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Conserved domains on  [gi|71991483|ref|NP_493711|]
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EF-hand domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EFh_CREC super family cl25354
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 231-390 2.08e-12

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.


The actual alignment was detected with superfamily member cd16226:

Pssm-ID: 330175 [Multi-domain]  Cd Length: 264  Bit Score: 67.61  E-value: 2.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 231 MVGSVDENMDGELNAPEFADFERIIRARAI-ENSKKAMRVVDADNSGTLTLDEAKRVafeHYGFDEATLAPF-------- 301
Cdd:cd16226  40 IVDKIDKNGDGFVTEEELKDWIKYVQKKYIrEDVDRQWKEYDPNKDGKLSWEEYKKA---TYGFLDDEEEDDdlhesykk 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 302 --------FGQADENEDGQLDNVEFAGF---RSVIRARS--VRDAMDKmkrIDTNGDGLVSNAE------ATDSTKKEDD 362
Cdd:cd16226 117 mirrderrWKAADQDGDGKLTKEEFTAFlhpEEFPHMRDivVQETLED---IDKNKDGFISLEEyigdmyRDDDEEEDPD 193

                       170       180
                ....*....|....*....|....*...
gi 71991483 363 MDSEETLALFNIADQNKSGKLDKVELAD 390
Cdd:cd16226 194 WVKSEREQFKEFRDKNKDGKMDREEVKD 221
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
331-463 1.82e-09

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.34  E-value: 1.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 331 RDAMDKMKRIDTNGDGLVSNAEATDstkkeddMDSEETLALFNIADQNKSGKLDKVEL-ADFNRLVRLSSIKFATDHFKE 409
Cdd:COG5126   5 RKLDRRFDLLDADGDGVLERDDFEA-------LFRRLWATLFSEADTDGDGRISREEFvAGMESLFEATVEPFARAAFDL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 71991483 410 FDLDGNDAVTFDEIALLIEQkYGIPRSMIKTFFDRIDVDGSGDLMPAEIVDFRH 463
Cdd:COG5126  78 LDTDGDGKISADEFRRLLTA-LGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
EFh_SPARC_EC super family cl25349
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 92-142 2.56e-07

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.


The actual alignment was detected with superfamily member cd00252:

Pssm-ID: 330171  Cd Length: 107  Bit Score: 49.29  E-value: 2.56e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71991483  92 FKQVDTNRDNVLDAREFDAIRmLVLEKAENAALRYLQNVDTDRDGLLSLQE 142
Cdd:cd00252  51 FDNLDNNKDGKLDKRELAPFR-APLMPLEHCARGFFESCDLNKDKKISLQE 100
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
88-215 3.08e-07

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.79  E-value: 3.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  88 VEDLFKQVDTNRDNVLDAREFDAIRMLVLEKAENAAlrylqnvDTDRDGLLSLQEAQIYLLREYGIGYHDVARLW-KLVP 166
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEA-------DTDGDGRISREEFVAGMESLFEATVEPFARAAfDLLD 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71991483 167 ADLSDRMNSTLFSKLRRrVRGMTIRLARQIMKNADLNGDGHISVDEAQA 215
Cdd:COG5126  80 TDGDGKISADEFRRLLT-ALGVSEEEADELFARLDTDGDGKISFEEFVA 127
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
60-110 6.20e-05

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 6.20e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71991483  60 VDVNEDGVLDIDEIRyAAFVHHGLSASVVEDLFKQVDTNRDNVLDAREFDA 110
Cdd:COG5126  78 LDTDGDGKISADEFR-RLLTALGVSEEEADELFARLDTDGDGKISFEEFVA 127
 
Name Accession Description Interval E-value
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 231-390 2.08e-12

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: 67.61  E-value: 2.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 231 MVGSVDENMDGELNAPEFADFERIIRARAI-ENSKKAMRVVDADNSGTLTLDEAKRVafeHYGFDEATLAPF-------- 301
Cdd:cd16226  40 IVDKIDKNGDGFVTEEELKDWIKYVQKKYIrEDVDRQWKEYDPNKDGKLSWEEYKKA---TYGFLDDEEEDDdlhesykk 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 302 --------FGQADENEDGQLDNVEFAGF---RSVIRARS--VRDAMDKmkrIDTNGDGLVSNAE------ATDSTKKEDD 362
Cdd:cd16226 117 mirrderrWKAADQDGDGKLTKEEFTAFlhpEEFPHMRDivVQETLED---IDKNKDGFISLEEyigdmyRDDDEEEDPD 193

                       170       180
                ....*....|....*....|....*...
gi 71991483 363 MDSEETLALFNIADQNKSGKLDKVELAD 390
Cdd:cd16226 194 WVKSEREQFKEFRDKNKDGKMDREEVKD 221
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
201-319 4.13e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 60.96  E-value: 4.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 201 DLNGDGHISVDEAQAIAfeqegigAGDVASMVGSVDENMDGELNAPEFADFERIIRARAIENS-KKAMRVVDADNSGTLT 279
Cdd:COG5126  15 DADGDGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFaRAAFDLLDTDGDGKIS 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 71991483 280 LDEAKRvAFEHYGFDEATLAPFFGQADENEDGQLDNVEFA 319
Cdd:COG5126  88 ADEFRR-LLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
331-463 1.82e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.34  E-value: 1.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 331 RDAMDKMKRIDTNGDGLVSNAEATDstkkeddMDSEETLALFNIADQNKSGKLDKVEL-ADFNRLVRLSSIKFATDHFKE 409
Cdd:COG5126   5 RKLDRRFDLLDADGDGVLERDDFEA-------LFRRLWATLFSEADTDGDGRISREEFvAGMESLFEATVEPFARAAFDL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 71991483 410 FDLDGNDAVTFDEIALLIEQkYGIPRSMIKTFFDRIDVDGSGDLMPAEIVDFRH 463
Cdd:COG5126  78 LDTDGDGKISADEFRRLLTA-LGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 92-142 2.56e-07

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: 49.29  E-value: 2.56e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71991483  92 FKQVDTNRDNVLDAREFDAIRmLVLEKAENAALRYLQNVDTDRDGLLSLQE 142
Cdd:cd00252  51 FDNLDNNKDGKLDKRELAPFR-APLMPLEHCARGFFESCDLNKDKKISLQE 100
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
88-215 3.08e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.79  E-value: 3.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  88 VEDLFKQVDTNRDNVLDAREFDAIRMLVLEKAENAAlrylqnvDTDRDGLLSLQEAQIYLLREYGIGYHDVARLW-KLVP 166
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEA-------DTDGDGRISREEFVAGMESLFEATVEPFARAAfDLLD 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71991483 167 ADLSDRMNSTLFSKLRRrVRGMTIRLARQIMKNADLNGDGHISVDEAQA 215
Cdd:COG5126  80 TDGDGKISADEFRRLLT-ALGVSEEEADELFARLDTDGDGKISFEEFVA 127
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 405-465 4.58e-06

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 46.45  E-value: 4.58e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71991483 405 DHFKEFDLDGNDAVTFDEI-ALLIEQKYGIPRSMIKTFFDRIDVDGSGDLMPAEIVDFRHLI 465
Cdd:cd16202   4 DQFRKADKNGDGKLSFKECkKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQFYNRL 65
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
270-389 1.63e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 46.21  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  270 VDADNSGTLTLDEAKRVAFEhyGFDE---ATLAPFFGQADENEDGQLDNVEFAGFR-----SVIRARSVRDAMDKMKRID 341
Cdd:NF041410  36 LDSDGDGSVSQDELSSALSS--KSDDgslIDLSELFSDLDSDGDGSLSSDELAAAApppppPPDQAPSTELADDLLSALD 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 71991483  342 TNGDGLVSNAE-ATDSTKKEDDMDSEEtlaLFNIADQNKSGKLDKVELA 389
Cdd:NF041410 114 TDGDGSISSDElSAGLTSAGSSADSSQ---LFSALDSDGDGSVSSDELA 159
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 88-282 3.20e-05

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: 46.14  E-value: 3.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  88 VEDLFKQVDTNRDNVLDAREFDA-IRMLV---LEKAENAALRYLQNVDTDRDGLLSLQEAQIYLLR----------EYGI 153
Cdd:cd16225  36 LKEIFKKVDVNTDGFLSAEELEDwIMEKTqehFQEAVEENEQIFKAVDTDKDGNVSWEEYRVHFLLskgyseeeaeEKIK 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 154 GY----------HDVARL---WKLVPADLSDRMNSTLFSKLR--RRVRGMTIRLARQIMKNADLNGDGHISVDEAQAIAF 218
Cdd:cd16225 116 NNeelkldeddkEVLDRYkdrWSQADEPEDGLLDVEEFLSFRhpEHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPP 195

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71991483 219 EQEGIGAGDVASM---------VGSVDENMDGELNAPEFADF-----ERiiraRAIENSKKAMRVVDADNSGTLTLDE 282
Cdd:cd16225 196 GTVEEQQAEDDDEwkkerkkefEEVIDLNHDGKVTKEELEEYmdprnER----HALNEAKQLIAVADENKDGKLSLEE 269
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
60-110 6.20e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 6.20e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71991483  60 VDVNEDGVLDIDEIRyAAFVHHGLSASVVEDLFKQVDTNRDNVLDAREFDA 110
Cdd:COG5126  78 LDTDGDGKISADEFR-RLLTALGVSEEEADELFARLDTDGDGKISFEEFVA 127
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
338-457 1.21e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.90  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  338 KRIDTNGDGLVSNAEATDS-TKKEDDMDSEETLALFNIADQNKSGKLDKVELADFNRL-----VRLSSIKFATDHFKEFD 411
Cdd:NF041410  34 AKLDSDGDGSVSQDELSSAlSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPpppppDQAPSTELADDLLSALD 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 71991483  412 LDGNDAVTFDEIALLIEQKYGIPRSmiKTFFDRIDVDGSGDLMPAE 457
Cdd:NF041410 114 TDGDGSISSDELSAGLTSAGSSADS--SQLFSALDSDGDGSVSSDE 157
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
59-215 1.34e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.52  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483   59 SVDVNEDGVLDIDEIRYAAFVHHGLSASV-VEDLFKQVDTNRDNVLDAREFDAirMLVL-------EKAENAALRYLQNV 130
Cdd:NF041410  35 KLDSDGDGSVSQDELSSALSSKSDDGSLIdLSELFSDLDSDGDGSLSSDELAA--AAPPpppppdqAPSTELADDLLSAL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  131 DTDRDGLLSLQEaqiyllreygigyhdvarLWKLVPADLSDRMNSTLFSKLrrrvrgmtirlarqimknaDLNGDGHISV 210
Cdd:NF041410 113 DTDGDGSISSDE------------------LSAGLTSAGSSADSSQLFSAL-------------------DSDGDGSVSS 155


                 ....*
gi 71991483  211 DEAQA 215
Cdd:NF041410 156 DELAA 160
PTZ00183 PTZ00183
centrin; Provisional
 201-318 2.24e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 41.98  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  201 DLNGDGHISVDE----AQAIAFEQEgigAGDVASMVGSVDENMDGELNAPEFADF------ERIIRaraiENSKKAMRVV 270
Cdd:PTZ00183  27 DTDGSGTIDPKElkvaMRSLGFEPK---KEEIKQMIADVDKDGSGKIDFEEFLDImtkklgERDPR----EEILKAFRLF 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 71991483  271 DADNSGTLTLDEAKRVAFE-HYGFDEATLAPFFGQADENEDGQLDNVEF 318
Cdd:PTZ00183 100 DDDKTGKISLKNLKRVAKElGETITDEELQEMIDEADRNGDGEISEEEF 148
EF-hand_7 pfam13499
EF-hand domain pair;
86-142 3.67e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 3.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483    86 SVVEDLFKQVDTNRDNVLDAREF-DAIRMLVLEK--AENAALRYLQNVDTDRDGLLSLQE 142
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELkKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISFEE 61
EF-hand_7 pfam13499
EF-hand domain pair;
371-422 4.39e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 4.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 71991483   371 LFNIADQNKSGKLDKVELADFNRLVRLS---SIKFATDHFKEFDLDGNDAVTFDE 422
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEEGeplSDEEVEELFKEFDLDKDGRISFEE 61
EF-hand_7 pfam13499
EF-hand domain pair;
332-391 5.55e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.69  E-value: 5.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71991483   332 DAMDKMKRIDTNGDGLVSNAE---ATDSTKKEDDMDSEETLALFNIADQNKSGKLDKVELADF 391
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEElkkLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLEL 65
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
187-282 5.73e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 38.51  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  187 GMTIRLArQIMKNADLNGDGHISVDE-AQAIAF---EQEGIGAGDVA-SMVGSVDENMDGELNAPEFADFerIIRARAIE 261
Cdd:NF041410  60 GSLIDLS-ELFSDLDSDGDGSLSSDElAAAAPPpppPPDQAPSTELAdDLLSALDTDGDGSISSDELSAG--LTSAGSSA 136

                         90       100
                 ....*....|....*....|.
gi 71991483  262 NSKKAMRVVDADNSGTLTLDE 282
Cdd:NF041410 137 DSSQLFSALDSDGDGSVSSDE 157
 
Name Accession Description Interval E-value
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 231-390 2.08e-12

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: 67.61  E-value: 2.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 231 MVGSVDENMDGELNAPEFADFERIIRARAI-ENSKKAMRVVDADNSGTLTLDEAKRVafeHYGFDEATLAPF-------- 301
Cdd:cd16226  40 IVDKIDKNGDGFVTEEELKDWIKYVQKKYIrEDVDRQWKEYDPNKDGKLSWEEYKKA---TYGFLDDEEEDDdlhesykk 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 302 --------FGQADENEDGQLDNVEFAGF---RSVIRARS--VRDAMDKmkrIDTNGDGLVSNAE------ATDSTKKEDD 362
Cdd:cd16226 117 mirrderrWKAADQDGDGKLTKEEFTAFlhpEEFPHMRDivVQETLED---IDKNKDGFISLEEyigdmyRDDDEEEDPD 193

                       170       180
                ....*....|....*....|....*...
gi 71991483 363 MDSEETLALFNIADQNKSGKLDKVELAD 390
Cdd:cd16226 194 WVKSEREQFKEFRDKNKDGKMDREEVKD 221
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
201-319 4.13e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 60.96  E-value: 4.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 201 DLNGDGHISVDEAQAIAfeqegigAGDVASMVGSVDENMDGELNAPEFADFERIIRARAIENS-KKAMRVVDADNSGTLT 279
Cdd:COG5126  15 DADGDGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFaRAAFDLLDTDGDGKIS 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 71991483 280 LDEAKRvAFEHYGFDEATLAPFFGQADENEDGQLDNVEFA 319
Cdd:COG5126  88 ADEFRR-LLTALGVSEEEADELFARLDTDGDGKISFEEFV 126
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
298-436 1.34e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 59.42  E-value: 1.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 298 LAPFFGQADENEDGQLDNVEFAGFRSVIRARSVRDAmdkmkriDTNGDGLVSNAEATDSTKKEDDMDSEETL-ALFNIAD 376
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEA-------DTDGDGRISREEFVAGMESLFEATVEPFArAAFDLLD 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 377 QNKSGKLDKVELADFNRLVRLSSIKfATDHFKEFDLDGNDAVTFDEIALLIEQkYGIPRS 436
Cdd:COG5126  80 TDGDGKISADEFRRLLTALGVSEEE-ADELFARLDTDGDGKISFEEFVAAVRD-YYTPDA 137
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
259-391 1.94e-10

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 59.04  E-value: 1.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 259 AIENSKKAMRVVDADNSGTLTLDEAKRVAfehygfdEATLAPFFGQADENEDGQLDNVEFAGFRSVIRARSVRDAMDKM- 337
Cdd:COG5126   3 QRRKLDRRFDLLDADGDGVLERDDFEALF-------RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAf 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 71991483 338 KRIDTNGDGLVSNAEATDSTkKEDDMDSEETLALFNIADQNKSGKLDKVELADF 391
Cdd:COG5126  76 DLLDTDGDGKISADEFRRLL-TALGVSEEEADELFARLDTDGDGKISFEEFVAA 128
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
331-463 1.82e-09

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 56.34  E-value: 1.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 331 RDAMDKMKRIDTNGDGLVSNAEATDstkkeddMDSEETLALFNIADQNKSGKLDKVEL-ADFNRLVRLSSIKFATDHFKE 409
Cdd:COG5126   5 RKLDRRFDLLDADGDGVLERDDFEA-------LFRRLWATLFSEADTDGDGRISREEFvAGMESLFEATVEPFARAAFDL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 71991483 410 FDLDGNDAVTFDEIALLIEQkYGIPRSMIKTFFDRIDVDGSGDLMPAEIVDFRH 463
Cdd:COG5126  78 LDTDGDGKISADEFRRLLTA-LGVSEEEADELFARLDTDGDGKISFEEFVAAVR 130
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
236-352 6.72e-08

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 51.72  E-value: 6.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 236 DENMDGELNAPEF-ADFERIIRARAIEnskkamrvVDADNSGTLTLDEAkrVAFEHYGFD---EATLAPFFGQADENEDG 311
Cdd:COG5126  15 DADGDGVLERDDFeALFRRLWATLFSE--------ADTDGDGRISREEF--VAGMESLFEatvEPFARAAFDLLDTDGDG 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 71991483 312 QLDNVEFAGFRSVIRA-RSVRDAMdkMKRIDTNGDGLVSNAE 352
Cdd:COG5126  85 KISADEFRRLLTALGVsEEEADEL--FARLDTDGDGKISFEE 124
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 194-423 1.24e-07

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


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 53.21  E-value: 1.24e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 194 RQIMKNADLNGDGHISVDEAQA-IAFeqegigagdvasmvgsvdenmdgelnapEFADFERiiraraiENSKKAMRVVDA 272
Cdd:cd15899  38 GVIVSKMDVDKDGFISAKELHSwILE----------------------------SFKRHAM-------EESKEQFRAVDP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 273 DNSGTLTLDEAKRVAFEHYGFDE-----------------ATLAPFFGQADENEDGQLDNVEFAGFRSVIRARSVRDAM- 334
Cdd:cd15899  83 DEDGHVSWDEYKNDTYGSVGDDEenvadnikedeeykkllLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYMLDFVi 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 335 -DKMKRIDTNGDGLVSNAEATDSTKKEDDMDSEETLALF------NIADQNKSGKLDKVELADFnrlVRLSSIKFATDH- 406
Cdd:cd15899 163 kETLEDLDKNGDGFISLEEFISDPYSADENEEEPEWVKVekerfvELRDKDKDGKLDGEELLSW---VDPSNQEIALEEa 239

                       250       260
                ....*....|....*....|
gi 71991483 407 ---FKEFDLDGNDAVTFDEI 423
Cdd:cd15899 240 khlIAESDENKDGKLSPEEI 259
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 92-142 2.56e-07

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: 49.29  E-value: 2.56e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71991483  92 FKQVDTNRDNVLDAREFDAIRmLVLEKAENAALRYLQNVDTDRDGLLSLQE 142
Cdd:cd00252  51 FDNLDNNKDGKLDKRELAPFR-APLMPLEHCARGFFESCDLNKDKKISLQE 100
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
88-215 3.08e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.79  E-value: 3.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  88 VEDLFKQVDTNRDNVLDAREFDAIRMLVLEKAENAAlrylqnvDTDRDGLLSLQEAQIYLLREYGIGYHDVARLW-KLVP 166
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLWATLFSEA-------DTDGDGRISREEFVAGMESLFEATVEPFARAAfDLLD 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 71991483 167 ADLSDRMNSTLFSKLRRrVRGMTIRLARQIMKNADLNGDGHISVDEAQA 215
Cdd:COG5126  80 TDGDGKISADEFRRLLT-ALGVSEEEADELFARLDTDGDGKISFEEFVA 127
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 230-460 3.77e-07

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


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 51.67  E-value: 3.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 230 SMVGSVDENMDGELNAPEFADFerIIRAR---AIENSKKAMRVVDADNSGTLTLDEAKRVAFEHYGFDE----------- 295
Cdd:cd15899  39 VIVSKMDVDKDGFISAKELHSW--ILESFkrhAMEESKEQFRAVDPDEDGHVSWDEYKNDTYGSVGDDEenvadnikede 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 296 ------ATLAPFFGQADENEDGQLDNVEFAGFRSVIRARSVRDAM--DKMKRIDTNGDGLVSNAEATDSTKKEDDMDSEE 367
Cdd:cd15899 117 eykkllLKDKKRFEAADQDGDLILTLEEFLAFLHPEESPYMLDFVikETLEDLDKNGDGFISLEEFISDPYSADENEEEP 196

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 368 TLALF------NIADQNKSGKLDKVELADFnrlvrlssikfatdhfkefdLDGNDavtfdeiallieqkYGIPRSMIKTF 441
Cdd:cd15899 197 EWVKVekerfvELRDKDKDGKLDGEELLSW--------------------VDPSN--------------QEIALEEAKHL 242

                       250
                ....*....|....*....
gi 71991483 442 FDRIDVDGSGDLMPAEIVD 460
Cdd:cd15899 243 IAESDENKDGKLSPEEILD 261
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
188-291 6.65e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 49.02  E-value: 6.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 188 MTIRLARQIMKNADLNGDGHISVDE-AQAIAFEQEGIGAGDVASMVGSVDENMDGELNAPEFADFERIIRARAiENSKKA 266
Cdd:COG5126  30 LFRRLWATLFSEADTDGDGRISREEfVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLLTALGVSE-EEADEL 108

                        90       100
                ....*....|....*....|....*
gi 71991483 267 MRVVDADNSGTLTLDEAKRVAFEHY 291
Cdd:COG5126 109 FARLDTDGDGKISFEEFVAAVRDYY 133
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 198-391 2.23e-06

EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF SSP 9302, 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 is highly expressed in various brain regions. Thus it plays an important role in migration and differentiation of neurons, and/or in Ca2+ signaling between glial cells and neurons. Calumenin is involved in Ca2+ homeostasis through interacting with ryanodine receptor RyR2 and SERCA2. It acts as a novel regulator of SERCA2, and its expressional changes are tightly coupled with Ca2+-cycling of cardiomyocytes. Calumenin also forms a Ca2+-dependent complex with thrombospondin-1, which is broadly involved in haemostasis and thrombosis. Moreover, calumenin is a molecular chaperone that endogenously regulates the vitamin K-dependent gamma-carboxylation of several proteins, including blood coagulation factors (such as FII, FVII, FIX, FX, and proteins C, S and Z), cell survival factors (Gas6) and bone metabolism proteins (such as matrix Gla protein or MGP, osteocalcin and periostin), through targeting the gamma-glutamyl carboxylase. It also functions as a charged F508del-cystic fibrosis transmembrane regulator (CFTR) folding modulator, as well as a G551D-CFTR associated protein. Furthermore, the extracellular calumenin acts as a suppressor of cell migration and tumor metastasis. It binds to and stabilizes fibulin-1, and further inactivates extracellular signal-regulated kinases 1 and 2 (ERK1/2) signaling.


Pssm-ID: 320026 [Multi-domain]  Cd Length: 263  Bit Score: 49.55  E-value: 2.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 198 KNADLNGDGHISVDEAQAiaFEQ-------EGIGagdvaSMVGSVDENMDGELNAPEFADFERIIRARAI-ENSKKAMRV 269
Cdd:cd16228   7 QNFDYDHDAFLGAEEAKT--FDQltpeeskERLG-----KIVGKIDEDKDGFVTEDELKAWIKFAQKRWIyEDVERQWKG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 270 VDADNSGTLTLDEAKRVAFEHY--------GFDEATLAPF----FGQADENEDGQLDNVEFAGFRSVIRARSVRD--AMD 335
Cdd:cd16228  80 HDLNEDGLVSWEEYKNATYGYIlddpdpddGFNYKQMMVRderrFKMADKDGDLRATKEEFTAFLHPEEYDYMKDivVLE 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71991483 336 KMKRIDTNGDGLVSNAE------ATDSTKKEDDMDSEETLALFNIADQNKSGKLDKVELADF 391
Cdd:cd16228 160 TMEDIDKNGDGFIDLEEyigdmySQDGDADEPEWVKTEREQFTEFRDKNKDGKMDKEETKDW 221
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 405-465 4.58e-06

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 46.45  E-value: 4.58e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71991483 405 DHFKEFDLDGNDAVTFDEI-ALLIEQKYGIPRSMIKTFFDRIDVDGSGDLMPAEIVDFRHLI 465
Cdd:cd16202   4 DQFRKADKNGDGKLSFKECkKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQFYNRL 65
EFh_CREC_RCN1 cd16229
EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic ...
 228-388 4.73e-06

EF-hand, calcium binding motif, found in reticulocalbin-1 (RCN-1); RCN-1 is an endoplasmic reticulum resident low-affinity Ca2+-binding protein with six EF-hand motifs and a carboxyl-terminal His-Asp-Glu-Leu (HDEL) tetrapeptide signal. It is expressed at the cell surface. RCN-1 acts as a potential negative regulator of B-RAF activation and can negatively modulate cardiomyocyte hypertrophy by inhibition of the mitogen-activated protein kinase signaling cascade. It also plays a key role in the development of doxorubicin-associated resistance.


Pssm-ID: 320027 [Multi-domain]  Cd Length: 267  Bit Score: 48.34  E-value: 4.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 228 VASMVGSVDENMDGELNAPEFADFERIIRARAI-ENSKKAMRVVDADNSGTLTLDEAKRVAFEHY-----GFDEAT---- 297
Cdd:cd16229  37 LGKIVDRIDDDKDGFVTTEELKAWIKRVQKRYIyENVAKVWKDYDLNKDNKISWEEYKQATYGYYlgnpeEFQDATdqfs 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 298 ---LAPF----FGQADENEDGQLDNVEFAGFRSVIRARSVRD--AMDKMKRIDTNGDGLVSNAE------ATDSTKKEDD 362
Cdd:cd16229 117 fkkMLPRderrFKAADLDGDLAATREEFTAFLHPEEFEHMKDivVLETLEDIDKNGDGFVDEDEyiadmfSHEEGGPEPD 196

                       170       180
                ....*....|....*....|....*.
gi 71991483 363 MDSEETLALFNIADQNKSGKLDKVEL 388
Cdd:cd16229 197 WVKTEREQFSDFRDLNKDGKMDKEEI 222
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
270-389 1.63e-05

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 46.21  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  270 VDADNSGTLTLDEAKRVAFEhyGFDE---ATLAPFFGQADENEDGQLDNVEFAGFR-----SVIRARSVRDAMDKMKRID 341
Cdd:NF041410  36 LDSDGDGSVSQDELSSALSS--KSDDgslIDLSELFSDLDSDGDGSLSSDELAAAApppppPPDQAPSTELADDLLSALD 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 71991483  342 TNGDGLVSNAE-ATDSTKKEDDMDSEEtlaLFNIADQNKSGKLDKVELA 389
Cdd:NF041410 114 TDGDGSISSDElSAGLTSAGSSADSSQ---LFSALDSDGDGSVSSDELA 159
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 236-423 1.93e-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: 46.54  E-value: 1.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 236 DENMDGELNAPEFADF-ERIIRARAIENSKKAMRVVDADNSGTLTLDEakrVAFEHYGFDEATLAP-------------- 300
Cdd:cd16227  46 DLNDDGFIDRKELKAWiLRSFKMLDEEEANERFEEADEDGDGKVTWEE---YLADSFGYDDEDNEEmikdsteddlklle 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 301 ----FFGQADENEDGQLDNVEFAGFRS---------VIRARSVRDAmdkmkriDTNGDGLVSNAEATDSTKkeDDMDSE- 366
Cdd:cd16227 123 ddkeMFEAADLNKDGKLDKTEFSAFQHpeeyphmhpVLIEQTLRDK-------DKDNDGFISFQEFLGDRA--GHEDKEw 193

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71991483 367 ---ETLALFNIADQNKSGKLDKVELAdfnRLVRLSSIKFAT---DH-FKEFDLDGNDAVTFDEI 423
Cdd:cd16227 194 llvEKDRFDEDYDKDGDGKLDGEEIL---SWLVPDNEEIAEeevDHlFASADDDHDDRLSFDEI 254
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 288-422 2.23e-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: 46.16  E-value: 2.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 288 FEHYGFDEAT--LAPFFGQADENEDGQLDNVEFAGF--RSVIRArSVRDAMDKMKRIDTNGDGLVS-----------NAE 352
Cdd:cd16227  26 FDELPPEEAKrrLAVLAKKMDLNDDGFIDRKELKAWilRSFKML-DEEEANERFEEADEDGDGKVTweeyladsfgyDDE 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 353 ATDSTKKEDDMDSEETLA----LFNIADQNKSGKLDKVELADFnrlvrlssikFATDHF------------KEFDLDGND 416
Cdd:cd16227 105 DNEEMIKDSTEDDLKLLEddkeMFEAADLNKDGKLDKTEFSAF----------QHPEEYphmhpvlieqtlRDKDKDNDG 174


                ....*.
gi 71991483 417 AVTFDE 422
Cdd:cd16227 175 FISFQE 180
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 198-392 2.56e-05

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: 46.14  E-value: 2.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 198 KNADLNGDGHISV---DEAQAIAFEQEGIGAGDVASMVGSVDENMDGELNAPEFADfeRIIR------ARAIENSKKAMR 268
Cdd:cd16225   3 RDGHLNKEFHKEVflgNEKEEFEEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELED--WIMEktqehfQEAVEENEQIFK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 269 VVDADNSGTLTLDEAKRVAFEHYGFDEATLAPF-----------------------FGQADENEDGQLDNVEFAGFRSVI 325
Cdd:cd16225  81 AVDTDKDGNVSWEEYRVHFLLSKGYSEEEAEEKiknneelkldeddkevldrykdrWSQADEPEDGLLDVEEFLSFRHPE 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71991483 326 RARSVRDAM--DKMKRIDTNGDGLVSNAE--------ATDSTKKEDDMDSEETLALFNIA-DQNKSGKLDKVELADFN 392
Cdd:cd16225 161 HSRGMLKNMvkEILHDLDQDGDEKLTLDEfvslppgtVEEQQAEDDDEWKKERKKEFEEViDLNHDGKVTKEELEEYM 238
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 88-282 3.20e-05

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: 46.14  E-value: 3.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  88 VEDLFKQVDTNRDNVLDAREFDA-IRMLV---LEKAENAALRYLQNVDTDRDGLLSLQEAQIYLLR----------EYGI 153
Cdd:cd16225  36 LKEIFKKVDVNTDGFLSAEELEDwIMEKTqehFQEAVEENEQIFKAVDTDKDGNVSWEEYRVHFLLskgyseeeaeEKIK 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 154 GY----------HDVARL---WKLVPADLSDRMNSTLFSKLR--RRVRGMTIRLARQIMKNADLNGDGHISVDEAQAIAF 218
Cdd:cd16225 116 NNeelkldeddkEVLDRYkdrWSQADEPEDGLLDVEEFLSFRhpEHSRGMLKNMVKEILHDLDQDGDEKLTLDEFVSLPP 195

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71991483 219 EQEGIGAGDVASM---------VGSVDENMDGELNAPEFADF-----ERiiraRAIENSKKAMRVVDADNSGTLTLDE 282
Cdd:cd16225 196 GTVEEQQAEDDDEwkkerkkefEEVIDLNHDGKVTKEELEEYmdprnER----HALNEAKQLIAVADENKDGKLSLEE 269
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 229-423 3.75e-05

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


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 45.50  E-value: 3.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 229 ASMVGSVDENMDGELNAPEFADF-ERIIRARAIENSKKAMRVVDADNSGTLTLDEAKRVAFEH-YGFDEATL-------- 298
Cdd:cd16224  39 KSIIKKIDTDSDGFLTEEELSSWiQQSFRHYALEDAKQQFPEYDKDGDGAVTWDEYNMQMYDRvIDYDEDTVlddeeees 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 299 --------APFFGQADENEDGQLDNVEFAGFR-----SVIRARSVRDAMDKMkriDTNGDGLVSNAE-----ATDSTKKE 360
Cdd:cd16224 119 frqlhlkdKKRFDKANTDGGPGLNLTEFIAFEhpeevDYMTEFVIQEALEEH---DKDGDGFISLEEflgdyRKDPTANE 195

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71991483 361 D-DMDSEETLALFNIADQNKSGKLDKVELADFNRLVRLSSIKFATDHF-KEFDLDGNDAVTFDEI 423
Cdd:cd16224 196 DpEWIIVEKDRFVNDYDKDNDGKLDPQELLPWVVPNNYGIAQEEALHLiDEMDLNGDGRLSEEEI 260
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
60-110 6.20e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 43.24  E-value: 6.20e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 71991483  60 VDVNEDGVLDIDEIRyAAFVHHGLSASVVEDLFKQVDTNRDNVLDAREFDA 110
Cdd:COG5126  78 LDTDGDGKISADEFR-RLLTALGVSEEEADELFARLDTDGDGKISFEEFVA 127
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 193-390 9.03e-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: 44.62  E-value: 9.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 193 ARQIMKNADLNGDGHISVDEAQAIAFeqegigagdvasmvGSVDENMDgELNAPEFADFERIiraraIENSKKAMRVVDA 272
Cdd:cd16227  74 ANERFEEADEDGDGKVTWEEYLADSF--------------GYDDEDNE-EMIKDSTEDDLKL-----LEDDKEMFEAADL 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 273 DNSGTLTLDEAkrVAFEHYGFDEATLAPFFGQA----DENEDGQLDNVEFAGFRSVIRARSVRDA-MDKMKR-IDTNGDG 346
Cdd:cd16227 134 NKDGKLDKTEF--SAFQHPEEYPHMHPVLIEQTlrdkDKDNDGFISFQEFLGDRAGHEDKEWLLVeKDRFDEdYDKDGDG 211

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 71991483 347 LVSNAE-ATDSTKKEDDMDSEETLALFNIADQNKSGKLDKVELAD 390
Cdd:cd16227 212 KLDGEEiLSWLVPDNEEIAEEEVDHLFASADDDHDDRLSFDEILD 256
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 407-461 1.14e-04

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 40.22  E-value: 1.14e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71991483 407 FKEFDLDGNDAVTFDE-IALLIEQKYGIPRSMIKTFFDRIDVDGSGDLMPAEIVDF 461
Cdd:cd00051   6 FRLFDKDGDGTISADElKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
338-457 1.21e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.90  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  338 KRIDTNGDGLVSNAEATDS-TKKEDDMDSEETLALFNIADQNKSGKLDKVELADFNRL-----VRLSSIKFATDHFKEFD 411
Cdd:NF041410  34 AKLDSDGDGSVSQDELSSAlSSKSDDGSLIDLSELFSDLDSDGDGSLSSDELAAAAPPpppppDQAPSTELADDLLSALD 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 71991483  412 LDGNDAVTFDEIALLIEQKYGIPRSmiKTFFDRIDVDGSGDLMPAE 457
Cdd:NF041410 114 TDGDGSISSDELSAGLTSAGSSADS--SQLFSALDSDGDGSVSSDE 157
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
59-215 1.34e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 43.52  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483   59 SVDVNEDGVLDIDEIRYAAFVHHGLSASV-VEDLFKQVDTNRDNVLDAREFDAirMLVL-------EKAENAALRYLQNV 130
Cdd:NF041410  35 KLDSDGDGSVSQDELSSALSSKSDDGSLIdLSELFSDLDSDGDGSLSSDELAA--AAPPpppppdqAPSTELADDLLSAL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  131 DTDRDGLLSLQEaqiyllreygigyhdvarLWKLVPADLSDRMNSTLFSKLrrrvrgmtirlarqimknaDLNGDGHISV 210
Cdd:NF041410 113 DTDGDGSISSDE------------------LSAGLTSAGSSADSSQLFSAL-------------------DSDGDGSVSS 155


                 ....*
gi 71991483  211 DEAQA 215
Cdd:NF041410 156 DELAA 160
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 91-212 2.10e-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: 43.20  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  91 LFKQVDTNRDNVLDAREFDA-IRMLVLEKAENAALRYLQNVDTDRDGLLSLQEaqiYLLREYGIGYHD------------ 157
Cdd:cd15899  40 IVSKMDVDKDGFISAKELHSwILESFKRHAMEESKEQFRAVDPDEDGHVSWDE---YKNDTYGSVGDDeenvadnikede 116

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991483 158 --------VARLWKLV--PADLS-DRMNSTLFSKlRRRVRGMTIRLARQIMKNADLNGDGHISVDE 212
Cdd:cd15899 117 eykklllkDKKRFEAAdqDGDLIlTLEEFLAFLH-PEESPYMLDFVIKETLEDLDKNGDGFISLEE 181
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 91-313 2.10e-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: 43.46  E-value: 2.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  91 LFKQVDTNRDNVLDAREFDA--IRMLVLEKAENAALRyLQNVDTDRDGLLSLQEaqiYLLREYGIGYHDVARLWKLVPAD 168
Cdd:cd16227  41 LAKKMDLNDDGFIDRKELKAwiLRSFKMLDEEEANER-FEEADEDGDGKVTWEE---YLADSFGYDDEDNEEMIKDSTED 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 169 lsdrmnstlFSKLrrrvrgmtIRLARQIMKNADLNGDGHIsvDEAQAIAFEQegigAGDVASMVGSV--------DENMD 240
Cdd:cd16227 117 ---------DLKL--------LEDDKEMFEAADLNKDGKL--DKTEFSAFQH----PEEYPHMHPVLieqtlrdkDKDND 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 241 GELNAPEFadferiIRARAIENSKKAMRV--------VDADNSGTLTLDEAKRVA---FEHYGFDEATlaPFFGQADENE 309
Cdd:cd16227 174 GFISFQEF------LGDRAGHEDKEWLLVekdrfdedYDKDGDGKLDGEEILSWLvpdNEEIAEEEVD--HLFASADDDH 245


                ....
gi 71991483 310 DGQL 313
Cdd:cd16227 246 DDRL 249
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 264-319 2.11e-04

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 39.45  E-value: 2.11e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71991483 264 KKAMRVVDADNSGTLTLDEAKRVAFEHY-GFDEATLAPFFGQADENEDGQLDNVEFA 319
Cdd:cd00051   3 REAFRLFDKDGDGTISADELKAALKSLGeGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
PTZ00183 PTZ00183
centrin; Provisional
 201-318 2.24e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 41.98  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  201 DLNGDGHISVDE----AQAIAFEQEgigAGDVASMVGSVDENMDGELNAPEFADF------ERIIRaraiENSKKAMRVV 270
Cdd:PTZ00183  27 DTDGSGTIDPKElkvaMRSLGFEPK---KEEIKQMIADVDKDGSGKIDFEEFLDImtkklgERDPR----EEILKAFRLF 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 71991483  271 DADNSGTLTLDEAKRVAFE-HYGFDEATLAPFFGQADENEDGQLDNVEF 318
Cdd:PTZ00183 100 DDDKTGKISLKNLKRVAKElGETITDEELQEMIDEADRNGDGEISEEEF 148
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 204-348 3.06e-04

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


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 41.65  E-value: 3.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 204 GDGHISVDEAQA------IAFEQEGIGAGDVASMVGSVDENMDGELNAPEFADFERIIRARaiensKKAMRVVDADNSGT 277
Cdd:cd15897  12 DDGEISATELQQalsnvgWTHFDLGFSLETCRSMIAMMDRDHSGKLNFSEFKGLWNYIKAW-----QEIFRTYDTDGSGT 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71991483 278 LTLDEAkRVAFEHYGF--DEATLAPFFGQADEnEDGQLDnveFAGFRS-VIRARSVRDAmdkMKRIDTNGDGLV 348
Cdd:cd15897  87 IDSNEL-RQALSGAGYrlSEQTYDIIIRRYDR-GRGNID---FDDFIQcCVRLQRLTDA---FRRYDKDQDGQI 152
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 281-392 6.11e-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: 41.80  E-value: 6.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 281 DEAKRvaFEHYGFDEAT--LAPFFGQADENEDGQLDNVEFAGFRSVIRARSVRDAMDK-MKRIDTNGDGLVSNAEATDST 357
Cdd:cd16226  20 EEAKE--FDQLTPEESKerLGIIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDRqWKEYDPNKDGKLSWEEYKKAT 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 71991483 358 -KKEDDMDSEETLAL------------FNIADQNKSGKLDKVELADFN 392
Cdd:cd16226  98 yGFLDDEEEDDDLHEsykkmirrderrWKAADQDGDGKLTKEEFTAFL 145
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 59-218 6.76e-04

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: 40.66  E-value: 6.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  59 SVDVNEDGVLDIDEIRYAAFV-HHGLSASVVEDLFKQVDTNRDNVLDAREFdairmlvlekaenAAL-RYLQNV------ 130
Cdd:cd16185   8 AVDRDRSGSIDVNELQKALAGgGLLFSLATAEKLIRMFDRDGNGTIDFEEF-------------AALhQFLSNMqngfeq 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 131 -DTDRDGLLSLQEAQIYLLReygIGYHdvarlwklvpadLSDRMNSTLFSKLRRRVRGM-----------TIRLARQIMK 198
Cdd:cd16185  75 rDTSRSGRLDANEVHEALAA---SGFQ------------LDPPAFQALFRKFDPDRGGSlgfddyielciFLASARNLFQ 139

                       170       180
                ....*....|....*....|
gi 71991483 199 NADLNGDGHISVDEAQAIAF 218
Cdd:cd16185 140 AFDRQRTGRVTLDFNQFVYA 159
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 367-422 7.49e-04

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 37.91  E-value: 7.49e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71991483 367 ETLALFNIADQNKSGKLDKVELADF-NRLVRLSSIKFATDHFKEFDLDGNDAVTFDE 422
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAAlKSLGEGLSEEEIDEMIREVDKDGDGKIDFEE 57
EFh_SPARC_EC cd00252
EF-hand, extracellular calcium-binding (EC) motif, found in secreted protein acidic and rich ...
 350-422 1.27e-03

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: 38.51  E-value: 1.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71991483 350 NAEATDSTKKEDDMDSEETLA--LFNIADQNKSGKLDKVELADFNRLVRLssIKFATDHF-KEFDLDGNDAVTFDE 422
Cdd:cd00252  27 RSYDNNKRGHDLSGTMRKEIAqwEFDNLDNNKDGKLDKRELAPFRAPLMP--LEHCARGFfESCDLNKDKKISLQE 100
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 268-421 1.41e-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: 39.51  E-value: 1.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 268 RVVDADNSGTLTLDEAKRVAFE---HYGFDEAT-LAPFFgqaDENEDGQLDNVEFAGFRSVIraRSVRDAmdkMKRIDTN 343
Cdd:cd16185   7 RAVDRDRSGSIDVNELQKALAGgglLFSLATAEkLIRMF---DRDGNGTIDFEEFAALHQFL--SNMQNG---FEQRDTS 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71991483 344 GDGLVSNAEATDSTKKEDDMDSEETL-ALFNIADQNKSGKLDkveLADFNRLVrlSSIKFATDHFKEFDLDGNDAVTFD 421
Cdd:cd16185  79 RSGRLDANEVHEALAASGFQLDPPAFqALFRKFDPDRGGSLG---FDDYIELC--IFLASARNLFQAFDRQRTGRVTLD 152
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 338-391 2.46e-03

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: 36.37  E-value: 2.46e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71991483 338 KRIDTNGDGLVSNAE-ATDSTKKEDDMDSEETLALFNIADQNKSGKLDKVELADF 391
Cdd:cd00051   7 RLFDKDGDGTISADElKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 194-391 2.53e-03

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


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 40.03  E-value: 2.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 194 RQIMKNADLNGDGHISVDE-AQAIAFEQEGIGA-GDVASMVGSV---------DENMDGELNAPEFADF---------ER 253
Cdd:cd15902  47 KEFMEKYDENEDGKIEIRElANILPTEENFLLLfRREQPLISSVefmkiwrkyDTDGSGFIEAKELKGFlkdlllknkKH 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 254 IIRARAIENSKKAMRVVDADNSGTLTLDE------AKRVAFEHYGFDEAT------LAPFFGQADENEDGQLDNVEFAGF 321
Cdd:cd15902 127 VSPPKLDEYTKLILKEFDANKDGKLELDEmakllpVQENFLLKFQILGAMdltkedFEKVFEHYDKDNNGVIEGNELDAL 206

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71991483 322 rsvirarsVRDAMDKmkridtngdglvsnaeatdsTKKEDDMDSEETL--ALFNIADQNKSGKLDKVELADF 391
Cdd:cd15902 207 --------LKDLLEK--------------------NKADIDKPDLENFrdAILRACDKNKDGKIQKTELALF 250
EFh_SPARC_SMOC cd16234
EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding ...
 86-142 2.64e-03

EF-hand, extracellular calcium-binding (EC) motif, found in secreted modular calcium-binding protein SMOC-1, SMOC-2, and similar proteins; SMOC proteins corresponds to a group matricellular proteins that are involved in direct or indirect modulation of growth factor signaling pathways and play diverse roles in physiological processes involving extensive tissue remodeling, migration, proliferation, and angiogenesis. They may mediate intercellular signaling and cell type-specific differentiation during gonad and reproductive tract development. SMOC-1 is localized in basement membranes. Its mutations have been found to be associated with individuals with Warrdenburg Anopthalmia Syndrome. SMOC-2 is ubiquitously expressed and is involved in angiogenesis and the regulation of cell cycle progression. It enhances the angiogenic effect of basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF). It has also been implicated in generalized vitiligo. SMOC proteins consist of a follistatin-like (FS) domain, two thyroglobulin-like (TY) domains, a novel domain conserved only in SMOC proteins, and an extracellular calcium-binding (EC) domain with two EF-hand calcium-binding motifs.


Pssm-ID: 320013  Cd Length: 104  Bit Score: 37.64  E-value: 2.64e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71991483  86 SVVEDLFKQVDTNRDNVLDAREFDAIRMLVLEKAE--NAALRYLQNVDTDRDGLLSLQE 142
Cdd:cd16234  39 QVLDWKFSQLDKNKNGVLERKEWKPFKRLLKKAVKpkKCARKFPKYCDVNKDKKISLTE 97
EFh_PI-PLCdelta4 cd16219
EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, ...
 335-414 2.73e-03

EF-hand motif found in phosphoinositide phospholipase C delta 4 (PI-PLC-delta4); PI-PLC-delta4, also termed 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4 (PLCD4), or phospholipase C-delta-4 (PLC-delta-4), is expressed in various tissues with the highest levels detected selectively in the brain, skeletal muscle, testis and kidney. It plays a significant role in cell growth, cell proliferation, tumorigenesis, and in an early stage of fertilization. PI-PLC-delta4 may function as a key enzyme in the regulation of PtdIns(4,5)P2 levels and Ca2+ metabolism in nuclei in response to growth factors, and its expression may be partially regulated by an increase in cytoplasmic Ca2+. Moreover, PI-PLC-delta4 binds glutamate receptor-interacting protein1 (GRIP1) in testis and is required for calcium mobilization essential for the zona pellucida-induced acrosome reaction in sperm. Overexpression or dysregulated expression of PLCdelta4 may initiate oncogenesis in certain tissues through upregulating erbB1/2 expression, extracellular signal-regulated kinase (ERK) signaling pathway, and proliferation in MCF-7 cells. PI-PLC-delta4 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core domain, and a C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Unlike PI-PLC-delta 1 and 3, a putative nuclear export sequence (NES) located in the EF-hand domain, which may be responsible transporting PI-PLC-delta1 and 3 from the cell nucleus, is not present in PI-PLC-delta4.


Pssm-ID: 320049 [Multi-domain]  Cd Length: 140  Bit Score: 38.29  E-value: 2.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 335 DKMKRIDTNGDGLVSNAEATDSTKKED-DMDSEETLALFNIADQNKSGKLDKVELADFNRLvrLSSIKFATDHFKEFDLD 413
Cdd:cd16219   4 DWFQKADKNKDGRMNFKEVRDLLKMMNvDMNEEHALRLFQMADKSESGTLEGEEFVLFYKA--LTQREDVLKIFQDFSAD 81


                .
gi 71991483 414 G 414
Cdd:cd16219  82 G 82
EF-hand_7 pfam13499
EF-hand domain pair;
86-142 3.67e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 3.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483    86 SVVEDLFKQVDTNRDNVLDAREF-DAIRMLVLEK--AENAALRYLQNVDTDRDGLLSLQE 142
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELkKLLRKLEEGEplSDEEVEELFKEFDLDKDGRISFEE 61
EF-hand_7 pfam13499
EF-hand domain pair;
371-422 4.39e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 36.08  E-value: 4.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 71991483   371 LFNIADQNKSGKLDKVELADFNRLVRLS---SIKFATDHFKEFDLDGNDAVTFDE 422
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEEGeplSDEEVEELFKEFDLDKDGRISFEE 61
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 61-150 5.49e-03

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 37.59  E-value: 5.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  61 DVNEDGVLDIDEIRyaAFVHH---GLSASVVEDLFKQVDTNRDNVLDAREFDAIRMLVLEKAEnaaLRYLQNVDTDRDGL 137
Cdd:cd16202  10 DKNGDGKLSFKECK--KLLKKlnvKVDKDYAKKLFQEADTSGEDVLDEEEFVQFYNRLTKRPE---IEELFKKYSGDDEA 84

                        90
                ....*....|...
gi 71991483 138 LSLQEAQIYLLRE 150
Cdd:cd16202  85 LTVEELRRFLQEE 97
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 355-463 5.51e-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: 39.10  E-value: 5.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 355 DSTKKEDDMDSEET---LA-LFNIADQNKSGKLDKVELADFNRLVRLSSIKFATD-HFKEFDLDGNDAVTFDEIallIEQ 429
Cdd:cd16226  20 EEAKEFDQLTPEESkerLGiIVDKIDKNGDGFVTEEELKDWIKYVQKKYIREDVDrQWKEYDPNKDGKLSWEEY---KKA 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 71991483 430 KYGIP-------------RSMI---KTFFDRIDVDGSGDLMPAEIVDFRH 463
Cdd:cd16226  97 TYGFLddeeedddlhesyKKMIrrdERRWKAADQDGDGKLTKEEFTAFLH 146
EF-hand_7 pfam13499
EF-hand domain pair;
332-391 5.55e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.69  E-value: 5.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71991483   332 DAMDKMKRIDTNGDGLVSNAE---ATDSTKKEDDMDSEETLALFNIADQNKSGKLDKVELADF 391
Cdd:pfam13499   3 KLKEAFKLLDSDGDGYLDVEElkkLLRKLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLEL 65
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
187-282 5.73e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 38.51  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483  187 GMTIRLArQIMKNADLNGDGHISVDE-AQAIAF---EQEGIGAGDVA-SMVGSVDENMDGELNAPEFADFerIIRARAIE 261
Cdd:NF041410  60 GSLIDLS-ELFSDLDSDGDGSLSSDElAAAAPPpppPPDQAPSTELAdDLLSALDTDGDGSISSDELSAG--LTSAGSSA 136

                         90       100
                 ....*....|....*....|.
gi 71991483  262 NSKKAMRVVDADNSGTLTLDE 282
Cdd:NF041410 137 DSSQLFSALDSDGDGSVSSDE 157
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 370-453 9.92e-03

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 37.12  E-value: 9.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71991483 370 ALFNIADQNKSGKLDKVEL------ADFNRLvRLSSIKFAtdhFKEFDLDGNDAVTFDEIALL---IEQKYGIprsmikt 440
Cdd:cd16180   4 RIFQAVDRDRSGRISAKELqralsnGDWTPF-SIETVRLM---INMFDRDRSGTINFDEFVGLwkyIQDWRRL------- 72

                        90
                ....*....|...
gi 71991483 441 fFDRIDVDGSGDL 453
Cdd:cd16180  73 -FRRFDRDRSGSI 84
 
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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