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Conserved domains on  [gi|2062782441|ref|XP_042087574|]
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lysophosphatidylcholine acyltransferase 2 isoform X3 [Ovis aries]

Protein Classification

LPLAT_LPCAT1-like and EFh domain-containing protein( domain architecture ID 12959271)

LPLAT_LPCAT1-like and EFh domain-containing protein

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; ...
 117-327 4.07e-88

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: 267.16  E-value: 4.07e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 117 AMFFSMGF-VVTVKGKIATPlEAPIFVVAPHSTFFDGIACVAAGLPSIVSRNENVQVPLIGRILRALQPVLVSRVDPDSR 195
Cdd:cd07991     3 VLLFAFGFyVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPKDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 196 KNTINEIIRRATSGgEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPILLRYPNKLDTVTWTWQGYTFIQLCVLTWC 275
Cdd:cd07991    82 KKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRLLT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2062782441 276 QPFTRVEVEFMPVQVPSdEERSDPVLFASTIRNVMAEALKIPVTDHTYEDCR 327
Cdd:cd07991   161 QPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
353-439 1.69e-06

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: 47.09  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 353 LKLDWDGIRKHLdeyAAIASSSKGGRIGIEEFAEYLKLPVSDV----LRQLFALFDRNHDGSIDFREYViglAVLCNPAN 428
Cdd:COG5126    27 FEALFRRLWATL---FSEADTDGDGRISREEFVAGMESLFEATvepfARAAFDLLDTDGDGKISADEFR---RLLTALGV 100

                          90
                  ....*....|.
gi 2062782441 429 TEEIIQVAFKR 439
Cdd:COG5126   101 SEEEADELFAR 111
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 117-327 4.07e-88

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: 267.16  E-value: 4.07e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 117 AMFFSMGF-VVTVKGKIATPlEAPIFVVAPHSTFFDGIACVAAGLPSIVSRNENVQVPLIGRILRALQPVLVSRVDPDSR 195
Cdd:cd07991     3 VLLFAFGFyVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPKDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 196 KNTINEIIRRATSGgEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPILLRYPNKLDTVTWTWQGYTFIQLCVLTWC 275
Cdd:cd07991    82 KKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRLLT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2062782441 276 QPFTRVEVEFMPVQVPSdEERSDPVLFASTIRNVMAEALKIPVTDHTYEDCR 327
Cdd:cd07991   161 QPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 102-315 4.66e-24

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: 99.31  E-value: 4.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 102 WKRKITHPVLKFLGHAMFFSMGFVVTVKGKIATPLEAPIFVVAPHSTFFDGIAcVAAGLP---SIVSRNENVQVPLIGRI 178
Cdd:COG0204     7 LLRRFRYRLVRLWARLLLRLLGVRVRVEGLENLPADGPVLIVANHQSWLDILL-LLAALPrpvRFVAKKELFKIPLLGWL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 179 LRALQPVLVSRVDPDSRKNTINEIIRRATSGGewpQILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPILLRYpnkl 254
Cdd:COG0204    86 LRALGAIPVDRSKRRAALRALRQAVEALKAGE---SLVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG---- 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2062782441 255 dtvTWTWQGYTFIQLcvltwcqpFTRVEVEFMPVQVPSDEERSDPVLFASTIRNVMAEALK 315
Cdd:COG0204   159 ---TERALPKGFLPR--------PGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 142-250 2.90e-19

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: 83.17  E-value: 2.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441  142 VVAPHSTFFDGIACVAA-----GLPSIVSRNENVQVPLIGRILRALQPVLVSRVDPDSRKNTINEIIRRATSGGewpQIL 216
Cdd:smart00563   3 VVANHQSFLDPLVLSALlprklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGE---WLL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2062782441  217 VFPEGTCTNRSCLITFKPGAFI----PGVPVQPILLRY 250
Cdd:smart00563  80 IFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 126-246 2.22e-13

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: 66.92  E-value: 2.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 126 VTVKGKIATPLEAPIFVVAPHSTFFDGI--ACVAA---GLPSIVSRNENVQVPLIGRILRALQPVLVSRVDPDSRKNTIn 200
Cdd:pfam01553   2 IEVHGLENLPRGGPAIVVANHQSYLDVLllSLALYkrgRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2062782441 201 EIIRRATSGGEWpqILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPI 246
Cdd:pfam01553  81 EYLVELLREGKL--VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPV 128
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 123-249 2.49e-07

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: 49.65  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 123 GFVVTVKGKIATPLEAPIFVVAPHSTFFDGIACVAAGLP--SIVSRNENVQVPLIGRILRALQPVLVSRVDP---DSRKN 197
Cdd:TIGR00530   1 GLKVEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFPPpiVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2062782441 198 TINEIIRRATSggewpqILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPILLR 249
Cdd:TIGR00530  81 AAIEVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
353-439 1.69e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.09  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 353 LKLDWDGIRKHLdeyAAIASSSKGGRIGIEEFAEYLKLPVSDV----LRQLFALFDRNHDGSIDFREYViglAVLCNPAN 428
Cdd:COG5126    27 FEALFRRLWATL---FSEADTDGDGRISREEFVAGMESLFEATvepfARAAFDLLDTDGDGKISADEFR---RLLTALGV 100

                          90
                  ....*....|.
gi 2062782441 429 TEEIIQVAFKR 439
Cdd:COG5126   101 SEEEADELFAR 111
PLN02833 PLN02833
glycerol acyltransferase family protein
 103-312 9.27e-06

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 47.46  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 103 KRKITHPVLKFLGHAMFFSMGFVVTVKGKIATPLEAPIFVvAPHSTFFDGIA-CVAAGLPSIVSRNENVQVPLIGRILRA 181
Cdd:PLN02833  129 RKKIERKLVELICSAFVASWTGVIKYHGPRPSRRPKQVFV-ANHTSMIDFIVlEQMTPFAVIMQKHPGWVGFLQNTILES 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 182 LQPVLVSRVDPDSRkNTINEIIRRATSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPILLRYPNKLDTVTWTW 261
Cdd:PLN02833  208 VGCIWFNRTEAKDR-EVVAKKLRDHVQDPDRNPLLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKYNKIFVDAFWNS 286

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2062782441 262 QGYTFIQ-LCVL--TWCqpfTRVEVEFMPVQVPSDEErsDPVLFASTIRNVMAE 312
Cdd:PLN02833  287 RKQSFTMhLLRLmtSWA---VVCDVWYLEPQTLRPGE--TPIEFAERVRDMIAK 335
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 383-425 3.20e-05

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: 42.09  E-value: 3.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2062782441 383 EFAEYLKLPVS-DVLRQLFALFDRNHDGSIDFREY---VIGLAVLCN 425
Cdd:cd00213    39 ELPNFLKNQKDpEAVDKIMKDLDVNKDGKVDFQEFlvlIGKLAVACH 85
EF-hand_7 pfam13499
EF-hand domain pair;
377-417 5.95e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 5.95e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2062782441 377 GRIGIEEFAEYLK-----LPVSD-VLRQLFALFDRNHDGSIDFREYV 417
Cdd:pfam13499  17 GYLDVEELKKLLRkleegEPLSDeEVEELFKEFDLDKDGRISFEEFL 63
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 396-421 8.06e-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: 36.59  E-value: 8.06e-04
                           10        20
                   ....*....|....*....|....*.
gi 2062782441  396 LRQLFALFDRNHDGSIDFREYVIGLA 421
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 117-327 4.07e-88

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: 267.16  E-value: 4.07e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 117 AMFFSMGF-VVTVKGKIATPlEAPIFVVAPHSTFFDGIACVAAGLPSIVSRNENVQVPLIGRILRALQPVLVSRVDPDSR 195
Cdd:cd07991     3 VLLFAFGFyVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPKDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 196 KNTINEIIRRATSGgEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPILLRYPNKLDTVTWTWQGYTFIQLCVLTWC 275
Cdd:cd07991    82 KKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRLLT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2062782441 276 QPFTRVEVEFMPVQVPSdEERSDPVLFASTIRNVMAEALKIPVTDHTYEDCR 327
Cdd:cd07991   161 QPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 102-315 4.66e-24

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: 99.31  E-value: 4.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 102 WKRKITHPVLKFLGHAMFFSMGFVVTVKGKIATPLEAPIFVVAPHSTFFDGIAcVAAGLP---SIVSRNENVQVPLIGRI 178
Cdd:COG0204     7 LLRRFRYRLVRLWARLLLRLLGVRVRVEGLENLPADGPVLIVANHQSWLDILL-LLAALPrpvRFVAKKELFKIPLLGWL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 179 LRALQPVLVSRVDPDSRKNTINEIIRRATSGGewpQILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPILLRYpnkl 254
Cdd:COG0204    86 LRALGAIPVDRSKRRAALRALRQAVEALKAGE---SLVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG---- 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2062782441 255 dtvTWTWQGYTFIQLcvltwcqpFTRVEVEFMPVQVPSDEERSDPVLFASTIRNVMAEALK 315
Cdd:COG0204   159 ---TERALPKGFLPR--------PGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 142-250 2.90e-19

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: 83.17  E-value: 2.90e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441  142 VVAPHSTFFDGIACVAA-----GLPSIVSRNENVQVPLIGRILRALQPVLVSRVDPDSRKNTINEIIRRATSGGewpQIL 216
Cdd:smart00563   3 VVANHQSFLDPLVLSALlprklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGE---WLL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2062782441  217 VFPEGTCTNRSCLITFKPGAFI----PGVPVQPILLRY 250
Cdd:smart00563  80 IFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 116-272 1.97e-18

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: 82.70  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 116 HAMFFSMGFVVTVKGKIATPLEAPIFVVAPHSTFFDGIACVAAGLPSI--VSRNENVQVPLIGRILRALQPVLVSRVDPD 193
Cdd:cd07989     2 RLLLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALPRPIrfVAKKELFKIPFLGWLLRLLGAIPIDRGNGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 194 SRKNTINEIIRRATSGGewpQILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPILLRYPNKLDTVTWTWQGYTFIQL 269
Cdd:cd07989    82 SAREALREAIEALKEGE---SVVIFPEGTRSRDGELLPFKSGAFRlakeAGVPIVPVAISGTWGSLPKGKKLPRPGRVTV 158


                  ...
gi 2062782441 270 CVL 272
Cdd:cd07989   159 RIG 161
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 126-246 2.22e-13

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: 66.92  E-value: 2.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 126 VTVKGKIATPLEAPIFVVAPHSTFFDGI--ACVAA---GLPSIVSRNENVQVPLIGRILRALQPVLVSRVDPDSRKNTIn 200
Cdd:pfam01553   2 IEVHGLENLPRGGPAIVVANHQSYLDVLllSLALYkrgRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL- 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2062782441 201 EIIRRATSGGEWpqILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPI 246
Cdd:pfam01553  81 EYLVELLREGKL--VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPV 128
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 120-252 4.00e-13

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: 67.44  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 120 FSMGFVVTVKGKIATPLEAPIFVVAPHSTFFDG---IACVAAGLPS----IVSRNENVQVPLIGRilraLQPVLVSRVDP 192
Cdd:cd06551     8 FFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGlilFLLLERGLRRdvygLMDEELLERYPFFTR----LGAFSVDRDSP 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2062782441 193 DSRKNTINEIIRRATSGGEWpqILVFPEGTCTNRS-CLITFKPGAFIP----GVPVQPILLRYPN 252
Cdd:cd06551    84 RSAAKSLKYVARLLSKPGSV--VWIFPEGTRTRRDkRPLQFKPGVAHLaekaGVPIVPVALRYTF 146
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 126-253 9.69e-09

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: 54.96  E-value: 9.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 126 VTVKGKIATPLEAPIFVVAPHS-TFFDG--IACVAAGLPSIVSRNENVQVPLIGRILRALQPVLVSRVdPDSRKNTINEI 202
Cdd:cd07992    16 ITVVGRENVPKDGPVIFLGNHPnALIDPllLAATLRRPVRFLAKADLFKNPLIGWLLESFGAIPVYRP-KDLARGGIGKI 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2062782441 203 IRRAT--------SGGEWpqILVFPEGTCTNRSCLITFKPGAFI----------PGVPVQPILLRYPNK 253
Cdd:cd07992    95 SNAAVfdavgealKAGGA--IGIFPEGGSHDRPRLLPLKAGAARmalealeagqKDVKIVPVGLNYEDK 161
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 123-249 2.49e-07

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: 49.65  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 123 GFVVTVKGKIATPLEAPIFVVAPHSTFFDGIACVAAGLP--SIVSRNENVQVPLIGRILRALQPVLVSRVDP---DSRKN 197
Cdd:TIGR00530   1 GLKVEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFPPpiVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2062782441 198 TINEIIRRATSggewpqILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPILLR 249
Cdd:TIGR00530  81 AAIEVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
353-439 1.69e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.09  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 353 LKLDWDGIRKHLdeyAAIASSSKGGRIGIEEFAEYLKLPVSDV----LRQLFALFDRNHDGSIDFREYViglAVLCNPAN 428
Cdd:COG5126    27 FEALFRRLWATL---FSEADTDGDGRISREEFVAGMESLFEATvepfARAAFDLLDTDGDGKISADEFR---RLLTALGV 100

                          90
                  ....*....|.
gi 2062782441 429 TEEIIQVAFKR 439
Cdd:COG5126   101 SEEEADELFAR 111
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
377-427 2.16e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.09  E-value: 2.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2062782441 377 GRIGIEEFAEYLK-LPVSD-VLRQLFALFDRNHDGSIDFREYVIGLAVLCNPA 427
Cdd:COG5126    84 GKISADEFRRLLTaLGVSEeEADELFARLDTDGDGKISFEEFVAAVRDYYTPD 136
PLN02833 PLN02833
glycerol acyltransferase family protein
 103-312 9.27e-06

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 47.46  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 103 KRKITHPVLKFLGHAMFFSMGFVVTVKGKIATPLEAPIFVvAPHSTFFDGIA-CVAAGLPSIVSRNENVQVPLIGRILRA 181
Cdd:PLN02833  129 RKKIERKLVELICSAFVASWTGVIKYHGPRPSRRPKQVFV-ANHTSMIDFIVlEQMTPFAVIMQKHPGWVGFLQNTILES 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 182 LQPVLVSRVDPDSRkNTINEIIRRATSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPILLRYPNKLDTVTWTW 261
Cdd:PLN02833  208 VGCIWFNRTEAKDR-EVVAKKLRDHVQDPDRNPLLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKYNKIFVDAFWNS 286

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2062782441 262 QGYTFIQ-LCVL--TWCqpfTRVEVEFMPVQVPSDEErsDPVLFASTIRNVMAE 312
Cdd:PLN02833  287 RKQSFTMhLLRLmtSWA---VVCDVWYLEPQTLRPGE--TPIEFAERVRDMIAK 335
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 102-248 1.47e-05

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


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 45.88  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2062782441 102 WKRKITHPVLKF---LGHAMFFSmgfvVTVKGKIATP-LEAPIFVVAPHSTFFDGIACVAAGLP-SIVSRNENVQVPLIG 176
Cdd:PLN02901   14 YRRKAQHFINKVwatLSTSPFYK----IEVEGLENLPsPDEPAVYVSNHQSFLDIYTLFHLGRPfKFISKTSIFLIPIIG 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2062782441 177 RILRALQPVLVSRVDPDSRKNTIN---EIIRRATSggewpqILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPILL 248
Cdd:PLN02901   90 WAMYMTGHIPLKRMDRRSQLECLKrcmELLKKGAS------VFFFPEGTRSKDGKLAAFKKGAFSvaakTGVPVVPITL 162
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 383-425 3.20e-05

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: 42.09  E-value: 3.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2062782441 383 EFAEYLKLPVS-DVLRQLFALFDRNHDGSIDFREY---VIGLAVLCN 425
Cdd:cd00213    39 ELPNFLKNQKDpEAVDKIMKDLDVNKDGKVDFQEFlvlIGKLAVACH 85
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 377-417 1.54e-04

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 39.45  E-value: 1.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2062782441 377 GRIGIEEFAEYLKL----PVSDVLRQLFALFDRNHDGSIDFREYV 417
Cdd:cd00051    15 GTISADELKAALKSlgegLSEEEIDEMIREVDKDGDGKIDFEEFL 59
EF-hand_7 pfam13499
EF-hand domain pair;
377-417 5.95e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 38.00  E-value: 5.95e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2062782441 377 GRIGIEEFAEYLK-----LPVSD-VLRQLFALFDRNHDGSIDFREYV 417
Cdd:pfam13499  17 GYLDVEELKKLLRkleegEPLSDeEVEELFKEFDLDKDGRISFEEFL 63
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 389-420 6.21e-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: 37.97  E-value: 6.21e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2062782441 389 KLPvSDVLRQLFALFDRNHDGSIDFREYVIGL 420
Cdd:cd00052    29 GLP-RSVLAQIWDLADTDKDGKLDKEEFAIAM 59
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 396-421 8.06e-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: 36.59  E-value: 8.06e-04
                           10        20
                   ....*....|....*....|....*.
gi 2062782441  396 LRQLFALFDRNHDGSIDFREYVIGLA 421
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 396-438 1.52e-03

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


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 36.76  E-value: 1.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2062782441 396 LRQLFALFDRNHDGSIDFREYVIGLAVLcNPANTEEIIQVAFK 438
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEMIR 43
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 396-423 2.16e-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: 35.45  E-value: 2.16e-03
                          10        20
                  ....*....|....*....|....*...
gi 2062782441 396 LRQLFALFDRNHDGSIDFREYVIGLAVL 423
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
IF2_N pfam04760
Translation initiation factor IF-2, N-terminal region; This conserved feature at the ...
 381-413 3.76e-03

Translation initiation factor IF-2, N-terminal region; This conserved feature at the N-terminus of bacterial translation initiation factor IF2 has recently had its structure solved. It shows structural similarity to the tRNA anticodon Stem Contact Fold domains of the methionyl-tRNA and glutaminyl-tRNA synthetases, and a similar fold is also found in the B5 domain of the phenylalanine-tRNA synthetase.


Pssm-ID: 428110 [Multi-domain]  Cd Length: 52  Bit Score: 35.52  E-value: 3.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2062782441 381 IEEFAEYLKLPVSDVLRQLFAL-FDRNHDGSIDF 413
Cdd:pfam04760   6 VYELAKELGVSSKELIKKLFKLgIMKSHNSTLDE 39
EF-hand_6 pfam13405
EF-hand domain;
396-415 5.74e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.46  E-value: 5.74e-03
                          10        20
                  ....*....|....*....|
gi 2062782441 396 LRQLFALFDRNHDGSIDFRE 415
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEE 21
EF-hand_7 pfam13499
EF-hand domain pair;
394-438 6.76e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 34.92  E-value: 6.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2062782441 394 DVLRQLFALFDRNHDGSIDFREYVIGLAVLCNPAN-TEEIIQVAFK 438
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPlSDEEVEELFK 47
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 372-417 9.16e-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: 36.81  E-value: 9.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2062782441 372 SSSKGGRIGIEEFAEYLKLPVS----DVLRQLFALFDRNHDGSIDFREYV 417
Cdd:cd16185    10 DRDRSGSIDVNELQKALAGGGLlfslATAEKLIRMFDRDGNGTIDFEEFA 59
 
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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