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Conserved domains on  [gi|49781263|gb|AAT68467|]
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KCHIP2 [Mus musculus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000101)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
103-210 7.59e-19

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 79.45  E-value: 7.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263 103 LFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIydmmgkytypalreEAPRE 182
Cdd:COG5126  38 LFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEE 103

                        90       100
                ....*....|....*....|....*...
gi 49781263 183 HVESFFQKMDRNKDGVVTIEEFIESCQQ 210
Cdd:COG5126 104 EADELFARLDTDGDGKISFEEFVAAVRD 131
EF-hand_8 pfam13833
EF-hand domain pair;
74-124 1.61e-04

EF-hand domain pair;


:

Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.45  E-value: 1.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 49781263    74 PSGIVNEENFKQIYSQFFPQGDSSNYATFLFNAFDTNHDGSVSFEDFVAGL 124
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
103-210 7.59e-19

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 79.45  E-value: 7.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263 103 LFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIydmmgkytypalreEAPRE 182
Cdd:COG5126  38 LFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEE 103

                        90       100
                ....*....|....*....|....*...
gi 49781263 183 HVESFFQKMDRNKDGVVTIEEFIESCQQ 210
Cdd:COG5126 104 EADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 135-206 4.36e-13

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: 61.79  E-value: 4.36e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49781263 135 RLNWAFNLYDLNKDGCITKEEMLDIMKSIYDMMgkytypalreeaPREHVESFFQKMDRNKDGVVTIEEFIE 206
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGL------------SEEEIDEMIREVDKDGDGKIDFEEFLE 60
EF-hand_7 pfam13499
EF-hand domain pair;
133-206 3.06e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 57.26  E-value: 3.06e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49781263   133 DDRLNWAFNLYDLNKDGCITKEEMLDIMKSIydmmgkytypALREEAPREHVESFFQKMDRNKDGVVTIEEFIE 206
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKL----------EEGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 103-189 1.01e-05

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 43.03  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263    103 LFNAFDTNHDGSVSFEDFVA-----GLSvilrgtiDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIYDMMGKYTYPAlre 177
Cdd:smart00027  15 IFRSLDKNQDGTVTGAQAKPillksGLP-------QTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPA--- 84

                           90
                   ....*....|..
gi 49781263    178 EAPREHVESFFQ 189
Cdd:smart00027  85 SLPPSLIPPSKR 96
PTZ00183 PTZ00183
centrin; Provisional
 139-222 3.04e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.75  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263  139 AFNLYDLNKDGCITKEEMLDIMKSiydmmgkytypaLREEAPREHVESFFQKMDRNKDGVVTIEEFIESCQQ-------D 211
Cdd:PTZ00183  22 AFDLFDTDGSGTIDPKELKVAMRS------------LGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKklgerdpR 89

                         90
                 ....*....|.
gi 49781263  212 ENIMRSMQLFD 222
Cdd:PTZ00183  90 EEILKAFRLFD 100
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
93-222 4.77e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.13  E-value: 4.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263   93 QGDSSNYATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIydmmgkyty 172
Cdd:NF041410  22 SARSQQFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPP--------- 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 49781263  173 PALREEAP-REHVESFFQKMDRNKDGVVTIEEFIESCQQDENIMRSMQLFD 222
Cdd:NF041410  93 PPPPDQAPsTELADDLLSALDTDGDGSISSDELSAGLTSAGSSADSSQLFS 143
EF-hand_8 pfam13833
EF-hand domain pair;
74-124 1.61e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.45  E-value: 1.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 49781263    74 PSGIVNEENFKQIYSQFFPQGDSSNYATFLFNAFDTNHDGSVSFEDFVAGL 124
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
103-210 7.59e-19

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 79.45  E-value: 7.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263 103 LFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIydmmgkytypalreEAPRE 182
Cdd:COG5126  38 LFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTAL--------------GVSEE 103

                        90       100
                ....*....|....*....|....*...
gi 49781263 183 HVESFFQKMDRNKDGVVTIEEFIESCQQ 210
Cdd:COG5126 104 EADELFARLDTDGDGKISFEEFVAAVRD 131
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 135-206 4.36e-13

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: 61.79  E-value: 4.36e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49781263 135 RLNWAFNLYDLNKDGCITKEEMLDIMKSIYDMMgkytypalreeaPREHVESFFQKMDRNKDGVVTIEEFIE 206
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGL------------SEEEIDEMIREVDKDGDGKIDFEEFLE 60
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 99-161 3.06e-12

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: 59.48  E-value: 3.06e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 49781263  99 YATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLNWAFNLYDLNKDGCITKEEMLDIMK 161
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
133-206 3.06e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 57.26  E-value: 3.06e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49781263   133 DDRLNWAFNLYDLNKDGCITKEEMLDIMKSIydmmgkytypALREEAPREHVESFFQKMDRNKDGVVTIEEFIE 206
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKL----------EEGEPLSDEEVEELFKEFDLDKDGRISFEEFLE 64
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
103-164 7.97e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 55.18  E-value: 7.97e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49781263 103 LFNAFDTNHDGSVSFEDFVAGLSVIlrGTIDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIY 164
Cdd:COG5126  74 AFDLLDTDGDGKISADEFRRLLTAL--GVSEEEADELFARLDTDGDGKISFEEFVAAVRDYY 133
EF-hand_7 pfam13499
EF-hand domain pair;
102-161 6.60e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 45.32  E-value: 6.60e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49781263   102 FLFNAFDTNHDGSVSFEDFVAGLSVILRG--TIDDRLNWAFNLYDLNKDGCITKEEMLDIMK 161
Cdd:pfam13499   6 EAFKLLDSDGDGYLDVEELKKLLRKLEEGepLSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 107-206 9.20e-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: 48.08  E-value: 9.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263 107 FDTNHDGSVSFEDFVAGL----SVILRGTIDDRLNwafNLYDLNKDGCITKEEMLdimksiydmmgKYTYPALrEEAPRE 182
Cdd:cd16227 168 KDKDNDGFISFQEFLGDRagheDKEWLLVEKDRFD---EDYDKDGDGKLDGEEIL-----------SWLVPDN-EEIAEE 232

                        90       100
                ....*....|....*....|....
gi 49781263 183 HVESFFQKMDRNKDGVVTIEEFIE 206
Cdd:cd16227 233 EVDHLFASADDDHDDRLSFDEILD 256
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 103-189 1.01e-05

Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe (NPF) sequences.


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 43.03  E-value: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263    103 LFNAFDTNHDGSVSFEDFVA-----GLSvilrgtiDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIYDMMGKYTYPAlre 177
Cdd:smart00027  15 IFRSLDKNQDGTVTGAQAKPillksGLP-------QTLLAKIWNLADIDNDGELDKDEFALAMHLIYRKLNGYPIPA--- 84

                           90
                   ....*....|..
gi 49781263    178 EAPREHVESFFQ 189
Cdd:smart00027  85 SLPPSLIPPSKR 96
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 104-205 1.25e-05

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: 45.00  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263 104 FNAFDTNHDGSVSFEDFVAG---------LSVILRGTIDDRLNWA-----FNLYDLNKDGCITKEEMLdimksiydmmgK 169
Cdd:cd16227  78 FEEADEDGDGKVTWEEYLADsfgyddednEEMIKDSTEDDLKLLEddkemFEAADLNKDGKLDKTEFS-----------A 146

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 49781263 170 YTYPalrEEAPREH---VESFFQKMDRNKDGVVTIEEFI 205
Cdd:cd16227 147 FQHP---EEYPHMHpvlIEQTLRDKDKDNDGFISFQEFL 182
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 136-163 1.77e-05

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: 40.44  E-value: 1.77e-05
                           10        20
                   ....*....|....*....|....*...
gi 49781263    136 LNWAFNLYDLNKDGCITKEEMLDIMKSI 163
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
PTZ00183 PTZ00183
centrin; Provisional
 139-222 3.04e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.75  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263  139 AFNLYDLNKDGCITKEEMLDIMKSiydmmgkytypaLREEAPREHVESFFQKMDRNKDGVVTIEEFIESCQQ-------D 211
Cdd:PTZ00183  22 AFDLFDTDGSGTIDPKELKVAMRS------------LGFEPKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKklgerdpR 89

                         90
                 ....*....|.
gi 49781263  212 ENIMRSMQLFD 222
Cdd:PTZ00183  90 EEILKAFRLFD 100
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 136-206 3.14e-05

EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich in cysteine (SPARC)-like proteins; The SPARC protein family represents a diverse group of proteins that share a follistatin-like (FS) domain and an extracellular calcium-binding (EC) domain with two EF-hand motifs. It includes SPARC (for secreted protein acidic and rich in cysteine, also termed osteonectin/ON, or basement-membrane protein 40/BM-40), SPARC-like protein 1 (for secreted protein, acidic and rich in cysteines-like 1/ SPARCL1, also termed high endothelial venule protein/Hevi, or MAST 9, or SC-1, or RAGS-1, or QR1, or ECM 2), testicans 1, 2, and 3 (also termed SPARC/osteonectin, CWCV, and Kazal-like domains proteoglycans, or SPOCK), secreted modular calcium-binding protein SMOC-1 (also termed SPARC-related modular calcium-binding protein 1) and SMOC-2 (also termed SPARC-related modular calcium-binding protein 2, or smooth muscle-associated protein 2/SMAP-2), follistatin-related protein 1 (FRP-1, also termed follistatin-like protein 1/fstl-1, TSC-36/Flik, TGF-beta inducible protein). The SPARC proteins have been implicated in modulating cell interaction with the extracellular milieu, including regulation of extracellular matrix assembly and deposition, counter-adhesion, effects on extracellular protease activity, and modulation of growth factor/cytokine signaling pathways, as well as in development and disease.


Pssm-ID: 320009  Cd Length: 107  Bit Score: 41.59  E-value: 3.14e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49781263 136 LNWAFNLYDLNKDGCITKEEMLDImksIYDMMgkytypalreeaPREH-VESFFQKMDRNKDGVVTIEEFIE 206
Cdd:cd00252  47 AQWEFDNLDNNKDGKLDKRELAPF---RAPLM------------PLEHcARGFFESCDLNKDKKISLQEWLG 103
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 104-205 3.50e-05

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: 43.73  E-value: 3.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263 104 FNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLNWA------------FNLYDLNKDGCITKEEMLDIMksiydmmgkyt 171
Cdd:cd16226  77 WKEYDPNKDGKLSWEEYKKATYGFLDDEEEDDDLHEsykkmirrderrWKAADQDGDGKLTKEEFTAFL----------- 145

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 49781263 172 YPalrEEAP--RE-HVESFFQKMDRNKDGVVTIEEFI 205
Cdd:cd16226 146 HP---EEFPhmRDiVVQETLEDIDKNKDGFISLEEYI 179
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 103-208 3.54e-05

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: 42.52  E-value: 3.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263 103 LFNAFDTNHDGSVSFEDFVAglsviLRGTIDDrlnW--AFNLYDLNKDGCITKEEMLDIMKSI-YDMmgkytypalreea 179
Cdd:cd16180  42 MINMFDRDRSGTINFDEFVG-----LWKYIQD---WrrLFRRFDRDRSGSIDFNELQNALSSFgYRL------------- 100

                        90       100
                ....*....|....*....|....*....
gi 49781263 180 PREHVESFFQKMDRNKDGVVTIEEFIESC 208
Cdd:cd16180 101 SPQFVQLLVRKFDRRRRGSISFDDFVEAC 129
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
93-222 4.77e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.13  E-value: 4.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263   93 QGDSSNYATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIydmmgkyty 172
Cdd:NF041410  22 SARSQQFQKQLFAKLDSDGDGSVSQDELSSALSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPP--------- 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 49781263  173 PALREEAP-REHVESFFQKMDRNKDGVVTIEEFIESCQQDENIMRSMQLFD 222
Cdd:NF041410  93 PPPPDQAPsTELADDLLSALDTDGDGSISSDELSAGLTSAGSSADSSQLFS 143
EF-hand_8 pfam13833
EF-hand domain pair;
74-124 1.61e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.45  E-value: 1.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 49781263    74 PSGIVNEENFKQIYSQFFPQGDSSNYATFLFNAFDTNHDGSVSFEDFVAGL 124
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEFCVLL 51
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 135-163 2.43e-04

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: 37.38  E-value: 2.43e-04
                          10        20
                  ....*....|....*....|....*....
gi 49781263   135 RLNWAFNLYDLNKDGCITKEEMLDIMKSI 163
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 108-206 3.29e-04

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: 40.64  E-value: 3.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263 108 DTNHDGSVSFEDFVAGLsVILRGTIDDrLNW------AFNLY-DLNKDGCITKEEMLD-IMKSIYDmmgkytyPAlREEA 179
Cdd:cd16226 166 DKNKDGFISLEEYIGDM-YRDDDEEED-PDWvksereQFKEFrDKNKDGKMDREEVKDwILPEDYD-------HA-EAEA 235

                        90       100
                ....*....|....*....|....*..
gi 49781263 180 prEHVesfFQKMDRNKDGVVTIEEFIE 206
Cdd:cd16226 236 --KHL---IYEADDDKDGKLTKEEILD 257
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 104-214 3.37e-04

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 39.57  E-value: 3.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263 104 FNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLNWAFNLYDLNKDGCITKEEMLDIMKSiydmmgkytypaLREeapREH 183
Cdd:cd15898   6 WIKADKDGDGKLSLKEIKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKS------------LTE---RPE 70

                        90       100       110
                ....*....|....*....|....*....|...
gi 49781263 184 VESFFQKMDRNKDGVVTIEEFIESCQ--QDENI 214
Cdd:cd15898  71 LEPIFKKYAGTNRDYMTLEEFIRFLReeQGENV 103
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 140-204 4.49e-04

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: 40.36  E-value: 4.49e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49781263 140 FNLYDLNKDGCITKEEMLD-IMKSIYDMMgkytypalrEEAPREHvESFFQKMDRNKDGVVTIEEF 204
Cdd:cd16225  40 FKKVDVNTDGFLSAEELEDwIMEKTQEHF---------QEAVEEN-EQIFKAVDTDKDGNVSWEEY 95
EF-hand_6 pfam13405
EF-hand domain;
135-163 5.12e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 36.39  E-value: 5.12e-04
                          10        20
                  ....*....|....*....|....*....
gi 49781263   135 RLNWAFNLYDLNKDGCITKEEMLDIMKSI 163
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 108-206 5.65e-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: 40.12  E-value: 5.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263 108 DTNHDGSVSFEDFVAglsvILRGTIDDR--LNWAF-------NLYDLNKDGCITKEEMLDimksiydmmgkYTYPALREE 178
Cdd:cd15899 170 DKNGDGFISLEEFIS----DPYSADENEeePEWVKvekerfvELRDKDKDGKLDGEELLS-----------WVDPSNQEI 234

                        90       100
                ....*....|....*....|....*...
gi 49781263 179 APREhVESFFQKMDRNKDGVVTIEEFIE 206
Cdd:cd15899 235 ALEE-AKHLIAESDENKDGKLSPEEILD 261
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 102-167 6.96e-04

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 38.79  E-value: 6.96e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 49781263 102 FLFNAFDTNHDGSVSFEDFVAGLSVILRGTIDDRLNWAFNLYDlNKDGCITKEEMLDIMKsiyDMM 167
Cdd:cd15901  58 WLLNLYDRNRTGCIRLLSVKIALITLCAASLLDKYRYLFGQLA-DSSGFISRERLTQFLQ---DLL 119
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
133-206 1.13e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.85  E-value: 1.13e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 49781263 133 DDRLNWAFNLYDLNKDGCITKEEMLDIMKSIYDMMgkytypalreeaprehvesfFQKMDRNKDGVVTIEEFIE 206
Cdd:COG5126   4 RRKLDRRFDLLDADGDGVLERDDFEALFRRLWATL--------------------FSEADTDGDGRISREEFVA 57
SPARC_Ca_bdg pfam10591
Secreted protein acidic and rich in cysteine Ca binding region; The SPARC_Ca_bdg domain of ...
 105-204 1.57e-03

Secreted protein acidic and rich in cysteine Ca binding region; The SPARC_Ca_bdg domain of Secreted Protein Acidic and Rich in Cysteine is responsible for the anti-spreading activity of human urothelial cells. It is rich in alpha-helices. This extracellular calcium-binding domain contains two EF-hands that each coordinates one Ca2+ ion, forming a helix-loop-helix structure that not only drives the conformation of the protein but is also necessary for biological activity. The anti-spreading activity was dependent on the coordination of Ca2+ by a Glu residue at the Z position of EF-hand 2.


Pssm-ID: 463162  Cd Length: 111  Bit Score: 36.94  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263   105 NAFDTNHDGSVSFEDFVAGLSVIlrgtiDDRLNWAFNLYDLNKDGCITKEEmLDIMKSIYDMMGKYTYPalreeaprehv 184
Cdd:pfam10591  29 RRERKDHSSTLEKRDESLLYPCC-----KDPLGWMFKRLDTNDDLLLDHEE-LAPIRAPLKPEEHCIKP----------- 91

                          90       100
                  ....*....|....*....|
gi 49781263   185 esFFQKMDRNKDGVVTIEEF 204
Cdd:pfam10591  92 --FFESCDANKDKLISLEEW 109
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 135-206 2.21e-03

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: 37.26  E-value: 2.21e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 49781263 135 RLNWAFNLYDLNKDGCITKEEMLDIMKSiydmmgkytypaLREEAPREHVESFFQKMDRNKDGVVTIEEFIE 206
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKEIKKLLKR------------LNIRVSEKELKKLFKEVDTNGDGTLTFDEFEE 60
EF-hand_7 pfam13499
EF-hand domain pair;
75-125 3.24e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.92  E-value: 3.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 49781263    75 SGIVNEENFKQIYSQFFPQGD-SSNYATFLFNAFDTNHDGSVSFEDFVAGLS 125
Cdd:pfam13499  16 DGYLDVEELKKLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 75-205 4.22e-03

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: 36.11  E-value: 4.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263  75 SGIVNEENFKQIYSQFFPQGDSSnYATFLFNAFDTNHDGSVSFEDFVaglSVILRGTIDDRLNWAFNLYDLNKDGCITKE 154
Cdd:cd15898  14 DGKLSLKEIKKLLKRLNIRVSEK-ELKKLFKEVDTNGDGTLTFDEFE---ELYKSLTERPELEPIFKKYAGTNRDYMTLE 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 49781263 155 EMLDIMKSIydmmgkytypaLREEAPREHVESFFQKMDRN-KDGVVTIEEFI 205
Cdd:cd15898  90 EFIRFLREE-----------QGENVSEEECEELIEKYEPErENRQLSFEGFT 130
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 99-203 4.66e-03

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 37.39  E-value: 4.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263  99 YATFLFNAFDTNHDGSVSF----------EDFVA-----GLSVILRGTIDDrlnwAFNLYDLNKDGCITKEEMLDIMKSI 163
Cdd:cd16179 142 YTDTILQLFDRNKDGKLQLsemarllpvkENFLCrpifkGAGKLTREDIDR----VFALYDRDNNGTIENEELTGFLKDL 217

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 49781263 164 YDMMGK-YTypalrEEAPREHVESFFQKMDRNKDGVVTIEE 203
Cdd:cd16179 218 LELVQEdYD-----EQDLEEFKEIILRGWDFNNDGKISRKE 253
PTZ00183 PTZ00183
centrin; Provisional
 103-221 5.91e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 36.21  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 49781263  103 LFNAFDTNHDGSVSFEDFVAGLSVILrGTIDDR--LNWAFNLYDLNKDGCITkeemLDIMKSIYDMMGKytypALREEAP 180
Cdd:PTZ00183  58 MIADVDKDGSGKIDFEEFLDIMTKKL-GERDPReeILKAFRLFDDDKTGKIS----LKNLKRVAKELGE----TITDEEL 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 49781263  181 REHVEsffqKMDRNKDGVVTIEEFIescqqdeNIMRSMQLF 221
Cdd:PTZ00183 129 QEMID----EADRNGDGEISEEEFY-------RIMKKTNLF 158
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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