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Conserved domains on  [gi|2217365158|ref|XP_016867152|]
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electrogenic aspartate/glutamate antiporter SLC25A13, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 12145057)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction; similar to Homo sapiens calcium-binding mitochondrial carrier protein Aralar2 that catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
562-657 1.82e-31

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 117.76  E-value: 1.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 562 GQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGV 641
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 2217365158 642 TLLTYELLQRWFYIDF 657
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
375-468 5.23e-27

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 105.05  E-value: 5.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 375 AYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELMyknsFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIK 454
Cdd:pfam00153   6 LASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGI----LDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|....
gi 2217365158 455 LTVNDFVRDKFMHK 468
Cdd:pfam00153  82 FGTYETLKRLLLKK 95
Mito_carr pfam00153
Mitochondrial carrier protein;
470-557 1.08e-18

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 81.55  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 470 GSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDL----GFFGIYKGAKACFLRDIPFSAI 545
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|..
gi 2217365158 546 YFPCYAHVKASF 557
Cdd:pfam00153  81 YFGTYETLKRLL 92
EFh_PEF super family cl25352
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 102-229 8.83e-06

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+.


The actual alignment was detected with superfamily member cd16185:

Pssm-ID: 355382 [Multi-domain]  Cd Length: 163  Bit Score: 46.44  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 102 KTVELLSGVVDQTKDGLISFQEFVA---FESVLCApdalfmvAFQLFDKAGKGEVTFEDVKQVFgqttihQHIPFNWDSE 178
Cdd:cd16185    36 ATAEKLIRMFDRDGNGTIDFEEFAAlhqFLSNMQN-------GFEQRDTSRSGRLDANEVHEAL------AASGFQLDPP 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217365158 179 FVQ---LHFGKERKRHLTYAEFTQFLLEIQLehAKQAFVQRDNARTGRVTaIDF 229
Cdd:cd16185   103 AFQalfRKFDPDRGGSLGFDDYIELCIFLAS--ARNLFQAFDRQRTGRVT-LDF 153
EF-hand_7 pfam13499
EF-hand domain pair;
66-127 4.67e-05

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 4.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217365158  66 LQFKYASIEKNGEFFMSPNDFVtRYLNIFGESQP-NPKTVELLSGVVDQTKDGLISFQEFVAF 127
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELK-KLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
562-657 1.82e-31

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 117.76  E-value: 1.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 562 GQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGV 641
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 2217365158 642 TLLTYELLQRWFYIDF 657
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
375-468 5.23e-27

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 105.05  E-value: 5.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 375 AYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELMyknsFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIK 454
Cdd:pfam00153   6 LASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGI----LDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|....
gi 2217365158 455 LTVNDFVRDKFMHK 468
Cdd:pfam00153  82 FGTYETLKRLLLKK 95
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 378-634 7.18e-25

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 105.62  E-value: 7.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 378 FGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELM--YKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKL 455
Cdd:PTZ00169   11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGKVprYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 456 TVNDFVRDKF----MHKDGSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLqvAGEIT-------TGPRVSALSVVRDLG 524
Cdd:PTZ00169   91 AFKDYFKNMFpkynQKTDFWKFFGVNILSGGLAGASSLLIVYPLDFARTRL--ASDIGkggdrefTGLFDCLMKISKQTG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 525 FFGIYKGAKACFLRDIPFSAIYFPCYAHVKASFANEDGQVSpgsLLLAGAIAG--MPAASLVT-PADVIKTRLQVAA--- 598
Cdd:PTZ00169  169 FLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNTN---ILYKWAVAQtvTILAGLISyPFDTVRRRMMMMSgrk 245

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2217365158 599 RAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFR 634
Cdd:PTZ00169  246 AKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLR 281
Mito_carr pfam00153
Mitochondrial carrier protein;
470-557 1.08e-18

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 81.55  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 470 GSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDL----GFFGIYKGAKACFLRDIPFSAI 545
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|..
gi 2217365158 546 YFPCYAHVKASF 557
Cdd:pfam00153  81 YFGTYETLKRLL 92
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 475-632 4.14e-07

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 52.46  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 475 AAEILAGGCAGGSQVIFTNPLEIVKIRLQVAG---EITTG--PRVSAL-----SVVRDLGFFGIYKGAKACFLRDIPFSA 544
Cdd:PTZ00169    8 ATDFLMGGISAAISKTAVAPIERVKMLIQTQDsipEIKSGkvPRYSGIvncfrRVSKEQGVLSLWRGNTANVIRYFPTQA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 545 IYFPCYAHVKASFA--NEDGQVSP--GSLLLAGAIAGMPAASLVTPADVIKTRLQV-AARAGQTTYSGVIDCFRKILREE 619
Cdd:PTZ00169   88 FNFAFKDYFKNMFPkyNQKTDFWKffGVNILSGGLAGASSLLIVYPLDFARTRLASdIGKGGDREFTGLFDCLMKISKQT 167

                         170
                  ....*....|...
gi 2217365158 620 GPKALWKGAGARV 632
Cdd:PTZ00169  168 GFLSLYQGFGVSV 180
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 102-229 8.83e-06

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: 46.44  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 102 KTVELLSGVVDQTKDGLISFQEFVA---FESVLCApdalfmvAFQLFDKAGKGEVTFEDVKQVFgqttihQHIPFNWDSE 178
Cdd:cd16185    36 ATAEKLIRMFDRDGNGTIDFEEFAAlhqFLSNMQN-------GFEQRDTSRSGRLDANEVHEAL------AASGFQLDPP 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217365158 179 FVQ---LHFGKERKRHLTYAEFTQFLLEIQLehAKQAFVQRDNARTGRVTaIDF 229
Cdd:cd16185   103 AFQalfRKFDPDRGGSLGFDDYIELCIFLAS--ARNLFQAFDRQRTGRVT-LDF 153
EF-hand_7 pfam13499
EF-hand domain pair;
66-127 4.67e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 4.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217365158  66 LQFKYASIEKNGEFFMSPNDFVtRYLNIFGESQP-NPKTVELLSGVVDQTKDGLISFQEFVAF 127
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELK-KLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLEL 65
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
76-164 5.44e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158  76 NGEFFMSPNDFVTRYLNIFGESQPNpkTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALFMVAFQLFDKAGKGEVTF 155
Cdd:COG5126    45 DGDGRISREEFVAGMESLFEATVEP--FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISF 122


                  ....*....
gi 2217365158 156 EDVKQVFGQ 164
Cdd:COG5126   123 EEFVAAVRD 131
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
562-657 1.82e-31

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 117.76  E-value: 1.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 562 GQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGV 641
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 2217365158 642 TLLTYELLQRWFYIDF 657
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
375-468 5.23e-27

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 105.05  E-value: 5.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 375 AYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELMyknsFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIK 454
Cdd:pfam00153   6 LASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGI----LDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|....
gi 2217365158 455 LTVNDFVRDKFMHK 468
Cdd:pfam00153  82 FGTYETLKRLLLKK 95
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 378-634 7.18e-25

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 105.62  E-value: 7.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 378 FGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELM--YKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKL 455
Cdd:PTZ00169   11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGKVprYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 456 TVNDFVRDKF----MHKDGSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLqvAGEIT-------TGPRVSALSVVRDLG 524
Cdd:PTZ00169   91 AFKDYFKNMFpkynQKTDFWKFFGVNILSGGLAGASSLLIVYPLDFARTRL--ASDIGkggdrefTGLFDCLMKISKQTG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 525 FFGIYKGAKACFLRDIPFSAIYFPCYAHVKASFANEDGQVSpgsLLLAGAIAG--MPAASLVT-PADVIKTRLQVAA--- 598
Cdd:PTZ00169  169 FLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNTN---ILYKWAVAQtvTILAGLISyPFDTVRRRMMMMSgrk 245

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2217365158 599 RAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFR 634
Cdd:PTZ00169  246 AKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLR 281
Mito_carr pfam00153
Mitochondrial carrier protein;
470-557 1.08e-18

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 81.55  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 470 GSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDL----GFFGIYKGAKACFLRDIPFSAI 545
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|..
gi 2217365158 546 YFPCYAHVKASF 557
Cdd:pfam00153  81 YFGTYETLKRLL 92
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 373-636 1.48e-12

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 68.41  E-value: 1.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 373 ESAYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTgsfvgelmyknSFDCFKKvlryegffgLYRGLLPQLLGVAPEKA 452
Cdd:PTZ00168    2 EHFHNLVTGALSGVIVDAVLYPIDSIKTNIQAKKSF-----------SFSDIKK---------LYSGILPTLVGTVPASA 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 453 IKLTVNDFVRDKFMHKDGSVPLAA-EILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDLGFFgIYKG 531
Cdd:PTZ00168   62 FFYCFYELSKKLLTEYRENISKTNlYLISTSIAEITACIVRLPFEIVKQNMQVSGNISVLKTIYEITQREGLPSF-LGKS 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 532 AKACFLRDIPFSAIYFPCYAHVKASFANEDGQVS---PG-SLLLAGAIAGMPAASLVTPADVIKTRlqvaaragQTTY-S 606
Cdd:PTZ00168  141 YFVMIVREIPFDCIQYFLWETLKEKAKKDFGKFSkkyPSiTSAICGGLAGGIAGFLTTPVDVIKSR--------QIIYgK 212

                         250       260       270
                  ....*....|....*....|....*....|
gi 2217365158 607 GVIDCFRKIlREEGPKALWKGAgarVFRSS 636
Cdd:PTZ00168  213 SYIETVTEI-AEEGYLTFYKGC---CFRSS 238
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 475-632 4.14e-07

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 52.46  E-value: 4.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 475 AAEILAGGCAGGSQVIFTNPLEIVKIRLQVAG---EITTG--PRVSAL-----SVVRDLGFFGIYKGAKACFLRDIPFSA 544
Cdd:PTZ00169    8 ATDFLMGGISAAISKTAVAPIERVKMLIQTQDsipEIKSGkvPRYSGIvncfrRVSKEQGVLSLWRGNTANVIRYFPTQA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 545 IYFPCYAHVKASFA--NEDGQVSP--GSLLLAGAIAGMPAASLVTPADVIKTRLQV-AARAGQTTYSGVIDCFRKILREE 619
Cdd:PTZ00169   88 FNFAFKDYFKNMFPkyNQKTDFWKffGVNILSGGLAGASSLLIVYPLDFARTRLASdIGKGGDREFTGLFDCLMKISKQT 167

                         170
                  ....*....|...
gi 2217365158 620 GPKALWKGAGARV 632
Cdd:PTZ00169  168 GFLSLYQGFGVSV 180
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 102-229 8.83e-06

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: 46.44  E-value: 8.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 102 KTVELLSGVVDQTKDGLISFQEFVA---FESVLCApdalfmvAFQLFDKAGKGEVTFEDVKQVFgqttihQHIPFNWDSE 178
Cdd:cd16185    36 ATAEKLIRMFDRDGNGTIDFEEFAAlhqFLSNMQN-------GFEQRDTSRSGRLDANEVHEAL------AASGFQLDPP 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217365158 179 FVQ---LHFGKERKRHLTYAEFTQFLLEIQLehAKQAFVQRDNARTGRVTaIDF 229
Cdd:cd16185   103 AFQalfRKFDPDRGGSLGFDDYIELCIFLAS--ARNLFQAFDRQRTGRVT-LDF 153
EF-hand_7 pfam13499
EF-hand domain pair;
66-127 4.67e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 41.86  E-value: 4.67e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217365158  66 LQFKYASIEKNGEFFMSPNDFVtRYLNIFGESQP-NPKTVELLSGVVDQTKDGLISFQEFVAF 127
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELK-KLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLEL 65
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 100-233 1.35e-04

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: 43.02  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 100 NPKTVELLSGVVDQTKDGLISFQEFvafesvlcapDALF------MVAFQLFDKAGKGEVTFEDVKQVFGQttihqhIPF 173
Cdd:cd16184    35 NDETCRLMIGMFDKDKSGTIDIYEF----------QALWnyiqqwKQVFQQFDRDRSGSIDENELHQALSQ------MGY 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217365158 174 NWDSEFVQL---HFGKERKRHLTYAEFTQflLEIQLEHAKQAFVQRDNARTGRVTaIDFRDIM 233
Cdd:cd16184    99 RLSPQFVQFlvsKYDPRARRSLTLDQFIQ--VCVQLQSLTDAFRQRDTQMTGTIT-ISYEDFL 158
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 571-637 2.55e-04

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 43.60  E-value: 2.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217365158 571 LAGAIAGMPAASLVTPADVIKTRLQVA-----ARAGQTT-YSGVIDCFRKILREEGPKALWKGAGARVFRSSP 637
Cdd:PTZ00169   12 LMGGISAAISKTAVAPIERVKMLIQTQdsipeIKSGKVPrYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFP 84
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
76-164 5.44e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 40.55  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158  76 NGEFFMSPNDFVTRYLNIFGESQPNpkTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALFMVAFQLFDKAGKGEVTF 155
Cdd:COG5126    45 DGDGRISREEFVAGMESLFEATVEP--FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADELFARLDTDGDGKISF 122


                  ....*....
gi 2217365158 156 EDVKQVFGQ 164
Cdd:COG5126   123 EEFVAAVRD 131
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 111-208 6.44e-04

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: 40.34  E-value: 6.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 111 VDQTKDGLISFQEFVAFESVL--CAPDALFMVAFQLFDKAGKGEVTFEDVKQVFGQTTIHQHIpfnwDSEFVQlhFGKER 188
Cdd:cd15898     9 ADKDGDGKLSLKEIKKLLKRLniRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPEL----EPIFKK--YAGTN 82

                          90       100
                  ....*....|....*....|
gi 2217365158 189 KRHLTYAEFTQFLLEIQLEH 208
Cdd:cd15898    83 RDYMTLEEFIRFLREEQGEN 102
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 138-207 8.61e-04

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: 40.29  E-value: 8.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158 138 FMVAFQLFDKAGKGEVTFEDVKQVFG----QTTIHQ---------HIPFNWDSEFVQLHFGKERKRHLTYAEFTQFLLEI 204
Cdd:cd15900     2 FEIAFKMFDLDGDGELDKEEFNKVQSiirsQTSVGQrhrdhtngeSTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQENL 81


                  ...
gi 2217365158 205 QLE 207
Cdd:cd15900    82 QEE 84
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 91-202 3.92e-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: 38.03  E-value: 3.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217365158  91 LNIfgesQPNPKTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALfMVAFQLFDKAGKGEVTFEDVkQVFGQTTIHQH 170
Cdd:cd15898    29 LNI----RVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPEL-EPIFKKYAGTNRDYMTLEEF-IRFLREEQGEN 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2217365158 171 IPFNWDSEFVQLHFGKERKRHLTYAEFTQFLL 202
Cdd:cd15898   103 VSEEECEELIEKYEPERENRQLSFEGFTNFLL 134
 
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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