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Conserved domains on  [gi|768003955|ref|XP_011526576|]
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mitochondrial adenyl nucleotide antiporter SLC25A23 isoform X1 [Homo sapiens]

Protein Classification

calcium-binding mitochondrial carrier protein( domain architecture ID 12839457)

calcium-binding mitochondrial carrier protein similar to Homo sapiens SCaMC (short calcium-binding mitochondrial carriers), which may function in nucleotide transport in mitochondria, such as ATP-Mg/Pi exchange or related transport systems, in a calcium-regulated mode

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00169 super family cl36523
ADP/ATP transporter on adenylate translocase; Provisional
 237-510 4.11e-31

ADP/ATP transporter on adenylate translocase; Provisional


The actual alignment was detected with superfamily member PTZ00169:

Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 123.34  E-value: 4.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 237 VAGAVAGAVSRTGTAPLDRLKVFMQVHAS-------KTNRLN-ILGGLRSMVLEGGIRSLWRGNGINVLKIAPESAIKFM 308
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQTQDSipeiksgKVPRYSgIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 309 AYEQIKRAILGQQETLHVQERFVA----GSLAGATAQTIIYPMEVLKTRLT--LRRTG--QYKGLLDCARRILEREGPRA 380
Cdd:PTZ00169  92 FKDYFKNMFPKYNQKTDFWKFFGVnilsGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 381 FYRGYLPNVLGIIPYAGIDLAVYETLKNWWLQqyshDSADPGILVLLACGTISSTCGQIASYPLALVRTRMQAQASIEGG 460
Cdd:PTZ00169 172 LYQGFGVSVQGIIVYRGAYFGLYDSAKALLFG----NDKNTNILYKWAVAQTVTILAGLISYPFDTVRRRMMMMSGRKAK 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768003955 461 PQL---SMLGLLRHILSQEGMRGLYRGIAPNFMKVIPAvSISYVVYENMKQAL 510
Cdd:PTZ00169 248 SEIqytGTLDCWKKILKNEGLGGFFKGAWANVLRGAGG-ALVLVFYDELQKLL 299
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-142 5.01e-23

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 95.24  E-value: 5.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955   8 AERRQRWGRLFEELDSNKDGRVDVHELRQGLARLgggnpdpgaQQGISSEGDADPDGGLDLEEF-----SRYLQEREQRL 82
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRL---------WATLFSEADTDGDGRISREEFvagmeSLFEATVEPFA 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  83 LLMFHSLDRNQDGHIDVSEIQQSFRALGisISLEQAEKILHSMDRDGTMTIDWQEWRDHF 142
Cdd:COG5126   72 RAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAV 129
 
Name Accession Description Interval E-value
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 237-510 4.11e-31

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 123.34  E-value: 4.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 237 VAGAVAGAVSRTGTAPLDRLKVFMQVHAS-------KTNRLN-ILGGLRSMVLEGGIRSLWRGNGINVLKIAPESAIKFM 308
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQTQDSipeiksgKVPRYSgIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 309 AYEQIKRAILGQQETLHVQERFVA----GSLAGATAQTIIYPMEVLKTRLT--LRRTG--QYKGLLDCARRILEREGPRA 380
Cdd:PTZ00169  92 FKDYFKNMFPKYNQKTDFWKFFGVnilsGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 381 FYRGYLPNVLGIIPYAGIDLAVYETLKNWWLQqyshDSADPGILVLLACGTISSTCGQIASYPLALVRTRMQAQASIEGG 460
Cdd:PTZ00169 172 LYQGFGVSVQGIIVYRGAYFGLYDSAKALLFG----NDKNTNILYKWAVAQTVTILAGLISYPFDTVRRRMMMMSGRKAK 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768003955 461 PQL---SMLGLLRHILSQEGMRGLYRGIAPNFMKVIPAvSISYVVYENMKQAL 510
Cdd:PTZ00169 248 SEIqytGTLDCWKKILKNEGLGGFFKGAWANVLRGAGG-ALVLVFYDELQKLL 299
Mito_carr pfam00153
Mitochondrial carrier protein;
322-411 4.50e-29

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 110.82  E-value: 4.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  322 ETLHVQERFVAGSLAGATAQTIIYPMEVLKTRLTLRRT---GQYKGLLDCARRILEREGPRAFYRGYLPNVLGIIPYAGI 398
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGsgkSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|...
gi 768003955  399 DLAVYETLKNWWL 411
Cdd:pfam00153  81 YFGTYETLKRLLL 93
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-142 5.01e-23

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 95.24  E-value: 5.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955   8 AERRQRWGRLFEELDSNKDGRVDVHELRQGLARLgggnpdpgaQQGISSEGDADPDGGLDLEEF-----SRYLQEREQRL 82
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRL---------WATLFSEADTDGDGRISREEFvagmeSLFEATVEPFA 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  83 LLMFHSLDRNQDGHIDVSEIQQSFRALGisISLEQAEKILHSMDRDGTMTIDWQEWRDHF 142
Cdd:COG5126   72 RAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAV 129
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 12-138 7.01e-11

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: 61.08  E-value: 7.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  12 QRWgrlFEELDSNKDGRVDVHELRQGLArlgGGNPDPG---AQQGISSEgDADPDGGLDLEEFS---RYLQEREQRlllm 85
Cdd:cd16185    3 RQW---FRAVDRDRSGSIDVNELQKALA---GGGLLFSlatAEKLIRMF-DRDGNGTIDFEEFAalhQFLSNMQNG---- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768003955  86 FHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEW 138
Cdd:cd16185   72 FEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
EF-hand_7 pfam13499
EF-hand domain pair;
79-137 2.17e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 53.80  E-value: 2.17e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768003955   79 EQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGISISL--EQAEKILHSMDRDGTMTIDWQE 137
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEE 61
PTZ00184 PTZ00184
calmodulin; Provisional
 18-138 5.71e-09

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 55.15  E-value: 5.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  18 FEELDSNKDGRVDVHELRQGLARLGGgNPDPGAQQGISSEGDADPDGGLDLEEFSRYLQER------EQRLLLMFHSLDR 91
Cdd:PTZ00184  17 FSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEVDADGNGTIDFPEFLTLMARKmkdtdsEEEIKEAFKVFDR 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 768003955  92 NQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEW 138
Cdd:PTZ00184  96 DGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEF 142
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
16-134 3.12e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 45.83  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  16 RLFEELDSNKDGRVDVHELRQGLArlggGNPDPGAQQGIS---SEGDADPDGGLDLEEFSRYL------QEREQRLLL-- 84
Cdd:NF041410  31 QLFAKLDSDGDGSVSQDELSSALS----SKSDDGSLIDLSelfSDLDSDGDGSLSSDELAAAAppppppPDQAPSTELad 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768003955  85 -MFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSmDRDGTMTID 134
Cdd:NF041410 107 dLLSALDTDGDGSISSDELSAGLTSAGSSADSSQLFSALDS-DGDGSVSSD 156
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 16-41 5.52e-03

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 34.66  E-value: 5.52e-03
                           10        20
                   ....*....|....*....|....*.
gi 768003955    16 RLFEELDSNKDGRVDVHELRQGLARL 41
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 237-510 4.11e-31

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 123.34  E-value: 4.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 237 VAGAVAGAVSRTGTAPLDRLKVFMQVHAS-------KTNRLN-ILGGLRSMVLEGGIRSLWRGNGINVLKIAPESAIKFM 308
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQTQDSipeiksgKVPRYSgIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 309 AYEQIKRAILGQQETLHVQERFVA----GSLAGATAQTIIYPMEVLKTRLT--LRRTG--QYKGLLDCARRILEREGPRA 380
Cdd:PTZ00169  92 FKDYFKNMFPKYNQKTDFWKFFGVnilsGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 381 FYRGYLPNVLGIIPYAGIDLAVYETLKNWWLQqyshDSADPGILVLLACGTISSTCGQIASYPLALVRTRMQAQASIEGG 460
Cdd:PTZ00169 172 LYQGFGVSVQGIIVYRGAYFGLYDSAKALLFG----NDKNTNILYKWAVAQTVTILAGLISYPFDTVRRRMMMMSGRKAK 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768003955 461 PQL---SMLGLLRHILSQEGMRGLYRGIAPNFMKVIPAvSISYVVYENMKQAL 510
Cdd:PTZ00169 248 SEIqytGTLDCWKKILKNEGLGGFFKGAWANVLRGAGG-ALVLVFYDELQKLL 299
Mito_carr pfam00153
Mitochondrial carrier protein;
322-411 4.50e-29

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 110.82  E-value: 4.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  322 ETLHVQERFVAGSLAGATAQTIIYPMEVLKTRLTLRRT---GQYKGLLDCARRILEREGPRAFYRGYLPNVLGIIPYAGI 398
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGsgkSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|...
gi 768003955  399 DLAVYETLKNWWL 411
Cdd:pfam00153  81 YFGTYETLKRLLL 93
Mito_carr pfam00153
Mitochondrial carrier protein;
232-319 5.19e-26

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 101.96  E-value: 5.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  232 WWKQLVAGAVAGAVSRTGTAPLDRLKVFMQVHA--SKTNRLNILGGLRSMVLEGGIRSLWRGNGINVLKIAPESAIKFMA 309
Cdd:pfam00153   5 FLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGgsGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFGT 84

                          90
                  ....*....|
gi 768003955  310 YEQIKRAILG 319
Cdd:pfam00153  85 YETLKRLLLK 94
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-142 5.01e-23

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 95.24  E-value: 5.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955   8 AERRQRWGRLFEELDSNKDGRVDVHELRQGLARLgggnpdpgaQQGISSEGDADPDGGLDLEEF-----SRYLQEREQRL 82
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRL---------WATLFSEADTDGDGRISREEFvagmeSLFEATVEPFA 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  83 LLMFHSLDRNQDGHIDVSEIQQSFRALGisISLEQAEKILHSMDRDGTMTIDWQEWRDHF 142
Cdd:COG5126   72 RAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAV 129
Mito_carr pfam00153
Mitochondrial carrier protein;
420-511 5.88e-23

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 93.49  E-value: 5.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  420 DPGILVLLACGTISSTCGQIASYPLALVRTRMQAQASIEGGPQLSMLGLLRHILSQEGMRGLYRGIAPNFMKVIPAVSIS 499
Cdd:pfam00153   2 ELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIY 81

                          90
                  ....*....|..
gi 768003955  500 YVVYENMKQALG 511
Cdd:pfam00153  82 FGTYETLKRLLL 93
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-107 3.12e-15

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 72.90  E-value: 3.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955   8 AERRQRWGRLFEELDSNKDGRVDVHELRQGLARLGGGNPDPGAQQGISSeGDADPDGGLDLEEFSRYLQE---REQRLLL 84
Cdd:COG5126   29 ALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDL-LDTDGDGKISADEFRRLLTAlgvSEEEADE 107

                         90       100
                 ....*....|....*....|...
gi 768003955  85 MFHSLDRNQDGHIDVSEIQQSFR 107
Cdd:COG5126  108 LFARLDTDGDGKISFEEFVAAVR 130
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 12-138 7.01e-11

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: 61.08  E-value: 7.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  12 QRWgrlFEELDSNKDGRVDVHELRQGLArlgGGNPDPG---AQQGISSEgDADPDGGLDLEEFS---RYLQEREQRlllm 85
Cdd:cd16185    3 RQW---FRAVDRDRSGSIDVNELQKALA---GGGLLFSlatAEKLIRMF-DRDGNGTIDFEEFAalhQFLSNMQNG---- 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768003955  86 FHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEW 138
Cdd:cd16185   72 FEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 85-142 7.95e-11

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: 57.94  E-value: 7.95e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768003955  85 MFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEWRDHF 142
Cdd:cd00051    5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 217-390 1.63e-10

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 62.48  E-value: 1.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 217 TVPDEFSKQEKLTGMW---WKQLVAGAVAGAVSRTGTAPLDRLKVFMQVHASKTNRLNILG---GLRSMVLEGGIRSLWR 290
Cdd:PTZ00169  95 YFKNMFPKYNQKTDFWkffGVNILSGGLAGASSLLIVYPLDFARTRLASDIGKGGDREFTGlfdCLMKISKQTGFLSLYQ 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 291 GNGINVLKIAPESAIKFMAYEQIKRAILGQQETLHVQERFVAGSLAGATAQTIIYPMEVLKTRLTL---RRTG---QYKG 364
Cdd:PTZ00169 175 GFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNTNILYKWAVAQTVTILAGLISYPFDTVRRRMMMmsgRKAKseiQYTG 254

                        170       180
                 ....*....|....*....|....*.
gi 768003955 365 LLDCARRILEREGPRAFYRGYLPNVL 390
Cdd:PTZ00169 255 TLDCWKKILKNEGLGGFFKGAWANVL 280
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 16-133 2.82e-10

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: 59.46  E-value: 2.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  16 RLFEELDSNKDGRVDVHELRQGLaRLGGGNPdpgaqqgISSEG--------DADPDGGLDLEEFS---RYLQeREQRLll 84
Cdd:cd16180    4 RIFQAVDRDRSGRISAKELQRAL-SNGDWTP-------FSIETvrlminmfDRDRSGTINFDEFVglwKYIQ-DWRRL-- 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 768003955  85 mFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTI 133
Cdd:cd16180   73 -FRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSI 120
EF-hand_7 pfam13499
EF-hand domain pair;
79-137 2.17e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 53.80  E-value: 2.17e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768003955   79 EQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGISISL--EQAEKILHSMDRDGTMTIDWQE 137
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEE 61
PTZ00184 PTZ00184
calmodulin; Provisional
 18-138 5.71e-09

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 55.15  E-value: 5.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  18 FEELDSNKDGRVDVHELRQGLARLGGgNPDPGAQQGISSEGDADPDGGLDLEEFSRYLQER------EQRLLLMFHSLDR 91
Cdd:PTZ00184  17 FSLFDKDGDGTITTKELGTVMRSLGQ-NPTEAELQDMINEVDADGNGTIDFPEFLTLMARKmkdtdsEEEIKEAFKVFDR 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 768003955  92 NQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEW 138
Cdd:PTZ00184  96 DGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEF 142
PTZ00183 PTZ00183
centrin; Provisional
 18-137 6.07e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 55.47  E-value: 6.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  18 FEELDSNKDGRVDVHELRQGLARLGGGNPDPGAQQGISsEGDADPDGGLDLEEF----SRYLQEREQR--LLLMFHSLDR 91
Cdd:PTZ00183  23 FDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIA-DVDKDGSGKIDFEEFldimTKKLGERDPReeILKAFRLFDD 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 768003955  92 NQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQE 137
Cdd:PTZ00183 102 DKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEE 147
EF-hand_7 pfam13499
EF-hand domain pair;
11-76 2.53e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.71  E-value: 2.53e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768003955   11 RQRWGRLFEELDSNKDGRVDVHELRQGLARLGGGNP-DPGAQQGISSEGDADPDGGLDLEEFSRYLQ 76
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 12-134 1.19e-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: 51.88  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  12 QRWgrlFEELDSNKDGRVDVHELRQGLARLGGGN-PDPGAQQGISSeGDADPDGGLDLEEFS---RYLQEREQrlllMFH 87
Cdd:cd16184    3 QQW---FQAVDRDRSGKISAKELQQALVNGNWSHfNDETCRLMIGM-FDKDKSGTIDIYEFQalwNYIQQWKQ----VFQ 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 768003955  88 SLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDG--TMTID 134
Cdd:cd16184   75 QFDRDRSGSIDENELHQALSQMGYRLSPQFVQFLVSKYDPRArrSLTLD 123
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 14-134 2.36e-07

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: 50.72  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  14 WGrLFEELDSNKDGRVDVHELRQGLARlGGGNP-DPGAQQGISSEGDADPDGGLDLEEFS---RYLQEREQrlllMFHSL 89
Cdd:cd16183    3 WN-VFQRVDKDRSGQISATELQQALSN-GTWTPfNPETVRLMIGMFDRDNSGTINFQEFAalwKYITDWQN----CFRSF 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 768003955  90 DRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTID 134
Cdd:cd16183   77 DRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIA 121
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 18-76 2.63e-07

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: 47.93  E-value: 2.63e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768003955  18 FEELDSNKDGRVDVHELRQGLARLGGGNPDPGAQQGIsSEGDADPDGGLDLEEFSRYLQ 76
Cdd:cd00051    6 FRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMI-REVDKDGDGKIDFEEFLELMA 63
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 330-508 5.00e-07

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 51.46  E-value: 5.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 330 FVAGSLAGATAQTIIYPMEVLKTRLTlrrtgqykglldcARRILEREGPRAFYRGYLPNVLGIIPYAGIDLAVYETLKNw 409
Cdd:PTZ00168   7 LVTGALSGVIVDAVLYPIDSIKTNIQ-------------AKKSFSFSDIKKLYSGILPTLVGTVPASAFFYCFYELSKK- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 410 WLQQYSHDSADPGILVllacgtISSTCGQIAS----YPLALVRTRMQAQASIeggpqlSMLGLLRHILSQEGMRgLYRGI 485
Cdd:PTZ00168  73 LLTEYRENISKTNLYL------ISTSIAEITAcivrLPFEIVKQNMQVSGNI------SVLKTIYEITQREGLP-SFLGK 139

                        170       180
                 ....*....|....*....|....*
gi 768003955 486 APNFMKV--IPAVSISYVVYENMKQ 508
Cdd:PTZ00168 140 SYFVMIVreIPFDCIQYFLWETLKE 164
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 18-101 9.82e-07

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


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 50.52  E-value: 9.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  18 FEELDSNKDGRVDVHELRQGLARLGGGNPDPGAQQGISSE---------------GDADPDGGLDLEEFSRYLQEREQRL 82
Cdd:cd15899   77 FRAVDPDEDGHVSWDEYKNDTYGSVGDDEENVADNIKEDEeykklllkdkkrfeaADQDGDLILTLEEFLAFLHPEESPY 156

                         90       100
                 ....*....|....*....|....*
gi 768003955  83 LLMF------HSLDRNQDGHIDVSE 101
Cdd:cd15899  157 MLDFviketlEDLDKNGDGFISLEE 181
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 77-137 1.14e-06

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


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 50.39  E-value: 1.14e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768003955  77 EREQRLLLMFHSLDRNQDGHIDVSE----IQQSFRALgisiSLEQAEKILHSMDRDGTMTIDWQE 137
Cdd:cd16227   33 EAKRRLAVLAKKMDLNDDGFIDRKElkawILRSFKML----DEEEANERFEEADEDGDGKVTWEE 93
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 81-158 1.65e-06

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 47.66  E-value: 1.65e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768003955  81 RLLLMFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEWRDhfLLHSLENVEDVLYFWK 158
Cdd:cd15898    1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEE--LYKSLTERPELEPIFK 76
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 234-484 2.05e-06

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 49.54  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 234 KQLVAGAVAGAVSRTGTAPLDRLKVFMQVHasktNRLNIlgglrsmvleGGIRSLWRGNGINVLKIAPESAIKFMAYEQI 313
Cdd:PTZ00168   5 HNLVTGALSGVIVDAVLYPIDSIKTNIQAK----KSFSF----------SDIKKLYSGILPTLVGTVPASAFFYCFYELS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 314 KRAILGQQETLHVQERF-VAGSLAGATAQTIIYPMEVLKTRLtlrrtgQYKGLLDCARRILE---REGPRAFY-RGYLPN 388
Cdd:PTZ00168  71 KKLLTEYRENISKTNLYlISTSIAEITACIVRLPFEIVKQNM------QVSGNISVLKTIYEitqREGLPSFLgKSYFVM 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955 389 VLGIIPYAGIDLAVYETLKNWWLQQYSHDSADPGILVLLACGTISSTCGQIASYPLALVRTR--MQAQASIEGGPQlsml 466
Cdd:PTZ00168 145 IVREIPFDCIQYFLWETLKEKAKKDFGKFSKKYPSITSAICGGLAGGIAGFLTTPVDVIKSRqiIYGKSYIETVTE---- 220

                        250
                 ....*....|....*...
gi 768003955 467 gllrhiLSQEGMRGLYRG 484
Cdd:PTZ00168 221 ------IAEEGYLTFYKG 232
EFh_PEF_CAPN13_14 cd16195
Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and ...
 23-138 3.22e-06

Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and similar proteins; CAPN13, also termed calcium-activated neutral proteinase 13 (CANP 13), a 63.6 kDa calpain large subunit that exhibits a restricted tissue distribution with low levels of expression detected only in human testis and lung. In calpain family, CAPN13 is most closely related to calpain-14 (CAPN14). CAPN14, also termed calcium-activated neutral proteinase 14 (CANP 14), is a 76.7 kDa calpain large subunit that is most highly expressed in the oesophagus. Its expression and calpain activity can be induced by IL-13. Both CAPN13 and CAPN14 contain a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain.


Pssm-ID: 320070 [Multi-domain]  Cd Length: 168  Bit Score: 47.58  E-value: 3.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  23 SNKDGRVDVHELR--------QGLARLGGG-NPDpgAQQGISSEGDADPDGGLDLEEFSRyLQEREQRLLLMFHSLDRNQ 93
Cdd:cd16195   10 ADQGGELDAEQLQkllnenllKGLAGSGGGfSLD--ACRSMVALMDLSVNGRLSLEEFSR-LWKKLRKYKDIFQKADVSK 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768003955  94 DGHIDVSEIQQSFRALGISIS-----------------------------LEQAEKILHSMDRDG-TMTIDWQEW 138
Cdd:cd16195   87 SGFLSLSELRNAIQAAGIRVSddllnlmalrygdssgrisfesficlmlrLECMAKIFRNLSKDGgGIYLTESEW 161
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 59-104 7.30e-06

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: 43.69  E-value: 7.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768003955  59 DADPDGGLDLEEFSRYLQER-----EQRLLLMFHSLDRNQDGHIDVSEIQQ 104
Cdd:cd00051   10 DKDGDGTISADELKAALKSLgeglsEEEIDEMIREVDKDGDGKIDFEEFLE 60
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 65-154 8.52e-06

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 47.68  E-value: 8.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  65 GLDLEEFSRYLQEREQRLLL-MFHSLDRNQDGHIDVSEIQQSFR---ALGISISLEQAEKILHSMDRDGTMTIDWQEWRD 140
Cdd:cd16225   18 GNEKEEFEEDSEPKKRKKLKeIFKKVDVNTDGFLSAEELEDWIMektQEHFQEAVEENEQIFKAVDTDKDGNVSWEEYRV 97

                         90
                 ....*....|....*..
gi 768003955 141 HFLL---HSLENVEDVL 154
Cdd:cd16225   98 HFLLskgYSEEEAEEKI 114
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 64-140 1.32e-05

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


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 44.44  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  64 GGLDLEEFSRYLQ------EREQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGIS-----ISLEQAEKILHSMDRDGTMT 132
Cdd:cd16252   15 GSFNYSKFFEYMQkfqtseQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSmpvapLSDEEAEAMIQAADTDGDGR 94


                 ....*...
gi 768003955 133 IDWQEWRD 140
Cdd:cd16252   95 IDFQEFSD 102
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 82-137 1.95e-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: 45.28  E-value: 1.95e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768003955  82 LLLMFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQE 137
Cdd:cd16185    2 LRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEE 57
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
16-134 3.12e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 45.83  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  16 RLFEELDSNKDGRVDVHELRQGLArlggGNPDPGAQQGIS---SEGDADPDGGLDLEEFSRYL------QEREQRLLL-- 84
Cdd:NF041410  31 QLFAKLDSDGDGSVSQDELSSALS----SKSDDGSLIDLSelfSDLDSDGDGSLSSDELAAAAppppppPDQAPSTELad 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768003955  85 -MFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSmDRDGTMTID 134
Cdd:NF041410 107 dLLSALDTDGDGSISSDELSAGLTSAGSSADSSQLFSALDS-DGDGSVSSD 156
PTZ00183 PTZ00183
centrin; Provisional
 76-140 1.08e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 43.14  E-value: 1.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768003955  76 QEREQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEWRD 140
Cdd:PTZ00183  13 EDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLD 77
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 19-132 1.81e-04

EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand calcium-binding protein RLP49, is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal His-Asp-Glu-Leu (HDEL) tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320028 [Multi-domain]  Cd Length: 268  Bit Score: 43.81  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  19 EELDSNKDGRVDVHELRQGLARLGGGNPDPGAQQgissegdadpdggldlEEFSRYLQEReqrlllmfhslDRNQDGHID 98
Cdd:cd16230  167 EDLDKNKDGYVQVEEYIADLYSGEPGEEEPAWVQ----------------TERQQFRQFR-----------DLNKDGRLD 219

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 768003955  99 VSEIQQSFRALGISISLEQAEKILH--SMDRDGTMT 132
Cdd:cd16230  220 GSEVGHWVLPPSQDQPLVEANHLLHesDTDKDGRLS 255
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 18-107 1.85e-04

EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-1, or phospholipase C-eta-1 (PLC-eta-1), or phospholipase C-like protein 3 (PLC-L3), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the zona incerta and in the spinal cord. PI-PLC-eta1 may perform a fundamental role in the brain. It may also act in synergy with other PLC subtypes. For instance, it is activated via intracellular Ca2+ mobilization and then plays a role in the amplification of GPCR (G-protein-coupled receptor)-mediated PLC-beta signals. In addition, its activity can be stimulated by ionomycin. PI-PLC-eta1 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320050 [Multi-domain]  Cd Length: 141  Bit Score: 41.93  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  18 FEELDSNKDGRVDVHELRQGLARLGGGNPDPGAQQgISSEGDADPD-GGLDLEEFSRYLQ----EREQRLLLMFHSLDRN 92
Cdd:cd16220    6 FEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQ-MFQEADTDENqGTLTFEEFCVFYKmmslRRDLYLLLLSYSDKKD 84

                         90
                 ....*....|....*
gi 768003955  93 qdgHIDVSEIQQSFR 107
Cdd:cd16220   85 ---HLTVEELAQFLK 96
EF-hand_6 pfam13405
EF-hand domain;
13-42 1.93e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 38.70  E-value: 1.93e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 768003955   13 RWGRLFEELDSNKDGRVDVHELRQGLARLG 42
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 16-135 2.47e-04

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


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 42.03  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  16 RLFEELDSnKDGRVDVHELRQGLARLGGGNPDPGAQ----QGISSEGDADPDGGLDLEEFsRYLQEREQRLLLMFHSLDR 91
Cdd:cd15897    4 NVFQAVAG-DDGEISATELQQALSNVGWTHFDLGFSletcRSMIAMMDRDHSGKLNFSEF-KGLWNYIKAWQEIFRTYDT 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 768003955  92 NQDGHIDVSEIQQSFRALGISISlEQAEKILHSMDRDGTMTIDW 135
Cdd:cd15897   82 DGSGTIDSNELRQALSGAGYRLS-EQTYDIIIRRYDRGRGNIDF 124
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 19-102 4.23e-04

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


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 42.43  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  19 EELDSNKDGRVDVHELrqgLARLGGGNPDPGAQQGISSE-------GDADPDGGLDLEEFSRYL-----QEREQRLLLMF 86
Cdd:cd15899  167 EDLDKNGDGFISLEEF---ISDPYSADENEEEPEWVKVEkerfvelRDKDKDGKLDGEELLSWVdpsnqEIALEEAKHLI 243

                         90
                 ....*....|....*.
gi 768003955  87 HSLDRNQDGHIDVSEI 102
Cdd:cd15899  244 AESDENKDGKLSPEEI 259
EF-hand_6 pfam13405
EF-hand domain;
81-110 4.77e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 37.54  E-value: 4.77e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 768003955   81 RLLLMFHSLDRNQDGHIDVSEIQQSFRALG 110
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 19-102 1.04e-03

EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins; The family corresponds to a group of six EF-hand Ca2+-binding proteins, including calumenin (also known as crocalbin or CBP-50), reticulocalbin-1 (RCN-1), reticulocalbin-3 (RCN-3), and similar proteins. Calumenin is an endo/sarcoplasmic reticulum (ER/SR) resident low-affinity Ca2+-binding protein that contains six EF-hand domains and a C-terminal SR retention signal His-Asp-Glu-Phe (HDEF) tetrapeptide. It functions as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. It is also broadly involved in haemostasis and in the pathophysiology of thrombosis. Moreover, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. RCN-1 is an endoplasmic reticulum resident Ca2+-binding protein with a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signalling cascade. It also plays a key role in the development of doxorubicin-associated resistance. RCN-3 is a putative six EF-hand Ca2+-binding protein that contains five RXXR (X is any amino acid) motifs and a C-terminal ER retrieval signal HDEL tetrapeptide. The RXXR motif represents the target sequence of subtilisin-like proprotein convertases (SPCs). RCN-3 is specifically bound to the paired basic amino-acid-cleaving enzyme-4 (PACE4) precursor protein and plays an important role in the biosynthesis of PACE4.


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 41.42  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  19 EELDSNKDGRVDVHELRQGLARLGGGNPDPG----AQQGISSEGDADPDGGLDLEEF------SRYLQEREQRLLLMFHS 88
Cdd:cd16226  163 EDIDKNKDGFISLEEYIGDMYRDDDEEEDPDwvksEREQFKEFRDKNKDGKMDREEVkdwilpEDYDHAEAEAKHLIYEA 242

                         90
                 ....*....|....
gi 768003955  89 lDRNQDGHIDVSEI 102
Cdd:cd16226  243 -DDDKDGKLTKEEI 255
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 16-139 1.08e-03

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 41.52  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  16 RLFEELDSNKDGRV------------------DVHELRQGLARLGGgnpDPGAQQGIS------SEGDADPDGGLDLEEF 71
Cdd:cd16225   77 QIFKAVDTDKDGNVsweeyrvhfllskgyseeEAEEKIKNNEELKL---DEDDKEVLDrykdrwSQADEPEDGLLDVEEF 153

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768003955  72 SRYLQEREQRLLL------MFHSLDRNQDGHIDVSEiqqsFRALGISISLEQAEKilhsmDRDgtmtiDWQEWR 139
Cdd:cd16225  154 LSFRHPEHSRGMLknmvkeILHDLDQDGDEKLTLDE----FVSLPPGTVEEQQAE-----DDD-----EWKKER 213
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 13-100 1.25e-03

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


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 40.11  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  13 RWGRLFEELDSNKDGRVDVHELRQGLArLGGGNPDPGAQQGISSEGDaDPDGGLDLEEFSRyLQEREQRLLLMFHSLDRN 92
Cdd:cd15897   71 AWQEIFRTYDTDGSGTIDSNELRQALS-GAGYRLSEQTYDIIIRRYD-RGRGNIDFDDFIQ-CCVRLQRLTDAFRRYDKD 147


                 ....*...
gi 768003955  93 QDGHIDVS 100
Cdd:cd15897  148 QDGQIQVN 155
EFh_PEF_Group_II_sorcin_like cd16181
Penta-EF hand, calcium binding motifs, found in sorcin, grancalcin, and similar proteins; The ...
 26-134 1.51e-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: 39.66  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  26 DGRVDVHELRQGLARLG-GGNPDPgaqqgISSEG--------DADPDGGLDLEEFSRYLQEREQrLLLMFHSLDRNQDGH 96
Cdd:cd16181   13 DGQIDADELQRCLTQSGiSGNYQP-----FSLETcrlmiamlDRDHSGKMGFNEFKELWAALNQ-WKTTFMQYDRDRSGT 86

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 768003955  97 IDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTID 134
Cdd:cd16181   87 VEPQELQQAIRSFGYNLSPQALNVIVKRYSKNGRITFD 124
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 67-152 1.94e-03

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


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 40.49  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  67 DLEEFSRYLQEREQ-RLLLMFHSLDRNQDGHIDVSE----IQQSFRalgiSISLEQAEKILHSMDRDGTMTIDWQEWRDH 141
Cdd:cd16224   22 DADEFAKLSPEEQQkRLKSIIKKIDTDSDGFLTEEElsswIQQSFR----HYALEDAKQQFPEYDKDGDGAVTWDEYNMQ 97

                         90
                 ....*....|.
gi 768003955 142 FLLHSLENVED 152
Cdd:cd16224   98 MYDRVIDYDED 108
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 81-137 2.13e-03

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 39.43  E-value: 2.13e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768003955  81 RLLLMFHSLDRNQDGHIDVSEIQQSFR-ALGISISLEQAEKILHSMDRDGTMTIDWQE 137
Cdd:cd16180    1 ELRRIFQAVDRDRSGRISAKELQRALSnGDWTPFSIETVRLMINMFDRDRSGTINFDE 58
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 16-41 3.20e-03

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


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 35.45  E-value: 3.20e-03
                          10        20
                  ....*....|....*....|....*.
gi 768003955   16 RLFEELDSNKDGRVDVHELRQGLARL 41
Cdd:pfam00036   4 EIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_PI-PLCeta cd16205
EF-hand motif found in phosphoinositide phospholipase C eta (PI-PLC-eta); PI-PLC-eta isozymes ...
 17-104 3.83e-03

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


Pssm-ID: 320035 [Multi-domain]  Cd Length: 141  Bit Score: 38.13  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  17 LFEELDSNKDGRVDVHELRQGLARLGGGNPDPGAQQgISSEGDADP-DGGLDLEEFSRYLQ----EREQRLLLMFHSldr 91
Cdd:cd16205    5 TFEEADKNGDGLLSIGEILQLMHKLNVNLPRRKVRQ-MFKEADTDDnQGTLDFEEFCAFYKmmstRRELYLLLLSYS--- 80

                         90
                 ....*....|...
gi 768003955  92 NQDGHIDVSEIQQ 104
Cdd:cd16205   81 NKKDYLTLEDLAR 93
EFh_PI-PLCeta2 cd16221
EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also ...
 18-104 4.82e-03

EF-hand motif found in phosphoinositide phospholipase C eta 2 (PI-PLC-eta2); PI-PLC-eta2, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2, or phosphoinositide phospholipase C-like 4, or phospholipase C-like protein 4 (PLC-L4), or phospholipase C-eta-2 (PLC-eta2), is a neuron-specific PI-PLC that is most abundant in the brain, particularly in the hippocampus, habenula, olfactory bulb, cerebellum, and throughout the cerebral cortex. It is also expressed in the pituitary gland, pineal gland, retina, and lung, as well as in neuroendocrine cells. PI-PLC-eta2 has been implicated in the regulation of neuronal differentiation/maturation. It is required for retinoic acid-stimulated neurite growth. It may also in part function downstream of G-protein-coupled receptors and play an important role in the formation and maintenance of the neuronal network in the postnatal brain. Moreover, PI-PLC-eta2 acts as a Ca2+ sensor that shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Its activation can be triggered either by intracellular calcium mobilization or by G beta-gamma signaling. PI-PLC-eta2 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, a C2 domain, and a unique C-terminal tail that terminates with a PDZ-binding motif, a potential interaction site for other signaling proteins. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. The C-terminal tail harbors a number of proline-rich motifs which may interact with SH3 (Src homology 3) domain-containing proteins, as well as many serine/threonine residues, suggesting possible regulation of interactions by protein kinases/phosphatases.


Pssm-ID: 320051 [Multi-domain]  Cd Length: 141  Bit Score: 37.99  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  18 FEELDSNKDGRVDVHELRQGLARLGGGNPDPGAQQGISSEGDADPDGGLDLEEFSRYLQ----EREQRLLLMFHSldrNQ 93
Cdd:cd16221    6 FDEADKNGDGSLSIGEVLQLLHKLNVNLPRQKVKQMFKEADTDDNQGTLGFEEFCAFYKmmstRRDLYLLMLTYS---NH 82

                         90
                 ....*....|.
gi 768003955  94 DGHIDVSEIQQ 104
Cdd:cd16221   83 KDHLDTNDLQR 93
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 16-41 5.52e-03

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 34.66  E-value: 5.52e-03
                           10        20
                   ....*....|....*....|....*.
gi 768003955    16 RLFEELDSNKDGRVDVHELRQGLARL 41
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PEF_CAPN8 cd16191
Penta-EF hand, calcium binding motifs, found in calpain-8 (CAPN8); CAPN8, also termed new ...
 12-100 6.73e-03

Penta-EF hand, calcium binding motifs, found in calpain-8 (CAPN8); CAPN8, also termed new calpain 2 (nCL-2), or stomach-specific M-type calpain, is a calpain large subunit predominantly expressed in the stomach. It appears to be involved in membrane trafficking in the gastric surface mucus cells (pit cells), via its location at the Golgi and interaction with the beta-subunit of coatomer complex (beta-COP) of vesicles derived from the Golgi. Moreover, CAPN8, together with CAPN9, forms an active protease complex, G-calpain, in which both proteins are essential for stability and activity. The G-Calpain has been implicated in gastric mucosal defense. CAPN8 exists as both a monomer and homo-oligomer, but not as a heterodimer with the conventional calpain regulatory subunit (30K). The monomer and homodimer forms predominate. CAPN8 contains 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.


Pssm-ID: 320066 [Multi-domain]  Cd Length: 168  Bit Score: 37.84  E-value: 6.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768003955  12 QRWGRLFEELDSNKDGRVDVHELRQGLaRLGGGNPDPGAQQGISSEGdADPDGGLDLEEFSRYLQeREQRLLLMFHSLDR 91
Cdd:cd16191   73 QKYLAIYKKVDSDRSGTIDAHEMRNAL-QEAGFTLNNKIQQSIVQRY-ASNKLTINFDGFIACMI-RLETLFKMFQLLDK 149


                 ....*....
gi 768003955  92 NQDGHIDVS 100
Cdd:cd16191  150 DKSGVVQLS 158
EF-hand_5 pfam13202
EF hand;
17-36 8.70e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 34.22  E-value: 8.70e-03
                          10        20
                  ....*....|....*....|
gi 768003955   17 LFEELDSNKDGRVDVHELRQ 36
Cdd:pfam13202   4 TFRQIDLNGDGKISKEELRR 23
 
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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