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Conserved domains on  [gi|530378964|ref|XP_005248430|]
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lysophosphatidylcholine acyltransferase 1 isoform X2 [Homo sapiens]

Protein Classification

LPLAT_LPCAT1-like and EF-hand_8 domain-containing protein( domain architecture ID 12959277)

protein containing domains LPLAT_LPCAT1-like, EFh_PEF, and EF-hand_8

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; ...
 55-266 2.17e-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: 294.90  E-value: 2.17e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  55 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQD 133
Cdd:cd07991    1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 134 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPNKLDTITWTWQGPGALEILWLT 213
Cdd:cd07991   80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530378964 214 LCQFHNQVEIEFLPVYSPSEEEKrNPALYASNVRRVMAEALGVSVTDYTFEDC 266
Cdd:cd07991  159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
EF-hand_8 pfam13833
EF-hand domain pair;
384-435 3.36e-07

EF-hand domain pair;


:

Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 46.92  E-value: 3.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530378964  384 EDGSVGEGDLSCILKTaLGVAELT---VTDLFRAIDQEEKGKITFADFHRFAEMY 435
Cdd:pfam13833   1 EKGVITREELKRALAL-LGLKDLSedeVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
322-446 1.52e-05

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


The actual alignment was detected with superfamily member COG5126:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 322 AEFAASLEvpvsDLLEDMFSLFDESGSGEVDLREcVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILkTAL 401
Cdd:COG5126   25 DDFEALFR----RLWATLFSEADTDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL-TAL 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530378964 402 GVAELTVTDLFRAIDQEEKGKITFADFHrfaemypAFAEEYLYPD 446
Cdd:COG5126   99 GVSEEEADELFARLDTDGDGKISFEEFV-------AAVRDYYTPD 136
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 55-266 2.17e-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: 294.90  E-value: 2.17e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  55 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQD 133
Cdd:cd07991    1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 134 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPNKLDTITWTWQGPGALEILWLT 213
Cdd:cd07991   80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530378964 214 LCQFHNQVEIEFLPVYSPSEEEKrNPALYASNVRRVMAEALGVSVTDYTFEDC 266
Cdd:cd07991  159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 40-255 3.45e-27

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


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 108.56  E-value: 3.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  40 PALWRKVVDFLLKAIMRTMWFAGGFhRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPIWG 116
Cdd:COG0204    5 FLLLRRFRYRLVRLWARLLLRLLGV-RVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPrpvRFVAKKELFKIPLLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 117 TLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLRYpn 192
Cdd:COG0204   84 WLLRALGAIPVDRSKRRAALRALRQAVEALK-AGES--LVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG-- 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530378964 193 kldtiTWTWQGPGALeilwltlcQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAEALG 255
Cdd:COG0204  159 -----TERALPKGFL--------PRPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 81-190 2.09e-22

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


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 92.03  E-value: 2.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964    81 ILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKwpq 154
Cdd:smart00563   1 ALVVANHQSFLDPLvlsallPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGEW--- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 530378964   155 IMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLRY 190
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 66-188 6.23e-20

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


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 85.41  E-value: 6.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964   66 RVAVKGRQALPTEAAILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTV 139
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLllslalYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530378964  140 EEIKRRaQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVL 188
Cdd:pfam01553  81 EYLVEL-LREGKL--VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPVAI 130
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 67-189 9.58e-14

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


Pssm-ID: 129621 [Multi-domain]  Cd Length: 130  Bit Score: 68.14  E-value: 9.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964   67 VAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ---DSRRKTVE 140
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFpppIVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALKAAI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530378964  141 EIKRRAQSngkwpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLR 189
Cdd:TIGR00530  84 EVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
EF-hand_8 pfam13833
EF-hand domain pair;
384-435 3.36e-07

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 46.92  E-value: 3.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530378964  384 EDGSVGEGDLSCILKTaLGVAELT---VTDLFRAIDQEEKGKITFADFHRFAEMY 435
Cdd:pfam13833   1 EKGVITREELKRALAL-LGLKDLSedeVDILFREFDTDGDGYISFDEFCVLLERR 54
PLN02833 PLN02833
glycerol acyltransferase family protein
 3-194 4.90e-07

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 51.70  E-value: 4.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964   3 LTLFPVRLLVaaamMLLAWPLALVASLGS--AEKEPEQPPALWRKVVDFLLKAimrtmwFAGGFHRVaVKGRQALPTE-A 79
Cdd:PLN02833  95 GILFPVRVLL----LAIGWIIFLSAFIPVhfLLKGHKLRKKIERKLVELICSA------FVASWTGV-IKYHGPRPSRrP 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  80 AILTLAPHSSYFDAIPVT-MTMSSIVMKAEsrdiPIWGTLIQ-----YIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWP 153
Cdd:PLN02833 164 KQVFVANHTSMIDFIVLEqMTPFAVIMQKH----PGWVGFLQntileSVGCIWFNRTEAKDREVVAKKLRDHVQDPDRNP 239

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530378964 154 qIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYpNKL 194
Cdd:PLN02833 240 -LLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKY-NKI 278
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
322-446 1.52e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 322 AEFAASLEvpvsDLLEDMFSLFDESGSGEVDLREcVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILkTAL 401
Cdd:COG5126   25 DDFEALFR----RLWATLFSEADTDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL-TAL 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530378964 402 GVAELTVTDLFRAIDQEEKGKITFADFHrfaemypAFAEEYLYPD 446
Cdd:COG5126   99 GVSEEEADELFARLDTDGDGKISFEEFV-------AAVRDYYTPD 136
PTZ00184 PTZ00184
calmodulin; Provisional
 336-430 3.11e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 41.29  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 336 LEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILkTALG--VAELTVTDLFR 413
Cdd:PTZ00184  49 LQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEVDEMIR 127

                         90
                 ....*....|....*..
gi 530378964 414 AIDQEEKGKITFADFHR 430
Cdd:PTZ00184 128 EADVDGDGQINYEEFVK 144
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 318-434 2.22e-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: 38.66  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 318 KIGIAEFAAslevpVSDLLEDM---FSLFDESGSGEVDLRECVVALsvvcrpaRTL------DTIQLAFKMYGAQEDGSV 388
Cdd:cd16180   53 TINFDEFVG-----LWKYIQDWrrlFRRFDRDRSGSIDFNELQNAL-------SSFgyrlspQFVQLLVRKFDRRRRGSI 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530378964 389 GEGD---LSCILKtalgvaelTVTDLFRAIDQEEKGKITFaDFHRFAEM 434
Cdd:cd16180  121 SFDDfveACVTLK--------RLTDAFRKYDTNRTGYATI-SYEDFLTM 160
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 55-266 2.17e-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: 294.90  E-value: 2.17e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  55 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQD 133
Cdd:cd07991    1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 134 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPNKLDTITWTWQGPGALEILWLT 213
Cdd:cd07991   80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530378964 214 LCQFHNQVEIEFLPVYSPSEEEKrNPALYASNVRRVMAEALGVSVTDYTFEDC 266
Cdd:cd07991  159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 40-255 3.45e-27

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


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 108.56  E-value: 3.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  40 PALWRKVVDFLLKAIMRTMWFAGGFhRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPIWG 116
Cdd:COG0204    5 FLLLRRFRYRLVRLWARLLLRLLGV-RVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPrpvRFVAKKELFKIPLLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 117 TLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLRYpn 192
Cdd:COG0204   84 WLLRALGAIPVDRSKRRAALRALRQAVEALK-AGES--LVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG-- 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530378964 193 kldtiTWTWQGPGALeilwltlcQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAEALG 255
Cdd:COG0204  159 -----TERALPKGFL--------PRPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 59-251 3.57e-26

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


Pssm-ID: 153244 [Multi-domain]  Cd Length: 187  Bit Score: 104.80  E-value: 3.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  59 WFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTM-------TMSSIVMKAES-RDIPIWGTLiqyiRPVFVSRS 130
Cdd:cd06551    6 LNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLllerglrRDVYGLMDEELlERYPFFTRL----GAFSVDRD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 131 DQDSRRKTVEEIKRRAQSNGKWpqIMIFPEGTCTN-RTCLITFKPGAFIP----GAPVQPVVLRYPNkldtitwtwqgpg 205
Cdd:cd06551   82 SPRSAAKSLKYVARLLSKPGSV--VWIFPEGTRTRrDKRPLQFKPGVAHLaekaGVPIVPVALRYTF------------- 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 530378964 206 aleilWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMA 251
Cdd:cd06551  147 -----ELFEQFPEIFVRIGPPIPYAETALGEELAAELANRLTRLLD 187
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 58-237 1.00e-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: 98.11  E-value: 1.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  58 MWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDS 134
Cdd:cd07989    3 LLLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALprpIRFVAKKELFKIPFLGWLLRLLGAIPIDRGNGRS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 135 RRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLRYPNKLDTITWTWQGPGaleil 210
Cdd:cd07989   83 AREALREAIEALK-EGES--VVIFPEGTRSRDGELLPFKSGAFRlakeAGVPIVPVAISGTWGSLPKGKKLPRPG----- 154

                        170       180
                 ....*....|....*....|....*..
gi 530378964 211 wltlcqfhnQVEIEFLPVYSPSEEEKR 237
Cdd:cd07989  155 ---------RVTVRIGEPIPPEGLELA 172
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 81-190 2.09e-22

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


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 92.03  E-value: 2.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964    81 ILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKwpq 154
Cdd:smart00563   1 ALVVANHQSFLDPLvlsallPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGEW--- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 530378964   155 IMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLRY 190
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 66-188 6.23e-20

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


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 85.41  E-value: 6.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964   66 RVAVKGRQALPTEAAILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQDSRRKTV 139
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLllslalYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530378964  140 EEIKRRaQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVL 188
Cdd:pfam01553  81 EYLVEL-LREGKL--VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPVAI 130
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 67-189 9.58e-14

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


Pssm-ID: 129621 [Multi-domain]  Cd Length: 130  Bit Score: 68.14  E-value: 9.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964   67 VAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ---DSRRKTVE 140
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFpppIVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALKAAI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530378964  141 EIKRRAQSngkwpqIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVLR 189
Cdd:TIGR00530  84 EVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 43-193 1.02e-10

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


Pssm-ID: 153254 [Multi-domain]  Cd Length: 203  Bit Score: 61.12  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  43 WRKVVDFLLKaimrtmWFaggFHRVAVKGRQALPTEAAILTLAPHS-SYFDAIPVTMTMS---SIVMKAESRDIPIWGTL 118
Cdd:cd07992    1 VRLLSRVILR------IY---FRRITVVGRENVPKDGPVIFLGNHPnALIDPLLLAATLRrpvRFLAKADLFKNPLIGWL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 119 IQYIRPVFVSRsDQDSRRKTVEEIK--------RRAQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----------PG 180
Cdd:cd07992   72 LESFGAIPVYR-PKDLARGGIGKISnaavfdavGEALKAGGA--IGIFPEGGSHDRPRLLPLKAGAARmalealeagqKD 148

                        170
                 ....*....|...
gi 530378964 181 APVQPVVLRYPNK 193
Cdd:cd07992  149 VKIVPVGLNYEDK 161
EF-hand_8 pfam13833
EF-hand domain pair;
384-435 3.36e-07

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 46.92  E-value: 3.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530378964  384 EDGSVGEGDLSCILKTaLGVAELT---VTDLFRAIDQEEKGKITFADFHRFAEMY 435
Cdd:pfam13833   1 EKGVITREELKRALAL-LGLKDLSedeVDILFREFDTDGDGYISFDEFCVLLERR 54
PLN02833 PLN02833
glycerol acyltransferase family protein
 3-194 4.90e-07

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 51.70  E-value: 4.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964   3 LTLFPVRLLVaaamMLLAWPLALVASLGS--AEKEPEQPPALWRKVVDFLLKAimrtmwFAGGFHRVaVKGRQALPTE-A 79
Cdd:PLN02833  95 GILFPVRVLL----LAIGWIIFLSAFIPVhfLLKGHKLRKKIERKLVELICSA------FVASWTGV-IKYHGPRPSRrP 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  80 AILTLAPHSSYFDAIPVT-MTMSSIVMKAEsrdiPIWGTLIQ-----YIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWP 153
Cdd:PLN02833 164 KQVFVANHTSMIDFIVLEqMTPFAVIMQKH----PGWVGFLQntileSVGCIWFNRTEAKDREVVAKKLRDHVQDPDRNP 239

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 530378964 154 qIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYpNKL 194
Cdd:PLN02833 240 -LLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKY-NKI 278
EF-hand_7 pfam13499
EF-hand domain pair;
371-432 1.74e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 45.32  E-value: 1.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530378964  371 DTIQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELT---VTDLFRAIDQEEKGKITFADFHRFA 432
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSdeeVEELFKEFDLDKDGRISFEEFLELY 66
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 44-189 5.90e-06

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 49.15  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964   44 RKVVDFLLKAIMrtMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPiwgtliq 120
Cdd:PRK08633  408 LLLPDSLLRFLL--LLLMHTRYRLRVEGRENIPAKGGALLLGNHVSWIDWALLQAASPrpiRFVMERSIYEKW------- 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  121 YIRPVF-------VSrsdQDSRRKTVEEIkRRAQSNGKwpQIMIFPEGTCTNRTCLITFKPG----AFIPGAPVQPVVLR 189
Cdd:PRK08633  479 YLKWFFklfgvipIS---SGGSKESLEFI-RKALDDGE--VVCIFPEGAITRNGQLNEFKRGfeliVKGTDVPIIPFYIR 552
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
322-446 1.52e-05

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 44.78  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 322 AEFAASLEvpvsDLLEDMFSLFDESGSGEVDLREcVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILkTAL 401
Cdd:COG5126   25 DDFEALFR----RLWATLFSEADTDGDGRISREE-FVAGMESLFEATVEPFARAAFDLLDTDGDGKISADEFRRLL-TAL 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530378964 402 GVAELTVTDLFRAIDQEEKGKITFADFHrfaemypAFAEEYLYPD 446
Cdd:COG5126   99 GVSEEEADELFARLDTDGDGKISFEEFV-------AAVRDYYTPD 136
PTZ00184 PTZ00184
calmodulin; Provisional
 336-430 3.11e-04

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 41.29  E-value: 3.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 336 LEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDTIQLAFKMYGAQEDGSVGEGDLSCILkTALG--VAELTVTDLFR 413
Cdd:PTZ00184  49 LQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEVDEMIR 127

                         90
                 ....*....|....*..
gi 530378964 414 AIDQEEKGKITFADFHR 430
Cdd:PTZ00184 128 EADVDGDGQINYEEFVK 144
LPLAT_LCLAT1-like cd07990
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; ...
 75-162 1.21e-03

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as Lysocardiolipin acyltransferase 1 (LCLAT1) or 1-acyl-sn-glycerol-3-phosphate acyltransferase and similar proteins.


Pssm-ID: 153252 [Multi-domain]  Cd Length: 193  Bit Score: 39.91  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  75 LPTEAAILtLAPHSSYFDAIpVTMTMSS---------IVMKAESRDIPI--WGTLIQYIrpVFVSRS---DQDSRRKTVE 140
Cdd:cd07990   21 LPKERALI-ISNHRSEVDWL-VLWMLADrfgrlgrlkIVLKDSLKYPPLggWGWQLGEF--IFLKRKwekDEKTIKRQLK 96

                         90       100
                 ....*....|....*....|..
gi 530378964 141 EIKRRAQSNgkwpQIMIFPEGT 162
Cdd:cd07990   97 RLKDSPEPF----WLLIFPEGT 114
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 64-188 2.09e-03

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


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 39.71  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964  64 FHRVAVKGRQALPT-EAAILTLAPHSSYFDaIPVTMTMS---SIVMKAESRDIPIWGTLIQYIRPVFVSRSDqdsRRKTV 139
Cdd:PLN02901  34 FYKIEVEGLENLPSpDEPAVYVSNHQSFLD-IYTLFHLGrpfKFISKTSIFLIPIIGWAMYMTGHIPLKRMD---RRSQL 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530378964 140 EEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFI----PGAPVQPVVL 188
Cdd:PLN02901 110 ECLKRCMELLKKGASVFFFPEGTRSKDGKLAAFKKGAFSvaakTGVPVVPITL 162
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 318-434 2.22e-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: 38.66  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 318 KIGIAEFAAslevpVSDLLEDM---FSLFDESGSGEVDLRECVVALsvvcrpaRTL------DTIQLAFKMYGAQEDGSV 388
Cdd:cd16180   53 TINFDEFVG-----LWKYIQDWrrlFRRFDRDRSGSIDFNELQNAL-------SSFgyrlspQFVQLLVRKFDRRRRGSI 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 530378964 389 GEGD---LSCILKtalgvaelTVTDLFRAIDQEEKGKITFaDFHRFAEM 434
Cdd:cd16180  121 SFDDfveACVTLK--------RLTDAFRKYDTNRTGYATI-SYEDFLTM 160
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 318-431 8.22e-03

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


Pssm-ID: 320060 [Multi-domain]  Cd Length: 163  Bit Score: 37.19  E-value: 8.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530378964 318 KIGIAEFAAslevpVSDLLEDM---FSLFDESGSGEVDLRECVVALSvvcRPARTLD--TIQLAFKMYGAQEDGSVGEGD 392
Cdd:cd16185   52 TIDFEEFAA-----LHQFLSNMqngFEQRDTSRSGRLDANEVHEALA---ASGFQLDppAFQALFRKFDPDRGGSLGFDD 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530378964 393 ---LSCILKTAlgvaeltvTDLFRAIDQEEKGKITFaDFHRF 431
Cdd:cd16185  124 yieLCIFLASA--------RNLFQAFDRQRTGRVTL-DFNQF 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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