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Conserved domains on  [gi|1958647007|ref|XP_038937140|]
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lysophosphatidylcholine acyltransferase 1 isoform X1 [Rattus norvegicus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 1-212 4.36e-99

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: 4.36e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007   1 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQD 79
Cdd:cd07991     1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  80 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNKLDTITWTWQGPGALKILWLT 159
Cdd:cd07991    80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958647007 160 LCQFQNQVEIEFLPVYCPSEEEKrNPALYASNVRRVMAKALGVSVTDYTFEDC 212
Cdd:cd07991   159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
EF-hand_8 pfam13833
EF-hand domain pair;
330-381 3.81e-09

EF-hand domain pair;


:

Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 52.32  E-value: 3.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958647007 330 EDGSIDEADLSCILKTAL--GISELTVTDLFQAIDQEERGRITFDDFCGFAEMY 381
Cdd:pfam13833   1 EKGVITREELKRALALLGlkDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
282-392 1.49e-07

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: 50.18  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 282 LEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTlATIQLAFKMYGSPEDGSIDEADLSCILkTALGISELTVTDLFQAI 361
Cdd:COG5126    35 WATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL-TALGVSEEEADELFARL 112

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958647007 362 DQEERGRITFDDFCgfaemypDFAEDYLYPD 392
Cdd:COG5126   113 DTDGDGKISFEEFV-------AAVRDYYTPD 136
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 248-310 5.74e-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.


The actual alignment was detected with superfamily member cd05025:

Pssm-ID: 415501 [Multi-domain]  Cd Length: 92  Bit Score: 36.02  E-value: 5.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 248 KDLDKY----SESARMKRGEkirLPEFAAYLEVPvsDALEDMFSLFDESGGGEIDLREYVV---ALSVVC 310
Cdd:cd05025    21 KEGDKYklskKELKDLLQTE---LSDFLDAQKDA--DAVDKIMKELDENGDGEVDFQEFVVlvaALTVAC 85
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 1-212 4.36e-99

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: 4.36e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007   1 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQD 79
Cdd:cd07991     1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  80 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNKLDTITWTWQGPGALKILWLT 159
Cdd:cd07991    80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958647007 160 LCQFQNQVEIEFLPVYCPSEEEKrNPALYASNVRRVMAKALGVSVTDYTFEDC 212
Cdd:cd07991   159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 1-201 1.12e-26

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


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 106.63  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007   1 MRTMWFAGGFhRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPIWGTLIRYIRPVFVSRSD 77
Cdd:COG0204    20 ARLLLRLLGV-RVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPrpvRFVAKKELFKIPLLGWLLRALGAIPVDRSK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  78 QDSRRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRYpnkldtiTWTWQGPGAL 153
Cdd:COG0204    99 RRAALRALRQAVEALK-AGES--LVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG-------TERALPKGFL 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958647007 154 KilwltlcqFQNQVEIEFLPVYCPSEEEKRNPALYASNVRRVMAKALG 201
Cdd:COG0204   169 P--------RPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 27-136 4.37e-24

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: 96.27  E-value: 4.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007   27 ILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKwpq 100
Cdd:smart00563   1 ALVVANHQSFLDPLvlsallPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGEW--- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958647007  101 IMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRY 136
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 12-134 7.50e-22

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: 90.42  E-value: 7.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  12 RVAVKGRQALPTEAAILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTV 85
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLllslalYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958647007  86 EEIKRRaQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVL 134
Cdd:pfam01553  81 EYLVEL-LREGKL--VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPVAI 130
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 13-135 5.56e-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: 68.53  E-value: 5.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  13 VAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQ---DSRRKTVE 86
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFpppIVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALKAAI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958647007  87 EIKRRAQSngkwpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLR 135
Cdd:TIGR00530  84 EVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
EF-hand_8 pfam13833
EF-hand domain pair;
330-381 3.81e-09

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 52.32  E-value: 3.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958647007 330 EDGSIDEADLSCILKTAL--GISELTVTDLFQAIDQEERGRITFDDFCGFAEMY 381
Cdd:pfam13833   1 EKGVITREELKRALALLGlkDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
282-392 1.49e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 282 LEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTlATIQLAFKMYGSPEDGSIDEADLSCILkTALGISELTVTDLFQAI 361
Cdd:COG5126    35 WATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL-TALGVSEEEADELFARL 112

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958647007 362 DQEERGRITFDDFCgfaemypDFAEDYLYPD 392
Cdd:COG5126   113 DTDGDGKISFEEFV-------AAVRDYYTPD 136
PTZ00184 PTZ00184
calmodulin; Provisional
 277-375 2.23e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.06  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 277 PVSDALEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTLATIQLAFKMYGSPEDGSIDEADLSCILkTALG--ISELTV 354
Cdd:PTZ00184   44 PTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEV 122

                          90       100
                  ....*....|....*....|.
gi 1958647007 355 TDLFQAIDQEERGRITFDDFC 375
Cdd:PTZ00184  123 DEMIREADVDGDGQINYEEFV 143
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 283-374 3.11e-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: 46.82  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 283 EDMFSLFDESGGGEIDLREYVvALSvvcrpsQTLATIQLAFKMYGSPEDGSIDEADLSCILKTA-LGISELTVTDLFQAI 361
Cdd:cd16185    39 EKLIRMFDRDGNGTIDFEEFA-ALH------QFLSNMQNGFEQRDTSRSGRLDANEVHEALAASgFQLDPPAFQALFRKF 111

                          90
                  ....*....|...
gi 1958647007 362 DQEERGRITFDDF 374
Cdd:cd16185   112 DPDRGGSLGFDDY 124
PLN02833 PLN02833
glycerol acyltransferase family protein
 31-140 4.13e-06

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 48.62  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  31 APHSSYFDAIPVT-MTMSSIVMKAEsrdiPIW-----GTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWPqIMIF 104
Cdd:PLN02833  169 ANHTSMIDFIVLEqMTPFAVIMQKH----PGWvgflqNTILESVGCIWFNRTEAKDREVVAKKLRDHVQDPDRNP-LLIF 243

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958647007 105 PEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYpNKL 140
Cdd:PLN02833  244 PEGTCVNNEYTVMFKKGAFELGCTVCPIAIKY-NKI 278
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 286-374 9.20e-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: 39.82  E-value: 9.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 286 FSLFDESGGGEIDLREYVVAL-SVVCRPSQTlaTIQLAFKMYGSPEDGSIDEAD---LSCILKtalgiselTVTDLFQAI 361
Cdd:cd16180    73 FRRFDRDRSGSIDFNELQNALsSFGYRLSPQ--FVQLLVRKFDRRRRGSISFDDfveACVTLK--------RLTDAFRKY 142

                          90
                  ....*....|....*
gi 1958647007 362 DQEERGRIT--FDDF 374
Cdd:cd16180   143 DTNRTGYATisYEDF 157
S-100A1 cd05025
S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding ...
 248-310 5.74e-03

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


Pssm-ID: 240152 [Multi-domain]  Cd Length: 92  Bit Score: 36.02  E-value: 5.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 248 KDLDKY----SESARMKRGEkirLPEFAAYLEVPvsDALEDMFSLFDESGGGEIDLREYVV---ALSVVC 310
Cdd:cd05025    21 KEGDKYklskKELKDLLQTE---LSDFLDAQKDA--DAVDKIMKELDENGDGEVDFQEFVVlvaALTVAC 85
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 1-212 4.36e-99

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: 4.36e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007   1 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQD 79
Cdd:cd07991     1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  80 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNKLDTITWTWQGPGALKILWLT 159
Cdd:cd07991    80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958647007 160 LCQFQNQVEIEFLPVYCPSEEEKrNPALYASNVRRVMAKALGVSVTDYTFEDC 212
Cdd:cd07991   159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 5-197 2.85e-27

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: 107.50  E-value: 2.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007   5 WFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTM-------TMSSIVMKAES-RDIPIWGTLiryiRPVFVSRS 76
Cdd:cd06551     6 LNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLllerglrRDVYGLMDEELlERYPFFTRL----GAFSVDRD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  77 DQDSRRKTVEEIKRRAQSNGKWpqIMIFPEGTCTN-RTCLITFKPGAFIP----GVPVQPVVLRYPNkldtitwtwqgpg 151
Cdd:cd06551    82 SPRSAAKSLKYVARLLSKPGSV--VWIFPEGTRTRrDKRPLQFKPGVAHLaekaGVPIVPVALRYTF------------- 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958647007 152 alkilWLTLCQFQNQVEIEFLPVYCPSEEEKRNPALYASNVRRVMA 197
Cdd:cd06551   147 -----ELFEQFPEIFVRIGPPIPYAETALGEELAAELANRLTRLLD 187
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 1-201 1.12e-26

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


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 106.63  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007   1 MRTMWFAGGFhRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPIWGTLIRYIRPVFVSRSD 77
Cdd:COG0204    20 ARLLLRLLGV-RVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPrpvRFVAKKELFKIPLLGWLLRALGAIPVDRSK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  78 QDSRRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRYpnkldtiTWTWQGPGAL 153
Cdd:COG0204    99 RRAALRALRQAVEALK-AGES--LVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG-------TERALPKGFL 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958647007 154 KilwltlcqFQNQVEIEFLPVYCPSEEEKRNPALYASNVRRVMAKALG 201
Cdd:COG0204   169 P--------RPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 4-155 1.88e-25

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: 102.35  E-value: 1.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007   4 MWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDS 80
Cdd:cd07989     3 LLLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALprpIRFVAKKELFKIPFLGWLLRLLGAIPIDRGNGRS 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958647007  81 RRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRYPNKLDTITWTWQGPGALKI 155
Cdd:cd07989    83 AREALREAIEALK-EGES--VVIFPEGTRSRDGELLPFKSGAFRlakeAGVPIVPVAISGTWGSLPKGKKLPRPGRVTV 158
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 27-136 4.37e-24

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: 96.27  E-value: 4.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007   27 ILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKwpq 100
Cdd:smart00563   1 ALVVANHQSFLDPLvlsallPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGEW--- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1958647007  101 IMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRY 136
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 12-134 7.50e-22

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: 90.42  E-value: 7.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  12 RVAVKGRQALPTEAAILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTV 85
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLllslalYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958647007  86 EEIKRRaQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVL 134
Cdd:pfam01553  81 EYLVEL-LREGKL--VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPVAI 130
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 13-135 5.56e-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: 68.53  E-value: 5.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  13 VAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQ---DSRRKTVE 86
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFpppIVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALKAAI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958647007  87 EIKRRAQSngkwpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLR 135
Cdd:TIGR00530  84 EVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 10-139 2.05e-11

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: 63.05  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  10 FHRVAVKGRQALPTEAAILTLAPHS-SYFDAIPVTMTMS---SIVMKAESRDIPIWGTLIRYIRPVFVSRsDQDSRRKTV 85
Cdd:cd07992    13 FRRITVVGRENVPKDGPVIFLGNHPnALIDPLLLAATLRrpvRFLAKADLFKNPLIGWLLESFGAIPVYR-PKDLARGGI 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958647007  86 EEIK--------RRAQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----------PGVPVQPVVLRYPNK 139
Cdd:cd07992    92 GKISnaavfdavGEALKAGGA--IGIFPEGGSHDRPRLLPLKAGAARmalealeagqKDVKIVPVGLNYEDK 161
EF-hand_8 pfam13833
EF-hand domain pair;
330-381 3.81e-09

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 52.32  E-value: 3.81e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958647007 330 EDGSIDEADLSCILKTAL--GISELTVTDLFQAIDQEERGRITFDDFCGFAEMY 381
Cdd:pfam13833   1 EKGVITREELKRALALLGlkDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
EF-hand_7 pfam13499
EF-hand domain pair;
319-378 4.22e-09

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 52.64  E-value: 4.22e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958647007 319 IQLAFKMYGSPEDGSIDEADLSCILKTALGISELT---VTDLFQAIDQEERGRITFDDFCGFA 378
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSdeeVEELFKEFDLDKDGRISFEEFLELY 66
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
282-392 1.49e-07

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 50.18  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 282 LEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTlATIQLAFKMYGSPEDGSIDEADLSCILkTALGISELTVTDLFQAI 361
Cdd:COG5126    35 WATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL-TALGVSEEEADELFARL 112

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958647007 362 DQEERGRITFDDFCgfaemypDFAEDYLYPD 392
Cdd:COG5126   113 DTDGDGKISFEEFV-------AAVRDYYTPD 136
PTZ00184 PTZ00184
calmodulin; Provisional
 277-375 2.23e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.06  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 277 PVSDALEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTLATIQLAFKMYGSPEDGSIDEADLSCILkTALG--ISELTV 354
Cdd:PTZ00184   44 PTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEV 122

                          90       100
                  ....*....|....*....|.
gi 1958647007 355 TDLFQAIDQEERGRITFDDFC 375
Cdd:PTZ00184  123 DEMIREADVDGDGQINYEEFV 143
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 283-374 3.11e-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: 46.82  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 283 EDMFSLFDESGGGEIDLREYVvALSvvcrpsQTLATIQLAFKMYGSPEDGSIDEADLSCILKTA-LGISELTVTDLFQAI 361
Cdd:cd16185    39 EKLIRMFDRDGNGTIDFEEFA-ALH------QFLSNMQNGFEQRDTSRSGRLDANEVHEALAASgFQLDPPAFQALFRKF 111

                          90
                  ....*....|...
gi 1958647007 362 DQEERGRITFDDF 374
Cdd:cd16185   112 DPDRGGSLGFDDY 124
PLN02833 PLN02833
glycerol acyltransferase family protein
 31-140 4.13e-06

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 48.62  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  31 APHSSYFDAIPVT-MTMSSIVMKAEsrdiPIW-----GTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKWPqIMIF 104
Cdd:PLN02833  169 ANHTSMIDFIVLEqMTPFAVIMQKH----PGWvgflqNTILESVGCIWFNRTEAKDREVVAKKLRDHVQDPDRNP-LLIF 243

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958647007 105 PEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYpNKL 140
Cdd:PLN02833  244 PEGTCVNNEYTVMFKKGAFELGCTVCPIAIKY-NKI 278
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 4-135 1.59e-05

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 47.23  E-value: 1.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007    4 MWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPiwgtlirYIRPVF-------V 73
Cdd:PRK08633   420 LLLMHTRYRLRVEGRENIPAKGGALLLGNHVSWIDWALLQAASPrpiRFVMERSIYEKW-------YLKWFFklfgvipI 492

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958647007   74 SrsdQDSRRKTVEEIkRRAQSNGKwpQIMIFPEGTCTNRTCLITFKPG----AFIPGVPVQPVVLR 135
Cdd:PRK08633   493 S---SGGSKESLEFI-RKALDDGE--VVCIFPEGAITRNGQLNEFKRGfeliVKGTDVPIIPFYIR 552
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 282-344 1.17e-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: 39.84  E-value: 1.17e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958647007 282 LEDMFSLFDESGGGEIDLREYVVALSvVCRPSQTLATIQLAFKMYGSPEDGSIDEADLSCILK 344
Cdd:cd00051     2 LREAFRLFDKDGDGTISADELKAALK-SLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 10-134 7.02e-04

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


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 40.87  E-value: 7.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  10 FHRVAVKGRQALPT-EAAILTLAPHSSYFDaIPVTMTMS---SIVMKAESRDIPIWGTLIRYIRPVFVSRSDqdsRRKTV 85
Cdd:PLN02901   34 FYKIEVEGLENLPSpDEPAVYVSNHQSFLD-IYTLFHLGrpfKFISKTSIFLIPIIGWAMYMTGHIPLKRMD---RRSQL 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958647007  86 EEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVL 134
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 ...
 286-374 9.20e-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: 39.82  E-value: 9.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 286 FSLFDESGGGEIDLREYVVAL-SVVCRPSQTlaTIQLAFKMYGSPEDGSIDEAD---LSCILKtalgiselTVTDLFQAI 361
Cdd:cd16180    73 FRRFDRDRSGSIDFNELQNALsSFGYRLSPQ--FVQLLVRKFDRRRRGSISFDDfveACVTLK--------RLTDAFRKY 142

                          90
                  ....*....|....*
gi 1958647007 362 DQEERGRIT--FDDF 374
Cdd:cd16180   143 DTNRTGYATisYEDF 157
LPLAT_LCLAT1-like cd07990
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; ...
 21-108 9.21e-04

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: 40.30  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007  21 LPTEAAILtLAPHSSYFDAIpVTMTMSS---------IVMKAESRDIPI--WGTLI-RYIrpvFVSRS---DQDSRRKTV 85
Cdd:cd07990    21 LPKERALI-ISNHRSEVDWL-VLWMLADrfgrlgrlkIVLKDSLKYPPLggWGWQLgEFI---FLKRKwekDEKTIKRQL 95

                          90       100
                  ....*....|....*....|...
gi 1958647007  86 EEIKRRAQSNgkwpQIMIFPEGT 108
Cdd:cd07990    96 KRLKDSPEPF----WLLIFPEGT 114
S-100A1 cd05025
S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding ...
 248-310 5.74e-03

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


Pssm-ID: 240152 [Multi-domain]  Cd Length: 92  Bit Score: 36.02  E-value: 5.74e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958647007 248 KDLDKY----SESARMKRGEkirLPEFAAYLEVPvsDALEDMFSLFDESGGGEIDLREYVV---ALSVVC 310
Cdd:cd05025    21 KEGDKYklskKELKDLLQTE---LSDFLDAQKDA--DAVDKIMKELDENGDGEVDFQEFVVlvaALTVAC 85
 
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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