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Conserved domains on  [gi|392920887|ref|NP_001256365|]
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EF-hand domain-containing protein [Caenorhabditis elegans]

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
 253-511 9.96e-36

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: 135.28  E-value: 9.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 253 VAGGAAGAVSRTCTAPFDRIKVYLQ-------VNSSKTNRL-GVMSCLKLLHAEGGIKSFWRGNGINVIKIAPESAIKFM 324
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQtqdsipeIKSGKVPRYsGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 325 CYDQLKRLIQKKKGNEEISTF--ERLCAGSAAGAISQSTIYPMEVMKTRLA--LRKTGQLD-RGIIHFAHKMYTKEGIRC 399
Cdd:PTZ00169  92 FKDYFKNMFPKYNQKTDFWKFfgVNILSGGLAGASSLLIVYPLDFARTRLAsdIGKGGDREfTGLFDCLMKISKQTGFLS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 400 FYKGYLPNLIGIIPYAGIDLAIYETLKRTyvrYYETNSSEPGVLALLACGTCSSTCGqLSSYPFALVRTRLQALSITRYS 479
Cdd:PTZ00169 172 LYQGFGVSVQGIIVYRGAYFGLYDSAKAL---LFGNDKNTNILYKWAVAQTVTILAG-LISYPFDTVRRRMMMMSGRKAK 247

                        250       260       270
                 ....*....|....*....|....*....|....
gi 392920887 480 P--QPDTMFGQFKYILQNEGVTGFYRGITPNFLK 511
Cdd:PTZ00169 248 SeiQYTGTLDCWKKILKNEGLGGFFKGAWANVLR 281
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
72-212 1.70e-15

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 73.29  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  72 EEKERQIRDIYDRLDIDNDGTIDIRDLTLALkhetPHIPANLApvimSKMSPDDEGRVDFYSFSSYVL-----ENEQKLA 146
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFEALF----RRLWATLF----SEADTDGDGRISREEFVAGMEslfeaTVEPFAR 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392920887 147 EMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDhkAQHIVNKMDQTGSASVDLKEFQEFMMLYPSSD 212
Cdd:COG5126   73 AAFDLLDTDGDGKISADEFRRLLTALGVSEEE--ADELFARLDTDGDGKISFEEFVAAVRDYYTPD 136
 
Name Accession Description Interval E-value
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 253-511 9.96e-36

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 135.28  E-value: 9.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 253 VAGGAAGAVSRTCTAPFDRIKVYLQ-------VNSSKTNRL-GVMSCLKLLHAEGGIKSFWRGNGINVIKIAPESAIKFM 324
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQtqdsipeIKSGKVPRYsGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 325 CYDQLKRLIQKKKGNEEISTF--ERLCAGSAAGAISQSTIYPMEVMKTRLA--LRKTGQLD-RGIIHFAHKMYTKEGIRC 399
Cdd:PTZ00169  92 FKDYFKNMFPKYNQKTDFWKFfgVNILSGGLAGASSLLIVYPLDFARTRLAsdIGKGGDREfTGLFDCLMKISKQTGFLS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 400 FYKGYLPNLIGIIPYAGIDLAIYETLKRTyvrYYETNSSEPGVLALLACGTCSSTCGqLSSYPFALVRTRLQALSITRYS 479
Cdd:PTZ00169 172 LYQGFGVSVQGIIVYRGAYFGLYDSAKAL---LFGNDKNTNILYKWAVAQTVTILAG-LISYPFDTVRRRMMMMSGRKAK 247

                        250       260       270
                 ....*....|....*....|....*....|....
gi 392920887 480 P--QPDTMFGQFKYILQNEGVTGFYRGITPNFLK 511
Cdd:PTZ00169 248 SeiQYTGTLDCWKKILKNEGLGGFFKGAWANVLR 281
Mito_carr pfam00153
Mitochondrial carrier protein;
248-337 3.03e-30

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 113.52  E-value: 3.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  248 WWRHLVAGGAAGAVSRTCTAPFDRIKVYLQVNS--SKTNRLGVMSCLKLLHAEGGIKSFWRGNGINVIKIAPESAIKFMC 325
Cdd:pfam00153   5 FLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGgsGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFGT 84

                          90
                  ....*....|..
gi 392920887  326 YDQLKRLIQKKK 337
Cdd:pfam00153  85 YETLKRLLLKKL 96
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
72-212 1.70e-15

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 73.29  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  72 EEKERQIRDIYDRLDIDNDGTIDIRDLTLALkhetPHIPANLApvimSKMSPDDEGRVDFYSFSSYVL-----ENEQKLA 146
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFEALF----RRLWATLF----SEADTDGDGRISREEFVAGMEslfeaTVEPFAR 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392920887 147 EMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDhkAQHIVNKMDQTGSASVDLKEFQEFMMLYPSSD 212
Cdd:COG5126   73 AAFDLLDTDGDGKISADEFRRLLTALGVSEEE--ADELFARLDTDGDGKISFEEFVAAVRDYYTPD 136
EF-hand_7 pfam13499
EF-hand domain pair;
142-206 2.92e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 61.89  E-value: 2.92e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392920887  142 EQKLAEMFADMDRNHDGLVDVVEMKNYCK--DIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEFMM 206
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRklEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 144-206 2.72e-10

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 56.02  E-value: 2.72e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392920887 144 KLAEMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEFMM 206
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00183 PTZ00183
centrin; Provisional
 69-205 4.25e-10

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 58.55  E-value: 4.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  69 GMSEEKERQIRDIYDRLDIDNDGTIDIRDLTLALKH-----ETPHIPAnlapvIMSKMSPDDEGRVDFYSF----SSYVL 139
Cdd:PTZ00183  10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSlgfepKKEEIKQ-----MIADVDKDGSGKIDFEEFldimTKKLG 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392920887 140 E--NEQKLAEMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEFM 205
Cdd:PTZ00183  85 ErdPREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
 
Name Accession Description Interval E-value
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 253-511 9.96e-36

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 135.28  E-value: 9.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 253 VAGGAAGAVSRTCTAPFDRIKVYLQ-------VNSSKTNRL-GVMSCLKLLHAEGGIKSFWRGNGINVIKIAPESAIKFM 324
Cdd:PTZ00169  12 LMGGISAAISKTAVAPIERVKMLIQtqdsipeIKSGKVPRYsGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 325 CYDQLKRLIQKKKGNEEISTF--ERLCAGSAAGAISQSTIYPMEVMKTRLA--LRKTGQLD-RGIIHFAHKMYTKEGIRC 399
Cdd:PTZ00169  92 FKDYFKNMFPKYNQKTDFWKFfgVNILSGGLAGASSLLIVYPLDFARTRLAsdIGKGGDREfTGLFDCLMKISKQTGFLS 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 400 FYKGYLPNLIGIIPYAGIDLAIYETLKRTyvrYYETNSSEPGVLALLACGTCSSTCGqLSSYPFALVRTRLQALSITRYS 479
Cdd:PTZ00169 172 LYQGFGVSVQGIIVYRGAYFGLYDSAKAL---LFGNDKNTNILYKWAVAQTVTILAG-LISYPFDTVRRRMMMMSGRKAK 247

                        250       260       270
                 ....*....|....*....|....*....|....
gi 392920887 480 P--QPDTMFGQFKYILQNEGVTGFYRGITPNFLK 511
Cdd:PTZ00169 248 SeiQYTGTLDCWKKILKNEGLGGFFKGAWANVLR 281
Mito_carr pfam00153
Mitochondrial carrier protein;
248-337 3.03e-30

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 113.52  E-value: 3.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  248 WWRHLVAGGAAGAVSRTCTAPFDRIKVYLQVNS--SKTNRLGVMSCLKLLHAEGGIKSFWRGNGINVIKIAPESAIKFMC 325
Cdd:pfam00153   5 FLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGgsGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFGT 84

                          90
                  ....*....|..
gi 392920887  326 YDQLKRLIQKKK 337
Cdd:pfam00153  85 YETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
340-433 8.75e-28

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 106.59  E-value: 8.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  340 EEISTFERLCAGSAAGAISQSTIYPMEVMKTRLALRKTGQLDR--GIIHFAHKMYTKEGIRCFYKGYLPNLIGIIPYAGI 417
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKgrGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*.
gi 392920887  418 DLAIYETLKRTYVRYY 433
Cdd:pfam00153  81 YFGTYETLKRLLLKKL 96
Mito_carr pfam00153
Mitochondrial carrier protein;
438-531 5.82e-22

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 90.41  E-value: 5.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  438 SEPGVLALLACGTCSSTCGQLSSYPFALVRTRLQALSITRYSPQPDtMFGQFKYILQNEGVTGFYRGITPNFLKVIPAVS 517
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRG-ILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAA 79

                          90
                  ....*....|....
gi 392920887  518 ISYVVYEKVRTGLG 531
Cdd:pfam00153  80 IYFGTYETLKRLLL 93
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
72-212 1.70e-15

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 73.29  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  72 EEKERQIRDIYDRLDIDNDGTIDIRDLTLALkhetPHIPANLApvimSKMSPDDEGRVDFYSFSSYVL-----ENEQKLA 146
Cdd:COG5126    1 DLQRRKLDRRFDLLDADGDGVLERDDFEALF----RRLWATLF----SEADTDGDGRISREEFVAGMEslfeaTVEPFAR 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392920887 147 EMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDhkAQHIVNKMDQTGSASVDLKEFQEFMMLYPSSD 212
Cdd:COG5126   73 AAFDLLDTDGDGKISADEFRRLLTALGVSEEE--ADELFARLDTDGDGKISFEEFVAAVRDYYTPD 136
EF-hand_7 pfam13499
EF-hand domain pair;
142-206 2.92e-12

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 61.89  E-value: 2.92e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392920887  142 EQKLAEMFADMDRNHDGLVDVVEMKNYCK--DIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEFMM 206
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRklEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 144-206 2.72e-10

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 56.02  E-value: 2.72e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392920887 144 KLAEMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEFMM 206
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00183 PTZ00183
centrin; Provisional
 69-205 4.25e-10

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 58.55  E-value: 4.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  69 GMSEEKERQIRDIYDRLDIDNDGTIDIRDLTLALKH-----ETPHIPAnlapvIMSKMSPDDEGRVDFYSF----SSYVL 139
Cdd:PTZ00183  10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSlgfepKKEEIKQ-----MIADVDKDGSGKIDFEEFldimTKKLG 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392920887 140 E--NEQKLAEMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEFM 205
Cdd:PTZ00183  85 ErdPREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYRIM 152
PTZ00184 PTZ00184
calmodulin; Provisional
 70-206 1.76e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 50.53  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  70 MSEEKERQIRDIYDRLDIDNDGTIDIRDLTLALKH--ETPhIPANLAPVImSKMSPDDEGRVDFYSFSSYVL------EN 141
Cdd:PTZ00184   5 LTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSlgQNP-TEAELQDMI-NEVDADGNGTIDFPEFLTLMArkmkdtDS 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392920887 142 EQKLAEMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEFMM 206
Cdd:PTZ00184  83 EEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMMM 147
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 244-409 1.88e-07

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 52.85  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 244 QEGIWWR----HLVAGGAAGAVSRTCTAPFDRIKVYLQVNSSKTNR---LGVMSCLKLLHAEGGIKSFWRGNGINVIKIA 316
Cdd:PTZ00169 105 QKTDFWKffgvNILSGGLAGASSLLIVYPLDFARTRLASDIGKGGDrefTGLFDCLMKISKQTGFLSLYQGFGVSVQGII 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 317 PESAIKFMCYDQLKRLIQKKKGNEEIsTFERLCAGS---AAGAISqstiYPMEVMKTRLAL---RKTGQ--LDRGIIHFA 388
Cdd:PTZ00169 185 VYRGAYFGLYDSAKALLFGNDKNTNI-LYKWAVAQTvtiLAGLIS----YPFDTVRRRMMMmsgRKAKSeiQYTGTLDCW 259

                        170       180
                 ....*....|....*....|.
gi 392920887 389 HKMYTKEGIRCFYKGYLPNLI 409
Cdd:PTZ00169 260 KKILKNEGLGGFFKGAWANVL 280
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
52-175 5.83e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 5.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  52 GKVTKEAAIATHSALhggMSEEKERQIRDIYDRLDIDNDGTIDIRDLTLALKhetphipanlapviMSKMSPDDegrvdf 131
Cdd:COG5126   48 GRISREEFVAGMESL---FEATVEPFARAAFDLLDTDGDGKISADEFRRLLT--------------ALGVSEEE------ 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 392920887 132 ysfssyvleneqkLAEMFADMDRNHDGLVDVVEMKNYCKDIGVP 175
Cdd:COG5126  105 -------------ADELFARLDTDGDGKISFEEFVAAVRDYYTP 135
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 250-504 2.23e-05

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 46.07  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 250 RHLVAGGAAGAVSRTCTAPFDRIKVYLQVNSSktnrlgvmsclkllHAEGGIKSFWRGNGINVIKIAPESAIKFMCYDQL 329
Cdd:PTZ00168   5 HNLVTGALSGVIVDAVLYPIDSIKTNIQAKKS--------------FSFSDIKKLYSGILPTLVGTVPASAFFYCFYELS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 330 KRLIQKKkgNEEISTFERLCAGSAAGAISQSTI-YPMEVMKTRLALRKTGQLDRGIihfaHKMYTKEGIRCFY-KGYLPN 407
Cdd:PTZ00168  71 KKLLTEY--RENISKTNLYLISTSIAEITACIVrLPFEIVKQNMQVSGNISVLKTI----YEITQREGLPSFLgKSYFVM 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 408 LIGIIPYAGIDLAIYETLKRTYVRYYETNSSE-PGVLALLACGTCSSTCGQLSSyPFALVRTRlqalsitryspqpDTMF 486
Cdd:PTZ00168 145 IVREIPFDCIQYFLWETLKEKAKKDFGKFSKKyPSITSAICGGLAGGIAGFLTT-PVDVIKSR-------------QIIY 210

                        250       260
                 ....*....|....*....|...
gi 392920887 487 GQfKYI-----LQNEGVTGFYRG 504
Cdd:PTZ00168 211 GK-SYIetvteIAEEGYLTFYKG 232
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 144-206 3.29e-05

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: 43.81  E-value: 3.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392920887 144 KLAEMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEFMM 206
Cdd:cd15898    1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYK 63
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 77-201 3.50e-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: 44.13  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  77 QIRDIYDRLDIDNDGTIDIRDLTLALKHETPHIPANLAPVIMSKMSPDDEGRVDFYSFSS--YVLENEQKLAEMFadmDR 154
Cdd:cd16185    1 ELRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAAlhQFLSNMQNGFEQR---DT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 392920887 155 NHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQTGSASVDLKEF 201
Cdd:cd16185   78 SRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 345-471 2.53e-04

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 42.99  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887 345 FERLCAGSAAGAISQSTIYPMEVMKTRLAlrktgqldrgiihfAHKMYTKEGIRCFYKGYLPNLIGIIPYAGIDLAIYET 424
Cdd:PTZ00168   4 FHNLVTGALSGVIVDAVLYPIDSIKTNIQ--------------AKKSFSFSDIKKLYSGILPTLVGTVPASAFFYCFYEL 69

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 392920887 425 LKRTYVRYYETNSSEPgvLALLACGTCSSTCGQLsSYPFALVRTRLQ 471
Cdd:PTZ00168  70 SKKLLTEYRENISKTN--LYLISTSIAEITACIV-RLPFEIVKQNMQ 113
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 77-165 2.87e-04

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 39.07  E-value: 2.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  77 QIRDIYDRLDIDNDGTIDIRDLTLALKhetphipanlapVIMSKMSpddegrvdfysfssyvlenEQKLAEMFADMDRNH 156
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALK------------SLGEGLS-------------------EEEIDEMIREVDKDG 49


                 ....*....
gi 392920887 157 DGLVDVVEM 165
Cdd:cd00051   50 DGKIDFEEF 58
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 77-206 3.22e-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: 41.11  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  77 QIRDIYDRLDIDNDGTIDIRDLTLALKHETPHIPANLAPVIMSKMSPDDEGRVDFYSFSS-YVLENEQK-LAEMFADMDR 154
Cdd:cd15898    1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEElYKSLTERPeLEPIFKKYAG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 392920887 155 NHDGLVDVVEMKNYCKDI-GVPLDDHKAQHIVNKMDQTGSAS-VDLKEFQEFMM 206
Cdd:cd15898   81 TNRDYMTLEEFIRFLREEqGENVSEEECEELIEKYEPERENRqLSFEGFTNFLL 134
EFh_PI-PLCdelta1 cd16217
EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, ...
 153-204 6.53e-04

EF-hand motif found in phosphoinositide phospholipase C delta 1 (PI-PLC-delta1); PI-PLC-delta1, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 (PLCD1), or phospholipase C-III (PLC-III), or phospholipase C-delta-1 (PLC-delta-1), is present in high abundancy in the brain, heart, lung, skeletal muscle and testis. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. PI-PLC-delta1 is required for maintenance of homeostasis in skin and metabolic tissues. Moreover, it is essential in trophoblasts for placental development. Simultaneous loss of PI-PLC-delta1 may cause placental vascular defects, leading to embryonic lethality. PI-PLC-delta1 can be positively or negatively regulated by several binding partners, including p122/Rho GTPase activating protein (RhoGAP), Gha/Transglutaminase II, RalA, and calmodulin. It is involved in Alzheimer's disease and hypertension. Furthermore, PI-PLC-delta1 regulates cell proliferation and cell-cycle progression from G1- to S-phase by control of cyclin E-CDK2 activity and p27 levels. It can be activated by alpha1-adrenoreceptors (AR) in a calcium-dependent manner and may be important for G protein-coupled receptors (GPCR) responses in vascular smooth muscle (VSM). PI-PLC-delta1 may also be involved in noradrenaline (NA)-induced phosphatidylinositol-4,5-bisphosphate (PIP2) hydrolysis and modulate sustained contraction of mesenteric small arteries. In addition, it inhibits thermogenesis and induces lipid accumulation, and therefore contributes to the development of obesity. PI-PLC-delta1 contains a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. In addition, PI-PLC-delta1 possesses a classical leucine-rich nuclear export sequence (NES) located in the EF hand motifs, as well as a nuclear localization signal within its linker region, both of which may be responsible for translocating PI-PLC-delta1 into and out of the cell nucleus.


Pssm-ID: 320047 [Multi-domain]  Cd Length: 139  Bit Score: 40.11  E-value: 6.53e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 392920887 153 DRNHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEF 204
Cdd:cd16217   10 DKNKDNKMSFKELKDFLKEINIEVDDDYAEKLFKECDKSKSGFLEGEEIEEF 61
EFh_PEF_CPNS1_2 cd16188
Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit ...
 81-162 6.57e-04

Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit CAPNS1 and CAPNS2; CAPNS1, also termed calpain small subunit 1 (CSS1), or calcium-activated neutral proteinase small subunit (CANP small subunit), or calcium-dependent protease small subunit (CDPS), or calpain regulatory subunit, is a common 28-kDa regulatory calpain subunit encoded by the calpain small 1 (Capns1, also known as Capn4) gene. It acts as a binding partner to form a heterodimer with the 80 kDa calpain large catalytic subunit and is required in maintaining the activity of calpain. CAPNS1 plays a significant role in tumor progression of human cancer, and functions as a potential therapeutic target in human hepatocellular carcinoma (HCC), nasopharyngeal carcinoma (NPC), glioma, and clear cell renal cell carcinoma (ccRCC). It may be involved in regulating migration and cell survival through binding to the SH3 domain of Ras GTPase-activating protein (RasGAP). It may also modulate Akt/FoxO3A signaling and apoptosis through PP2A. CAPNS1 contains an N-terminal glycine rich domain and a C-terminal PEF-hand domain. CAPNS2, also termed calpain small subunit 2 (CSS2), is a novel tissue-specific 30 kDa calpain small subunit that lacks two oligo-Gly stretches characteristic of the N-terminal Gly-rich domain of CAPNS1. CAPNS2 acts as a chaperone for the calpain large subunit, and appears to be the functional equivalent of CAPNS1. However, CAPNS2 binds the large subunit much more weakly than CAPNS1 and it does not undergo the autolytic conversion typical of CAPNS1.


Pssm-ID: 320063 [Multi-domain]  Cd Length: 169  Bit Score: 40.49  E-value: 6.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  81 IYDRLDIDNDGTIDIRDLTLALKHETPHIPANLAPVIMSKMSpDDEGRVDFYSFSSYVLeneqKLAEM---FADMDRNHD 157
Cdd:cd16188   78 IYKQFDTDRSGTIGSQELPGAFEAAGFHLNEQLYQMIIRRYS-DEDGNMDFDNFISCLV----RLDAMfraFKSLDKDGT 152


                 ....*
gi 392920887 158 GLVDV 162
Cdd:cd16188  153 GQIQV 157
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 77-201 7.27e-04

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


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 40.49  E-value: 7.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  77 QIRDIYDRLDIDnDGTIDIRDLTLALKHET---PHIPANLAPV--IMSKMSPDDEGRVDFYSFSsYVLENEQKLAEMFAD 151
Cdd:cd15897    1 QLRNVFQAVAGD-DGEISATELQQALSNVGwthFDLGFSLETCrsMIAMMDRDHSGKLNFSEFK-GLWNYIKAWQEIFRT 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 392920887 152 MDRNHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQtGSASVDLKEF 201
Cdd:cd15897   79 YDTDGSGTIDSNELRQALSGAGYRLSEQTYDIIIRRYDR-GRGNIDFDDF 127
EFh_PEF_CAPN1_like cd16189
Penta-EF hand, calcium binding motifs, found in mu-type calpain (CAPN1), m-type calpain (CAPN2) ...
 80-160 3.26e-03

Penta-EF hand, calcium binding motifs, found in mu-type calpain (CAPN1), m-type calpain (CAPN2), and similar proteins; The family includes mu-type calpain (CAPN1) and m-type calpain (CAPN2), both of which are ubiquitously expressed 80-kDa Ca2+-dependent intracellular cysteine proteases that contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The catalytic subunit CAPN1 or CAPN2 in complex with a regulatory subunit encoded by CAPNS1 forms a mu- or m-calpain heterodimer, respectively.


Pssm-ID: 320064 [Multi-domain]  Cd Length: 168  Bit Score: 38.49  E-value: 3.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  80 DIYDRLDIDNDGTIDIRDLTLALKHETPHIPANLAPVIMSKMSpDDEGRVDFYSFSSYVLENEQkLAEMFADMDRNHDGL 159
Cdd:cd16189   77 KIYKKFDTDGSGTMSSYEMRLALEEAGFKLNNQLHQVLVARYA-DQELTIDFDNFVRCLVRLEL-LFKIFKQLDKDNTGT 154


                 .
gi 392920887 160 V 160
Cdd:cd16189  155 I 155
EFh_PEF_CAPN12 cd16194
Penta-EF hand, calcium binding motifs, found in calpain-12 (CAPN12); CAPN12, also termed ...
 73-160 3.90e-03

Penta-EF hand, calcium binding motifs, found in calpain-12 (CAPN12); CAPN12, also termed calcium-activated neutral proteinase 12 (CANP 12), is a calpain large subunit mainly expressed in the cortex of the hair follicle. It may affect apoptosis regulation. CAPN12 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: 320069 [Multi-domain]  Cd Length: 169  Bit Score: 38.32  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392920887  73 EKERQIRDIYDRLDIDNDGTIDIRDLTLALKHETPHIPANLAPVIMSKMSpDDEGRVDFYSFSSYVleneQKLAEMF--- 149
Cdd:cd16194   70 GYLLEWQAIFTKFDEDTSGTMDSYELRLALNAAGFHLNNQLTETLTSRYR-DSRLRVDFESFLSCL----AHLTCIFcqc 144

                         90
                 ....*....|.
gi 392920887 150 ADMDRNHDGLV 160
Cdd:cd16194  145 SQHDDGGEGVI 155
 
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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