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Conserved domains on  [gi|237649019|ref|NP_001153682|]
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electrogenic aspartate/glutamate antiporter SLC25A13, mitochondrial isoform 1 [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;
517-612 2.83e-31

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 117.37  E-value: 2.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  517 GQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGV 596
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 237649019  597 TLLTYELLQRWFYIDF 612
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
330-423 8.50e-27

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 104.66  E-value: 8.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  330 AYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELMyknsFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIK 409
Cdd:pfam00153   6 LASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGI----LDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|....
gi 237649019  410 LTVNDFVRDKFMHK 423
Cdd:pfam00153  82 FGTYETLKRLLLKK 95
Mito_carr pfam00153
Mitochondrial carrier protein;
425-512 1.56e-18

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 80.78  E-value: 1.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  425 GSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDL----GFFGIYKGAKACFLRDIPFSAI 500
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|..
gi 237649019  501 YFPCYAHVKASF 512
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 ...
 56-183 1.38e-05

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: 45.67  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  56 KTVELLSGVVDQTKDGLISFQEFVA---FESVLCApdalfmvAFQLFDKAGKGEVTFEDVKQVFgqttihQHIPFNWDSE 132
Cdd:cd16185   36 ATAEKLIRMFDRDGNGTIDFEEFAAlhqFLSNMQN-------GFEQRDTSRSGRLDANEVHEAL------AASGFQLDPP 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 237649019 133 FVQ---LHFGKERKRHLTYAEFTQFLLEIQLehAKQAFVQRDNARTGRVTaIDF 183
Cdd:cd16185  103 AFQalfRKFDPDRGGSLGFDDYIELCIFLAS--ARNLFQAFDRQRTGRVT-LDF 153
EF-hand_7 pfam13499
EF-hand domain pair;
16-81 2.49e-04

EF-hand domain pair;


:

Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 2.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237649019   16 ELRTIFlkyASIEKNGEFFMSPNDFVtRYLNIFGESQP-NPKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:pfam13499   3 KLKEAF---KLLDSDGDGYLDVEELK-KLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLEL 65
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
517-612 2.83e-31

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 117.37  E-value: 2.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  517 GQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGV 596
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 237649019  597 TLLTYELLQRWFYIDF 612
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
330-423 8.50e-27

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 104.66  E-value: 8.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  330 AYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELMyknsFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIK 409
Cdd:pfam00153   6 LASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGI----LDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|....
gi 237649019  410 LTVNDFVRDKFMHK 423
Cdd:pfam00153  82 FGTYETLKRLLLKK 95
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 333-589 1.08e-24

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 104.85  E-value: 1.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 333 FGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELM--YKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKL 410
Cdd:PTZ00169  11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGKVprYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 411 TVNDFVRDKF----MHKDGSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLqvAGEIT-------TGPRVSALSVVRDLG 479
Cdd:PTZ00169  91 AFKDYFKNMFpkynQKTDFWKFFGVNILSGGLAGASSLLIVYPLDFARTRL--ASDIGkggdrefTGLFDCLMKISKQTG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 480 FFGIYKGAKACFLRDIPFSAIYFPCYAHVKASFANEDGQVSpgsLLLAGAIAG--MPAASLVT-PADVIKTRLQVAA--- 553
Cdd:PTZ00169 169 FLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNTN---ILYKWAVAQtvTILAGLISyPFDTVRRRMMMMSgrk 245

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 237649019 554 RAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFR 589
Cdd:PTZ00169 246 AKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLR 281
Mito_carr pfam00153
Mitochondrial carrier protein;
425-512 1.56e-18

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 80.78  E-value: 1.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  425 GSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDL----GFFGIYKGAKACFLRDIPFSAI 500
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|..
gi 237649019  501 YFPCYAHVKASF 512
Cdd:pfam00153  81 YFGTYETLKRLL 92
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 430-587 4.89e-07

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 52.08  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 430 AAEILAGGCAGGSQVIFTNPLEIVKIRLQVAG---EITTG--PRVSAL-----SVVRDLGFFGIYKGAKACFLRDIPFSA 499
Cdd:PTZ00169   8 ATDFLMGGISAAISKTAVAPIERVKMLIQTQDsipEIKSGkvPRYSGIvncfrRVSKEQGVLSLWRGNTANVIRYFPTQA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 500 IYFPCYAHVKASFA--NEDGQVSP--GSLLLAGAIAGMPAASLVTPADVIKTRLQV-AARAGQTTYSGVIDCFRKILREE 574
Cdd:PTZ00169  88 FNFAFKDYFKNMFPkyNQKTDFWKffGVNILSGGLAGASSLLIVYPLDFARTRLASdIGKGGDREFTGLFDCLMKISKQT 167

                        170
                 ....*....|...
gi 237649019 575 GPKALWKGAGARV 587
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 ...
 56-183 1.38e-05

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: 45.67  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  56 KTVELLSGVVDQTKDGLISFQEFVA---FESVLCApdalfmvAFQLFDKAGKGEVTFEDVKQVFgqttihQHIPFNWDSE 132
Cdd:cd16185   36 ATAEKLIRMFDRDGNGTIDFEEFAAlhqFLSNMQN-------GFEQRDTSRSGRLDANEVHEAL------AASGFQLDPP 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 237649019 133 FVQ---LHFGKERKRHLTYAEFTQFLLEIQLehAKQAFVQRDNARTGRVTaIDF 183
Cdd:cd16185  103 AFQalfRKFDPDRGGSLGFDDYIELCIFLAS--ARNLFQAFDRQRTGRVT-LDF 153
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
13-118 2.10e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.70  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  13 DPAELRTIFLKY-----ASIEKNGEFFMSPNDFVTRYLNIFGESQPNpkTVELLSGVVDQTKDGLISFQEFVAFESVLCA 87
Cdd:COG5126   23 ERDDFEALFRRLwatlfSEADTDGDGRISREEFVAGMESLFEATVEP--FARAAFDLLDTDGDGKISADEFRRLLTALGV 100

                         90       100       110
                 ....*....|....*....|....*....|.
gi 237649019  88 PDALFMVAFQLFDKAGKGEVTFEDVKQVFGQ 118
Cdd:COG5126  101 SEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
16-81 2.49e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 2.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237649019   16 ELRTIFlkyASIEKNGEFFMSPNDFVtRYLNIFGESQP-NPKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:pfam13499   3 KLKEAF---KLLDSDGDGYLDVEELK-KLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLEL 65
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 19-81 5.08e-04

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: 39.40  E-value: 5.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237649019  19 TIFLKYASIEKNGEFfMSPNDF---VTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:cd00213   12 DVFHKYSGKEGDKDT-LSKKELkelLETELPNFLKNQKDPEAVDKIMKDLDVNKDGKVDFQEFLVL 76
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-90 4.06e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019   1 MAAAKVALTKRADPAELRTIFlkyASIEKNGEFFMSPNDFvTRYLNIFGESQPNpktVELLSGVVDQTKDGLISFQEFVA 80
Cdd:COG5126   55 FVAGMESLFEATVEPFARAAF---DLLDTDGDGKISADEF-RRLLTALGVSEEE---ADELFARLDTDGDGKISFEEFVA 127

                         90
                 ....*....|
gi 237649019  81 FESVLCAPDA 90
Cdd:COG5126  128 AVRDYYTPDA 137
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
517-612 2.83e-31

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 117.37  E-value: 2.83e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  517 GQVSPGSLLLAGAIAGMPAASLVTPADVIKTRLQVAARAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFRSSPQFGV 596
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 237649019  597 TLLTYELLQRWFYIDF 612
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
330-423 8.50e-27

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 104.66  E-value: 8.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  330 AYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELMyknsFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIK 409
Cdd:pfam00153   6 LASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGI----LDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|....
gi 237649019  410 LTVNDFVRDKFMHK 423
Cdd:pfam00153  82 FGTYETLKRLLLKK 95
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 333-589 1.08e-24

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 104.85  E-value: 1.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 333 FGLGSVAGAVGATAVYPIDLVKTRMQNQRSTGSFVGELM--YKNSFDCFKKVLRYEGFFGLYRGLLPQLLGVAPEKAIKL 410
Cdd:PTZ00169  11 FLMGGISAAISKTAVAPIERVKMLIQTQDSIPEIKSGKVprYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 411 TVNDFVRDKF----MHKDGSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLqvAGEIT-------TGPRVSALSVVRDLG 479
Cdd:PTZ00169  91 AFKDYFKNMFpkynQKTDFWKFFGVNILSGGLAGASSLLIVYPLDFARTRL--ASDIGkggdrefTGLFDCLMKISKQTG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 480 FFGIYKGAKACFLRDIPFSAIYFPCYAHVKASFANEDGQVSpgsLLLAGAIAG--MPAASLVT-PADVIKTRLQVAA--- 553
Cdd:PTZ00169 169 FLSLYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNTN---ILYKWAVAQtvTILAGLISyPFDTVRRRMMMMSgrk 245

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 237649019 554 RAGQTTYSGVIDCFRKILREEGPKALWKGAGARVFR 589
Cdd:PTZ00169 246 AKSEIQYTGTLDCWKKILKNEGLGGFFKGAWANVLR 281
Mito_carr pfam00153
Mitochondrial carrier protein;
425-512 1.56e-18

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 80.78  E-value: 1.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  425 GSVPLAAEILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDL----GFFGIYKGAKACFLRDIPFSAI 500
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIykeeGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|..
gi 237649019  501 YFPCYAHVKASF 512
Cdd:pfam00153  81 YFGTYETLKRLL 92
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 328-591 1.88e-12

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 68.03  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 328 ESAYRFGLGSVAGAVGATAVYPIDLVKTRMQNQRSTgsfvgelmyknSFDCFKKvlryegffgLYRGLLPQLLGVAPEKA 407
Cdd:PTZ00168   2 EHFHNLVTGALSGVIVDAVLYPIDSIKTNIQAKKSF-----------SFSDIKK---------LYSGILPTLVGTVPASA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 408 IKLTVNDFVRDKFMHKDGSVPLAA-EILAGGCAGGSQVIFTNPLEIVKIRLQVAGEITTGPRVSALSVVRDLGFFgIYKG 486
Cdd:PTZ00168  62 FFYCFYELSKKLLTEYRENISKTNlYLISTSIAEITACIVRLPFEIVKQNMQVSGNISVLKTIYEITQREGLPSF-LGKS 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 487 AKACFLRDIPFSAIYFPCYAHVKASFANEDGQVS---PG-SLLLAGAIAGMPAASLVTPADVIKTRlqvaaragQTTY-S 561
Cdd:PTZ00168 141 YFVMIVREIPFDCIQYFLWETLKEKAKKDFGKFSkkyPSiTSAICGGLAGGIAGFLTTPVDVIKSR--------QIIYgK 212

                        250       260       270
                 ....*....|....*....|....*....|
gi 237649019 562 GVIDCFRKIlREEGPKALWKGAgarVFRSS 591
Cdd:PTZ00168 213 SYIETVTEI-AEEGYLTFYKGC---CFRSS 238
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 430-587 4.89e-07

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 52.08  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 430 AAEILAGGCAGGSQVIFTNPLEIVKIRLQVAG---EITTG--PRVSAL-----SVVRDLGFFGIYKGAKACFLRDIPFSA 499
Cdd:PTZ00169   8 ATDFLMGGISAAISKTAVAPIERVKMLIQTQDsipEIKSGkvPRYSGIvncfrRVSKEQGVLSLWRGNTANVIRYFPTQA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019 500 IYFPCYAHVKASFA--NEDGQVSP--GSLLLAGAIAGMPAASLVTPADVIKTRLQV-AARAGQTTYSGVIDCFRKILREE 574
Cdd:PTZ00169  88 FNFAFKDYFKNMFPkyNQKTDFWKffGVNILSGGLAGASSLLIVYPLDFARTRLASdIGKGGDREFTGLFDCLMKISKQT 167

                        170
                 ....*....|...
gi 237649019 575 GPKALWKGAGARV 587
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 ...
 56-183 1.38e-05

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: 45.67  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  56 KTVELLSGVVDQTKDGLISFQEFVA---FESVLCApdalfmvAFQLFDKAGKGEVTFEDVKQVFgqttihQHIPFNWDSE 132
Cdd:cd16185   36 ATAEKLIRMFDRDGNGTIDFEEFAAlhqFLSNMQN-------GFEQRDTSRSGRLDANEVHEAL------AASGFQLDPP 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 237649019 133 FVQ---LHFGKERKRHLTYAEFTQFLLEIQLehAKQAFVQRDNARTGRVTaIDF 183
Cdd:cd16185  103 AFQalfRKFDPDRGGSLGFDDYIELCIFLAS--ARNLFQAFDRQRTGRVT-LDF 153
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 54-187 1.25e-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: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  54 NPKTVELLSGVVDQTKDGLISFQEFvafesvlcapDALF------MVAFQLFDKAGKGEVTFEDVKQVFGQttihqhIPF 127
Cdd:cd16184   35 NDETCRLMIGMFDKDKSGTIDIYEF----------QALWnyiqqwKQVFQQFDRDRSGSIDENELHQALSQ------MGY 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 237649019 128 NWDSEFVQL---HFGKERKRHLTYAEFTQflLEIQLEHAKQAFVQRDNARTGRVTaIDFRDIM 187
Cdd:cd16184   99 RLSPQFVQFlvsKYDPRARRSLTLDQFIQ--VCVQLQSLTDAFRQRDTQMTGTIT-ISYEDFL 158
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
13-118 2.10e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 41.70  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  13 DPAELRTIFLKY-----ASIEKNGEFFMSPNDFVTRYLNIFGESQPNpkTVELLSGVVDQTKDGLISFQEFVAFESVLCA 87
Cdd:COG5126   23 ERDDFEALFRRLwatlfSEADTDGDGRISREEFVAGMESLFEATVEP--FARAAFDLLDTDGDGKISADEFRRLLTALGV 100

                         90       100       110
                 ....*....|....*....|....*....|.
gi 237649019  88 PDALFMVAFQLFDKAGKGEVTFEDVKQVFGQ 118
Cdd:COG5126  101 SEEEADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_7 pfam13499
EF-hand domain pair;
16-81 2.49e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 39.54  E-value: 2.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 237649019   16 ELRTIFlkyASIEKNGEFFMSPNDFVtRYLNIFGESQP-NPKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:pfam13499   3 KLKEAF---KLLDSDGDGYLDVEELK-KLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLEL 65
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 526-592 2.74e-04

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 43.60  E-value: 2.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 237649019 526 LAGAIAGMPAASLVTPADVIKTRLQVA-----ARAGQTT-YSGVIDCFRKILREEGPKALWKGAGARVFRSSP 592
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQTQdsipeIKSGKVPrYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFP 84
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 19-81 5.08e-04

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: 39.40  E-value: 5.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237649019  19 TIFLKYASIEKNGEFfMSPNDF---VTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAF 81
Cdd:cd00213   12 DVFHKYSGKEGDKDT-LSKKELkelLETELPNFLKNQKDPEAVDKIMKDLDVNKDGKVDFQEFLVL 76
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 65-162 8.06e-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: 39.96  E-value: 8.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  65 VDQTKDGLISFQEFVAFESVL--CAPDALFMVAFQLFDKAGKGEVTFEDVKQVFGQTTIHQHIpfnwDSEFVQlhFGKER 142
Cdd:cd15898    9 ADKDGDGKLSLKEIKKLLKRLniRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPEL----EPIFKK--YAGTN 82

                         90       100
                 ....*....|....*....|
gi 237649019 143 KRHLTYAEFTQFLLEIQLEH 162
Cdd:cd15898   83 RDYMTLEEFIRFLREEQGEN 102
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 17-156 8.95e-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: 39.96  E-value: 8.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  17 LRTIFLKYasiEKNGEFFMSPNDFVT--RYLNIfgesQPNPKTVELLSGVVDQTKDGLISFQEFVAFESVLCAPDALfMV 94
Cdd:cd15898    2 LRRQWIKA---DKDGDGKLSLKEIKKllKRLNI----RVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPEL-EP 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 237649019  95 AFQLFDKAGKGEVTFEDVkQVFGQTTIHQHIPFNWDSEFVQLHFGKERKRHLTYAEFTQFLL 156
Cdd:cd15898   74 IFKKYAGTNRDYMTLEEF-IRFLREEQGENVSEEECEELIEKYEPERENRQLSFEGFTNFLL 134
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 92-161 1.32e-03

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: 39.90  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  92 FMVAFQLFDKAGKGEVTFEDVKQVFG----QTTIHQ---------HIPFNWDSEFVQLHFGKERKRHLTYAEFTQFLLEI 158
Cdd:cd15900    2 FEIAFKMFDLDGDGELDKEEFNKVQSiirsQTSVGQrhrdhtngeSTKLGMNSTLARYFFGKDGKQKLSIEKFLEFQENL 81


                 ...
gi 237649019 159 QLE 161
Cdd:cd15900   82 QEE 84
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 16-81 3.19e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 36.37  E-value: 3.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 237649019  16 ELRTIFLKYasiEKNGEFFMSPNDFVtRYLNIFGESQPNPKTVELLSgVVDQTKDGLISFQEFVAF 81
Cdd:cd00051    1 ELREAFRLF---DKDGDGTISADELK-AALKSLGEGLSEEEIDEMIR-EVDKDGDGKIDFEEFLEL 61
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
1-90 4.06e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019   1 MAAAKVALTKRADPAELRTIFlkyASIEKNGEFFMSPNDFvTRYLNIFGESQPNpktVELLSGVVDQTKDGLISFQEFVA 80
Cdd:COG5126   55 FVAGMESLFEATVEPFARAAF---DLLDTDGDGKISADEF-RRLLTALGVSEEE---ADELFARLDTDGDGKISFEEFVA 127

                         90
                 ....*....|
gi 237649019  81 FESVLCAPDA 90
Cdd:COG5126  128 AVRDYYTPDA 137
S-100A10_like cd05031
S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of ...
 17-94 7.27e-03

S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of the S100 family of EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1_like group belongs, 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. A unique feature of S100A10 is that it contains mutation in both of the calcium binding sites, making it calcium insensitive. S100A10 has been detected in brain, heart, gastrointestinal tract, kidney, liver, lung, spleen, testes, epidermis, aorta, and thymus. Structural data supports the homo- and hetero-dimeric as well as hetero-tetrameric nature of the protein. S100A10 has multiple binding partners in its calcium free state and is therefore involved in many diverse biological functions.


Pssm-ID: 240157 [Multi-domain]  Cd Length: 94  Bit Score: 36.25  E-value: 7.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 237649019  17 LRTIFLKYASIEKNGEFfMSPND---FVTRYLNIFGESQPNPKTVELLSGVVDQTKDGLISFQEFVAF-ESVLCAPDALF 92
Cdd:cd05031   10 LILTFHRYAGKDGDKNT-LSRKElkkLMEKELSEFLKNQKDPMAVDKIMKDLDQNRDGKVNFEEFVSLvAGLSIACEEYY 88


                 ..
gi 237649019  93 MV 94
Cdd:cd05031   89 VK 90
 
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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