NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1822620873|ref|NP_001365998|]
View 

mitochondrial adenyl nucleotide antiporter SLC25A23 isoform 4 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
223-316 1.83e-29

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 110.05  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 223 ETLHVQERFVAGSLAGATAQTIIYPMEVLKTRLTLRRT---GQYKGLLDCAKRILEREGPRAFYRGYLPNVLGIIPYAGI 299
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGsgkSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*..
gi 1822620873 300 DLAVYETLKnRWLQQYS 316
Cdd:pfam00153  81 YFGTYETLK-RLLLKKL 96
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-141 9.95e-23

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 92.93  E-value: 9.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873   8 AERRQRWGRLFEELDSNKDGRVDVHELRQGLarlgrgdpDRAQQGVSSDWDADPDGGLSLEEFTRY-----LQEREQRLL 82
Cdd:COG5126     1 DLQRRKLDRRFDLLDADGDGVLERDDFEALF--------RRLWATLFSEADTDGDGRISREEFVAGmeslfEATVEPFAR 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1822620873  83 LMFHSLDRNQDGHIDVSEIQQSFRALGisISLEQAEKILHSMDRDGTMTIDWQEWRDHF 141
Cdd:COG5126    73 AAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAV 129
Mito_carr pfam00153
Mitochondrial carrier protein;
322-412 1.29e-21

Mitochondrial carrier protein;


:

Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 88.48  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 322 PGILVLLGCGTISSTCGQIASYPLALVRTRMQAQASIEGGPQVSMVGLLRHILSQEGVWGLYRGIAPNFMKVIPAVSISY 401
Cdd:pfam00153   3 LSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYF 82

                          90
                  ....*....|.
gi 1822620873 402 VVYENMKQALG 412
Cdd:pfam00153  83 GTYETLKRLLL 93
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
223-316 1.83e-29

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 110.05  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 223 ETLHVQERFVAGSLAGATAQTIIYPMEVLKTRLTLRRT---GQYKGLLDCAKRILEREGPRAFYRGYLPNVLGIIPYAGI 299
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGsgkSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*..
gi 1822620873 300 DLAVYETLKnRWLQQYS 316
Cdd:pfam00153  81 YFGTYETLK-RLLLKKL 96
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-141 9.95e-23

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 92.93  E-value: 9.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873   8 AERRQRWGRLFEELDSNKDGRVDVHELRQGLarlgrgdpDRAQQGVSSDWDADPDGGLSLEEFTRY-----LQEREQRLL 82
Cdd:COG5126     1 DLQRRKLDRRFDLLDADGDGVLERDDFEALF--------RRLWATLFSEADTDGDGRISREEFVAGmeslfEATVEPFAR 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1822620873  83 LMFHSLDRNQDGHIDVSEIQQSFRALGisISLEQAEKILHSMDRDGTMTIDWQEWRDHF 141
Cdd:COG5126    73 AAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAV 129
Mito_carr pfam00153
Mitochondrial carrier protein;
322-412 1.29e-21

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 88.48  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 322 PGILVLLGCGTISSTCGQIASYPLALVRTRMQAQASIEGGPQVSMVGLLRHILSQEGVWGLYRGIAPNFMKVIPAVSISY 401
Cdd:pfam00153   3 LSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYF 82

                          90
                  ....*....|.
gi 1822620873 402 VVYENMKQALG 412
Cdd:pfam00153  83 GTYETLKRLLL 93
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 233-411 4.09e-18

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 84.05  E-value: 4.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 233 AGSLAGATAQTIIYPMEVLKTRLT--LRRTG--QYKGLLDCAKRILEREGPRAFYRGYLPNVLGIIPYAGIDLAVYETLK 308
Cdd:PTZ00169  119 SGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLSLYQGFGVSVQGIIVYRGAYFGLYDSAK 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 309 NRWLQQYSHESAnpgILVLLGCGTISSTCGqIASYPLALVRTRMQAQASIEGGPQVSMVG---LLRHILSQEGVWGLYRG 385
Cdd:PTZ00169  199 ALLFGNDKNTNI---LYKWAVAQTVTILAG-LISYPFDTVRRRMMMMSGRKAKSEIQYTGtldCWKKILKNEGLGGFFKG 274

                         170       180
                  ....*....|....*....|....*.
gi 1822620873 386 IAPNFMKVIPAvSISYVVYENMKQAL 411
Cdd:PTZ00169  275 AWANVLRGAGG-ALVLVFYDELQKLL 299
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 84-141 5.32e-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: 5.32e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822620873  84 MFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEWRDHF 141
Cdd:cd00051     5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EF-hand_7 pfam13499
EF-hand domain pair;
78-136 2.04e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 53.41  E-value: 2.04e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822620873  78 EQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGISISL--EQAEKILHSMDRDGTMTIDWQE 136
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEE 61
PTZ00183 PTZ00183
centrin; Provisional
 18-136 6.07e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 54.70  E-value: 6.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  18 FEELDSNKDGRVDVHELRQGLARLGRgDPDRAQ-QGVSSDWDADPDGGLSLEEF----TRYLQEREQR--LLLMFHSLDR 90
Cdd:PTZ00183   23 FDLFDTDGSGTIDPKELKVAMRSLGF-EPKKEEiKQMIADVDKDGSGKIDFEEFldimTKKLGERDPReeILKAFRLFDD 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1822620873  91 NQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQE 136
Cdd:PTZ00183  102 DKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEE 147
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 231-385 7.46e-09

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 56.70  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 231 FVAGSLAGATAQTIIYPMEVLKTRLTLRRT------GQ---YKGLLDCAKRILEREGPRAFYRGYLPNVLGIIPYAGIDL 301
Cdd:PTZ00169   11 FLMGGISAAISKTAVAPIERVKMLIQTQDSipeiksGKvprYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 302 AVYETLKNrWLQQYSHES-------ANpgilvLLGCGTISSTCGQIAsYPLALVRTRMQAQASIEGGPQVS-MVGLLRHI 373
Cdd:PTZ00169   91 AFKDYFKN-MFPKYNQKTdfwkffgVN-----ILSGGLAGASSLLIV-YPLDFARTRLASDIGKGGDREFTgLFDCLMKI 163

                         170
                  ....*....|..
gi 1822620873 374 LSQEGVWGLYRG 385
Cdd:PTZ00169  164 SKQTGFLSLYQG 175
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
16-133 3.31e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 44.67  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  16 RLFEELDSNKDGRVDVHELRQGLArlgrGDPDRAQQgVS-----SDWDADPDGGLSLEEFTRYL------QEREQRLLL- 83
Cdd:NF041410   31 QLFAKLDSDGDGSVSQDELSSALS----SKSDDGSL-IDlselfSDLDSDGDGSLSSDELAAAAppppppPDQAPSTELa 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1822620873  84 --MFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSmDRDGTMTID 133
Cdd:NF041410  106 ddLLSALDTDGDGSISSDELSAGLTSAGSSADSSQLFSALDS-DGDGSVSSD 156
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
17-75 8.92e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 40.43  E-value: 8.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1822620873  17 LFEELDSNKDGRVDVHELRQGLARLGRGDpDRAQqgVSSDWDADPDGGLSLEEFTRYLQ 75
Cdd:NF041410  108 LLSALDTDGDGSISSDELSAGLTSAGSSA-DSSQ--LFSALDSDGDGSVSSDELAAALQ 163
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 16-41 3.71e-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: 3.71e-03
                           10        20
                   ....*....|....*....|....*.
gi 1822620873   16 RLFEELDSNKDGRVDVHELRQGLARL 41
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
Mito_carr pfam00153
Mitochondrial carrier protein;
223-316 1.83e-29

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 110.05  E-value: 1.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 223 ETLHVQERFVAGSLAGATAQTIIYPMEVLKTRLTLRRT---GQYKGLLDCAKRILEREGPRAFYRGYLPNVLGIIPYAGI 299
Cdd:pfam00153   1 SELSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGsgkSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAI 80

                          90
                  ....*....|....*..
gi 1822620873 300 DLAVYETLKnRWLQQYS 316
Cdd:pfam00153  81 YFGTYETLK-RLLLKKL 96
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-141 9.95e-23

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 92.93  E-value: 9.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873   8 AERRQRWGRLFEELDSNKDGRVDVHELRQGLarlgrgdpDRAQQGVSSDWDADPDGGLSLEEFTRY-----LQEREQRLL 82
Cdd:COG5126     1 DLQRRKLDRRFDLLDADGDGVLERDDFEALF--------RRLWATLFSEADTDGDGRISREEFVAGmeslfEATVEPFAR 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1822620873  83 LMFHSLDRNQDGHIDVSEIQQSFRALGisISLEQAEKILHSMDRDGTMTIDWQEWRDHF 141
Cdd:COG5126    73 AAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAV 129
Mito_carr pfam00153
Mitochondrial carrier protein;
322-412 1.29e-21

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 88.48  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 322 PGILVLLGCGTISSTCGQIASYPLALVRTRMQAQASIEGGPQVSMVGLLRHILSQEGVWGLYRGIAPNFMKVIPAVSISY 401
Cdd:pfam00153   3 LSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYF 82

                          90
                  ....*....|.
gi 1822620873 402 VVYENMKQALG 412
Cdd:pfam00153  83 GTYETLKRLLL 93
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 233-411 4.09e-18

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 84.05  E-value: 4.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 233 AGSLAGATAQTIIYPMEVLKTRLT--LRRTG--QYKGLLDCAKRILEREGPRAFYRGYLPNVLGIIPYAGIDLAVYETLK 308
Cdd:PTZ00169  119 SGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLSLYQGFGVSVQGIIVYRGAYFGLYDSAK 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 309 NRWLQQYSHESAnpgILVLLGCGTISSTCGqIASYPLALVRTRMQAQASIEGGPQVSMVG---LLRHILSQEGVWGLYRG 385
Cdd:PTZ00169  199 ALLFGNDKNTNI---LYKWAVAQTVTILAG-LISYPFDTVRRRMMMMSGRKAKSEIQYTGtldCWKKILKNEGLGGFFKG 274

                         170       180
                  ....*....|....*....|....*.
gi 1822620873 386 IAPNFMKVIPAvSISYVVYENMKQAL 411
Cdd:PTZ00169  275 AWANVLRGAGG-ALVLVFYDELQKLL 299
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
8-106 8.42e-15

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 70.98  E-value: 8.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873   8 AERRQRWGRLFEELDSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSDWDADPDGGLSLEEFTRYLQE---REQRLLLM 84
Cdd:COG5126    29 ALFRRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAlgvSEEEADEL 108

                          90       100
                  ....*....|....*....|..
gi 1822620873  85 FHSLDRNQDGHIDVSEIQQSFR 106
Cdd:COG5126   109 FARLDTDGDGKISFEEFVAAVR 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 84-141 5.32e-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: 5.32e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822620873  84 MFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEWRDHF 141
Cdd:cd00051     5 AFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELM 62
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 12-137 7.58e-10

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: 57.22  E-value: 7.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  12 QRWgrlFEELDSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSDWDADPDGGLSLEEFT---RYLQEREQRlllmFHSL 88
Cdd:cd16185     3 RQW---FRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAalhQFLSNMQNG----FEQR 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1822620873  89 DRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEW 137
Cdd:cd16185    76 DTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
EF-hand_7 pfam13499
EF-hand domain pair;
78-136 2.04e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 53.41  E-value: 2.04e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1822620873  78 EQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGISISL--EQAEKILHSMDRDGTMTIDWQE 136
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEE 61
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 16-132 2.66e-09

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: 56.00  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  16 RLFEELDSNKDGRVDVHELRQGLarlgrgdpdraqqgVSSDW---------------DADPDGGLSLEEFT---RYLQeR 77
Cdd:cd16180     4 RIFQAVDRDRSGRISAKELQRAL--------------SNGDWtpfsietvrlminmfDRDRSGTINFDEFVglwKYIQ-D 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1822620873  78 EQRLllmFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTI 132
Cdd:cd16180    69 WRRL---FRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSI 120
EF-hand_7 pfam13499
EF-hand domain pair;
11-75 4.02e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 52.64  E-value: 4.02e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1822620873  11 RQRWGRLFEELDSNKDGRVDVHELRQGLARLGRGDPDRAQ--QGVSSDWDADPDGGLSLEEFTRYLQ 75
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEevEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00183 PTZ00183
centrin; Provisional
 18-136 6.07e-09

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 54.70  E-value: 6.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  18 FEELDSNKDGRVDVHELRQGLARLGRgDPDRAQ-QGVSSDWDADPDGGLSLEEF----TRYLQEREQR--LLLMFHSLDR 90
Cdd:PTZ00183   23 FDLFDTDGSGTIDPKELKVAMRSLGF-EPKKEEiKQMIADVDKDGSGKIDFEEFldimTKKLGERDPReeILKAFRLFDD 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1822620873  91 NQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQE 136
Cdd:PTZ00183  102 DKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEE 147
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 231-385 7.46e-09

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 56.70  E-value: 7.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 231 FVAGSLAGATAQTIIYPMEVLKTRLTLRRT------GQ---YKGLLDCAKRILEREGPRAFYRGYLPNVLGIIPYAGIDL 301
Cdd:PTZ00169   11 FLMGGISAAISKTAVAPIERVKMLIQTQDSipeiksGKvprYSGIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 302 AVYETLKNrWLQQYSHES-------ANpgilvLLGCGTISSTCGQIAsYPLALVRTRMQAQASIEGGPQVS-MVGLLRHI 373
Cdd:PTZ00169   91 AFKDYFKN-MFPKYNQKTdfwkffgVN-----ILSGGLAGASSLLIV-YPLDFARTRLASDIGKGGDREFTgLFDCLMKI 163

                         170
                  ....*....|..
gi 1822620873 374 LSQEGVWGLYRG 385
Cdd:PTZ00169  164 SKQTGFLSLYQG 175
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 231-409 2.89e-08

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 54.55  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 231 FVAGSLAGATAQTIIYPMEVLKTRLTlrrtgqykglldcAKRILEREGPRAFYRGYLPNVLGIIPYAGIDLAVYEtLKNR 310
Cdd:PTZ00168    7 LVTGALSGVIVDAVLYPIDSIKTNIQ-------------AKKSFSFSDIKKLYSGILPTLVGTVPASAFFYCFYE-LSKK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873 311 WLQQYsHESANPGILVLLGCgTISSTCGQIASYPLALVRTRMQAQASIeggpqvSMVGLLRHILSQEGVWgLYRGIAPNF 390
Cdd:PTZ00168   73 LLTEY-RENISKTNLYLIST-SIAEITACIVRLPFEIVKQNMQVSGNI------SVLKTIYEITQREGLP-SFLGKSYFV 143

                         170       180
                  ....*....|....*....|.
gi 1822620873 391 MKV--IPAVSISYVVYENMKQ 409
Cdd:PTZ00168  144 MIVreIPFDCIQYFLWETLKE 164
PTZ00184 PTZ00184
calmodulin; Provisional
 18-137 3.48e-07

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 49.37  E-value: 3.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  18 FEELDSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSDWDADPDGGLSLEEFTRYLQER------EQRLLLMFHSLDRN 91
Cdd:PTZ00184   17 FSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTLMARKmkdtdsEEEIKEAFKVFDRD 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1822620873  92 QDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEW 137
Cdd:PTZ00184   97 GNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEF 142
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 18-75 4.13e-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: 46.77  E-value: 4.13e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822620873  18 FEELDSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSDWDADPDGGLSLEEFTRYLQ 75
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
7-76 4.40e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 4.40e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873   7 DAERRQRWGRLFEELDSNKDGRVDVHELRQGLARLGrGDPDRAQQGVSSdWDADPDGGLSLEEFTRYLQE 76
Cdd:COG5126    64 EATVEPFARAAFDLLDTDGDGKISADEFRRLLTALG-VSEEEADELFAR-LDTDGDGKISFEEFVAAVRD 131
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 6-136 6.16e-07

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: 6.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873   6 SDAERRQRWGRLFEELDSNKDGRVDVHELRQGLAR-LGRGDPDRAQQGVsSDWDADPDGGLSLEEftrYLQE-------- 76
Cdd:cd16227    30 PPEEAKRRLAVLAKKMDLNDDGFIDRKELKAWILRsFKMLDEEEANERF-EEADEDGDGKVTWEE---YLADsfgydded 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  77 ----------REQRLL----LMFHSLDRNQDGHIDVSEiqqsFRA----------LGISIsleqaEKILHSMDRDGTMTI 132
Cdd:cd16227   106 neemikdsteDDLKLLeddkEMFEAADLNKDGKLDKTE----FSAfqhpeeyphmHPVLI-----EQTLRDKDKDNDGFI 176


                  ....
gi 1822620873 133 DWQE 136
Cdd:cd16227   177 SFQE 180
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 80-157 1.25e-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: 1.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822620873  80 RLLLMFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEWRDhfLLHSLENVEDVLYFWK 157
Cdd:cd15898     1 WLRRQWIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEE--LYKSLTERPELEPIFK 76
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 12-133 1.95e-06

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: 47.64  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  12 QRWgrlFEELDSNKDGRVDVHELRQGLarlgrgdpdraqqgVSSDW---------------DADPDGGLSLEEFT---RY 73
Cdd:cd16184     3 QQW---FQAVDRDRSGKISAKELQQAL--------------VNGNWshfndetcrlmigmfDKDKSGTIDIYEFQalwNY 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1822620873  74 LQEREQrlllMFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDG--TMTID 133
Cdd:cd16184    66 IQQWKQ----VFQQFDRDRSGSIDENELHQALSQMGYRLSPQFVQFLVSKYDPRArrSLTLD 123
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 67-153 2.78e-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: 48.45  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  67 LEEFTRYLQEREQRLLL-MFHSLDRNQDGHIDVSEIQQSFR---ALGISISLEQAEKILHSMDRDGTMTIDWQEWRDHFL 142
Cdd:cd16225    21 KEEFEEDSEPKKRKKLKeIFKKVDVNTDGFLSAEELEDWIMektQEHFQEAVEENEQIFKAVDTDKDGNVSWEEYRVHFL 100

                          90
                  ....*....|....
gi 1822620873 143 L---HSLENVEDVL 153
Cdd:cd16225   101 LskgYSEEEAEEKI 114
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 14-133 3.63e-06

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 46.86  E-value: 3.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  14 WGrLFEELDSNKDGRVDVHELRQGLA------------RLGRGDPDRaqqgvssdwdaDPDGGLSLEEFT---RYLQERE 78
Cdd:cd16183     3 WN-VFQRVDKDRSGQISATELQQALSngtwtpfnpetvRLMIGMFDR-----------DNSGTINFQEFAalwKYITDWQ 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1822620873  79 QrlllMFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTID 133
Cdd:cd16183    71 N----CFRSFDRDNSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIA 121
EFh_PEF_CAPN13_14 cd16195
Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and ...
 23-137 9.78e-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: 45.66  E-value: 9.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  23 SNKDGRVDVHELR--------QGLARLGRGDPDRAQQGVSSDWDADPDGGLSLEEFTRyLQEREQRLLLMFHSLDRNQDG 94
Cdd:cd16195    10 ADQGGELDAEQLQkllnenllKGLAGSGGGFSLDACRSMVALMDLSVNGRLSLEEFSR-LWKKLRKYKDIFQKADVSKSG 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822620873  95 HIDVSEIQQSFRALGISIS-----------------------------LEQAEKILHSMDRDG-TMTIDWQEW 137
Cdd:cd16195    89 FLSLSELRNAIQAAGIRVSddllnlmalrygdssgrisfesficlmlrLECMAKIFRNLSKDGgGIYLTESEW 161
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 81-136 1.70e-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: 44.90  E-value: 1.70e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1822620873  81 LLLMFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQE 136
Cdd:cd16185     2 LRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEE 57
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 63-139 2.26e-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: 43.29  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  63 GGLSLEEFTRYLQ------EREQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGIS-----ISLEQAEKILHSMDRDGTMT 131
Cdd:cd16252    15 GSFNYSKFFEYMQkfqtseQQEEAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSmpvapLSDEEAEAMIQAADTDGDGR 94


                  ....*...
gi 1822620873 132 IDWQEWRD 139
Cdd:cd16252    95 IDFQEFSD 102
EFh_PI-PLCeta1 cd16220
EF-hand motif found in phosphoinositide phospholipase C eta 1 (PI-PLC-eta1); PI-PLC-eta1, also ...
 18-106 2.39e-05

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: 43.86  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  18 FEELDSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSDWDADPD-GGLSLEEFTRYLQ----EREQRLLLMFHSLDRNq 92
Cdd:cd16220     6 FEEADKNGDGLLNIEEIYQLMHKLNVNLPRRKVRQMFQEADTDENqGTLTFEEFCVFYKmmslRRDLYLLLLSYSDKKD- 84

                          90
                  ....*....|....
gi 1822620873  93 dgHIDVSEIQQSFR 106
Cdd:cd16220    85 --HLTVEELAQFLK 96
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
16-133 3.31e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 44.67  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  16 RLFEELDSNKDGRVDVHELRQGLArlgrGDPDRAQQgVS-----SDWDADPDGGLSLEEFTRYL------QEREQRLLL- 83
Cdd:NF041410   31 QLFAKLDSDGDGSVSQDELSSALS----SKSDDGSL-IDlselfSDLDSDGDGSLSSDELAAAAppppppPDQAPSTELa 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1822620873  84 --MFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSmDRDGTMTID 133
Cdd:NF041410  106 ddLLSALDTDGDGSISSDELSAGLTSAGSSADSSQLFSALDS-DGDGSVSSD 156
PTZ00183 PTZ00183
centrin; Provisional
 75-139 6.62e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 43.14  E-value: 6.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1822620873  75 QEREQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMDRDGTMTIDWQEWRD 139
Cdd:PTZ00183   13 EDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLD 77
EF-hand_6 pfam13405
EF-hand domain;
13-42 2.00e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 38.31  E-value: 2.00e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1822620873  13 RWGRLFEELDSNKDGRVDVHELRQGLARLG 42
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 56-128 2.72e-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: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  56 DWDADPDGGLSLEEF---TRYLQEREQRLLLM------FHSL-DRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSMD 125
Cdd:cd15899   168 DLDKNGDGFISLEEFisdPYSADENEEEPEWVkvekerFVELrDKDKDGKLDGEELLSWVDPSNQEIALEEAKHLIAESD 247


                  ...
gi 1822620873 126 RDG 128
Cdd:cd15899   248 ENK 250
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 16-134 2.97e-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: 41.26  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  16 RLFEELDSnKDGRVDVHELRQGLARLGRGDPDRAQQGVS-----SDWDADPDGGLSLEEFTrYLQEREQRLLLMFHSLDR 90
Cdd:cd15897     4 NVFQAVAG-DDGEISATELQQALSNVGWTHFDLGFSLETcrsmiAMMDRDHSGKLNFSEFK-GLWNYIKAWQEIFRTYDT 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1822620873  91 NQDGHIDVSEIQQSFRALGISISlEQAEKILHSMDRDGTMTIDW 134
Cdd:cd15897    82 DGSGTIDSNELRQALSGAGYRLS-EQTYDIIIRRYDRGRGNIDF 124
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 13-99 4.02e-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: 40.88  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  13 RWGRLFEELDSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSDWDaDPDGGLSLEEFTRyLQEREQRLLLMFHSLDRNQ 92
Cdd:cd15897    71 AWQEIFRTYDTDGSGTIDSNELRQALSGAGYRLSEQTYDIIIRRYD-RGRGNIDFDDFIQ-CCVRLQRLTDAFRRYDKDQ 148


                  ....*..
gi 1822620873  93 DGHIDVS 99
Cdd:cd15897   149 DGQIQVN 155
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 19-131 4.12e-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: 41.88  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  19 EELDSNKDGRVDVHELrqgLARLGRGDPdraqqgvssdwdADPDGGLSLEEFTRYLQEReqrlllmfhslDRNQDGHIDV 98
Cdd:cd16230   167 EDLDKNKDGYVQVEEY---IADLYSGEP------------GEEEPAWVQTERQQFRQFR-----------DLNKDGRLDG 220

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1822620873  99 SEIQQSFRALGISISLEQAEKILH--SMDRDGTMT 131
Cdd:cd16230   221 SEVGHWVLPPSQDQPLVEANHLLHesDTDKDGRLS 255
EF-hand_6 pfam13405
EF-hand domain;
80-109 4.74e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 37.16  E-value: 4.74e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1822620873  80 RLLLMFHSLDRNQDGHIDVSEIQQSFRALG 109
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 3-142 5.54e-04

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 41.18  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873   3 GGSSDAERRQRWGRLFEELDSNKDGRVDVHELRQGLA------RLGRGD-PDRAQQGVSSDW---DADPDGGLSLEEFTR 72
Cdd:cd15902    35 KDKTDDEVAEKKKEFMEKYDENEDGKIEIRELANILPteenflLLFRREqPLISSVEFMKIWrkyDTDGSGFIEAKELKG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  73 YLQE---------REQRLL----LMFHSLDRNQDGHIDVSE------IQQSFRA-----LGISISLEQAEKILHSMDRDG 128
Cdd:cd15902   115 FLKDlllknkkhvSPPKLDeytkLILKEFDANKDGKLELDEmakllpVQENFLLkfqilGAMDLTKEDFEKVFEHYDKDN 194

                         170
                  ....*....|....
gi 1822620873 129 TMTIDWQEWrDHFL 142
Cdd:cd15902   195 NGVIEGNEL-DALL 207
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
17-75 8.92e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 40.43  E-value: 8.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1822620873  17 LFEELDSNKDGRVDVHELRQGLARLGRGDpDRAQqgVSSDWDADPDGGLSLEEFTRYLQ 75
Cdd:NF041410  108 LLSALDTDGDGSISSDELSAGLTSAGSSA-DSSQ--LFSALDSDGDGSVSSDELAAALQ 163
EFh_PEF_CPNS1_2 cd16188
Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit ...
 16-133 9.12e-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: 39.72  E-value: 9.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  16 RLFEELdSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSD--------WDADPDGGLSLEEFtRYLQEREQRLLLMFHS 87
Cdd:cd16188     4 RLFVQL-AGDDMEVSATELMNILNKVVTRHPDLKTDGFGIDtcrsmvavMDSDTTGKLGFEEF-KYLWNNIKKWQGIYKQ 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1822620873  88 LDRNQDGHIDVSEIQQSFRALGISISLEQAEKILHSM-DRDGTMTID 133
Cdd:cd16188    82 FDTDRSGTIGSQELPGAFEAAGFHLNEQLYQMIIRRYsDEDGNMDFD 128
EFh_PEF_CAPN8 cd16191
Penta-EF hand, calcium binding motifs, found in calpain-8 (CAPN8); CAPN8, also termed new ...
 12-99 1.38e-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: 39.38  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  12 QRWGRLFEELDSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSDWdADPDGGLSLEEFTRYLQeREQRLLLMFHSLDRN 91
Cdd:cd16191    73 QKYLAIYKKVDSDRSGTIDAHEMRNALQEAGFTLNNKIQQSIVQRY-ASNKLTINFDGFIACMI-RLETLFKMFQLLDKD 150


                  ....*...
gi 1822620873  92 QDGHIDVS 99
Cdd:cd16191   151 KSGVVQLS 158
EFh_CREC_RCN3 cd16230
EF-hand, calcium binding motif, found in reticulocalbin-3 (RCN-3); RCN-3, also termed EF-hand ...
 10-100 1.67e-03

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: 39.96  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  10 RRQRWGRLFEELDSNKDGRVDVHELRQ--------GLARLGRGDPDRAQQGVSSD------WDADPDGGLSLEEFTRYLQ 75
Cdd:cd16230    71 IRDSVSAAWQTYDTDRDGRVGWEELRNatyghyepGEEFHDVEDAETYKKMLARDerrfrvADQDGDSMATREELTAFLH 150

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1822620873  76 ERE---QRLLLM---FHSLDRNQDGHIDVSE 100
Cdd:cd16230   151 PEEfphMRDIVVaetLEDLDKNKDGYVQVEE 181
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 16-138 1.81e-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: 39.98  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  16 RLFEELDSNKDGRV------------------DVHELRQGLARLGrGDPDrAQQGVSSD---W-DADP--DGGLSLEEFT 71
Cdd:cd16225    77 QIFKAVDTDKDGNVsweeyrvhfllskgyseeEAEEKIKNNEELK-LDED-DKEVLDRYkdrWsQADEpeDGLLDVEEFL 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822620873  72 RYLQEREQRLLL------MFHSLDRNQDGHIDVSEiqqsFRALGISISLEQAEKilhsmDRDgtmtiDWQEWR 138
Cdd:cd16225   155 SFRHPEHSRGMLknmvkeILHDLDQDGDEKLTLDE----FVSLPPGTVEEQQAE-----DDD-----EWKKER 213
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 12-99 1.99e-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: 38.66  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  12 QRWGRLFEELDSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSDWDADPDGGLSLEEFTR---YLqereQRLLLMFHSL 88
Cdd:cd16180    67 QDWRRLFRRFDRDRSGSIDFNELQNALSSFGYRLSPQFVQLLVRKFDRRRRGSISFDDFVEacvTL----KRLTDAFRKY 142

                          90
                  ....*....|.
gi 1822620873  89 DRNQDGHIDVS 99
Cdd:cd16180   143 DTNRTGYATIS 153
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 16-41 2.15e-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: 2.15e-03
                          10        20
                  ....*....|....*....|....*.
gi 1822620873  16 RLFEELDSNKDGRVDVHELRQGLARL 41
Cdd:pfam00036   4 EIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 19-101 2.21e-03

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: 39.73  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  19 EELDSNKDGRVDVHELrqgLARLGRGDPDRAQQG--------VSSDWDADPDGGLSLEEFTRYL-----QEREQRLLLMF 85
Cdd:cd15899   167 EDLDKNGDGFISLEEF---ISDPYSADENEEEPEwvkvekerFVELRDKDKDGKLDGEELLSWVdpsnqEIALEEAKHLI 243

                          90
                  ....*....|....*.
gi 1822620873  86 HSLDRNQDGHIDVSEI 101
Cdd:cd15899   244 AESDENKDGKLSPEEI 259
EFh_HEF_CR cd16177
EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is ...
 5-136 2.23e-03

EF-hand, calcium binding motif, found in calretinin (CR); CR, also termed 29 kDa calbindin, is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t specific neurons of the central and peripheral nervous system. It possibly functions as a calcium buffer, calcium sensor, and apoptosis regulator, which may be implicated in many biological processes, including cell proliferation, differentiation, and cell death. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. CR I-II consists of EF-hand motifs 1 and 2, and CR III-VI consists of EF-hand motifs 3-6. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. Thus, CR has two pairs of cooperative binding sites (I-II and III-IV), which display high affinity calcium-binding sites, and one independent calcium ion-binding site (V), which displays lower affinity binding.


Pssm-ID: 320077 [Multi-domain]  Cd Length: 248  Bit Score: 39.47  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873   5 SSDAERRQRWGRLFEELDSNKDGRVDVHELRQGLARlgrgDPD-----RAQQGVSSD-------WDADPDGGLSLEEFTR 72
Cdd:cd16177    39 SKSANFGEKMKEFMQKYDKNADGRIEMAELAQILPT----EENfllcfRQHVGSSSEfmeawrkYDTDRSGYIEANELKG 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  73 Y----------------LQEREQRLLLMFhslDRNQDGHIDVSE------IQQSF--RALGISISLEQAEKILHSMDRDG 128
Cdd:cd16177   115 FlsdllkkanrpydekkLQEYTQTILRMF---DLNGDGKLGLSEmarllpVQENFllKFQGMKLSSEEFNAIFAFYDKDG 191


                  ....*...
gi 1822620873 129 TMTIDWQE 136
Cdd:cd16177   192 SGYIDENE 199
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 80-136 2.29e-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: 38.66  E-value: 2.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1822620873  80 RLLLMFHSLDRNQDGHIDVSEIQQSFR-ALGISISLEQAEKILHSMDRDGTMTIDWQE 136
Cdd:cd16180     1 ELRRIFQAVDRDRSGRISAKELQRALSnGDWTPFSIETVRLMINMFDRDRSGTINFDE 58
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 68-187 2.35e-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: 39.34  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  68 EEFTRYLQEREQ-RLLLMFHSLDRNQDGHIDVSE----IQQSFRalgiSISLEQAEKILHSMDRDGTMTIDWQEWRDHFl 142
Cdd:cd16224    24 DEFAKLSPEEQQkRLKSIIKKIDTDSDGFLTEEElsswIQQSFR----HYALEDAKQQFPEYDKDGDGAVTWDEYNMQM- 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1822620873 143 lhslenvedvlyfwkHSTVLDIGEClTVPDEfSQEEKLTGMWWKQ 187
Cdd:cd16224    99 ---------------YDRVIDYDED-TVLDD-EEEESFRQLHLKD 126
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 18-99 3.36e-03

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: 37.96  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  18 FEELDSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSDWDADPDGGLSLEEFTR---YLQE-REQrlllmFHSLDRNQD 93
Cdd:cd16185    72 FEQRDTSRSGRLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDYIElciFLASaRNL-----FQAFDRQRT 146


                  ....*.
gi 1822620873  94 GHIDVS 99
Cdd:cd16185   147 GRVTLD 152
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 78-139 3.48e-03

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 35.79  E-value: 3.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1822620873  78 EQRLLLMFHSLDRNQDGHIDVSEIQQSFRALGIsisleqaekILHSMDRDG-TMTIDWQEWRD 139
Cdd:cd22949     2 EEKFREAFILFDRDGDGELTMYEAVLAMRSCGI---------PLTNDEKDAlPASMNWDQFEN 55
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 16-41 3.71e-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: 3.71e-03
                           10        20
                   ....*....|....*....|....*.
gi 1822620873   16 RLFEELDSNKDGRVDVHELRQGLARL 41
Cdd:smart00054   4 EAFRLFDKDGDGKIDFEEFKDLLKAL 29
EFh_PEF_CAPN11 cd16193
Penta-EF hand, calcium binding motifs, found in calpain-11 (CAPN11); CAPN11, also termed ...
 17-142 5.02e-03

Penta-EF hand, calcium binding motifs, found in calpain-11 (CAPN11); CAPN11, also termed calcium-activated neutral proteinase 11 (CANP 11), is a mammalian orthologue of micro/m calpain. It is one of the calpain large subunits that appears to be exclusively expressed in certain cells of the testis. It may be involved in regulating calcium-dependent signal transduction events during meiosis and sperm functional processes. CAPN11 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: 320068 [Multi-domain]  Cd Length: 169  Bit Score: 37.59  E-value: 5.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  17 LFEELdSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSD--------WDADPDGGLSLEEFtRYLQEREQRLLLMFHSL 88
Cdd:cd16193     5 LFKIV-ANEDKEVDMYELQKLLNRMAIKFKSFKTKGFSLDvcrrminlMDKDGSGKLGLHEF-KILWKKIKKWMEIFKEC 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1822620873  89 DRNQDGHIDVSEIQQSFRALGISISlEQAEKILHSMDRDGTMTIDWQEWRDHFL 142
Cdd:cd16193    83 DQDRSGNLNSYEMRLAIEKAGIKMN-NRVTEVVVARYADDNMIVDFDSFINCFL 135
EFh_PEF_CAPN1 cd16198
Penta-EF hand, calcium binding motifs, found in mu-type calpain (CAPN1); CAPN1, also termed ...
 10-96 6.88e-03

Penta-EF hand, calcium binding motifs, found in mu-type calpain (CAPN1); CAPN1, also termed calpain-1 80-kDa catalytic subunit, or calpain-1 large subunit, or micromolar-calpain (muCANP), or calcium-activated neutral proteinase 1 (CANP 1), or cell proliferation-inducing gene 30 protein, is a ubiquitously expressed 80-kDa Ca2+-dependent intracellular cysteine protease that 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. The catalytic subunit CAPN1 in complex with a regulatory subunit encoded by CAPNS1 forms a mu-calpain heterodimer. CAPN1 plays a central role in postmortem proteolysis and meat tenderization processes, as well as in regulation of proliferation and survival of skeletal satellite cells. It also acts as a novel regulator in IgE-mediated mast cell activation and could serve as a potential therapeutic target for the management of allergic inflammation. Moreover, CAPN1 is involved in neutrophil motility and functions as a potential target for intervention in inflammatory disease. It also facilitates age-associated aortic wall calcification and fibrosis through the regulation of matrix metalloproteinase 2 activity in vascular smooth muscle cells, and thus plays a role in hypertension and atherosclerosis. The proteolytic cleavage of beta-amyloid precursor protein and tau protein by CAPN1 may be involved in plaque formation. Furthermore, CAPN1 is activated in the brains of individuals with Alzheimer's disease. It is involved in the maintenance of a proliferative neural stem cell pool. The activation and macrophage inflammation of CAPN1 in hypercholesterolemic nephropathy is promoted by nicotinic acetylcholine receptor alpha1 (nAChRalpha1). In addition, CAPN1 displays a functional role in hemostasis, as well as in sickle cell disease.


Pssm-ID: 320073 [Multi-domain]  Cd Length: 169  Bit Score: 37.09  E-value: 6.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822620873  10 RRQRWGRLFEELDSNKDGRVDVHELRQGLARLGRGDPDRAQQGVSSDWdADPDGGLSLEEFTRYLQEREQrLLLMFHSLD 89
Cdd:cd16198    71 KIRNYLTIFRKFDLDKSGSMSAYEMRLALESAGFKLNNRLHQVIVARY-ADPNLAIDFDNFVCCLVRLET-MFRFFKQLD 148


                  ....*..
gi 1822620873  90 RNQDGHI 96
Cdd:cd16198   149 TEETGTI 155
EF-hand_5 pfam13202
EF hand;
17-36 9.86e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.45  E-value: 9.86e-03
                          10        20
                  ....*....|....*....|
gi 1822620873  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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH