NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1046873789|ref|XP_017446612|]
View 

solute carrier family 25, member 54 isoform X1 [Rattus norvegicus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00169 super family cl36523
ADP/ATP transporter on adenylate translocase; Provisional
 199-451 9.23e-28

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: 112.17  E-value: 9.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 199 VAAGIASAITRTCTAPLDRLKVMIQVQSS----KMSKLR----LVHVFKQMVKEGGLFSLWRGNGVNIFKITPETAIKIG 270
Cdd:PTZ00169   12 LMGGISAAISKTAVAPIERVKMLIQTQDSipeiKSGKVPrysgIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 271 AYEQYKKLLSFEDANLGFLQRFTA----GSMAGITSQTCVYPLEVIKTRLI--LGRTG--EFSGIIDCGRKLLRREGIQA 342
Cdd:PTZ00169   92 FKDYFKNMFPKYNQKTDFWKFFGVnilsGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 343 FSRGYVPNLLSIVPYAGLDLTIFELLKNYWLEHYAESSVNPGLAIVLGCSTLShtfgQLASFPLNLVRTRMQAAMLENET 422
Cdd:PTZ00169  172 LYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNTNILYKWAVAQTVTILA----GLISYPFDTVRRRMMMMSGRKAK 247

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1046873789 423 IPMM-----QLIQEIYTKEGKKGFFRGLTPNVLK 451
Cdd:PTZ00169  248 SEIQytgtlDCWKKILKNEGLGGFFKGAWANVLR 281
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-157 4.19e-19

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 83.30  E-value: 4.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  27 LFEDLDRNGDGVVDITELRDGLEHWNssfgidpeKKILKSADSNADSGLDFGEFVKY-----LQDHEKKMKLAFKSLDKN 101
Cdd:COG5126    10 RFDLLDADGDGVLERDDFEALFRRLW--------ATLFSEADTDGDGRISREEFVAGmeslfEATVEPFARAAFDLLDTD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046873789 102 ADGVIDASEVVAAMKSLGihISLAQANDILKSMDADGSMTVDWDEWRDYF--FFHPAK 157
Cdd:COG5126    82 GDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAVrdYYTPDA 137
 
Name Accession Description Interval E-value
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 199-451 9.23e-28

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 112.17  E-value: 9.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 199 VAAGIASAITRTCTAPLDRLKVMIQVQSS----KMSKLR----LVHVFKQMVKEGGLFSLWRGNGVNIFKITPETAIKIG 270
Cdd:PTZ00169   12 LMGGISAAISKTAVAPIERVKMLIQTQDSipeiKSGKVPrysgIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 271 AYEQYKKLLSFEDANLGFLQRFTA----GSMAGITSQTCVYPLEVIKTRLI--LGRTG--EFSGIIDCGRKLLRREGIQA 342
Cdd:PTZ00169   92 FKDYFKNMFPKYNQKTDFWKFFGVnilsGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 343 FSRGYVPNLLSIVPYAGLDLTIFELLKNYWLEHYAESSVNPGLAIVLGCSTLShtfgQLASFPLNLVRTRMQAAMLENET 422
Cdd:PTZ00169  172 LYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNTNILYKWAVAQTVTILA----GLISYPFDTVRRRMMMMSGRKAK 247

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1046873789 423 IPMM-----QLIQEIYTKEGKKGFFRGLTPNVLK 451
Cdd:PTZ00169  248 SEIQytgtlDCWKKILKNEGLGGFFKGAWANVLR 281
Mito_carr pfam00153
Mitochondrial carrier protein;
194-280 3.70e-26

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 101.58  E-value: 3.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 194 WWKRLVAAGIASAITRTCTAPLDRLKVMIQVQSSKMSKLR--LVHVFKQMVKEGGLFSLWRGNGVNIFKITPETAIKIGA 271
Cdd:pfam00153   5 FLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGrgILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFGT 84


                  ....*....
gi 1046873789 272 YEQYKKLLS 280
Cdd:pfam00153  85 YETLKRLLL 93
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-157 4.19e-19

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 83.30  E-value: 4.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  27 LFEDLDRNGDGVVDITELRDGLEHWNssfgidpeKKILKSADSNADSGLDFGEFVKY-----LQDHEKKMKLAFKSLDKN 101
Cdd:COG5126    10 RFDLLDADGDGVLERDDFEALFRRLW--------ATLFSEADTDGDGRISREEFVAGmeslfEATVEPFARAAFDLLDTD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046873789 102 ADGVIDASEVVAAMKSLGihISLAQANDILKSMDADGSMTVDWDEWRDYF--FFHPAK 157
Cdd:COG5126    82 GDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAVrdYYTPDA 137
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 28-147 2.02e-14

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: 70.71  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  28 FEDLDRNGDGVVDITELRDGLEHWNSSFGIDPEKKILKSADSNADSGLDFGEFV---KYLQDhekkMKLAFKSLDKNADG 104
Cdd:cd16185     6 FRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAalhQFLSN----MQNGFEQRDTSRSG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1046873789 105 VIDASEVVAAMKSLGIHISLAQANDILKSMDADGSMTVDWDEW 147
Cdd:cd16185    82 RLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
PTZ00184 PTZ00184
calmodulin; Provisional
 17-147 1.52e-11

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 62.09  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  17 SDYDDLAFEILFEDLDRNGDGVVDITELRDGLEhwnsSFGIDPE----KKILKSADSNADSGLDFGEFVKYLQ------D 86
Cdd:PTZ00184    6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMR----SLGQNPTeaelQDMINEVDADGNGTIDFPEFLTLMArkmkdtD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046873789  87 HEKKMKLAFKSLDKNADGVIDASEVVAAMKSLGIHISLAQANDILKSMDADGSMTVDWDEW 147
Cdd:PTZ00184   82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEF 142
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
27-146 9.86e-11

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 61.62  E-value: 9.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  27 LFEDLDRNGDGVVDITELRDGL-EHWNSSFGIDpEKKILKSADSNADSGLDFGEFVKYL------QDHEKKMKLA---FK 96
Cdd:NF041410   32 LFAKLDSDGDGSVSQDELSSALsSKSDDGSLID-LSELFSDLDSDGDGSLSSDELAAAAppppppPDQAPSTELAddlLS 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1046873789  97 SLDKNADGVIDASEVVAAMKSLGihiSLAQANDILKSMDADGSMTVDWDE 146
Cdd:NF041410  111 ALDTDGDGSISSDELSAGLTSAG---SSADSSQLFSALDSDGDGSVSSDE 157
EF-hand_7 pfam13499
EF-hand domain pair;
88-151 2.15e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.02  E-value: 2.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046873789  88 EKKMKLAFKSLDKNADGVIDASEVVAAMKSLGIHISL--AQANDILKSMDADGSMTVDWDEWRDYF 151
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 90-118 5.48e-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: 34.28  E-value: 5.48e-03
                           10        20
                   ....*....|....*....|....*....
gi 1046873789   90 KMKLAFKSLDKNADGVIDASEVVAAMKSL 118
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 199-451 9.23e-28

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 112.17  E-value: 9.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 199 VAAGIASAITRTCTAPLDRLKVMIQVQSS----KMSKLR----LVHVFKQMVKEGGLFSLWRGNGVNIFKITPETAIKIG 270
Cdd:PTZ00169   12 LMGGISAAISKTAVAPIERVKMLIQTQDSipeiKSGKVPrysgIVNCFRRVSKEQGVLSLWRGNTANVIRYFPTQAFNFA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 271 AYEQYKKLLSFEDANLGFLQRFTA----GSMAGITSQTCVYPLEVIKTRLI--LGRTG--EFSGIIDCGRKLLRREGIQA 342
Cdd:PTZ00169   92 FKDYFKNMFPKYNQKTDFWKFFGVnilsGGLAGASSLLIVYPLDFARTRLAsdIGKGGdrEFTGLFDCLMKISKQTGFLS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 343 FSRGYVPNLLSIVPYAGLDLTIFELLKNYWLEHYAESSVNPGLAIVLGCSTLShtfgQLASFPLNLVRTRMQAAMLENET 422
Cdd:PTZ00169  172 LYQGFGVSVQGIIVYRGAYFGLYDSAKALLFGNDKNTNILYKWAVAQTVTILA----GLISYPFDTVRRRMMMMSGRKAK 247

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1046873789 423 IPMM-----QLIQEIYTKEGKKGFFRGLTPNVLK 451
Cdd:PTZ00169  248 SEIQytgtlDCWKKILKNEGLGGFFKGAWANVLR 281
Mito_carr pfam00153
Mitochondrial carrier protein;
194-280 3.70e-26

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 101.58  E-value: 3.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 194 WWKRLVAAGIASAITRTCTAPLDRLKVMIQVQSSKMSKLR--LVHVFKQMVKEGGLFSLWRGNGVNIFKITPETAIKIGA 271
Cdd:pfam00153   5 FLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGSGKSKGrgILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFGT 84


                  ....*....
gi 1046873789 272 YEQYKKLLS 280
Cdd:pfam00153  85 YETLKRLLL 93
Mito_carr pfam00153
Mitochondrial carrier protein;
286-376 4.08e-25

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 98.88  E-value: 4.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 286 LGFLQRFTAGSMAGITSQTCVYPLEVIKTRLILGRT---GEFSGIIDCGRKLLRREGIQAFSRGYVPNLLSIVPYAGLDL 362
Cdd:pfam00153   3 LSFLASLLAGGIAGAIAVTVTYPLDVVKTRLQVQGGsgkSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYF 82

                          90
                  ....*....|....
gi 1046873789 363 TIFELLKNYWLEHY 376
Cdd:pfam00153  83 GTYETLKRLLLKKL 96
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
27-157 4.19e-19

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 83.30  E-value: 4.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  27 LFEDLDRNGDGVVDITELRDGLEHWNssfgidpeKKILKSADSNADSGLDFGEFVKY-----LQDHEKKMKLAFKSLDKN 101
Cdd:COG5126    10 RFDLLDADGDGVLERDDFEALFRRLW--------ATLFSEADTDGDGRISREEFVAGmeslfEATVEPFARAAFDLLDTD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046873789 102 ADGVIDASEVVAAMKSLGihISLAQANDILKSMDADGSMTVDWDEWRDYF--FFHPAK 157
Cdd:COG5126    82 GDGKISADEFRRLLTALG--VSEEEADELFARLDTDGDGKISFEEFVAAVrdYYTPDA 137
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 28-147 2.02e-14

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: 70.71  E-value: 2.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  28 FEDLDRNGDGVVDITELRDGLEHWNSSFGIDPEKKILKSADSNADSGLDFGEFV---KYLQDhekkMKLAFKSLDKNADG 104
Cdd:cd16185     6 FRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEEFAalhQFLSN----MQNGFEQRDTSRSG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1046873789 105 VIDASEVVAAMKSLGIHISLAQANDILKSMDADGSMTVDWDEW 147
Cdd:cd16185    82 RLDANEVHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
Mito_carr pfam00153
Mitochondrial carrier protein;
389-471 7.02e-13

Mitochondrial carrier protein;


Pssm-ID: 395101 [Multi-domain]  Cd Length: 96  Bit Score: 64.21  E-value: 7.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 389 LGCSTLSHTFGQLASFPLNLVRTRMQA--AMLENETIPMMQLIQEIYTKEGKKGFFRGLTPNVLKLLPAVGIGCVAHELV 466
Cdd:pfam00153   9 LLAGGIAGAIAVTVTYPLDVVKTRLQVqgGSGKSKGRGILDCFKKIYKEEGIRGLYKGLLPNLLRVAPAAAIYFGTYETL 88


                  ....*
gi 1046873789 467 NLLFG 471
Cdd:pfam00153  89 KRLLL 93
PTZ00184 PTZ00184
calmodulin; Provisional
 17-147 1.52e-11

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 62.09  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  17 SDYDDLAFEILFEDLDRNGDGVVDITELRDGLEhwnsSFGIDPE----KKILKSADSNADSGLDFGEFVKYLQ------D 86
Cdd:PTZ00184    6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMR----SLGQNPTeaelQDMINEVDADGNGTIDFPEFLTLMArkmkdtD 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046873789  87 HEKKMKLAFKSLDKNADGVIDASEVVAAMKSLGIHISLAQANDILKSMDADGSMTVDWDEW 147
Cdd:PTZ00184   82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEF 142
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 27-168 2.49e-11

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: 62.06  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  27 LFEDLDrNGDGVVDITELRDGL-----EHWNSSFGIDPEKKILKSADSNADSGLDFGEFvKYLQDHEKKMKLAFKSLDKN 101
Cdd:cd15897     5 VFQAVA-GDDGEISATELQQALsnvgwTHFDLGFSLETCRSMIAMMDRDHSGKLNFSEF-KGLWNYIKAWQEIFRTYDTD 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046873789 102 ADGVIDASEVVAAMKSLGIHISlAQANDILKSMDADGSMTVDWDEWRDYFFFHPAknVTDIIRFWKH 168
Cdd:cd15897    83 GSGTIDSNELRQALSGAGYRLS-EQTYDIIIRRYDRGRGNIDFDDFIQCCVRLQR--LTDAFRRYDK 146
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 90-149 6.28e-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: 6.28e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  90 KMKLAFKSLDKNADGVIDASEVVAAMKSLGIHISLAQANDILKSMDADGSMTVDWDEWRD 149
Cdd:cd00051     1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLE 60
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
27-146 9.86e-11

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 61.62  E-value: 9.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  27 LFEDLDRNGDGVVDITELRDGL-EHWNSSFGIDpEKKILKSADSNADSGLDFGEFVKYL------QDHEKKMKLA---FK 96
Cdd:NF041410   32 LFAKLDSDGDGSVSQDELSSALsSKSDDGSLID-LSELFSDLDSDGDGSLSSDELAAAAppppppPDQAPSTELAddlLS 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1046873789  97 SLDKNADGVIDASEVVAAMKSLGihiSLAQANDILKSMDADGSMTVDWDE 146
Cdd:NF041410  111 ALDTDGDGSISSDELSAGLTSAG---SSADSSQLFSALDSDGDGSVSSDE 157
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 27-123 3.66e-08

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: 52.92  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  27 LFEDLDRNGDGVVDITELRDGLEHWN-SSFGIDPEKKILKSADSNADSGLDFGEFV---KYLQDhekkMKLAFKSLDKNA 102
Cdd:cd16180     5 IFQAVDRDRSGRISAKELQRALSNGDwTPFSIETVRLMINMFDRDRSGTINFDEFVglwKYIQD----WRRLFRRFDRDR 80

                          90       100
                  ....*....|....*....|.
gi 1046873789 103 DGVIDASEVVAAMKSLGIHIS 123
Cdd:cd16180    81 SGSIDFNELQNALSSFGYRLS 101
EF-hand_7 pfam13499
EF-hand domain pair;
88-151 2.15e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 48.02  E-value: 2.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046873789  88 EKKMKLAFKSLDKNADGVIDASEVVAAMKSLGIHISL--AQANDILKSMDADGSMTVDWDEWRDYF 151
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLsdEEVEELFKEFDLDKDGRISFEEFLELY 66
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 88-150 3.68e-07

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: 47.34  E-value: 3.68e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046873789  88 EKKMKLAFKSLDKNADGVIDASEVVAAMKSLGIhislaqandILKSMDADG-SMTVDWDEWRDY 150
Cdd:cd22949     2 EEKFREAFILFDRDGDGELTMYEAVLAMRSCGI---------PLTNDEKDAlPASMNWDQFENW 56
EFh_PEF_CPNS1_2 cd16188
Penta-EF hand, calcium binding motifs, found in calcium-dependent protease small subunit ...
 55-143 1.47e-06

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: 48.20  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  55 FGIDPEKKILKSADSNADSGLDFGEFvKYLQDHEKKMKLAFKSLDKNADGVIDASEVVAAMKSLGIHIslaqaNDILKSM 134
Cdd:cd16188    40 FGIDTCRSMVAVMDSDTTGKLGFEEF-KYLWNNIKKWQGIYKQFDTDRSGTIGSQELPGAFEAAGFHL-----NEQLYQM 113

                          90
                  ....*....|....*
gi 1046873789 135 ------DADGSMTVD 143
Cdd:cd16188   114 iirrysDEDGNMDFD 128
PTZ00183 PTZ00183
centrin; Provisional
 28-146 4.52e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 46.61  E-value: 4.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  28 FEDLDRNGDGVVDITELRDGLEhwnsSFGIDPEK----KILKSADSNADSGLDFGEFV----KYL--QDHEKKMKLAFKS 97
Cdd:PTZ00183   23 FDLFDTDGSGTIDPKELKVAMR----SLGFEPKKeeikQMIADVDKDGSGKIDFEEFLdimtKKLgeRDPREEILKAFRL 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1046873789  98 LDKNADGVIDASEVVAAMKSLGIHISLAQANDILKSMDADGSMTVDWDE 146
Cdd:PTZ00183   99 FDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEE 147
PTZ00183 PTZ00183
centrin; Provisional
 85-149 5.12e-06

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 46.61  E-value: 5.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046873789  85 QDHEKKMKLAFKSLDKNADGVIDASEVVAAMKSLGIHISLAQANDILKSMDADGSMTVDWDEWRD 149
Cdd:PTZ00183   13 EDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKDGSGKIDFEEFLD 77
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 28-85 5.70e-06

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 43.69  E-value: 5.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046873789  28 FEDLDRNGDGVVDITELRDGLEHWNSSFGIDPEKKILKSADSNADSGLDFGEFVKYLQ 85
Cdd:cd00051     6 FRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PTZ00169 PTZ00169
ADP/ATP transporter on adenylate translocase; Provisional
 283-444 9.17e-06

ADP/ATP transporter on adenylate translocase; Provisional


Pssm-ID: 240302 [Multi-domain]  Cd Length: 300  Bit Score: 47.46  E-value: 9.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 283 DANLGFLQRFTAGSMAGITSQTCVYPLEVIKTRL---------ILGRTGEFSGIIDCGRKLLRREGIQAFSRGYVPNLLS 353
Cdd:PTZ00169    2 DKKTNFATDFLMGGISAAISKTAVAPIERVKMLIqtqdsipeiKSGKVPRYSGIVNCFRRVSKEQGVLSLWRGNTANVIR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 354 IVPYAGLDLTIFELLKNYWLEHYAESSVNPGLAIVLGCSTLSHTFGQLASFPLNLVRTRMQAAMLEN---ETIPMMQLIQ 430
Cdd:PTZ00169   82 YFPTQAFNFAFKDYFKNMFPKYNQKTDFWKFFGVNILSGGLAGASSLLIVYPLDFARTRLASDIGKGgdrEFTGLFDCLM 161

                         170
                  ....*....|....
gi 1046873789 431 EIYTKEGKKGFFRG 444
Cdd:PTZ00169  162 KISKQTGFLSLYQG 175
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 28-117 9.27e-06

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


Pssm-ID: 320025 [Multi-domain]  Cd Length: 263  Bit Score: 46.93  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  28 FEDLDRNGDGVVDITElrdgleHWNSSFGIDPE--------------------KKILKSADSNADSGLDFGEFVKYLQDH 87
Cdd:cd16227    78 FEEADEDGDGKVTWEE------YLADSFGYDDEdneemikdsteddlklleddKEMFEAADLNKDGKLDKTEFSAFQHPE 151

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1046873789  88 E-KKM-----KLAFKSLDKNADGVIDASEVVAAMKS 117
Cdd:cd16227   152 EyPHMhpvliEQTLRDKDKDNDGFISFQEFLGDRAG 187
EFh_PEF_CAPN13_14 cd16195
Penta-EF hand, calcium binding motifs, found in calpain-13 (CAPN13), calpain-14 (CAPN14), and ...
 55-141 9.71e-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: 9.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  55 FGIDPEKKILKSADSNADSGLDFGEFVKyLQDHEKKMKLAFKSLDKNADGVIDASEVVAAMKSLGIHISlaqaNDILKSM 134
Cdd:cd16195    40 FSLDACRSMVALMDLSVNGRLSLEEFSR-LWKKLRKYKDIFQKADVSKSGFLSLSELRNAIQAAGIRVS----DDLLNLM 114

                          90
                  ....*....|..
gi 1046873789 135 -----DADGSMT 141
Cdd:cd16195   115 alrygDSSGRIS 126
EF-hand_7 pfam13499
EF-hand domain pair;
27-85 1.40e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 42.63  E-value: 1.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046873789  27 LFEDLDRNGDGVVDITELRDGLEHWNSSFGIDPE--KKILKSADSNADSGLDFGEFVKYLQ 85
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSDEevEELFKEFDLDKDGRISFEEFLELYS 67
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 28-145 2.52e-05

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: 44.55  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  28 FEDLDRNGDGVVDITELRDGLEHWN-SSFgiDPE--KKILKSADSNADSGLDFGEFV---KYLQDhekkMKLAFKSLDKN 101
Cdd:cd16183     6 FQRVDKDRSGQISATELQQALSNGTwTPF--NPEtvRLMIGMFDRDNSGTINFQEFAalwKYITD----WQNCFRSFDRD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1046873789 102 ADGVIDASEVVAAMKSLGIHISLAQANDILKSMDADGSMTVDWD 145
Cdd:cd16183    80 NSGNIDKNELKQALTSFGYRLSDQFYDILVRKFDRQGRGTIAFD 123
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 25-150 3.67e-05

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: 45.51  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  25 EILFEDLDRNGDGVVDITELRdGLEHwnssfgidPE----------KKILKSADSNADSGLDFGEFVKYLQDHE------ 88
Cdd:cd15899   126 KKRFEAADQDGDLILTLEEFL-AFLH--------PEespymldfviKETLEDLDKNGDGFISLEEFISDPYSADeneeep 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046873789  89 ---KKMKLAFKSL-DKNADGVIDASEVVAAMKSLGIHISLAQANDILKSMDADGSMTVDWDEWRDY 150
Cdd:cd15899   197 ewvKVEKERFVELrDKDKDGKLDGEELLSWVDPSNQEIALEEAKHLIAESDENKDGKLSPEEILDN 262
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
87-148 5.76e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.86  E-value: 5.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046873789  87 HEKKMKLAFKSLDKNADGVIDASEVVAAMkslgihisLAQANDILKSMDADGSMTVDWDEWR 148
Cdd:COG5126     3 QRRKLDRRFDLLDADGDGVLERDDFEALF--------RRLWATLFSEADTDGDGRISREEFV 56
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 25-111 1.01e-04

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: 43.84  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  25 EILFEDLDRNGDGVVDITELRDGL--EHWNSSFGIDPEKkILKSADSNADSGLDFGEFVKYLQDHEKKMKLA-----FKS 97
Cdd:cd16227   125 KEMFEAADLNKDGKLDKTEFSAFQhpEEYPHMHPVLIEQ-TLRDKDKDNDGFISFQEFLGDRAGHEDKEWLLvekdrFDE 203

                          90
                  ....*....|....*
gi 1046873789  98 -LDKNADGVIDASEV 111
Cdd:cd16227   204 dYDKDGDGKLDGEEI 218
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 88-146 5.05e-04

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: 41.92  E-value: 5.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046873789  88 EKKMKLA--FKSLDKNADGVIDASE----VVAAMKSLgihiSLAQANDILKSMDADGSMTVDWDE 146
Cdd:cd16227    33 EAKRRLAvlAKKMDLNDDGFIDRKElkawILRSFKML----DEEEANERFEEADEDGDGKVTWEE 93
EF-hand_6 pfam13405
EF-hand domain;
90-119 8.37e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.77  E-value: 8.37e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1046873789  90 KMKLAFKSLDKNADGVIDASEVVAAMKSLG 119
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 28-197 1.07e-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: 40.75  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  28 FEDLDRNGDGVVDITELRDGL-----EHWNSSfgIDPEKKILKSADSNADSGLDFGEF-VKYLQDHEKKMKLAFKSLDKN 101
Cdd:cd16225    40 FKKVDVNTDGFLSAEELEDWImektqEHFQEA--VEENEQIFKAVDTDKDGNVSWEEYrVHFLLSKGYSEEEAEEKIKNN 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 102 ADGVIDAS--EVVAAMKSlgihiSLAQANDilksmDADGSMTVdwDEWRDyfFFHPAKN-------VTDIIRfwKH---- 168
Cdd:cd16225   118 EELKLDEDdkEVLDRYKD-----RWSQADE-----PEDGLLDV--EEFLS--FRHPEHSrgmlknmVKEILH--DLdqdg 181

                         170       180       190
                  ....*....|....*....|....*....|
gi 1046873789 169 STIIDIGESVSIPDEF-TEQEKKSGEWWKR 197
Cdd:cd16225   182 DEKLTLDEFVSLPPGTvEEQQAEDDDEWKK 211
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 91-146 1.07e-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: 39.89  E-value: 1.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046873789  91 MKLAFKSLDKNADGVIDASEVVAAMKSLGIHISLAQANDILKSMDADGSMTVDWDE 146
Cdd:cd16185     2 LRQWFRAVDRDRSGSIDVNELQKALAGGGLLFSLATAEKLIRMFDRDGNGTIDFEE 57
EF-hand_7 pfam13499
EF-hand domain pair;
61-116 1.84e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.85  E-value: 1.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046873789  61 KKILKSADSNADSGLDFGEFVKYLQDHEKKMKLA-------FKSLDKNADGVIDASEVVAAMK 116
Cdd:pfam13499   5 KEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSdeeveelFKEFDLDKDGRISFEEFLELYS 67
EFh_PEF_CalpA_B cd16196
Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), ...
 36-143 2.28e-03

Penta-EF hand, calcium binding motifs, found in Drosophila melanogaster calpain-A (CalpA), calpain-B (CalpB), and similar proteins; The family contains two calpains that have been found in Drosophila, CalpA and CalpB. CalpA, also termed calcium-activated neutral proteinase A (CANP A), or calpain-A catalytic subunit, is a Drosophila calpain homolog specifically expressed in a few neurons in the central nervous system, in scattered endocrine cells in the midgut, and in blood cells. CalpB, also termed calcium-activated neutral proteinase B (CANP B), contains calpain-B catalytic subunit 1 and calpain-B catalytic subunit 2. Both CalpA and CalpB are closely related to that of vertebrate calpains, and they share similar domain architecture, which consists of four domains: the N-terminal domain I, the catalytic domain II carrying the three active site residues, Cys, His and Asn, the Ca2+-regulated phospholipid-binding domain III, and penta-EF-hand Ca2+-binding domain IV. Besides, CalpA and CalpB display some distinguishing structural features that are not found in mammalian typical calpains. CalpA harbors a 76 amino acid long hydrophobic stretch inserted in domain IV, which may be involved in membrane attachment of this enzyme. CalpB has an unusually long N-terminal tail of 224 amino acids, which belongs to the class of intrinsically unstructured proteins (IUP) and may become ordered upon binding to target protein(s). Moreover, they do not need small regulatory subunits for their catalytic activity, and their proteolytic function is not regulated by an intrinsic inhibitor as the Drosophila genome contains neither regulatory subunit nor calpastatin orthologs. As a result, they may exist as a monomer or perhaps as a homo- or heterodimer together with a second large subunit. Furthermore, both CalpA and CalpB are dispensable for viability and fertility and do not share vital functions during Drosophila development. Phosphatidylinositol 4,5-diphosphate, phosphatidylinositol 4-monophosphate, phosphatidylinositol, and phosphatidic acid can stimulate the activity and the rate of activation of CalpA, but not CalpB. Calpain A modulates Toll responses by limited Cactus/IkappaB proteolysis. CalpB directly interacts with talin, an important component of the focal adhesion complex, and functions as an important modulator in border cell migration within egg chambers, which may act via the digestion of talin. CalpB can be phosphorylated by cAMP-dependent protein kinase (protein kinase A, PKA; EC 2.7.11.11) at Ser240 and Ser845, as well as by mitogen-activated protein kinase (ERK1 and ERK2; EC 2.7.11.24) at Thr747. The activation of the ERK pathway by extracellular signals results in the phosphorylation and activation of calpain B. In Schneider cells (S2), calpain B was mainly in the cytoplasm and upon a rise in Ca2+ the enzyme adhered to intracellular membranes.


Pssm-ID: 320071 [Multi-domain]  Cd Length: 167  Bit Score: 38.72  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  36 DGVVDITELRDGLEHW------NSSFGIDPEKKILKSADSNADSGLDFGEFVKYLQDhEKKMKLAFKSLDKNADGVIDAS 109
Cdd:cd16196    13 DMEIDAYELQDILNTAfkkdfpFDGFSLDACRSMVAMMDVDRSGKLGFEEFKKLWED-LRSWKRVFKLFDTDGSGSFSSF 91

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1046873789 110 EVVAAMKSLGIHISlaqaNDILKSM-----DADGSMTVD 143
Cdd:cd16196    92 ELRNALNSAGFRLS----NATLNALvlrysNKDGRISFD 126
PTZ00168 PTZ00168
mitochondrial carrier protein; Provisional
 289-437 3.97e-03

mitochondrial carrier protein; Provisional


Pssm-ID: 185494 [Multi-domain]  Cd Length: 259  Bit Score: 39.14  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789 289 LQRFTAGSMAGITSQTCVYPLEVIKTRLILGRTGEFSGIidcgRKLLrregiqafsRGYVPNLLSIVPYAGLDLTIFELL 368
Cdd:PTZ00168    4 FHNLVTGALSGVIVDAVLYPIDSIKTNIQAKKSFSFSDI----KKLY---------SGILPTLVGTVPASAFFYCFYELS 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046873789 369 KNYwLEHYAESSVNPGLAIVlgCSTLSHTFGQLASFPLNLVRTRMQAAmlenETIPMMQLIQEIYTKEG 437
Cdd:PTZ00168   71 KKL-LTEYRENISKTNLYLI--STSIAEITACIVRLPFEIVKQNMQVS----GNISVLKTIYEITQREG 132
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 24-143 3.99e-03

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits 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 S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 37.97  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  24 FEILFEDLdRNGDGVVDITELRDGLEH-------WNSSFGIDPEKKILKSADSNADSGLDFGEFvKYLQDHEKKMKLAFK 96
Cdd:cd16182     2 VRELFEKL-AGEDEEIDAVELQKLLNAsllkdmpKFDGFSLETCRSLIALMDTNGSGRLDLEEF-KTLWSDLKKWQAIFK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1046873789  97 SLDKNADGVIDASEVVAAMKSLGIHISlaqaNDILKSM-----DADGSMTVD 143
Cdd:cd16182    80 KFDTDRSGTLSSYELRKALESAGFHLS----NKVLQALvlryaDSTGRITFE 127
PTZ00184 PTZ00184
calmodulin; Provisional
 28-84 5.24e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 37.43  E-value: 5.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046873789  28 FEDLDRNGDGVVDITELRDGLEHWNSSFGIDPEKKILKSADSNADSGLDFGEFVKYL 84
Cdd:PTZ00184   90 FKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVKMM 146
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 90-118 5.48e-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: 34.28  E-value: 5.48e-03
                           10        20
                   ....*....|....*....|....*....
gi 1046873789   90 KMKLAFKSLDKNADGVIDASEVVAAMKSL 118
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_8 pfam13833
EF-hand domain pair;
103-152 6.39e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 34.98  E-value: 6.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1046873789 103 DGVIDASEVVAAMKSLGI-HISLAQANDILKSMDADGSMTVDWDEWRDYFF 152
Cdd:pfam13833   2 KGVITREELKRALALLGLkDLSEDEVDILFREFDTDGDGYISFDEFCVLLE 52
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 90-118 8.58e-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: 33.91  E-value: 8.58e-03
                          10        20
                  ....*....|....*....|....*....
gi 1046873789  90 KMKLAFKSLDKNADGVIDASEVVAAMKSL 118
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 18-150 9.42e-03

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


Pssm-ID: 320024 [Multi-domain]  Cd Length: 264  Bit Score: 37.95  E-value: 9.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  18 DYDDLAFE-------ILFEDLDRNGDGVVDITELRDGLEHWNSSFGIDPEKKILKSADSNADSGLDFGEFVK--Y----- 83
Cdd:cd16226    24 EFDQLTPEeskerlgIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRQWKEYDPNKDGKLSWEEYKKatYgfldd 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046873789  84 ------LQDHEKKM----KLAFKSLDKNADGVIDASEVVA--------AMKslGIHISlaqanDILKSMDADGSMTVDWD 145
Cdd:cd16226   104 eeedddLHESYKKMirrdERRWKAADQDGDGKLTKEEFTAflhpeefpHMR--DIVVQ-----ETLEDIDKNKDGFISLE 176

                         170
                  ....*....|
gi 1046873789 146 E-----WRDY 150
Cdd:cd16226   177 EyigdmYRDD 186
 
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