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Conserved domains on  [gi|1985438074|ref|XP_039359518|]
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lysophosphatidylcholine acyltransferase 2 isoform X2 [Mauremys reevesii]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 12959272)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction; similar to Manduca sexta juvenile hormone diol kinase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 1-210 5.13e-92

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.


:

Pssm-ID: 153253 [Multi-domain]  Cd Length: 211  Bit Score: 277.18  E-value: 5.13e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   1 MFFLMGFQ-VEVKGKVAgPLEAPILVVAPHSSFFDGIVCILAGLPSIVSRLENLSAPVFGTILRSLQPVLVSRLDPDSRR 79
Cdd:cd07991     4 LLFAFGFYvIKVHGKPD-PPEAPRIIVANHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPKDRK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074  80 NTINEITKRATSGgQWPQVLIFPEGTCTNRSCLITFKQGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYSFKELCVMTFCQ 159
Cdd:cd07991    83 KVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRLLTQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1985438074 160 PLTRVEVEFLPVHVPTeEEKKDPTLFASKVRNTMATALNVPVTDHTFEDCR 210
Cdd:cd07991   162 PANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
242-374 9.47e-19

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 82.15  E-value: 9.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 242 PIRDQLDTFAAIAnASKGGRIGMEEFAEYLklpvSDVLKELFLLFDRNGDGTIDFREYVIGLSVLCNPANtEETIQMAFN 321
Cdd:COG5126     3 QRRKLDRRFDLLD-ADGDGVLERDDFEALF----RRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFARAAFD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1985438074 322 LFDVDDDGSITEEEFAcILRSSLGVPDLDVSQLFKEIDTDHSGKIAYNEFKDF 374
Cdd:COG5126    77 LLDTDGDGKISADEFR-RLLTALGVSEEEADELFARLDTDGDGKISFEEFVAA 128
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 1-210 5.13e-92

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.


Pssm-ID: 153253 [Multi-domain]  Cd Length: 211  Bit Score: 277.18  E-value: 5.13e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   1 MFFLMGFQ-VEVKGKVAgPLEAPILVVAPHSSFFDGIVCILAGLPSIVSRLENLSAPVFGTILRSLQPVLVSRLDPDSRR 79
Cdd:cd07991     4 LLFAFGFYvIKVHGKPD-PPEAPRIIVANHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPKDRK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074  80 NTINEITKRATSGgQWPQVLIFPEGTCTNRSCLITFKQGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYSFKELCVMTFCQ 159
Cdd:cd07991    83 KVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRLLTQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1985438074 160 PLTRVEVEFLPVHVPTeEEKKDPTLFASKVRNTMATALNVPVTDHTFEDCR 210
Cdd:cd07991   162 PANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 1-198 1.75e-27

1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 108.94  E-value: 1.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   1 MFFLMGFQVEVKGKVAGPLEAPILVVAPHSSFFDgIVCILAGLP---SIVSRLENLSAPVFGTILRSLQPVLVSRLDPDS 77
Cdd:COG0204    23 LLRLLGVRVRVEGLENLPADGPVLIVANHQSWLD-ILLLLAALPrpvRFVAKKELFKIPLLGWLLRALGAIPVDRSKRRA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074  78 RRNTINEITKRATSGGqwpQVLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPVLLRYpnkldtvTWTWQGYSFkelc 153
Cdd:COG0204   102 ALRALRQAVEALKAGE---SLVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG-------TERALPKGF---- 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1985438074 154 vmtFCQPlTRVEVEFLPVHVPTEEEKKDPTLFASKVRNTMATALN 198
Cdd:COG0204   168 ---LPRP-GKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 23-133 4.22e-20

Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 85.48  E-value: 4.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   23 ILVVAPHSSFFDGIVCILA-----GLPSIVSRLENLSAPVFGTILRSLQPVLVSRLDPDSRRNTINEItKRATSGGQWpq 97
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALlprklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREA-VELLKEGEW-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1985438074   98 VLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPVLLRY 133
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
242-374 9.47e-19

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 82.15  E-value: 9.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 242 PIRDQLDTFAAIAnASKGGRIGMEEFAEYLklpvSDVLKELFLLFDRNGDGTIDFREYVIGLSVLCNPANtEETIQMAFN 321
Cdd:COG5126     3 QRRKLDRRFDLLD-ADGDGVLERDDFEALF----RRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFARAAFD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1985438074 322 LFDVDDDGSITEEEFAcILRSSLGVPDLDVSQLFKEIDTDHSGKIAYNEFKDF 374
Cdd:COG5126    77 LLDTDGDGKISADEFR-RLLTALGVSEEEADELFARLDTDGDGKISFEEFVAA 128
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 8-129 7.04e-16

Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 73.85  E-value: 7.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   8 QVEVKGKVAGPLEAPILVVAPHSSFFDGIV--CILA---GLPSIVSRLENLSAPVFGTILRSLQPVLVSRLDPDSRRNTI 82
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLLlsLALYkrgRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1985438074  83 NEITKRATSGGQwpqVLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPV 129
Cdd:pfam01553  81 EYLVELLREGKL---VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPV 128
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 316-374 1.53e-13

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 65.26  E-value: 1.53e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 316 IQMAFNLFDVDDDGSITEEEFACILRS-SLGVPDLDVSQLFKEIDTDHSGKIAYNEFKDF 374
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALKSlGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
313-375 4.59e-13

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 63.81  E-value: 4.59e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985438074 313 EETIQMAFNLFDVDDDGSITEEEFACILRS-SLGVP--DLDVSQLFKEIDTDHSGKIAYNEFKDFA 375
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPlsDEEVEELFKEFDLDKDGRISFEEFLELY 66
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 6-132 9.99e-12

1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129621 [Multi-domain]  Cd Length: 130  Bit Score: 61.98  E-value: 9.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   6 GFQVEVKGKVAGPLEAPILVVAPHSSFFDgIVCILAGLP---SIVSRLENLSAPVFGTILRSLQPVLVSRldpDSRR--N 80
Cdd:TIGR00530   1 GLKVEVVGPENLPAKSPVLVVANHQSNLD-PLTLSAAFPppiVFIAKKELKWIPFFGIMLWLTGAIFIDR---ENIRaiA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1985438074  81 TINEITKRATSGGQwpQVLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPVLLR 132
Cdd:TIGR00530  77 TALKAAIEVLKQGR--SIGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
PTZ00184 PTZ00184
calmodulin; Provisional
 274-371 1.44e-11

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 62.09  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 274 PVSDVLKELFLLFDRNGDGTIDFREYVIGLSVLCNPANTEETIQMAFNLFDVDDDGSITEEEFACILrSSLG--VPDLDV 351
Cdd:PTZ00184   44 PTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEV 122

                          90       100
                  ....*....|....*....|
gi 1985438074 352 SQLFKEIDTDHSGKIAYNEF 371
Cdd:PTZ00184  123 DEMIREADVDGDGQINYEEF 142
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 7-131 2.72e-07

1-acyl-sn-glycerol-3-phosphate acyltransferase


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 50.88  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   7 FQVEVKGKVAGP-LEAPILVVAPHSSFFDGIVCILAGLP-SIVSRLENLSAPVFGTILRSLQPVLVSRLDPDSRRNTIN- 83
Cdd:PLN02901   35 YKIEVEGLENLPsPDEPAVYVSNHQSFLDIYTLFHLGRPfKFISKTSIFLIPIIGWAMYMTGHIPLKRMDRRSQLECLKr 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985438074  84 --EITKRATSggqwpqVLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPVLL 131
Cdd:PLN02901  115 cmELLKKGAS------VFFFPEGTRSKDGKLAAFKKGAFSvaakTGVPVVPITL 162
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
279-371 3.95e-07

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 50.83  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 279 LKELFLLFDRNGDGTIDFREyvigL-SVLCNPANTEETIQMA--FNLFDVDDDGSITEEEFACIL-----RSSLGVPDLD 350
Cdd:NF041410   29 QKQLFAKLDSDGDGSVSQDE----LsSALSSKSDDGSLIDLSelFSDLDSDGDGSLSSDELAAAApppppPPDQAPSTEL 104

                          90       100
                  ....*....|....*....|.
gi 1985438074 351 VSQLFKEIDTDHSGKIAYNEF 371
Cdd:NF041410  105 ADDLLSALDTDGDGSISSDEL 125
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
279-372 4.06e-07

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 50.83  E-value: 4.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 279 LKELFLLFDRNGDGTIDFREYVIGLSVLCNPANTEETIQMAFNLF---DVDDDGSITEEEFACILRSSLGvpDLDVSQLF 355
Cdd:NF041410   65 LSELFSDLDSDGDGSLSSDELAAAAPPPPPPPDQAPSTELADDLLsalDTDGDGSISSDELSAGLTSAGS--SADSSQLF 142

                          90
                  ....*....|....*..
gi 1985438074 356 KEIDTDHSGKIAYNEFK 372
Cdd:NF041410  143 SALDSDGDGSVSSDELA 159
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 279-304 1.33e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 38.90  E-value: 1.33e-04
                           10        20
                   ....*....|....*....|....*.
gi 1985438074  279 LKELFLLFDRNGDGTIDFREYVIGLS 304
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
259-337 3.30e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 38.89  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 259 GGRIGMEEFAEYLKLP--------VSDVLKELFLLFDRNGDGTIDFREYVIGLSVLCNPANTEETiqmaFNLFDVDDDGS 330
Cdd:NF041410   77 DGSLSSDELAAAAPPPppppdqapSTELADDLLSALDTDGDGSISSDELSAGLTSAGSSADSSQL----FSALDSDGDGS 152


                  ....*..
gi 1985438074 331 ITEEEFA 337
Cdd:NF041410  153 VSSDELA 159
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 1-210 5.13e-92

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.


Pssm-ID: 153253 [Multi-domain]  Cd Length: 211  Bit Score: 277.18  E-value: 5.13e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   1 MFFLMGFQ-VEVKGKVAgPLEAPILVVAPHSSFFDGIVCILAGLPSIVSRLENLSAPVFGTILRSLQPVLVSRLDPDSRR 79
Cdd:cd07991     4 LLFAFGFYvIKVHGKPD-PPEAPRIIVANHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPKDRK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074  80 NTINEITKRATSGgQWPQVLIFPEGTCTNRSCLITFKQGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYSFKELCVMTFCQ 159
Cdd:cd07991    83 KVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRLLTQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1985438074 160 PLTRVEVEFLPVHVPTeEEKKDPTLFASKVRNTMATALNVPVTDHTFEDCR 210
Cdd:cd07991   162 PANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 1-198 1.75e-27

1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 108.94  E-value: 1.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   1 MFFLMGFQVEVKGKVAGPLEAPILVVAPHSSFFDgIVCILAGLP---SIVSRLENLSAPVFGTILRSLQPVLVSRLDPDS 77
Cdd:COG0204    23 LLRLLGVRVRVEGLENLPADGPVLIVANHQSWLD-ILLLLAALPrpvRFVAKKELFKIPLLGWLLRALGAIPVDRSKRRA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074  78 RRNTINEITKRATSGGqwpQVLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPVLLRYpnkldtvTWTWQGYSFkelc 153
Cdd:COG0204   102 ALRALRQAVEALKAGE---SLVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG-------TERALPKGF---- 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1985438074 154 vmtFCQPlTRVEVEFLPVHVPTEEEKKDPTLFASKVRNTMATALN 198
Cdd:COG0204   168 ---LPRP-GKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 1-181 1.25e-23

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.


Pssm-ID: 153251 [Multi-domain]  Cd Length: 184  Bit Score: 97.34  E-value: 1.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   1 MFFLMGFQVEVKGKVAGPLEAPILVVAPHSSFFDGIVCILAGLPSI--VSRLENLSAPVFGTILRSLQPVLVSRLDPDSR 78
Cdd:cd07989     4 LLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALPRPIrfVAKKELFKIPFLGWLLRLLGAIPIDRGNGRSA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074  79 RNTINEITKRATSGGqwpQVLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPVLLRYPNKLdtvtWTWQGYSFKElcv 154
Cdd:cd07989    84 REALREAIEALKEGE---SVVIFPEGTRSRDGELLPFKSGAFRlakeAGVPIVPVAISGTWGS----LPKGKKLPRP--- 153

                         170       180
                  ....*....|....*....|....*..
gi 1985438074 155 mtfcqplTRVEVEFLPVHVPTEEEKKD 181
Cdd:cd07989   154 -------GRVTVRIGEPIPPEGLELAE 173
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 23-133 4.22e-20

Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 85.48  E-value: 4.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   23 ILVVAPHSSFFDGIVCILA-----GLPSIVSRLENLSAPVFGTILRSLQPVLVSRLDPDSRRNTINEItKRATSGGQWpq 97
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALlprklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREA-VELLKEGEW-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1985438074   98 VLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPVLLRY 133
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
242-374 9.47e-19

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 82.15  E-value: 9.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 242 PIRDQLDTFAAIAnASKGGRIGMEEFAEYLklpvSDVLKELFLLFDRNGDGTIDFREYVIGLSVLCNPANtEETIQMAFN 321
Cdd:COG5126     3 QRRKLDRRFDLLD-ADGDGVLERDDFEALF----RRLWATLFSEADTDGDGRISREEFVAGMESLFEATV-EPFARAAFD 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1985438074 322 LFDVDDDGSITEEEFAcILRSSLGVPDLDVSQLFKEIDTDHSGKIAYNEFKDF 374
Cdd:COG5126    77 LLDTDGDGKISADEFR-RLLTALGVSEEEADELFARLDTDGDGKISFEEFVAA 128
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 3-135 2.41e-16

Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).


Pssm-ID: 153244 [Multi-domain]  Cd Length: 187  Bit Score: 77.07  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   3 FLMGFQVEVKGKVAGPLEAPILVVAPHSSFFDGIVCILAGLPS-------IVSRLENLSAPVFGTilrsLQPVLVSRLDP 75
Cdd:cd06551     8 FFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLLLERGlrrdvygLMDEELLERYPFFTR----LGAFSVDRDSP 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985438074  76 DSRRNTINEITKRATSGGQWpqVLIFPEGTCTNRS-CLITFKQGAFIP----GVPVQPVLLRYPN 135
Cdd:cd06551    84 RSAAKSLKYVARLLSKPGSV--VWIFPEGTRTRRDkRPLQFKPGVAHLaekaGVPIVPVALRYTF 146
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 8-129 7.04e-16

Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 73.85  E-value: 7.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   8 QVEVKGKVAGPLEAPILVVAPHSSFFDGIV--CILA---GLPSIVSRLENLSAPVFGTILRSLQPVLVSRLDPDSRRNTI 82
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLLlsLALYkrgRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1985438074  83 NEITKRATSGGQwpqVLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPV 129
Cdd:pfam01553  81 EYLVELLREGKL---VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPV 128
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 316-374 1.53e-13

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 65.26  E-value: 1.53e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 316 IQMAFNLFDVDDDGSITEEEFACILRS-SLGVPDLDVSQLFKEIDTDHSGKIAYNEFKDF 374
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALKSlGEGLSEEEIDEMIREVDKDGDGKIDFEEFLEL 61
EF-hand_7 pfam13499
EF-hand domain pair;
313-375 4.59e-13

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 63.81  E-value: 4.59e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985438074 313 EETIQMAFNLFDVDDDGSITEEEFACILRS-SLGVP--DLDVSQLFKEIDTDHSGKIAYNEFKDFA 375
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPlsDEEVEELFKEFDLDKDGRISFEEFLELY 66
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 279-341 1.70e-12

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 62.18  E-value: 1.70e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985438074 279 LKELFLLFDRNGDGTIDFREYVIGLSVLcNPANTEETIQMAFNLFDVDDDGSITEEEFACILR 341
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 278-373 3.61e-12

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: 64.09  E-value: 3.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 278 VLKELFLLFDRNGDGTIDFREYVIGLSVLCNPANTEETIQMAFNLFDVDDDGSITEEEFaCILRSSLGvpdlDVSQLFKE 357
Cdd:cd16180     1 ELRRIFQAVDRDRSGRISAKELQRALSNGDWTPFSIETVRLMINMFDRDRSGTINFDEF-VGLWKYIQ----DWRRLFRR 75

                          90
                  ....*....|....*.
gi 1985438074 358 IDTDHSGKIAYNEFKD 373
Cdd:cd16180    76 FDRDRSGSIDFNELQN 91
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 6-132 9.99e-12

1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129621 [Multi-domain]  Cd Length: 130  Bit Score: 61.98  E-value: 9.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   6 GFQVEVKGKVAGPLEAPILVVAPHSSFFDgIVCILAGLP---SIVSRLENLSAPVFGTILRSLQPVLVSRldpDSRR--N 80
Cdd:TIGR00530   1 GLKVEVVGPENLPAKSPVLVVANHQSNLD-PLTLSAAFPppiVFIAKKELKWIPFFGIMLWLTGAIFIDR---ENIRaiA 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1985438074  81 TINEITKRATSGGQwpQVLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPVLLR 132
Cdd:TIGR00530  77 TALKAAIEVLKQGR--SIGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
PTZ00184 PTZ00184
calmodulin; Provisional
 274-371 1.44e-11

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 62.09  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 274 PVSDVLKELFLLFDRNGDGTIDFREYVIGLSVLCNPANTEETIQMAFNLFDVDDDGSITEEEFACILrSSLG--VPDLDV 351
Cdd:PTZ00184   44 PTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEV 122

                          90       100
                  ....*....|....*....|
gi 1985438074 352 SQLFKEIDTDHSGKIAYNEF 371
Cdd:PTZ00184  123 DEMIREADVDGDGQINYEEF 142
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 9-192 2.97e-10

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown AAK14816-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized glycerol-3-phosphate acyltransferases such as the Plasmodium falciparum locus AAK14816 putative acyltransferase, and similar proteins.


Pssm-ID: 153254 [Multi-domain]  Cd Length: 203  Bit Score: 59.58  E-value: 2.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   9 VEVKGKVAGPLEAPILVVAPHS-SFFDG--IVCILAGLPSIVSRLENLSAPVFGTILRSLQPVLVSRlDPDSRRNTINEI 85
Cdd:cd07992    16 ITVVGRENVPKDGPVIFLGNHPnALIDPllLAATLRRPVRFLAKADLFKNPLIGWLLESFGAIPVYR-PKDLARGGIGKI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074  86 TKRAT--------SGGQWpqVLIFPEGTCTNRSCLITFKQGAFI----------PGVPVQPVLLRYPNKldtvtwtwqgy 147
Cdd:cd07992    95 SNAAVfdavgealKAGGA--IGIFPEGGSHDRPRLLPLKAGAARmalealeagqKDVKIVPVGLNYEDK----------- 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1985438074 148 sfkelcvmtfCQPLTRVEVEF-LPVHVPTEEEKKDPTLFASKVRNT 192
Cdd:cd07992   162 ----------SRFRSRVLVEFgKPISVSAFEEAEASRDVEKKLINQ 197
EF-hand_7 pfam13499
EF-hand domain pair;
277-341 3.12e-10

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 55.72  E-value: 3.12e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985438074 277 DVLKELFLLFDRNGDGTIDFREYVIGLSVLCNPAN-TEETIQMAFNLFDVDDDGSITEEEFACILR 341
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00183 PTZ00183
centrin; Provisional
 243-372 9.06e-10

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 57.39  E-value: 9.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 243 IRDQLDTFaaiaNASKGGRIGMEEFAEYLKL----PVSDVLKELFLLFDRNGDGTIDFREYVIGLSVLCNPANTEETIQM 318
Cdd:PTZ00183   19 IREAFDLF----DTDGSGTIDPKELKVAMRSlgfePKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKKLGERDPREEILK 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1985438074 319 AFNLFDVDDDGSITEEEFACILRsSLG--VPDLDVSQLFKEIDTDHSGKIAYNEFK 372
Cdd:PTZ00183   95 AFRLFDDDKTGKISLKNLKRVAK-ELGetITDEELQEMIDEADRNGDGEISEEEFY 149
PTZ00184 PTZ00184
calmodulin; Provisional
 312-371 3.24e-08

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 52.46  E-value: 3.24e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985438074 312 TEETIQM---AFNLFDVDDDGSITEEEFACILRsSLGV--PDLDVSQLFKEIDTDHSGKIAYNEF 371
Cdd:PTZ00184    6 TEEQIAEfkeAFSLFDKDGDGTITTKELGTVMR-SLGQnpTEAELQDMINEVDADGNGTIDFPEF 69
PTZ00183 PTZ00183
centrin; Provisional
 308-378 5.53e-08

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 52.00  E-value: 5.53e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985438074 308 NPANTEETIQ---MAFNLFDVDDDGSITEEEFACILRsSLGV--PDLDVSQLFKEIDTDHSGKIAYNEFKDFAFKH 378
Cdd:PTZ00183    8 RPGLTEDQKKeirEAFDLFDTDGSGTIDPKELKVAMR-SLGFepKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKK 82
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 265-370 5.62e-08

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: 53.98  E-value: 5.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 265 EEFAEYLKLPVSDVLKELfllfDRNGDGTIDFREYvIGLSVLCNPANTE----ETIQMAF-NLFDVDDDGSITEEEF-AC 338
Cdd:cd15899   152 EESPYMLDFVIKETLEDL----DKNGDGFISLEEF-ISDPYSADENEEEpewvKVEKERFvELRDKDKDGKLDGEELlSW 226

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1985438074 339 ILRSSLGVPDLDVSQLFKEIDTDHSGKIAYNE 370
Cdd:cd15899   227 VDPSNQEIALEEAKHLIAESDENKDGKLSPEE 258
EF-hand_8 pfam13833
EF-hand domain pair;
327-377 6.75e-08

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 48.85  E-value: 6.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985438074 327 DDGSITEEEFACILRSsLGVPDL---DVSQLFKEIDTDHSGKIAYNEFKDFAFK 377
Cdd:pfam13833   1 EKGVITREELKRALAL-LGLKDLsedEVDILFREFDTDGDGYISFDEFCVLLER 53
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 316-406 9.85e-08

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 50.74  E-value: 9.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 316 IQMAFNLFDVDDDGSITEEEFACILRS-SLGVPDLDVSQLFKEIDTDHSGKIAYNEFKDF---AFKHPEYAKLFTTYLEL 391
Cdd:cd15898     2 LRRQWIKADKDGDGKLSLKEIKKLLKRlNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELyksLTERPELEPIFKKYAGT 81

                          90
                  ....*....|....*
gi 1985438074 392 QRcqlQTLDEEDYQT 406
Cdd:cd15898    82 NR---DYMTLEEFIR 93
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 250-371 1.11e-07

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: 51.06  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 250 FAAIaNASKGGRIGMEEFAEYLKLPVS----DVLKELFLLFDRNGDGTIDFREYViGLSVLCNpanteeTIQMAFNLFDV 325
Cdd:cd16185     6 FRAV-DRDRSGSIDVNELQKALAGGGLlfslATAEKLIRMFDRDGNGTIDFEEFA-ALHQFLS------NMQNGFEQRDT 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1985438074 326 DDDGSITEEE-FACILRSSLGVPDLDVSQLFKEIDTDHSGKIAYNEF 371
Cdd:cd16185    78 SRSGRLDANEvHEALAASGFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 7-131 2.72e-07

1-acyl-sn-glycerol-3-phosphate acyltransferase


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 50.88  E-value: 2.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074   7 FQVEVKGKVAGP-LEAPILVVAPHSSFFDGIVCILAGLP-SIVSRLENLSAPVFGTILRSLQPVLVSRLDPDSRRNTIN- 83
Cdd:PLN02901   35 YKIEVEGLENLPsPDEPAVYVSNHQSFLDIYTLFHLGRPfKFISKTSIFLIPIIGWAMYMTGHIPLKRMDRRSQLECLKr 114

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985438074  84 --EITKRATSggqwpqVLIFPEGTCTNRSCLITFKQGAFI----PGVPVQPVLL 131
Cdd:PLN02901  115 cmELLKKGAS------VFFFPEGTRSKDGKLAAFKKGAFSvaakTGVPVVPITL 162
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 260-374 2.89e-07

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: 50.22  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 260 GRIGMEEFA---EYLKlpvsdVLKELFLLFDRNGDGTIDFREYV-----IGLSVlcnpanTEETIQMAFNLFDVDDDGSI 331
Cdd:cd16180    52 GTINFDEFVglwKYIQ-----DWRRLFRRFDRDRSGSIDFNELQnalssFGYRL------SPQFVQLLVRKFDRRRRGSI 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1985438074 332 TEEEF--ACILRSSLgvpdldvSQLFKEIDTDHSGKIAYNeFKDF 374
Cdd:cd16180   121 SFDDFveACVTLKRL-------TDAFRKYDTNRTGYATIS-YEDF 157
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 278-403 2.93e-07

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 49.59  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 278 VLKELFLLFDRNGDGTIDFREyVIGLSVLCNPANTEETIQMAFNLFDVDDDGSITEEEFACILRSSLGVPDLDvsQLFKE 357
Cdd:cd15898     1 WLRRQWIKADKDGDGKLSLKE-IKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPELE--PIFKK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1985438074 358 IDTDHSGKIAYNEFKDFafkhpeyaklfttyleLQRCQLQTLDEED 403
Cdd:cd15898    78 YAGTNRDYMTLEEFIRF----------------LREEQGENVSEEE 107
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
279-371 3.95e-07

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 50.83  E-value: 3.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 279 LKELFLLFDRNGDGTIDFREyvigL-SVLCNPANTEETIQMA--FNLFDVDDDGSITEEEFACIL-----RSSLGVPDLD 350
Cdd:NF041410   29 QKQLFAKLDSDGDGSVSQDE----LsSALSSKSDDGSLIDLSelFSDLDSDGDGSLSSDELAAAApppppPPDQAPSTEL 104

                          90       100
                  ....*....|....*....|.
gi 1985438074 351 VSQLFKEIDTDHSGKIAYNEF 371
Cdd:NF041410  105 ADDLLSALDTDGDGSISSDEL 125
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
279-372 4.06e-07

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 50.83  E-value: 4.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 279 LKELFLLFDRNGDGTIDFREYVIGLSVLCNPANTEETIQMAFNLF---DVDDDGSITEEEFACILRSSLGvpDLDVSQLF 355
Cdd:NF041410   65 LSELFSDLDSDGDGSLSSDELAAAAPPPPPPPDQAPSTELADDLLsalDTDGDGSISSDELSAGLTSAGS--SADSSQLF 142

                          90
                  ....*....|....*..
gi 1985438074 356 KEIDTDHSGKIAYNEFK 372
Cdd:NF041410  143 SALDSDGDGSVSSDELA 159
PLN02833 PLN02833
glycerol acyltransferase family protein
 26-195 6.59e-07

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 51.31  E-value: 6.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074  26 VAPHSSFFDGIV-CILAGLPSIVSRLENLSAPVFGTILRSLQPVLVSRLDPDSRrNTINEITKRATSGGQWPQVLIFPEG 104
Cdd:PLN02833  168 VANHTSMIDFIVlEQMTPFAVIMQKHPGWVGFLQNTILESVGCIWFNRTEAKDR-EVVAKKLRDHVQDPDRNPLLIFPEG 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 105 TCTNRSCLITFKQGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYSFkelcVMTFCQPLTR----VEVEFLPVHvpTEEEKK 180
Cdd:PLN02833  247 TCVNNEYTVMFKKGAFELGCTVCPIAIKYNKIFVDAFWNSRKQSF----TMHLLRLMTSwavvCDVWYLEPQ--TLRPGE 320

                         170
                  ....*....|....*
gi 1985438074 181 DPTLFASKVRNTMAT 195
Cdd:PLN02833  321 TPIEFAERVRDMIAK 335
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 285-374 9.76e-07

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


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 50.10  E-value: 9.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 285 LFDRNGDGTIDFREYVIGLSV----LCNPAN------TEETIQMAFNLFDVDDDGSITEEEFACILRS--SLGVPDLDVS 352
Cdd:cd16179   149 LFDRNKDGKLQLSEMARLLPVkenfLCRPIFkgagklTREDIDRVFALYDRDNNGTIENEELTGFLKDllELVQEDYDEQ 228

                          90       100
                  ....*....|....*....|....*....
gi 1985438074 353 QL--FKEI-----DTDHSGKIAYNEFKDF 374
Cdd:cd16179   229 DLeeFKEIilrgwDFNNDGKISRKELTML 257
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 279-374 1.26e-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: 47.61  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 279 LKELFLLFDRNGDGTIDFREYVIGLSVLcNPANTEETIQMAFNLFDVDDDGSITEEEFACILRSSLGVPDLDvsQLFKEI 358
Cdd:cd16202     2 LKDQFRKADKNGDGKLSFKECKKLLKKL-NVKVDKDYAKKLFQEADTSGEDVLDEEEFVQFYNRLTKRPEIE--ELFKKY 78

                          90
                  ....*....|....*.
gi 1985438074 359 dTDHSGKIAYNEFKDF 374
Cdd:cd16202    79 -SGDDEALTVEELRRF 93
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 313-378 1.57e-05

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


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 42.34  E-value: 1.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985438074 313 EETIQMAFNLFDVDDDGSITEEEFACILRsSLGVPdldVSQlfKEIDtDHSGKIAYNEFKDFAFKH 378
Cdd:cd22949     2 EEKFREAFILFDRDGDGELTMYEAVLAMR-SCGIP---LTN--DEKD-ALPASMNWDQFENWAKKK 60
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 254-374 1.63e-05

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


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 44.58  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 254 ANASKGGRIGMEEFAEYLKL---PVSDV-LKELFLLFDRNGDGTIDFREYVIGLSVLCNPantEEtIQMAFNLFDVDDDG 329
Cdd:cd15898     9 ADKDGDGKLSLKEIKKLLKRlniRVSEKeLKKLFKEVDTNGDGTLTFDEFEELYKSLTER---PE-LEPIFKKYAGTNRD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1985438074 330 SITEEEFACILRSSLG--VPDLDVSQLFKEIDTD-HSGKIAYNEFKDF 374
Cdd:cd15898    85 YMTLEEFIRFLREEQGenVSEEECEELIEKYEPErENRQLSFEGFTNF 132
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 246-371 1.81e-05

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 44.83  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 246 QLDTFAAIANASKGGRIGMEEFAEYLKL----PVS-DVLKELFLLFDRNGDGTIDFREYViGLSvlcnpaNTEETIQMAF 320
Cdd:cd16180     1 ELRRIFQAVDRDRSGRISAKELQRALSNgdwtPFSiETVRLMINMFDRDRSGTINFDEFV-GLW------KYIQDWRRLF 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1985438074 321 NLFDVDDDGSITEEEFACILRsSLG--VPDLDVSQLFKEIDTDHSGKIAYNEF 371
Cdd:cd16180    74 RRFDRDRSGSIDFNELQNALS-SFGyrLSPQFVQLLVRKFDRRRRGSISFDDF 125
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 312-371 2.97e-05

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 42.91  E-value: 2.97e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985438074 312 TEETIQMAFNLFDVDDDGSITEEEFACILRS-SLGVPDL---DVSQLFKEIDTDHSGKIAYNEF 371
Cdd:cd16251    32 SEDQIKKVFQILDKDKSGFIEEEELKYILKGfSIAGRDLtdeETKALLAAGDTDGDGKIGVEEF 95
EF-hand_6 pfam13405
EF-hand domain;
316-342 5.64e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 39.85  E-value: 5.64e-05
                          10        20
                  ....*....|....*....|....*..
gi 1985438074 316 IQMAFNLFDVDDDGSITEEEFACILRS 342
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKALRS 28
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
260-310 5.93e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 42.86  E-value: 5.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1985438074 260 GRIGMEEFAEYLK-LPVSD-VLKELFLLFDRNGDGTIDFREYVIGLSVLCNPA 310
Cdd:COG5126    84 GKISADEFRRLLTaLGVSEeEADELFARLDTDGDGKISFEEFVAAVRDYYTPD 136
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 278-370 1.10e-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: 42.59  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 278 VLKELFLLFDRNGDGTIDFREYVIGLSVlCNPANTEETIQMAFNLFDVDDDGSITEEEFAcilrsSLGVPDLDVSQLFKE 357
Cdd:cd16185     1 ELRQWFRAVDRDRSGSIDVNELQKALAG-GGLLFSLATAEKLIRMFDRDGNGTIDFEEFA-----ALHQFLSNMQNGFEQ 74

                          90
                  ....*....|...
gi 1985438074 358 IDTDHSGKIAYNE 370
Cdd:cd16185    75 RDTSRSGRLDANE 87
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 279-304 1.33e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 38.90  E-value: 1.33e-04
                           10        20
                   ....*....|....*....|....*.
gi 1985438074  279 LKELFLLFDRNGDGTIDFREYVIGLS 304
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
LPLAT_ABO13168-like cd07988
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 23-142 2.36e-04

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ABO13168; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Acinetobacter baumannii ATCC 17978 locus ABO13168 putative acyltransferase, and similar proteins.


Pssm-ID: 153250 [Multi-domain]  Cd Length: 163  Bit Score: 41.43  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074  23 ILVVAPHSSFFDGIVCILA----GLPSIVSRLENLSAPVFGTILRSLQPVLVSRldpDSRRNTI----NEITKRATSggq 94
Cdd:cd07988    23 VVIGAPHTSNWDFVLGLLAafalGLKISFLGKHSLFKPPLGPFMRWLGGIPVDR---SRAGGLVeqvvEEFRRREEF--- 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1985438074  95 wpQVLIFPEGTctnRSCLITFKQG----AFIPGVPVQPVLLRYPNKldTVTW 142
Cdd:cd07988    97 --VLAIAPEGT---RSKVDKWKTGfyhiARGAGVPILLVYLDYKRK--TVGI 141
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 265-403 3.23e-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: 42.30  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 265 EEFAEylkLPVSDVLKELFLLF---DRNGDGTIDFREY----VIGLSVLcnpanTEETIQMAFNLFDVDDDGSITEEEfa 337
Cdd:cd16227    24 EEFDE---LPPEEAKRRLAVLAkkmDLNDDGFIDRKELkawiLRSFKML-----DEEEANERFEEADEDGDGKVTWEE-- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 338 cILRSSLGVPDLDVSQ------------------LFKEIDTDHSGKIAYNEFKdfAFKHPE-YAKLFTTYLElqrcqlQT 398
Cdd:cd16227    94 -YLADSFGYDDEDNEEmikdsteddlklleddkeMFEAADLNKDGKLDKTEFS--AFQHPEeYPHMHPVLIE------QT 164


                  ....*
gi 1985438074 399 LDEED 403
Cdd:cd16227   165 LRDKD 169
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 281-374 3.57e-04

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


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 41.96  E-value: 3.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 281 ELFLLFDRNGDGTIDFREYVIGLSVLCNPANTEETIQMAFNLF--------DVDDDGSITEEEFACIL-------RSSLG 345
Cdd:cd15902     3 EVWMHFDADGNGYIEGKELDSFLRELLKALNGKDKTDDEVAEKkkefmekyDENEDGKIEIRELANILpteenflLLFRR 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1985438074 346 VPDLDVSQLFKEI----DTDHSGKIAYNEFKDF 374
Cdd:cd15902    83 EQPLISSVEFMKIwrkyDTDGSGFIEAKELKGF 115
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 316-342 3.84e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.36  E-value: 3.84e-04
                           10        20
                   ....*....|....*....|....*..
gi 1985438074  316 IQMAFNLFDVDDDGSITEEEFACILRS 342
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
PTZ00184 PTZ00184
calmodulin; Provisional
 263-342 4.56e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 40.52  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 263 GMEEFAEYLKLPVS--------DVLKELFLLFDRNGDGTI---DFREYVIGLSVLCNPANTEETIQMAfnlfDVDDDGSI 331
Cdd:PTZ00184   62 GTIDFPEFLTLMARkmkdtdseEEIKEAFKVFDRDGNGFIsaaELRHVMTNLGEKLTDEEVDEMIREA----DVDGDGQI 137

                          90
                  ....*....|.
gi 1985438074 332 TEEEFACILRS 342
Cdd:PTZ00184  138 NYEEFVKMMMS 148
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 264-380 5.31e-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: 41.66  E-value: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 264 MEEFAEYlklpVSDVLKELFLLFDRNGDGTIDFREYVIGL---------SVLCNPANTEETIQM------AFNLFDVDDD 328
Cdd:cd15899    62 LESFKRH----AMEESKEQFRAVDPDEDGHVSWDEYKNDTygsvgddeeNVADNIKEDEEYKKLllkdkkRFEAADQDGD 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985438074 329 GSITEEEFACIL--RSSLGVPDLDVSQLFKEIDTDHSGKIAYNEFKDFAFKHPE 380
Cdd:cd15899   138 LILTLEEFLAFLhpEESPYMLDFVIKETLEDLDKNGDGFISLEEFISDPYSADE 191
EFh_CREC_Calumenin_like cd16226
EF-hand, calcium binding motif, found in calumenin, reticulocalbin-1 (RCN-1), reticulocalbin-3 ...
 275-371 5.88e-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: 41.42  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 275 VSDVLKELFLLFDRNGDGTIDFREYV-----IGLSVLCNPANTEETIQMA------FNLFDVDDDGSITEEEFACIL--R 341
Cdd:cd16226    69 IREDVDRQWKEYDPNKDGKLSWEEYKkatygFLDDEEEDDDLHESYKKMIrrderrWKAADQDGDGKLTKEEFTAFLhpE 148

                          90       100       110
                  ....*....|....*....|....*....|
gi 1985438074 342 SSLGVPDLDVSQLFKEIDTDHSGKIAYNEF 371
Cdd:cd16226   149 EFPHMRDIVVQETLEDIDKNKDGFISLEEY 178
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 276-349 6.79e-04

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


Pssm-ID: 319999  Cd Length: 163  Bit Score: 40.33  E-value: 6.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985438074 276 SDVLKELFL-LFDRNGDGTIDFREYVIGLSVLCNpANTEETIQMAFNLFDvDDDGSITEEEFACILRSSLGVPDL 349
Cdd:cd15901    52 SDLLLNWLLnLYDRNRTGCIRLLSVKIALITLCA-ASLLDKYRYLFGQLA-DSSGFISRERLTQFLQDLLQIPDL 124
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 263-383 7.75e-04

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 41.13  E-value: 7.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 263 GMEEFAEYLKLPVSDVLKELFLLFDRNGDGTIDFREYVIGLSVlcnpaNTEETIQMA-------FNLFDVDDDGSITEEE 335
Cdd:cd16225    20 EKEEFEEDSEPKKRKKLKEIFKKVDVNTDGFLSAEELEDWIME-----KTQEHFQEAveeneqiFKAVDTDKDGNVSWEE 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985438074 336 FACILRSSLGVPDLDVSQL-----------------------FKEIDTDHSGKIAYNEFkdFAFKHPEYAK 383
Cdd:cd16225    95 YRVHFLLSKGYSEEEAEEKiknneelkldeddkevldrykdrWSQADEPEDGLLDVEEF--LSFRHPEHSR 163
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 320-371 8.47e-04

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 37.58  E-value: 8.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1985438074 320 FNLFDVDDDGSITEEEFACILRSSlGVPDLDVSQLFKEIDTDHSGKIAYNEF 371
Cdd:cd00052     5 FRSLDPDGDGLISGDEARPFLGKS-GLPRSVLAQIWDLADTDKDGKLDKEEF 55
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 316-342 8.71e-04

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 36.61  E-value: 8.71e-04
                          10        20
                  ....*....|....*....|....*..
gi 1985438074 316 IQMAFNLFDVDDDGSITEEEFACILRS 342
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKK 28
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 280-403 1.13e-03

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


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 40.49  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 280 KELFLLFDRNGDGTIDFREYviglsvlcnpanteeTIQMAFNLFDVDDDGSITEEEfacilRSSLGVPDLDVSQLFKEID 359
Cdd:cd16224    75 KQQFPEYDKDGDGAVTWDEY---------------NMQMYDRVIDYDEDTVLDDEE-----EESFRQLHLKDKKRFDKAN 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1985438074 360 TDHSGKIAYNEFkdFAFKHPEYAKLFTTYLeLQrcqlQTLDEED 403
Cdd:cd16224   135 TDGGPGLNLTEF--IAFEHPEEVDYMTEFV-IQ----EALEEHD 171
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 279-306 1.27e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 36.22  E-value: 1.27e-03
                          10        20
                  ....*....|....*....|....*...
gi 1985438074 279 LKELFLLFDRNGDGTIDFREYVIGLSVL 306
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 266-308 1.44e-03

S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins.


Pssm-ID: 238131 [Multi-domain]  Cd Length: 88  Bit Score: 37.47  E-value: 1.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1985438074 266 EFAEYLKLPVS-DVLKELFLLFDRNGDGTIDFREY---VIGLSVLCN 308
Cdd:cd00213    39 ELPNFLKNQKDpEAVDKIMKDLDVNKDGKVDFQEFlvlIGKLAVACH 85
EFh_CREC_Calumenin cd16228
EF-hand, calcium binding motif, found in calumenin; Calumenin, also termed crocalbin, or IEF ...
 265-373 1.47e-03

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: 40.31  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 265 EEFAEYLKLPVSDVLKELFLL-----FDRNGDGTIDFREYVIGLSVLCNPANTEETIQMAFNLF----DVDDDGSITEEE 335
Cdd:cd16228   138 EEFTAFLHPEEYDYMKDIVVLetmedIDKNGDGFIDLEEYIGDMYSQDGDADEPEWVKTEREQFtefrDKNKDGKMDKEE 217

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1985438074 336 FA-CILRSSLGVPDLDVSQLFKEIDTDHSGKIAYNEFKD 373
Cdd:cd16228   218 TKdWILPSDYDHAEAEARHLVYESDQNKDGKLTKEEIVD 256
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 287-371 1.49e-03

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: 40.38  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 287 DRNGDGTIDFREYVI--------GLSVLCNPANTEETIQMA-----FNLFDVDDDGSITEEEFacilrSSLGVPD----- 348
Cdd:cd16227    82 DEDGDGKVTWEEYLAdsfgyddeDNEEMIKDSTEDDLKLLEddkemFEAADLNKDGKLDKTEF-----SAFQHPEeyphm 156

                          90       100
                  ....*....|....*....|....*
gi 1985438074 349 --LDVSQLFKEIDTDHSGKIAYNEF 371
Cdd:cd16227   157 hpVLIEQTLRDKDKDNDGFISFQEF 181
EFh_CREC_RCN2_like cd16227
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2) mainly from protostomes; This ...
 243-370 1.86e-03

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: 39.99  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 243 IRDQLDTFAAiANASKGGRIGMEEFAEY---------LKLPVSDVLKElfllFDRNGDGTIDFREYVIGLSVlcnpANTE 313
Cdd:cd16227   121 LEDDKEMFEA-ADLNKDGKLDKTEFSAFqhpeeyphmHPVLIEQTLRD----KDKDNDGFISFQEFLGDRAG----HEDK 191

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985438074 314 ETIQMAFNLF----DVDDDGSITEEEfaciLRSSLgVPDLD------VSQLFKEIDTDHSGKIAYNE 370
Cdd:cd16227   192 EWLLVEKDRFdedyDKDGDGKLDGEE----ILSWL-VPDNEeiaeeeVDHLFASADDDHDDRLSFDE 253
EF-hand_8 pfam13833
EF-hand domain pair;
290-336 1.94e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.14  E-value: 1.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1985438074 290 GDGTIDFREYVIGLSVLCNPANTEETIQMAFNLFDVDDDGSITEEEF 336
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
EFh_CREC_cab45 cd16225
EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also ...
 286-372 2.50e-03

EF-hand, calcium binding motif, found in 45 kDa calcium-binding protein (Cab45); Cab45, also termed stromal cell-derived factor 4 (SDF-4), is a soluble, lumenal Golgi resident low-affinity Ca2+-binding protein that contains six copies of the EF-hand Ca2+-binding motif. It is required for secretory pathway calcium ATPase1 (SPCA1)-dependent Ca2+ import into the trans-Golgi network (TGN) and plays an essential role in Ca2+-dependent secretory cargo sorting at the TGN.


Pssm-ID: 320023 [Multi-domain]  Cd Length: 278  Bit Score: 39.59  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 286 FDRNGDGTIDFREYVI------GLSVLCNPANTEETIQMaFNLFDVDDDGSITEEEFA-CILRSS---LGVPDLDVSQLF 355
Cdd:cd16225     1 LERDGHLNKEFHKEVFlgnekeEFEEDSEPKKRKKLKEI-FKKVDVNTDGFLSAEELEdWIMEKTqehFQEAVEENEQIF 79

                          90
                  ....*....|....*..
gi 1985438074 356 KEIDTDHSGKIAYNEFK 372
Cdd:cd16225    80 KAVDTDKDGNVSWEEYR 96
EFh_HEF_CB cd16176
EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or ...
 281-374 2.62e-03

EF-hand, calcium binding motif, found in calbindin (CB); CB, also termed calbindin D28, or D-28K, or avian-type vitamin D-dependent calcium-binding protein, is a unique intracellular calcium binding protein that functions as both a calcium sensor and buffer in eukaryotic cells, which undergoes a conformational change upon calcium binding and protects cells against insults of high intracellular calcium concentration. CB is highly expressed in brain and sensory neurons. It plays essential roles in neural functioning, altering synaptic interactions in the hippocampus, modulating calcium channel activity, calcium transients, and intrinsic neuronal firing activity. It prevents a neuronal death, as well as maintains and controls calcium homeostasis. CB also modulates the activity of proteins participating in the development of neurodegenerative disorders such as Alzheimer's disease, Huntington's disease, and bipolar disorder. Moreover, CB interacts with Ran-binding protein M, a protein known to involve in microtubule function. It also interacts with alkaline phosphatase and myo-inositol monophosphatase, as well as caspase 3, an enzyme that plays an important role in the regulation of apoptosis. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions with high affinity.


Pssm-ID: 320076 [Multi-domain]  Cd Length: 243  Bit Score: 39.44  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 281 ELFLLFDRNGDGTIDFRE---YVIGLSVLCNPANTEETIQM-AF-NLFDVDDDGSI----------TEEEFACILRSSLG 345
Cdd:cd16176     3 EIWHHYDNDGNGYIEGKElqsFIQELQQARKKAGLELSDQMkAFvDQYGQSTDGKIgivelaqilpTEENFLLFFRQQLK 82

                          90       100
                  ....*....|....*....|....*....
gi 1985438074 346 VPDlDVSQLFKEIDTDHSGKIAYNEFKDF 374
Cdd:cd16176    83 SSE-EFMQTWRKYDADHSGFIEADELKSF 110
EH smart00027
Eps15 homology domain; Pair of EF hand motifs that recognise proteins containing Asn-Pro-Phe ...
 320-371 2.74e-03

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


Pssm-ID: 197477 [Multi-domain]  Cd Length: 96  Bit Score: 36.87  E-value: 2.74e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1985438074  320 FNLFDVDDDGSITEEEFACILRSSlGVPDLDVSQLFKEIDTDHSGKIAYNEF 371
Cdd:smart00027  16 FRSLDKNQDGTVTGAQAKPILLKS-GLPQTLLAKIWNLADIDNDGELDKDEF 66
EFh_parvalbumin_alpha cd16254
EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2 ...
 292-371 2.76e-03

EF-hand, calcium binding motif, found in alpha-parvalbumin; Alpha-parvalbumin is cytosolic Ca2+/Mg2+-binding protein expressed mainly in fast-twitch skeletal myofibrils, where it may act as a soluble relaxing factor facilitating the Ca2+-mediated relaxation phase. It is also expressed in rapidly firing neurons, particularly GABA-ergic neurons, and thus may confer protection against Ca2+ toxicity. The major role of alpha-parvalbumin is metal buffering and transport of Ca2+. It binds different metal cations, and exhibits very high affinity for Ca2+ and physiologically significant affinity for Mg2+. Alpha-parvalbumin is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Both metal ion-binding sites in alpha-parvalbumin are high-affinity sites. Additionally, in contrast to beta-parvalbumin, alpha-parvalbumin is less acidic and has an additional residue in the C-terminal helix.


Pssm-ID: 319997 [Multi-domain]  Cd Length: 101  Bit Score: 37.11  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 292 GTIDFREY--VIGLSvlcnpANTEETIQMAFNLFDVDDDGSITEEEFACILR----SSLGVPDLDVSQLFKEIDTDHSGK 365
Cdd:cd16254    15 DSFDYKKFfeMVGLK-----KKSADDVKKVFHILDKDKSGFIEEDELKFVLKgfspDGRDLSDKETKALLAAGDKDGDGK 89


                  ....*.
gi 1985438074 366 IAYNEF 371
Cdd:cd16254    90 IGIDEF 95
S-100A10_like cd05031
S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of ...
 264-308 3.03e-03

S-100A10_like: S-100A10 domain found in proteins similar to S100A10. S100A10 is a member of the S100 family of EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1_like group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. A unique feature of S100A10 is that it contains mutation in both of the calcium binding sites, making it calcium insensitive. S100A10 has been detected in brain, heart, gastrointestinal tract, kidney, liver, lung, spleen, testes, epidermis, aorta, and thymus. Structural data supports the homo- and hetero-dimeric as well as hetero-tetrameric nature of the protein. S100A10 has multiple binding partners in its calcium free state and is therefore involved in many diverse biological functions.


Pssm-ID: 240157 [Multi-domain]  Cd Length: 94  Bit Score: 37.02  E-value: 3.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985438074 264 ME-EFAEYLK-----LPVSDVLKELfllfDRNGDGTIDFREY---VIGLSVLCN 308
Cdd:cd05031    36 MEkELSEFLKnqkdpMAVDKIMKDL----DQNRDGKVNFEEFvslVAGLSIACE 85
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
259-337 3.30e-03

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 38.89  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 259 GGRIGMEEFAEYLKLP--------VSDVLKELFLLFDRNGDGTIDFREYVIGLSVLCNPANTEETiqmaFNLFDVDDDGS 330
Cdd:NF041410   77 DGSLSSDELAAAAPPPppppdqapSTELADDLLSALDTDGDGSISSDELSAGLTSAGSSADSSQL----FSALDSDGDGS 152


                  ....*..
gi 1985438074 331 ITEEEFA 337
Cdd:NF041410  153 VSSDELA 159
EFh_PEF_peflin cd16184
EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed ...
 258-371 3.70e-03

EF-hand, calcium binding motif, found in peflin and similar proteins; Peflin, also termed penta-EF hand (PEF) protein with a long N-terminal hydrophobic domain, or penta-EF hand domain-containing protein 1, is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+. In lower vertebrates, peflin may interact with transient receptor potential N (TRPN1), suggesting a potential role of peflin in fast transducer channel adaptation.


Pssm-ID: 320059 [Multi-domain]  Cd Length: 165  Bit Score: 38.01  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 258 KGGRIGMEEFAE---YLKlpvsdVLKELFLLFDRNGDGTIDFREyviglsvLCNPAN------TEETIQMAFNLFDVDDD 328
Cdd:cd16184    50 KSGTIDIYEFQAlwnYIQ-----QWKQVFQQFDRDRSGSIDENE-------LHQALSqmgyrlSPQFVQFLVSKYDPRAR 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1985438074 329 GSITEEEF--ACILRSSLgvpdldvSQLFKEIDTDHSG--KIAYNEF 371
Cdd:cd16184   118 RSLTLDQFiqVCVQLQSL-------TDAFRQRDTQMTGtiTISYEDF 157
EFh_CREC_RCN2 cd16224
EF-hand, calcium binding motif, found in reticulocalbin-2 (RCN2); RCN2, also termed ...
 254-370 3.75e-03

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


Pssm-ID: 320022 [Multi-domain]  Cd Length: 268  Bit Score: 38.95  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 254 ANASKGGRIGMEEFAEY---------LKLPVSDVLKElfllFDRNGDGTIDFREYvigLSVLCNPANTEETIQMAF---- 320
Cdd:cd16224   133 ANTDGGPGLNLTEFIAFehpeevdymTEFVIQEALEE----HDKDGDGFISLEEF---LGDYRKDPTANEDPEWIIvekd 205

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1985438074 321 ---NLFDVDDDGSIT-EEEFACILRSSLGVPDLDVSQLFKEIDTDHSGKIAYNE 370
Cdd:cd16224   206 rfvNDYDKDNDGKLDpQELLPWVVPNNYGIAQEEALHLIDEMDLNGDGRLSEEE 259
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 279-374 4.17e-03

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


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 38.93  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 279 LKELFL-LFDRNGDGTIDFREyviglsvLCNPANTEETIQMafnLFDVDDDgsiteeefaciLRSSLgvpdlDVSQLFKE 357
Cdd:cd16179    50 LKEEFMeAYDENQDGRIDIRE-------LAQLLPTEENFLL---LFRRDNP-----------LDSSV-----EFMKVWRE 103

                          90
                  ....*....|....*..
gi 1985438074 358 IDTDHSGKIAYNEFKDF 374
Cdd:cd16179   104 YDKDNSGYIEADELKNF 120
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 221-366 4.92e-03

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 37.59  E-value: 4.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 221 PMEAGLVEFTKISKKLNLKWDPIRDQLDTFAA---IANASKG--GRIGMEEFAE---YLKLpvsdvLKELFLLFDRNGDG 292
Cdd:cd16182    13 DEEIDAVELQKLLNASLLKDMPKFDGFSLETCrslIALMDTNgsGRLDLEEFKTlwsDLKK-----WQAIFKKFDTDRSG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985438074 293 TID---FREYVIGLSVLCNPanteetiqmafNLFDV------DDDGSITEEEF-ACILRsslgvpdLDVS-QLFKEIDTD 361
Cdd:cd16182    88 TLSsyeLRKALESAGFHLSN-----------KVLQAlvlryaDSTGRITFEDFvSCLVR-------LKTAfETFSALDKK 149


                  ....*
gi 1985438074 362 HSGKI 366
Cdd:cd16182   150 NEGVI 154
S-100A1 cd05025
S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding ...
 275-308 4.95e-03

S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding protein belonging to a large S100 vertebrate-specific protein family within the EF-hand superfamily of calcium-binding proteins. Note that the S-100 hierarchy, to which this S-100A1 group belongs, contains only S-100 EF-hand domains, other EF-hands have been modeled separately. As is the case with many other members of S100 protein family, S100A1 is implicated in intracellular and extracellular regulatory activities, including interaction with myosin-associated twitchin kinase, actin-capping protein CapZ, sinapsin I, and tubulin. Structural data suggests that S100A1 proteins exist within cells as antiparallel homodimers, while heterodimers with S100A4 and S100B also has been reported. Upon binding calcium S100A1 changes conformation to expose a hydrophobic cleft which is the interaction site of S100A1 with its more that 20 known target proteins.


Pssm-ID: 240152 [Multi-domain]  Cd Length: 92  Bit Score: 36.40  E-value: 4.95e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1985438074 275 VSDVLKELfllfDRNGDGTIDFREYVI---GLSVLCN 308
Cdd:cd05025    54 VDKIMKEL----DENGDGEVDFQEFVVlvaALTVACN 86
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 350-374 6.41e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 33.91  E-value: 6.41e-03
                          10        20
                  ....*....|....*....|....*
gi 1985438074 350 DVSQLFKEIDTDHSGKIAYNEFKDF 374
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKEL 25
EF-hand_6 pfam13405
EF-hand domain;
279-306 6.89e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.07  E-value: 6.89e-03
                          10        20
                  ....*....|....*....|....*...
gi 1985438074 279 LKELFLLFDRNGDGTIDFREYVIGLSVL 306
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKALRSL 29
EFh_parvalbumins cd16253
EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, ...
 301-375 7.20e-03

EF-hand, calcium binding motif, found in parvalbumins; Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319996 [Multi-domain]  Cd Length: 101  Bit Score: 36.00  E-value: 7.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1985438074 301 IGLSvlcnpANTEETIQMAFNLFDVDDDGSITEEEFACILRS-SLGVPDL---DVSQLFKEIDTDHSGKIAYNEFKDFA 375
Cdd:cd16253    26 VGLS-----KKSPADIKKVFNILDQDKSGFIEEEELKLFLKNfSDGARVLsdkETKNFLAAGDSDGDGKIGVDEFKSMV 99
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 350-374 8.40e-03

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 33.89  E-value: 8.40e-03
                           10        20
                   ....*....|....*....|....*
gi 1985438074  350 DVSQLFKEIDTDHSGKIAYNEFKDF 374
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDL 25
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 308-372 9.08e-03

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


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 36.85  E-value: 9.08e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985438074 308 NPANtEETIQMAFNLFDVDDDGSITEEEFAcilrsSLGVPDLDVSQLFKEIDTDHSGKIAYNEFK 372
Cdd:cd16183    32 TPFN-PETVRLMIGMFDRDNSGTINFQEFA-----ALWKYITDWQNCFRSFDRDNSGNIDKNELK 90
 
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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