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Conserved domains on  [gi|33946291|ref|NP_079106|]
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lysophosphatidylcholine acyltransferase 1 [Homo sapiens]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 12959277)

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; ...
 103-314 6.29e-98

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: 295.28  E-value: 6.29e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 103 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQD 181
Cdd:cd07991   1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 182 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPNKLDTITWTWQGPGALEILWLT 261
Cdd:cd07991  80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 33946291 262 LCQFHNQVEIEFLPVYSPSEEEKrNPALYASNVRRVMAEALGVSVTDYTFEDC 314
Cdd:cd07991 159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
EF-hand_8 pfam13833
EF-hand domain pair;
432-483 2.47e-07

EF-hand domain pair;


:

Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 47.31  E-value: 2.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 33946291   432 EDGSVGEGDLSCILKTaLGVAELT---VTDLFRAIDQEEKGKITFADFHRFAEMY 483
Cdd:pfam13833   1 EKGVITREELKRALAL-LGLKDLSedeVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
370-494 1.17e-05

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 370 AEFAASLEvpvsDLLEDMFSLFDESGSGEVDLREcVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILkTAL 449
Cdd:COG5126  25 DDFEALFR----RLWATLFSEADTDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL-TAL 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 33946291 450 GVAELTVTDLFRAIDQEEKGKITFADFHrfaemypAFAEEYLYPD 494
Cdd:COG5126  99 GVSEEEADELFARLDTDGDGKISFEEFV-------AAVRDYYTPD 136
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 103-314 6.29e-98

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: 295.28  E-value: 6.29e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 103 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQD 181
Cdd:cd07991   1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 182 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPNKLDTITWTWQGPGALEILWLT 261
Cdd:cd07991  80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 33946291 262 LCQFHNQVEIEFLPVYSPSEEEKrNPALYASNVRRVMAEALGVSVTDYTFEDC 314
Cdd:cd07991 159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 88-303 1.30e-26

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: 107.40  E-value: 1.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291  88 PALWRKVVDFLLKAIMRTMWFAGGFhRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPIWG 164
Cdd:COG0204   5 FLLLRRFRYRLVRLWARLLLRLLGV-RVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPrpvRFVAKKELFKIPLLG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 165 TLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLRYPN 240
Cdd:COG0204  84 WLLRALGAIPVDRSKRRAALRALRQAVEALK-AGES--LVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDGTE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33946291 241 KLDTITWtWQGPGaleilwltlcqfhnQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAEALG 303
Cdd:COG0204 161 RALPKGF-LPRPG--------------KVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 129-238 4.30e-22

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: 91.65  E-value: 4.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291    129 ILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKwpq 202
Cdd:smart00563   1 ALVVANHQSFLDPLvlsallPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGEW--- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 33946291    203 IMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLRY 238
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 114-236 1.19e-19

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: 85.02  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291   114 RVAVKGRQALPTEAAILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTV 187
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLllslalYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 33946291   188 EEIKRRaQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVL 236
Cdd:pfam01553  81 EYLVEL-LREGKL--VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPVAI 130
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 115-237 1.07e-13

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: 68.14  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291   115 VAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ---DSRRKTVE 188
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFpppIVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALKAAI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 33946291   189 EIKRRAQSngkwpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLR 237
Cdd:TIGR00530  84 EVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
PLN02833 PLN02833
glycerol acyltransferase family protein
 46-242 2.25e-07

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 53.24  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291   46 VALMTLTLFPVRLLVaaamMLLAWPLALVASLGS--AEKEPEQPPALWRKVVDFLLKAimrtmwFAGGFHRVaVKGRQAL 123
Cdd:PLN02833  90 VVIRYGILFPVRVLL----LAIGWIIFLSAFIPVhfLLKGHKLRKKIERKLVELICSA------FVASWTGV-IKYHGPR 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291  124 PTE-AAILTLAPHSSYFDAIPVT-MTMSSIVMKAEsrdiPIWGTLIQ-----YIRPVFVSRSDQDSRRKTVEEIKRRAQS 196
Cdd:PLN02833 159 PSRrPKQVFVANHTSMIDFIVLEqMTPFAVIMQKH----PGWVGFLQntileSVGCIWFNRTEAKDREVVAKKLRDHVQD 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 33946291  197 NGKWPqIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYpNKL 242
Cdd:PLN02833 235 PDRNP-LLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKY-NKI 278
EF-hand_8 pfam13833
EF-hand domain pair;
432-483 2.47e-07

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 47.31  E-value: 2.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 33946291   432 EDGSVGEGDLSCILKTaLGVAELT---VTDLFRAIDQEEKGKITFADFHRFAEMY 483
Cdd:pfam13833   1 EKGVITREELKRALAL-LGLKDLSedeVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
370-494 1.17e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 370 AEFAASLEvpvsDLLEDMFSLFDESGSGEVDLREcVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILkTAL 449
Cdd:COG5126  25 DDFEALFR----RLWATLFSEADTDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL-TAL 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 33946291 450 GVAELTVTDLFRAIDQEEKGKITFADFHrfaemypAFAEEYLYPD 494
Cdd:COG5126  99 GVSEEEADELFARLDTDGDGKISFEEFV-------AAVRDYYTPD 136
PTZ00184 PTZ00184
calmodulin; Provisional
 384-478 2.93e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 41.29  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291  384 LEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILkTALG--VAELTVTDLFR 461
Cdd:PTZ00184  49 LQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEVDEMIR 127

                         90
                 ....*....|....*..
gi 33946291  462 AIDQEEKGKITFADFHR 478
Cdd:PTZ00184 128 EADVDGDGQINYEEFVK 144
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 366-482 2.20e-03

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 39.05  E-value: 2.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 366 KIGIAEFAAslevpVSDLLEDM---FSLFDESGSGEVDLRECVVALsvvcrpaRTL------DTIQLAFKMYGAQEDGSV 436
Cdd:cd16180  53 TINFDEFVG-----LWKYIQDWrrlFRRFDRDRSGSIDFNELQNAL-------SSFgyrlspQFVQLLVRKFDRRRRGSI 120

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 33946291 437 GEGD---LSCILKtalgvaelTVTDLFRAIDQEEKGKITFaDFHRFAEM 482
Cdd:cd16180 121 SFDDfveACVTLK--------RLTDAFRKYDTNRTGYATI-SYEDFLTM 160
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 103-314 6.29e-98

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: 295.28  E-value: 6.29e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 103 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQD 181
Cdd:cd07991   1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 182 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPNKLDTITWTWQGPGALEILWLT 261
Cdd:cd07991  80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 33946291 262 LCQFHNQVEIEFLPVYSPSEEEKrNPALYASNVRRVMAEALGVSVTDYTFEDC 314
Cdd:cd07991 159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 88-303 1.30e-26

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: 107.40  E-value: 1.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291  88 PALWRKVVDFLLKAIMRTMWFAGGFhRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPIWG 164
Cdd:COG0204   5 FLLLRRFRYRLVRLWARLLLRLLGV-RVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPrpvRFVAKKELFKIPLLG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 165 TLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLRYPN 240
Cdd:COG0204  84 WLLRALGAIPVDRSKRRAALRALRQAVEALK-AGES--LVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDGTE 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 33946291 241 KLDTITWtWQGPGaleilwltlcqfhnQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAEALG 303
Cdd:COG0204 161 RALPKGF-LPRPG--------------KVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 107-299 1.08e-25

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: 104.03  E-value: 1.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 107 WFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTM-------TMSSIVMKAES-RDIPIWGTLiqyiRPVFVSRS 178
Cdd:cd06551   6 LNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLllerglrRDVYGLMDEELlERYPFFTRL----GAFSVDRD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 179 DQDSRRKTVEEIKRRAQSNGKWpqIMIFPEGTCTN-RTCLITFKPGAFIP----GAPVQPVVLRYPNkldtitwtwqgpg 253
Cdd:cd06551  82 SPRSAAKSLKYVARLLSKPGSV--VWIFPEGTRTRrDKRPLQFKPGVAHLaekaGVPIVPVALRYTF------------- 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 33946291 254 aleilWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMA 299
Cdd:cd06551 147 -----ELFEQFPEIFVRIGPPIPYAETALGEELAAELANRLTRLLD 187
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 106-285 2.48e-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: 2.48e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 106 MWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDS 182
Cdd:cd07989   3 LLLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALprpIRFVAKKELFKIPFLGWLLRLLGAIPIDRGNGRS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 183 RRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLRYPNKLDTITWTWQGPGaleil 258
Cdd:cd07989  83 AREALREAIEALK-EGES--VVIFPEGTRSRDGELLPFKSGAFRlakeAGVPIVPVAISGTWGSLPKGKKLPRPG----- 154

                       170       180
                ....*....|....*....|....*..
gi 33946291 259 wltlcqfhnQVEIEFLPVYSPSEEEKR 285
Cdd:cd07989 155 ---------RVTVRIGEPIPPEGLELA 172
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 129-238 4.30e-22

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: 91.65  E-value: 4.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291    129 ILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKwpq 202
Cdd:smart00563   1 ALVVANHQSFLDPLvlsallPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGEW--- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 33946291    203 IMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLRY 238
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 114-236 1.19e-19

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: 85.02  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291   114 RVAVKGRQALPTEAAILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTV 187
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLllslalYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 33946291   188 EEIKRRaQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVL 236
Cdd:pfam01553  81 EYLVEL-LREGKL--VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPVAI 130
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 115-237 1.07e-13

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: 68.14  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291   115 VAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ---DSRRKTVE 188
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFpppIVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALKAAI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 33946291   189 EIKRRAQSngkwpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLR 237
Cdd:TIGR00530  84 EVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 91-241 2.00e-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: 60.35  E-value: 2.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291  91 WRKVVDFLLKaimrtmWFaggFHRVAVKGRQALPTEAAILTLAPHS-SYFDAIPVTMTMS---SIVMKAESRDIPIWGTL 166
Cdd:cd07992   1 VRLLSRVILR------IY---FRRITVVGRENVPKDGPVIFLGNHPnALIDPLLLAATLRrpvRFLAKADLFKNPLIGWL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 167 IQYIRPVFVSRsDQDSRRKTVEEIK--------RRAQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----------PG 228
Cdd:cd07992  72 LESFGAIPVYR-PKDLARGGIGKISnaavfdavGEALKAGGA--IGIFPEGGSHDRPRLLPLKAGAARmalealeagqKD 148

                       170
                ....*....|...
gi 33946291 229 APVQPVVLRYPNK 241
Cdd:cd07992 149 VKIVPVGLNYEDK 161
PLN02833 PLN02833
glycerol acyltransferase family protein
 46-242 2.25e-07

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 53.24  E-value: 2.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291   46 VALMTLTLFPVRLLVaaamMLLAWPLALVASLGS--AEKEPEQPPALWRKVVDFLLKAimrtmwFAGGFHRVaVKGRQAL 123
Cdd:PLN02833  90 VVIRYGILFPVRVLL----LAIGWIIFLSAFIPVhfLLKGHKLRKKIERKLVELICSA------FVASWTGV-IKYHGPR 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291  124 PTE-AAILTLAPHSSYFDAIPVT-MTMSSIVMKAEsrdiPIWGTLIQ-----YIRPVFVSRSDQDSRRKTVEEIKRRAQS 196
Cdd:PLN02833 159 PSRrPKQVFVANHTSMIDFIVLEqMTPFAVIMQKH----PGWVGFLQntileSVGCIWFNRTEAKDREVVAKKLRDHVQD 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 33946291  197 NGKWPqIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYpNKL 242
Cdd:PLN02833 235 PDRNP-LLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKY-NKI 278
EF-hand_8 pfam13833
EF-hand domain pair;
432-483 2.47e-07

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 47.31  E-value: 2.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 33946291   432 EDGSVGEGDLSCILKTaLGVAELT---VTDLFRAIDQEEKGKITFADFHRFAEMY 483
Cdd:pfam13833   1 EKGVITREELKRALAL-LGLKDLSedeVDILFREFDTDGDGYISFDEFCVLLERR 54
EF-hand_7 pfam13499
EF-hand domain pair;
419-480 1.57e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 45.71  E-value: 1.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33946291   419 DTIQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELT---VTDLFRAIDQEEKGKITFADFHRFA 480
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSdeeVEELFKEFDLDKDGRISFEEFLELY 66
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 92-237 7.42e-06

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 48.77  E-value: 7.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291    92 RKVVDFLLKAIMrtMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPiwgtliq 168
Cdd:PRK08633  408 LLLPDSLLRFLL--LLLMHTRYRLRVEGRENIPAKGGALLLGNHVSWIDWALLQAASPrpiRFVMERSIYEKW------- 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291   169 YIRPVF-------VSrsdQDSRRKTVEEIkRRAQSNGKwpQIMIFPEGTCTNRTCLITFKPG----AFIPGAPVQPVVLR 237
Cdd:PRK08633  479 YLKWFFklfgvipIS---SGGSKESLEFI-RKALDDGE--VVCIFPEGAITRNGQLNEFKRGfeliVKGTDVPIIPFYIR 552
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
370-494 1.17e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 45.17  E-value: 1.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 370 AEFAASLEvpvsDLLEDMFSLFDESGSGEVDLREcVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILkTAL 449
Cdd:COG5126  25 DDFEALFR----RLWATLFSEADTDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL-TAL 98

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 33946291 450 GVAELTVTDLFRAIDQEEKGKITFADFHrfaemypAFAEEYLYPD 494
Cdd:COG5126  99 GVSEEEADELFARLDTDGDGKISFEEFV-------AAVRDYYTPD 136
PTZ00184 PTZ00184
calmodulin; Provisional
 384-478 2.93e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 41.29  E-value: 2.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291  384 LEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILkTALG--VAELTVTDLFR 461
Cdd:PTZ00184  49 LQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEVDEMIR 127

                         90
                 ....*....|....*..
gi 33946291  462 AIDQEEKGKITFADFHR 478
Cdd:PTZ00184 128 EADVDGDGQINYEEFVK 144
LPLAT_LCLAT1-like cd07990
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; ...
 123-210 1.36e-03

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-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 Lysocardiolipin acyltransferase 1 (LCLAT1) or 1-acyl-sn-glycerol-3-phosphate acyltransferase and similar proteins.


Pssm-ID: 153252 [Multi-domain]  Cd Length: 193  Bit Score: 39.91  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 123 LPTEAAILtLAPHSSYFDAIpVTMTMSS---------IVMKAESRDIPI--WGTLIQYIrpVFVSRS---DQDSRRKTVE 188
Cdd:cd07990  21 LPKERALI-ISNHRSEVDWL-VLWMLADrfgrlgrlkIVLKDSLKYPPLggWGWQLGEF--IFLKRKwekDEKTIKRQLK 96

                        90       100
                ....*....|....*....|..
gi 33946291 189 EIKRRAQSNgkwpQIMIFPEGT 210
Cdd:cd07990  97 RLKDSPEPF----WLLIFPEGT 114
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 366-482 2.20e-03

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 39.05  E-value: 2.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 366 KIGIAEFAAslevpVSDLLEDM---FSLFDESGSGEVDLRECVVALsvvcrpaRTL------DTIQLAFKMYGAQEDGSV 436
Cdd:cd16180  53 TINFDEFVG-----LWKYIQDWrrlFRRFDRDRSGSIDFNELQNAL-------SSFgyrlspQFVQLLVRKFDRRRRGSI 120

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 33946291 437 GEGD---LSCILKtalgvaelTVTDLFRAIDQEEKGKITFaDFHRFAEM 482
Cdd:cd16180 121 SFDDfveACVTLK--------RLTDAFRKYDTNRTGYATI-SYEDFLTM 160
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 112-236 2.46e-03

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


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 39.33  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291  112 FHRVAVKGRQALPT-EAAILTLAPHSSYFDaIPVTMTMS---SIVMKAESRDIPIWGTLIQYIRPVFVSRSDqdsRRKTV 187
Cdd:PLN02901  34 FYKIEVEGLENLPSpDEPAVYVSNHQSFLD-IYTLFHLGrpfKFISKTSIFLIPIIGWAMYMTGHIPLKRMD---RRSQL 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 33946291  188 EEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVL 236
Cdd:PLN02901 110 ECLKRCMELLKKGASVFFFPEGTRSKDGKLAAFKKGAFSvaakTGVPVVPITL 162
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 366-479 9.20e-03

EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 37.19  E-value: 9.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33946291 366 KIGIAEFAAslevpVSDLLEDM---FSLFDESGSGEVDLRECVVALSvvcRPARTLD--TIQLAFKMYGAQEDGSVGEGD 440
Cdd:cd16185  52 TIDFEEFAA-----LHQFLSNMqngFEQRDTSRSGRLDANEVHEALA---ASGFQLDppAFQALFRKFDPDRGGSLGFDD 123

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 33946291 441 ---LSCILKTAlgvaeltvTDLFRAIDQEEKGKITFaDFHRF 479
Cdd:cd16185 124 yieLCIFLASA--------RNLFQAFDRQRTGRVTL-DFNQF 156
 
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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