLQVVARSGQTTYTGVWDATKKIMAEEGPRAFWKGTAARVFRSSPQFGVTLV 595
Cdd:pfam00153   4 SFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFG 83

                          90
                  ....*....|
gi 45552009   596 TYELLQRLFY 605
Cdd:pfam00153  84 TYETLKRLLL 93
Mito_carr pfam00153
Mitochondrial carrier protein;
421-511 6.51e-21

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 87.71  E-value: 6.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   421 GNIPTWAEVLAGGCAGASQVVFTNPLEIVKIRLQVAGEIASGSKIRAWSVVREL----GLFGLYKGARACLLRDVPFSAI 496
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*
gi 45552009   497 YFPTYAHTKAMMADK 511
Cdd:pfam00153  81 YFGTYETLKRLLLKK 95
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
16-162 6.65e-10

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.49  E-value: 6.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  16 TEKLREVFlkyASIQKNGEHYMTSEDFVRKFLGLFsesafndesvRLLANIADTSKDGLISFSEFQAF--EGLLCTPDAL 93
Cdd:COG5126   4 RRKLDRRF---DLLDADGDGVLERDDFEALFRRLW----------ATLFSEADTDGDGRISREEFVAGmeSLFEATVEPF 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552009  94 YRTAFQLFDRKGNGTVSYADFADVVQKtelhskipFSLDGPFIKRYF------GDKKqrlINYAEFTQLLHDFHE 162
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRLLTA--------LGVSEEEADELFarldtdGDGK---ISFEEFVAAVRDYYT 134
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
322-420 1.03e-28

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 110.05  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   322 QVLESSYRFTLGSFAGAVGATVVYPIDLVKTRMQNQRAGSYIGevaYRNSWDCFKKVVRHEGFMGLYRGLLPQLMGVAPE 401
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSK---GRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPA 77

                          90
                  ....*....|....*....
gi 45552009   402 KAIKLTVNDLVRDKLTDKK 420
Cdd:pfam00153  78 AAIYFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
516-605 8.49e-28

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 107.36  E-value: 8.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   516 HPLTLLAAGAIAGVPAASLVTPADVIKTRLQVVARSGQTTYTGVWDATKKIMAEEGPRAFWKGTAARVFRSSPQFGVTLV 595
Cdd:pfam00153   4 SFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFG 83

                          90
                  ....*....|
gi 45552009   596 TYELLQRLFY 605
Cdd:pfam00153  84 TYETLKRLLL 93
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 330-603 9.91e-25

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 104.85  E-value: 9.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  330 FTLGSFAGAVGATVVYPIDLVKTRMQNQRAGSYI--GEVA-YRNSWDCFKKVVRHEGFMGLYRGLLPQLMGVAPEKAIKL 406
Cdd:PTZ00169  11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIksGKVPrYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  407 TVNDLVRDKLTDKKGNIPTW----AEVLAGGCAGASQVVFTNPLEIVKIRLqvAGEIASGSKiRAWS--------VVREL 474
Cdd:PTZ00169  91 AFKDYFKNMFPKYNQKTDFWkffgVNILSGGLAGASSLLIVYPLDFARTRL--ASDIGKGGD-REFTglfdclmkISKQT 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  475 GLFGLYKGARACLLRDVPFSAIYFPTYAHTKAMMAdKDGYNHPLTLLAAGAIAGVPAASLVT-PADVIKTRLQVVA---R 550
Cdd:PTZ00169 168 GFLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALLF-GNDKNTNILYKWAVAQTVTILAGLISyPFDTVRRRMMMMSgrkA 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45552009  551 SGQTTYTGVWDATKKIMAEEGPRAFWKGTAARVFRSSPQfGVTLVTYELLQRL 603
Cdd:PTZ00169 247 KSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLRGAGG-ALVLVFYDELQKL 298
Mito_carr pfam00153
Mitochondrial carrier protein;
421-511 6.51e-21

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 87.71  E-value: 6.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   421 GNIPTWAEVLAGGCAGASQVVFTNPLEIVKIRLQVAGEIASGSKIRAWSVVREL----GLFGLYKGARACLLRDVPFSAI 496
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*
gi 45552009   497 YFPTYAHTKAMMADK 511
Cdd:pfam00153  81 YFGTYETLKRLLLKK 95
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
16-162 6.65e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.49  E-value: 6.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  16 TEKLREVFlkyASIQKNGEHYMTSEDFVRKFLGLFsesafndesvRLLANIADTSKDGLISFSEFQAF--EGLLCTPDAL 93
Cdd:COG5126   4 RRKLDRRF---DLLDADGDGVLERDDFEALFRRLW----------ATLFSEADTDGDGRISREEFVAGmeSLFEATVEPF 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552009  94 YRTAFQLFDRKGNGTVSYADFADVVQKtelhskipFSLDGPFIKRYF------GDKKqrlINYAEFTQLLHDFHE 162
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRLLTA--------LGVSEEEADELFarldtdGDGK---ISFEEFVAAVRDYYT 134
EF-hand_7 pfam13499
EF-hand domain pair;
17-83 2.65e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.02  E-value: 2.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552009    17 EKLREVFlkyASIQKNGEHYMTSEDFVRKFLGLFSESAFNDESVRLLANIADTSKDGLISFSEFQAF 83
Cdd:pfam13499   2 EKLKEAF---KLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLEL 65
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 53-187 4.24e-07

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: 50.22  E-value: 4.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  53 SAFNDESVRLLANIADTSKDGLISFSEfqaFEGLLCTPDAlYRTAFQLFDRKGNGTVSYADFadvvqKTELHSkIPFSLD 132
Cdd:cd16180  32 TPFSIETVRLMINMFDRDRSGTINFDE---FVGLWKYIQD-WRRLFRRFDRDRSGSIDFNEL-----QNALSS-FGYRLS 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552009 133 GPFIK---RYFGDKKQRLINYAEFTQL---LHdfheeHAMEAFRSKDPAGTGFISpLDFQD 187
Cdd:cd16180 102 PQFVQllvRKFDRRRRGSISFDDFVEAcvtLK-----RLTDAFRKYDTNRTGYAT-ISYED 156
PTZ00184 PTZ00184
calmodulin; Provisional
 17-157 1.96e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 39.36  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   17 EKLREVFLKYASIQKNGEHYMTSEDF--VRKFLGLF-SESAFNDesvrlLANIADTSKDGLISFSEF---QAFEGLLCTP 90
Cdd:PTZ00184   8 EQIAEFKEAFSLFDKDGDGTITTKELgtVMRSLGQNpTEAELQD-----MINEVDADGNGTIDFPEFltlMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552009   91 DALYRTAFQLFDRKGNGTVSYADFADVVqkTELHSKIPFSLDGPFIKR--YFGDKKqrlINYAEFTQLL 157
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVM--TNLGEKLTDEEVDEMIREadVDGDGQ---INYEEFVKMM 146
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
322-420 1.03e-28

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 110.05  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   322 QVLESSYRFTLGSFAGAVGATVVYPIDLVKTRMQNQRAGSYIGevaYRNSWDCFKKVVRHEGFMGLYRGLLPQLMGVAPE 401
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSK---GRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPA 77

                          90
                  ....*....|....*....
gi 45552009   402 KAIKLTVNDLVRDKLTDKK 420
Cdd:pfam00153  78 AAIYFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
516-605 8.49e-28

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 107.36  E-value: 8.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   516 HPLTLLAAGAIAGVPAASLVTPADVIKTRLQVVARSGQTTYTGVWDATKKIMAEEGPRAFWKGTAARVFRSSPQFGVTLV 595
Cdd:pfam00153   4 SFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFG 83

                          90
                  ....*....|
gi 45552009   596 TYELLQRLFY 605
Cdd:pfam00153  84 TYETLKRLLL 93
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 330-603 9.91e-25

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 104.85  E-value: 9.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  330 FTLGSFAGAVGATVVYPIDLVKTRMQNQRAGSYI--GEVA-YRNSWDCFKKVVRHEGFMGLYRGLLPQLMGVAPEKAIKL 406
Cdd:PTZ00169  11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIksGKVPrYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  407 TVNDLVRDKLTDKKGNIPTW----AEVLAGGCAGASQVVFTNPLEIVKIRLqvAGEIASGSKiRAWS--------VVREL 474
Cdd:PTZ00169  91 AFKDYFKNMFPKYNQKTDFWkffgVNILSGGLAGASSLLIVYPLDFARTRL--ASDIGKGGD-REFTglfdclmkISKQT 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  475 GLFGLYKGARACLLRDVPFSAIYFPTYAHTKAMMAdKDGYNHPLTLLAAGAIAGVPAASLVT-PADVIKTRLQVVA---R 550
Cdd:PTZ00169 168 GFLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALLF-GNDKNTNILYKWAVAQTVTILAGLISyPFDTVRRRMMMMSgrkA 246

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45552009  551 SGQTTYTGVWDATKKIMAEEGPRAFWKGTAARVFRSSPQfGVTLVTYELLQRL 603
Cdd:PTZ00169 247 KSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLRGAGG-ALVLVFYDELQKL 298
Mito_carr pfam00153
Mitochondrial carrier protein;
421-511 6.51e-21

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 87.71  E-value: 6.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   421 GNIPTWAEVLAGGCAGASQVVFTNPLEIVKIRLQVAGEIASGSKIRAWSVVREL----GLFGLYKGARACLLRDVPFSAI 496
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*
gi 45552009   497 YFPTYAHTKAMMADK 511
Cdd:pfam00153  81 YFGTYETLKRLLLKK 95
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 324-582 2.94e-20

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 90.75  E-value: 2.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  324 LESSYRFTLGSFAGAVGATVVYPIDLVKTRMQNQRAGSYigevayrnsWDCFKkvvrhegfmgLYRGLLPQLMGVAPEKA 403
Cdd:PTZ00168   1 MEHFHNLVTGALSGVIVDAVLYPIDSIKTNIQAKKSFSF---------SDIKK----------LYSGILPTLVGTVPASA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  404 IKLTVNDLVRDKLTDKKGNI-PTWAEVLAGGCAGASQVVFTNPLEIVKIRLQVAGEIASGSKIraWSVVRELGLFG-LYK 481
Cdd:PTZ00168  62 FFYCFYELSKKLLTEYRENIsKTNLYLISTSIAEITACIVRLPFEIVKQNMQVSGNISVLKTI--YEITQREGLPSfLGK 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  482 GARACLLRDVPFSAIYFPTYAHTKAmMADKDGYN----HP-LTLLAAGAIAGVPAASLVTPADVIKTRlqvvarsgQTTY 556
Cdd:PTZ00168 140 SYFVMIVREIPFDCIQYFLWETLKE-KAKKDFGKfskkYPsITSAICGGLAGGIAGFLTTPVDVIKSR--------QIIY 210

                        250       260
                 ....*....|....*....|....*.
gi 45552009  557 TGVWDATKKIMAEEGPRAFWKGTAAR 582
Cdd:PTZ00168 211 GKSYIETVTEIAEEGYLTFYKGCCFR 236
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
16-162 6.65e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 57.49  E-value: 6.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  16 TEKLREVFlkyASIQKNGEHYMTSEDFVRKFLGLFsesafndesvRLLANIADTSKDGLISFSEFQAF--EGLLCTPDAL 93
Cdd:COG5126   4 RRKLDRRF---DLLDADGDGVLERDDFEALFRRLW----------ATLFSEADTDGDGRISREEFVAGmeSLFEATVEPF 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45552009  94 YRTAFQLFDRKGNGTVSYADFADVVQKtelhskipFSLDGPFIKRYF------GDKKqrlINYAEFTQLLHDFHE 162
Cdd:COG5126  71 ARAAFDLLDTDGDGKISADEFRRLLTA--------LGVSEEEADELFarldtdGDGK---ISFEEFVAAVRDYYT 134
EF-hand_7 pfam13499
EF-hand domain pair;
17-83 2.65e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.02  E-value: 2.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45552009    17 EKLREVFlkyASIQKNGEHYMTSEDFVRKFLGLFSESAFNDESVRLLANIADTSKDGLISFSEFQAF 83
Cdd:pfam13499   2 EKLKEAF---KLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLEL 65
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 53-187 4.24e-07

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: 50.22  E-value: 4.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  53 SAFNDESVRLLANIADTSKDGLISFSEfqaFEGLLCTPDAlYRTAFQLFDRKGNGTVSYADFadvvqKTELHSkIPFSLD 132
Cdd:cd16180  32 TPFSIETVRLMINMFDRDRSGTINFDE---FVGLWKYIQD-WRRLFRRFDRDRSGSIDFNEL-----QNALSS-FGYRLS 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45552009 133 GPFIK---RYFGDKKQRLINYAEFTQL---LHdfheeHAMEAFRSKDPAGTGFISpLDFQD 187
Cdd:cd16180 102 PQFVQllvRKFDRRRRGSISFDDFVEAcvtLK-----RLTDAFRKYDTNRTGYAT-ISYED 156
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 53-189 4.66e-07

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, 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+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 49.96  E-value: 4.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  53 SAFNDESVRLLANIADTSKDGLISFSEFQafegllctpdALY------RTAFQLFDRKGNGTVSYadfadvvqkTELH-- 124
Cdd:cd16184  32 SHFNDETCRLMIGMFDKDKSGTIDIYEFQ----------ALWnyiqqwKQVFQQFDRDRSGSIDE---------NELHqa 92

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552009 125 -SKIPFSLDGPF----IKRYFGDKKQRLiNYAEFTQ---LLHDFheehaMEAFRSKDPAGTGFISpLDFQDII 189
Cdd:cd16184  93 lSQMGYRLSPQFvqflVSKYDPRARRSL-TLDQFIQvcvQLQSL-----TDAFRQRDTQMTGTIT-ISYEDFL 158
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 53-180 6.47e-06

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. 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.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 46.86  E-value: 6.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  53 SAFNDESVRLLANIADTSKDGLISFSEFQafegllctpdALY------RTAFQLFDRKGNGTVSyadfadvvqKTELHSK 126
Cdd:cd16183  32 TPFNPETVRLMIGMFDRDNSGTINFQEFA----------ALWkyitdwQNCFRSFDRDNSGNID---------KNELKQA 92

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45552009 127 IP---FSLDGPFIK---RYFGDKKQRLINYAEFTQ---LLHDFheehaMEAFRSKDPAGTGFI 180
Cdd:cd16183  93 LTsfgYRLSDQFYDilvRKFDRQGRGTIAFDDFIQccvVLQTL-----TDSFRRYDTDQDGWI 150
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 94-163 4.39e-05

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 44.14  E-value: 4.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  94 YRTAFQLFDRKGNGTVSYADF----------ADVVQKTELHSK---IPFSLDGPFIKRYFGDKKQRLINYAEFTQLLHDF 160
Cdd:cd15900   2 FEIAFKMFDLDGDGELDKEEFnkvqsiirsqTSVGQRHRDHTNgesTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQENL 81


                ...
gi 45552009 161 HEE 163
Cdd:cd15900  82 QEE 84
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 55-180 6.88e-05

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: 43.75  E-value: 6.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  55 FNDESVRLLANIADTSKDGLISFSEFQAFEGLLctpdALYRTAFQLFDRKGNGTVSYADFADVVQktelhsKIPFSLDGP 134
Cdd:cd16182  39 FSLETCRSLIALMDTNGSGRLDLEEFKTLWSDL----KKWQAIFKKFDTDRSGTLSSYELRKALE------SAGFHLSNK 108

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 45552009 135 F----IKRYfGDKKQRlINYAEFTQLLhdFHEEHAMEAFRSKDPAGTGFI 180
Cdd:cd16182 109 VlqalVLRY-ADSTGR-ITFEDFVSCL--VRLKTAFETFSALDKKNEGVI 154
EF-hand_7 pfam13499
EF-hand domain pair;
65-119 3.67e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.16  E-value: 3.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 45552009    65 NIADTSKDGLISFSEF----QAFEGLLCTPDALYRTAFQLFDRKGNGTVSYADFADVVQ 119
Cdd:pfam13499   9 KLLDSDGDGYLDVEELkkllRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-92 4.28e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.93  E-value: 4.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   8 PSLLKRAGTEKLREVFlkyASIQKNGEHYMTSEDFVRkflgLFSESAFNDESVRLLANIADTSKDGLISFSEFQAFEGLL 87
Cdd:COG5126  60 ESLFEATVEPFARAAF---DLLDTDGDGKISADEFRR----LLTALGVSEEEADELFARLDTDGDGKISFEEFVAAVRDY 132


                ....*
gi 45552009  88 CTPDA 92
Cdd:COG5126 133 YTPDA 137
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 68-119 5.03e-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: 38.68  E-value: 5.03e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 45552009  68 DTSKDGLISFSEFQAFEGLLC--TPDALYRTAFQLFDRKGNGTVSYADFADVVQ 119
Cdd:cd00051  10 DKDGDGTISADELKAALKSLGegLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
95-157 7.97e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.39  E-value: 7.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45552009    95 RTAFQLFDRKGNGTVSYADFADVVQKTELHSKI-PFSLDgpFIKRYFGDKKQRLINYAEFTQLL 157
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsDEEVE--ELFKEFDLDKDGRISFEEFLELY 66
EFh_PEF_Group_II_sorcin_like cd16181
Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The ...
 55-178 1.34e-03

Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The family corresponds to the second group of penta-EF hand (PEF) proteins that includes sorcin, grancalcin, and similar proteins. Sorcin, also termed 22 kDa Ca2+-binding protein, CP-22, or V19, is a soluble resistance-related calcium-binding protein that is expressed in normal mammalian tissues, such as the liver, lungs and heart. It contains a flexible glycine and proline-rich N-terminal extension and five EF-hand motifs that associate with membranes in a calcium-dependent manner. It may harbor three potential Ca2+ binding sites through its EF1, EF2 and EF3 hands. However, binding of only two Ca2+/monomer suffices to trigger the conformational change that exposes hydrophobic regions and leads to interaction with the respective targets. Sorcin forms homodimers through the association of the unpaired EF5 hand. Among the PEF proteins, sorcin is unique in that it contains potential phosphorylation sites by cAMP-dependent protein kinase (PKA), and it can form a tetramer at slightly acid pH values although remaining a stable dimer at neutral pH. Grancalcin (GCA) is a cytosolic Ca2+-binding protein specifically expressed in neutrophils and monocytes/macrophages. It can strongly interact with sorcin to form a heterodimer and further modulate the function of sorcin. GCA exists as homodimers in solution. It contains five EF-hand motifs attached to an N-terminal region of an approximately 50 residue-long segment rich in glycines and prolines. In contrast with sorcin, GCA binds two Ca2+ ions through its EF1 and EF3 hands.


Pssm-ID: 320056 [Multi-domain]  Cd Length: 165  Bit Score: 40.05  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  55 FNDESVRLLANIADTSKDGLISFSEFQAFEGLLctpdALYRTAFQLFDRKGNGTVSYAdfadvvqktELHSKI------- 127
Cdd:cd16181  37 FSLETCRLMIAMLDRDHSGKMGFNEFKELWAAL----NQWKTTFMQYDRDRSGTVEPQ---------ELQQAIrsfgynl 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 45552009 128 -PFSLDgPFIKRYfgdKKQRLINYAEFTQL------LHDFheehameaFRSKDPAGTG 178
Cdd:cd16181 104 sPQALN-VIVKRY---SKNGRITFDDFVACavrlraLTDR--------FRRRDTQQNG 149
PTZ00184 PTZ00184
calmodulin; Provisional
 17-157 1.96e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 39.36  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009   17 EKLREVFLKYASIQKNGEHYMTSEDF--VRKFLGLF-SESAFNDesvrlLANIADTSKDGLISFSEF---QAFEGLLCTP 90
Cdd:PTZ00184   8 EQIAEFKEAFSLFDKDGDGTITTKELgtVMRSLGQNpTEAELQD-----MINEVDADGNGTIDFPEFltlMARKMKDTDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45552009   91 DALYRTAFQLFDRKGNGTVSYADFADVVqkTELHSKIPFSLDGPFIKR--YFGDKKqrlINYAEFTQLL 157
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVM--TNLGEKLTDEEVDEMIREadVDGDGQ---INYEEFVKMM 146
EF-hand_8 pfam13833
EF-hand domain pair;
36-80 2.59e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.52  E-value: 2.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 45552009    36 YMTSEDFvRKFLGLFSESAFNDESVRLLANIADTSKDGLISFSEF 80
Cdd:pfam13833   4 VITREEL-KRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 67-161 6.95e-03

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 37.26  E-value: 6.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552009  67 ADTSKDGLISFSEFQA-FEGLL-CTPDALYRTAFQLFDRKGNGTVSYADFAD---------------------------- 116
Cdd:cd15898   9 ADKDGDGKLSLKEIKKlLKRLNiRVSEKELKKLFKEVDTNGDGTLTFDEFEElykslterpelepifkkyagtnrdymtl 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 45552009 117 --------VVQKTELHSKIPFSLdgpfIKRYFGDKKQRLINYAEFTQLLHDFH 161
Cdd:cd15898  89 eefirflrEEQGENVSEEECEEL----IEKYEPERENRQLSFEGFTNFLLSPE 137
EF-hand_8 pfam13833
EF-hand domain pair;
71-120 8.97e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 34.98  E-value: 8.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 45552009    71 KDGLISFSEFQ---AFEGLLCTPDALYRTAFQLFDRKGNGTVSYADFADVVQK 120
Cdd:pfam13833   1 EKGVITREELKralALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLLER 53
 
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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