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Conserved domains on  [gi|1191845820|ref|XP_020932320|]
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lysophosphatidylcholine acyltransferase 1 isoform X2 [Sus scrofa]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11578502)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 112-323 1.84e-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: 296.82  E-value: 1.84e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 112 MRAMWFAGGFHRVAVKGRQAPPaEATILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIKYIRPVFVSRSDQD 190
Cdd:cd07991     1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 191 SRRKTVEEIKRRAQaGGRWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNSLDTITWTWQGPGALKILWLT 270
Cdd:cd07991    80 DRKKVVEEIKERAT-DPNWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 271 LCQFHNQVEIEFLPVYHPSeEEKKDPALYASNVRRVMAQALGISVTDYTFEDC 323
Cdd:cd07991   159 LTQPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDK 210
EF-hand_8 pfam13833
EF-hand domain pair;
441-490 1.32e-06

EF-hand domain pair;


:

Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 45.38  E-value: 1.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 441 EGGSIDEDTLSSILKTaLGVAELT---VTGLFRAIDQEEKGRITFDDFKRFAE 490
Cdd:pfam13833   1 EKGVITREELKRALAL-LGLKDLSedeVDILFREFDTDGDGYISFDEFCVLLE 52
EFh_PEF super family cl25352
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 374-485 3.29e-06

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


The actual alignment was detected with superfamily member cd16185:

Pssm-ID: 355382 [Multi-domain]  Cd Length: 163  Bit Score: 47.21  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 374 GRVSLPEFAAQLEVP---QSEAL-QDLFSLFDESGSGEMDLREFvVALsvvcrpSRTLDTVQLAFKMYGSQEGGSIDEDT 449
Cdd:cd16185    15 GSIDVNELQKALAGGgllFSLATaEKLIRMFDRDGNGTIDFEEF-AAL------HQFLSNMQNGFEQRDTSRSGRLDANE 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1191845820 450 LSSILKTA-LGVAELTVTGLFRAIDQEEKGRITFDDF 485
Cdd:cd16185    88 VHEALAASgFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 112-323 1.84e-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: 296.82  E-value: 1.84e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 112 MRAMWFAGGFHRVAVKGRQAPPaEATILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIKYIRPVFVSRSDQD 190
Cdd:cd07991     1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 191 SRRKTVEEIKRRAQaGGRWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNSLDTITWTWQGPGALKILWLT 270
Cdd:cd07991    80 DRKKVVEEIKERAT-DPNWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 271 LCQFHNQVEIEFLPVYHPSeEEKKDPALYASNVRRVMAQALGISVTDYTFEDC 323
Cdd:cd07991   159 LTQPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDK 210
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 97-312 6.89e-28

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: 110.87  E-value: 6.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820  97 LALWRKVVDLLLKAIMRAMWFAGGFhRVAVKGRQAPPAEATILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPIWG 173
Cdd:COG0204     5 FLLLRRFRYRLVRLWARLLLRLLGV-RVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPrpvRFVAKKELFKIPLLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 174 TLIKYIRPVFVSRSDQDSRRKTVEEIKRRAQAGGrwpQIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRYpn 249
Cdd:COG0204    84 WLLRALGAIPVDRSKRRAALRALRQAVEALKAGE---SLVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG-- 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 250 sldtiTWTWQGPGALKilwltlcqFHNQVEIEFLPVYHPSEEEKKDPALYASNVRRVMAQALG 312
Cdd:COG0204   159 -----TERALPKGFLP--------RPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 138-247 5.23e-23

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: 93.96  E-value: 5.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820  138 ILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIKYIRPVFVSRSDQDSRRKTVEEIKRRAQAGGrwpQ 211
Cdd:smart00563   1 ALVVANHQSFLDPLvlsallPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGE---W 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1191845820  212 IMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRY 247
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 123-245 8.86e-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: 82.71  E-value: 8.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 123 RVAVKGRQAPPAEATILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIKYIRPVFVSRSDQDSRRKTV 196
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLllslalYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 197 EEIKRRAQAGGRwpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVL 245
Cdd:pfam01553  81 EYLVELLREGKL---VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPVAI 130
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 124-246 2.50e-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: 63.90  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 124 VAVKGRQAPPAEATILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIKYIRPVFVSRSDQ---DSRRKTVE 197
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFpppIVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALKAAI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 198 EIKRRAQAggrwpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLR 246
Cdd:TIGR00530  84 EVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
PLN02833 PLN02833
glycerol acyltransferase family protein
 55-247 6.24e-08

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 54.78  E-value: 6.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820  55 VAVMTLTLFPARLLFaafmMLLAWPLALVASLGSAEREPEQPL--ALWRKVVDLLlkaimrAMWFAGGFHRVAVKGRQAP 132
Cdd:PLN02833   90 VVIRYGILFPVRVLL----LAIGWIIFLSAFIPVHFLLKGHKLrkKIERKLVELI------CSAFVASWTGVIKYHGPRP 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 133 PAEATILTLAPHSSYFDAIPVT-MTMSSIVMKAEsrdiPIW-----GTLIKYIRPVFVSRSDQDSRRKTVEEIKRRAQAG 206
Cdd:PLN02833  160 SRRPKQVFVANHTSMIDFIVLEqMTPFAVIMQKH----PGWvgflqNTILESVGCIWFNRTEAKDREVVAKKLRDHVQDP 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1191845820 207 GRWPqIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRY 247
Cdd:PLN02833  236 DRNP-LLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKY 275
EF-hand_8 pfam13833
EF-hand domain pair;
441-490 1.32e-06

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 45.38  E-value: 1.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 441 EGGSIDEDTLSSILKTaLGVAELT---VTGLFRAIDQEEKGRITFDDFKRFAE 490
Cdd:pfam13833   1 EKGVITREELKRALAL-LGLKDLSedeVDILFREFDTDGDGYISFDEFCVLLE 52
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 374-485 3.29e-06

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: 47.21  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 374 GRVSLPEFAAQLEVP---QSEAL-QDLFSLFDESGSGEMDLREFvVALsvvcrpSRTLDTVQLAFKMYGSQEGGSIDEDT 449
Cdd:cd16185    15 GSIDVNELQKALAGGgllFSLATaEKLIRMFDRDGNGTIDFEEF-AAL------HQFLSNMQNGFEQRDTSRSGRLDANE 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1191845820 450 LSSILKTA-LGVAELTVTGLFRAIDQEEKGRITFDDF 485
Cdd:cd16185    88 VHEALAASgFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
374-488 3.51e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.71  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 374 GRVSLPEFAAQLEvpqsEALQDLFSLFDESGSGEMDLREFVVALSVVCRPSRTlDTVQLAFKMYGSQEGGSIDEDTLSSI 453
Cdd:COG5126    20 GVLERDDFEALFR----RLWATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRL 94

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1191845820 454 LkTALGVAELTVTGLFRAIDQEEKGRITFDDFKRF 488
Cdd:COG5126    95 L-TALGVSEEEADELFARLDTDGDGKISFEEFVAA 128
PTZ00184 PTZ00184
calmodulin; Provisional
 388-487 2.77e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 41.29  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 388 PQSEALQDLFSLFDESGSGEMDLREFVVALSVVCRPSRTLDTVQLAFKMYGSQEGGSIDEDTLSSILkTALG--VAELTV 465
Cdd:PTZ00184   44 PTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEV 122

                          90       100
                  ....*....|....*....|..
gi 1191845820 466 TGLFRAIDQEEKGRITFDDFKR 487
Cdd:PTZ00184  123 DEMIREADVDGDGQINYEEFVK 144
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 112-323 1.84e-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: 296.82  E-value: 1.84e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 112 MRAMWFAGGFHRVAVKGRQAPPaEATILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIKYIRPVFVSRSDQD 190
Cdd:cd07991     1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 191 SRRKTVEEIKRRAQaGGRWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNSLDTITWTWQGPGALKILWLT 270
Cdd:cd07991    80 DRKKVVEEIKERAT-DPNWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 271 LCQFHNQVEIEFLPVYHPSeEEKKDPALYASNVRRVMAQALGISVTDYTFEDC 323
Cdd:cd07991   159 LTQPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDK 210
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 97-312 6.89e-28

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: 110.87  E-value: 6.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820  97 LALWRKVVDLLLKAIMRAMWFAGGFhRVAVKGRQAPPAEATILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPIWG 173
Cdd:COG0204     5 FLLLRRFRYRLVRLWARLLLRLLGV-RVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPrpvRFVAKKELFKIPLLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 174 TLIKYIRPVFVSRSDQDSRRKTVEEIKRRAQAGGrwpQIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRYpn 249
Cdd:COG0204    84 WLLRALGAIPVDRSKRRAALRALRQAVEALKAGE---SLVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG-- 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 250 sldtiTWTWQGPGALKilwltlcqFHNQVEIEFLPVYHPSEEEKKDPALYASNVRRVMAQALG 312
Cdd:COG0204   159 -----TERALPKGFLP--------RPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 116-308 6.26e-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: 101.72  E-value: 6.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 116 WFAGGFHRVAVKGRQAPPAEATILTLAPHSSYFDAIPVTM-------TMSSIVMKAES-RDIPIWGTLikyiRPVFVSRS 187
Cdd:cd06551     6 LNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLllerglrRDVYGLMDEELlERYPFFTRL----GAFSVDRD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 188 DQDSRRKTVEEIKRRAQAGGRWpqIMIFPEGTCTN-RTCLITFKPGAFIP----GVPVQPVVLRYPNsldtitwtwqgpg 262
Cdd:cd06551    82 SPRSAAKSLKYVARLLSKPGSV--VWIFPEGTRTRrDKRPLQFKPGVAHLaekaGVPIVPVALRYTF------------- 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1191845820 263 alkilWLTLCQFHNQVEIEFLPVYHPSEEEKKDPALYASNVRRVMA 308
Cdd:cd06551   147 -----ELFEQFPEIFVRIGPPIPYAETALGEELAAELANRLTRLLD 187
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 115-295 5.09e-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: 96.19  E-value: 5.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 115 MWFAGGFHRVAVKGRQAPPAEATILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIKYIRPVFVSRSDQDS 191
Cdd:cd07989     3 LLLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALprpIRFVAKKELFKIPFLGWLLRLLGAIPIDRGNGRS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 192 RRKTVEEIKRRAQAGGRwpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRYpnsldtiTWTWQGPGALKIL 267
Cdd:cd07989    83 AREALREAIEALKEGES---VVIFPEGTRSRDGELLPFKSGAFRlakeAGVPIVPVAISG-------TWGSLPKGKKLPR 152

                         170       180
                  ....*....|....*....|....*...
gi 1191845820 268 WLTlcqfhnqVEIEFLPVYHPSEEEKKD 295
Cdd:cd07989   153 PGR-------VTVRIGEPIPPEGLELAE 173
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 138-247 5.23e-23

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: 93.96  E-value: 5.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820  138 ILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIKYIRPVFVSRSDQDSRRKTVEEIKRRAQAGGrwpQ 211
Cdd:smart00563   1 ALVVANHQSFLDPLvlsallPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGE---W 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1191845820  212 IMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRY 247
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 123-245 8.86e-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: 82.71  E-value: 8.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 123 RVAVKGRQAPPAEATILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIKYIRPVFVSRSDQDSRRKTV 196
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLllslalYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 197 EEIKRRAQAGGRwpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVL 245
Cdd:pfam01553  81 EYLVELLREGKL---VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPVAI 130
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 124-246 2.50e-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: 63.90  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 124 VAVKGRQAPPAEATILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIKYIRPVFVSRSDQ---DSRRKTVE 197
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFpppIVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALKAAI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 198 EIKRRAQAggrwpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLR 246
Cdd:TIGR00530  84 EVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 100-247 3.62e-08

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: 53.80  E-value: 3.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 100 WRKVVDLLLKaimramWFaggFHRVAVKGRQAPPAEATILTLAPHS-SYFDAIPVTMTMS---SIVMKAESRDIPIWGTL 175
Cdd:cd07992     1 VRLLSRVILR------IY---FRRITVVGRENVPKDGPVIFLGNHPnALIDPLLLAATLRrpvRFLAKADLFKNPLIGWL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 176 IKYIRPVFVSRsDQDSRRKTVEEIKRRA---------QAGGRwpqIMIFPEGTCTNRTCLITFKPGAFI----------P 236
Cdd:cd07992    72 LESFGAIPVYR-PKDLARGGIGKISNAAvfdavgealKAGGA---IGIFPEGGSHDRPRLLPLKAGAARmalealeagqK 147

                         170
                  ....*....|.
gi 1191845820 237 GVPVQPVVLRY 247
Cdd:cd07992   148 DVKIVPVGLNY 158
PLN02833 PLN02833
glycerol acyltransferase family protein
 55-247 6.24e-08

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 54.78  E-value: 6.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820  55 VAVMTLTLFPARLLFaafmMLLAWPLALVASLGSAEREPEQPL--ALWRKVVDLLlkaimrAMWFAGGFHRVAVKGRQAP 132
Cdd:PLN02833   90 VVIRYGILFPVRVLL----LAIGWIIFLSAFIPVHFLLKGHKLrkKIERKLVELI------CSAFVASWTGVIKYHGPRP 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 133 PAEATILTLAPHSSYFDAIPVT-MTMSSIVMKAEsrdiPIW-----GTLIKYIRPVFVSRSDQDSRRKTVEEIKRRAQAG 206
Cdd:PLN02833  160 SRRPKQVFVANHTSMIDFIVLEqMTPFAVIMQKH----PGWvgflqNTILESVGCIWFNRTEAKDREVVAKKLRDHVQDP 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1191845820 207 GRWPqIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRY 247
Cdd:PLN02833  236 DRNP-LLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKY 275
EF-hand_8 pfam13833
EF-hand domain pair;
441-490 1.32e-06

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 45.38  E-value: 1.32e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 441 EGGSIDEDTLSSILKTaLGVAELT---VTGLFRAIDQEEKGRITFDDFKRFAE 490
Cdd:pfam13833   1 EKGVITREELKRALAL-LGLKDLSedeVDILFREFDTDGDGYISFDEFCVLLE 52
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 374-485 3.29e-06

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: 47.21  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 374 GRVSLPEFAAQLEVP---QSEAL-QDLFSLFDESGSGEMDLREFvVALsvvcrpSRTLDTVQLAFKMYGSQEGGSIDEDT 449
Cdd:cd16185    15 GSIDVNELQKALAGGgllFSLATaEKLIRMFDRDGNGTIDFEEF-AAL------HQFLSNMQNGFEQRDTSRSGRLDANE 87

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1191845820 450 LSSILKTA-LGVAELTVTGLFRAIDQEEKGRITFDDF 485
Cdd:cd16185    88 VHEALAASgFQLDPPAFQALFRKFDPDRGGSLGFDDY 124
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
374-488 3.51e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.71  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 374 GRVSLPEFAAQLEvpqsEALQDLFSLFDESGSGEMDLREFVVALSVVCRPSRTlDTVQLAFKMYGSQEGGSIDEDTLSSI 453
Cdd:COG5126    20 GVLERDDFEALFR----RLWATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRL 94

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1191845820 454 LkTALGVAELTVTGLFRAIDQEEKGRITFDDFKRF 488
Cdd:COG5126    95 L-TALGVSEEEADELFARLDTDGDGKISFEEFVAA 128
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 374-491 5.54e-06

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: 46.44  E-value: 5.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 374 GRVSLPEFAAQLEVPQSeaLQDLFSLFDESGSGEMDLREFVVALSvvcRPSRTLD--TVQLAFKMYGSQEGGSIDEDTLS 451
Cdd:cd16185    51 GTIDFEEFAALHQFLSN--MQNGFEQRDTSRSGRLDANEVHEALA---ASGFQLDppAFQALFRKFDPDRGGSLGFDDYI 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1191845820 452 SIlktalgVAELTVTG-LFRAIDQEEKGRITFdDFKRFAEA 491
Cdd:cd16185   126 EL------CIFLASARnLFQAFDRQRTGRVTL-DFNQFVYA 159
EF-hand_7 pfam13499
EF-hand domain pair;
433-489 1.18e-05

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 43.01  E-value: 1.18e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 433 AFKMYGSQEGGSIDEDTLSSILKTALGVAELT---VTGLFRAIDQEEKGRITFDDFKRFA 489
Cdd:pfam13499   7 AFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSdeeVEELFKEFDLDKDGRISFEEFLELY 66
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 394-485 1.12e-04

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


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 42.90  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 394 QDLFSLFDESGSGEMDLREFVVAL-SVVCRPSRtlDTVQLAFKMYGSQEGGSIDEDT---LSSILKtalgvaelTVTGLF 469
Cdd:cd16180    70 RRLFRRFDRDRSGSIDFNELQNALsSFGYRLSP--QFVQLLVRKFDRRRRGSISFDDfveACVTLK--------RLTDAF 139

                          90
                  ....*....|....*...
gi 1191845820 470 RAIDQEEKGRIT--FDDF 485
Cdd:cd16180   140 RKYDTNRTGYATisYEDF 157
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 101-246 2.10e-04

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 44.14  E-value: 2.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820  101 RKVVDLLLKAIMraMWFAGGFHRVAVKGRQAPPAEATILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPiwgtlik 177
Cdd:PRK08633   408 LLLPDSLLRFLL--LLLMHTRYRLRVEGRENIPAKGGALLLGNHVSWIDWALLQAASPrpiRFVMERSIYEKW------- 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820  178 YIRPVF-------VSrsdQDSRRKTVEEIKRRAQAGgrwPQIMIFPEGTCTNRTCLITFKPG----AFIPGVPVQPVVLR 246
Cdd:PRK08633   479 YLKWFFklfgvipIS---SGGSKESLEFIRKALDDG---EVVCIFPEGAITRNGQLNEFKRGfeliVKGTDVPIIPFYIR 552
PTZ00184 PTZ00184
calmodulin; Provisional
 388-487 2.77e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 41.29  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 388 PQSEALQDLFSLFDESGSGEMDLREFVVALSVVCRPSRTLDTVQLAFKMYGSQEGGSIDEDTLSSILkTALG--VAELTV 465
Cdd:PTZ00184   44 PTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEV 122

                          90       100
                  ....*....|....*....|..
gi 1191845820 466 TGLFRAIDQEEKGRITFDDFKR 487
Cdd:PTZ00184  123 DEMIREADVDGDGQINYEEFVK 144
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
389-491 1.17e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 389 QSEALQDLFSLFDESGSGEMDLREFVVALSVVCRPsrtldtvqlAFKMYGSQEGGSIDEDTL-SSILKTALGVAELTVTG 467
Cdd:COG5126     3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLWAT---------LFSEADTDGDGRISREEFvAGMESLFEATVEPFARA 73

                          90       100
                  ....*....|....*....|....
gi 1191845820 468 LFRAIDQEEKGRITFDDFKRFAEA 491
Cdd:COG5126    74 AFDLLDTDGDGKISADEFRRLLTA 97
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 392-486 1.19e-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: 39.82  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 392 ALQDLFSLFDESGSGEMDLREFVVALSVVCRPSRTLDTVQLAFKMYGSQEGGSIDEDTLSSILKtalgvaelTVT---GL 468
Cdd:cd16180     1 ELRRIFQAVDRDRSGRISAKELQRALSNGDWTPFSIETVRLMINMFDRDRSGTINFDEFVGLWK--------YIQdwrRL 72

                          90
                  ....*....|....*...
gi 1191845820 469 FRAIDQEEKGRITFDDFK 486
Cdd:cd16180    73 FRRFDRDRSGSIDFNELQ 90
PTZ00183 PTZ00183
centrin; Provisional
 374-487 1.93e-03

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 39.29  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 374 GRVSLPEFAAQLEV----PQSEALQDLFSLFDESGSGEMDLREFVVALSVVCRPSRTLDTVQLAFKMYGSQEGGSIdedT 449
Cdd:PTZ00183   32 GTIDPKELKVAMRSlgfePKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKKLGERDPREEILKAFRLFDDDKTGKI---S 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1191845820 450 LSSILKTALGVAE-LTVTGLFRAIDQEEK---GRITFDDFKR 487
Cdd:PTZ00183  109 LKNLKRVAKELGEtITDEELQEMIDEADRngdGEISEEEFYR 150
LPLAT_LCLAT1-like cd07990
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; ...
 160-219 2.46e-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: 39.14  E-value: 2.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1191845820 160 IVMKAESRDIPI--WGTLI-KYIrpvFVSRS---DQDSRRKTVEEIKRRaqaggRWP-QIMIFPEGT 219
Cdd:cd07990    56 IVLKDSLKYPPLggWGWQLgEFI---FLKRKwekDEKTIKRQLKRLKDS-----PEPfWLLIFPEGT 114
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
374-423 3.02e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 38.23  E-value: 3.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1191845820 374 GRVSLPEFAAQLEV--PQSEALQDLFSLFDESGSGEMDLREFVVALSVVCRP 423
Cdd:COG5126    84 GKISADEFRRLLTAlgVSEEEADELFARLDTDGDGKISFEEFVAAVRDYYTP 135
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 121-245 5.82e-03

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


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 38.56  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1191845820 121 FHRVAVKGRQ-APPAEATILTLAPHSSYFDaIPVTMTMS---SIVMKAESRDIPIWGTLIKYIRPVFVSRSDQDSRRKTV 196
Cdd:PLN02901   34 FYKIEVEGLEnLPSPDEPAVYVSNHQSFLD-IYTLFHLGrpfKFISKTSIFLIPIIGWAMYMTGHIPLKRMDRRSQLECL 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1191845820 197 EEIKRRAQAGGrwpQIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVL 245
Cdd:PLN02901  113 KRCMELLKKGA---SVFFFPEGTRSKDGKLAAFKKGAFSvaakTGVPVVPITL 162
 
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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