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Conserved domains on  [gi|110815903|sp|Q3TFD2|]
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RecName: Full=Lysophosphatidylcholine acyltransferase 1; Short=LPC acyltransferase 1; Short=LPCAT-1; Short=LysoPC acyltransferase 1; Short=mLPCAT1; AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase; AltName: Full=1-acylglycerophosphocholine O-acyltransferase; AltName: Full=1-alkenylglycerophosphocholine O-acyltransferase; AltName: Full=1-alkylglycerophosphocholine O-acetyltransferase; AltName: Full=Acetyl-CoA:lyso-platelet-activating factor acetyltransferase; Short=Acetyl-CoA:lyso-PAF acetyltransferase; Short=Lyso-PAF acetyltransferase; Short=LysoPAFAT; AltName: Full=Acyltransferase-like 2

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 103-314 1.67e-97

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: 294.13  E-value: 1.67e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 103 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQD 181
Cdd:cd07991    1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 182 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNKLDTITWTWQGPGALKILWLT 261
Cdd:cd07991   80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 110815903 262 LCQFQNQVEIEFLPVYCPSEEEKrNPALYASNVRRVMAKALGVSVTDYTFEDC 314
Cdd:cd07991  159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
EF-hand_8 pfam13833
EF-hand domain pair;
432-483 2.93e-09

EF-hand domain pair;


:

Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 53.09  E-value: 2.93e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110815903  432 EDGSIDEANLSCILKTAL--GVSELTVTDLFQAIDQEDKGRITFDDFCGFAEMY 483
Cdd:pfam13833   1 EKGVITREELKRALALLGlkDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
FRQ1 super family cl34916
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
384-494 1.45e-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: 47.86  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 384 LEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTlATIQLAFKMYGSPEDGSIDEANLSCILkTALGVSELTVTDLFQAI 463
Cdd:COG5126   35 WATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL-TALGVSEEEADELFARL 112

                         90       100       110
                 ....*....|....*....|....*....|.
gi 110815903 464 DQEDKGRITFDDFCgfaemypDYAEDYLYPD 494
Cdd:COG5126  113 DTDGDGKISFEEFV-------AAVRDYYTPD 136
EFh super family cl08302
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 350-412 7.24e-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: 7.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 350 KDLDKY----SESARMKRGEkirLPEFAAYLEVPvsDALEDMFSLFDESGGGEIDLREYVV---ALSVVC 412
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; ...
 103-314 1.67e-97

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: 294.13  E-value: 1.67e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 103 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQD 181
Cdd:cd07991    1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 182 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNKLDTITWTWQGPGALKILWLT 261
Cdd:cd07991   80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 110815903 262 LCQFQNQVEIEFLPVYCPSEEEKrNPALYASNVRRVMAKALGVSVTDYTFEDC 314
Cdd:cd07991  159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 88-303 5.82e-28

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


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 111.25  E-value: 5.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903  88 LALWRKVVDFLLKAIMRTMWFAGGFhRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPIWG 164
Cdd:COG0204    5 FLLLRRFRYRLVRLWARLLLRLLGV-RVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPrpvRFVAKKELFKIPLLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 165 TLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRYpn 240
Cdd:COG0204   84 WLLRALGAIPVDRSKRRAALRALRQAVEALK-AGES--LVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG-- 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815903 241 kldtiTWTWQGPGALKilwltlcqFQNQVEIEFLPVYCPSEEEKRNPALYASNVRRVMAKALG 303
Cdd:COG0204  159 -----TERALPKGFLP--------RPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 129-238 1.79e-23

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


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 95.50  E-value: 1.79e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903   129 ILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKwpq 202
Cdd:smart00563   1 ALVVANHQSFLDPLvlsallPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGEW--- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 110815903   203 IMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRY 238
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 114-236 2.99e-21

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: 89.65  E-value: 2.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903  114 RVAVKGRQALPTEAAILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTV 187
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLllslalYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110815903  188 EEIKRRaQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVL 236
Cdd:pfam01553  81 EYLVEL-LREGKL--VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPVAI 130
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 115-237 7.28e-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: 7.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903  115 VAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQ---DSRRKTVE 188
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFpppIVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALKAAI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110815903  189 EIKRRAQSngkwpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLR 237
Cdd:TIGR00530  84 EVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
EF-hand_8 pfam13833
EF-hand domain pair;
432-483 2.93e-09

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 53.09  E-value: 2.93e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110815903  432 EDGSIDEANLSCILKTAL--GVSELTVTDLFQAIDQEDKGRITFDDFCGFAEMY 483
Cdd:pfam13833   1 EKGVITREELKRALALLGlkDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
PLN02833 PLN02833
glycerol acyltransferase family protein
 46-242 7.45e-08

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 54.39  E-value: 7.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903  46 VAFMTLTLFPIRLLFaafmMLLAWpFALLASLGPPD---KEPEQPLALWRKVVDFLLKAimrtmwFAGGFHRVaVKGRQA 122
Cdd:PLN02833  90 VVIRYGILFPVRVLL----LAIGW-IIFLSAFIPVHfllKGHKLRKKIERKLVELICSA------FVASWTGV-IKYHGP 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 123 LPTE-AAILTLAPHSSYFDAIPVT-MTMSSIVMKAEsrdiPIW-----GTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQ 195
Cdd:PLN02833 158 RPSRrPKQVFVANHTSMIDFIVLEqMTPFAVIMQKH----PGWvgflqNTILESVGCIWFNRTEAKDREVVAKKLRDHVQ 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 110815903 196 SNGKWPqIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYpNKL 242
Cdd:PLN02833 234 DPDRNP-LLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKY-NKI 278
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
384-494 1.45e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 384 LEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTlATIQLAFKMYGSPEDGSIDEANLSCILkTALGVSELTVTDLFQAI 463
Cdd:COG5126   35 WATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL-TALGVSEEEADELFARL 112

                         90       100       110
                 ....*....|....*....|....*....|.
gi 110815903 464 DQEDKGRITFDDFCgfaemypDYAEDYLYPD 494
Cdd:COG5126  113 DTDGDGKISFEEFV-------AAVRDYYTPD 136
PTZ00184 PTZ00184
calmodulin; Provisional
 379-477 2.48e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.45  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 379 PVSDALEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTLATIQLAFKMYGSPEDGSIDEANLSCILkTALG--VSELTV 456
Cdd:PTZ00184  44 PTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEV 122

                         90       100
                 ....*....|....*....|.
gi 110815903 457 TDLFQAIDQEDKGRITFDDFC 477
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 ...
 385-476 2.15e-05

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: 44.90  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 385 EDMFSLFDESGGGEIDLREYVvALSvvcrpsQTLATIQLAFKMYGSPEDGSIDEANLSCILKTA-LGVSELTVTDLFQAI 463
Cdd:cd16185   39 EKLIRMFDRDGNGTIDFEEFA-ALH------QFLSNMQNGFEQRDTSRSGRLDANEVHEALAASgFQLDPPAFQALFRKF 111

                         90
                 ....*....|...
gi 110815903 464 DQEDKGRITFDDF 476
Cdd:cd16185  112 DPDRGGSLGFDDY 124
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 421-477 1.15e-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: 37.53  E-value: 1.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 110815903 421 IQLAFKMYGSPEDGSIDEANLSCILKTA-LGVSELTVTDLFQAIDQEDKGRITFDDFC 477
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLgEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
S-100A1 cd05025
S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding ...
 350-412 7.24e-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: 7.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 350 KDLDKY----SESARMKRGEkirLPEFAAYLEVPvsDALEDMFSLFDESGGGEIDLREYVV---ALSVVC 412
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; ...
 103-314 1.67e-97

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: 294.13  E-value: 1.67e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 103 MRTMWFAGGFHRVAVKGRQALPtEAAILTLAPHSSYFDAIPVT-MTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQD 181
Cdd:cd07991    1 ARVLLFAFGFYVIKVHGKPDPP-EAPRIIVANHTSFIDPLILFsDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 182 SRRKTVEEIKRRAQSNgKWPQIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYPNKLDTITWTWQGPGALKILWLT 261
Cdd:cd07991   80 DRKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 110815903 262 LCQFQNQVEIEFLPVYCPSEEEKrNPALYASNVRRVMAKALGVSVTDYTFEDC 314
Cdd:cd07991  159 LTQPANVLEVEFLPVYTPSEEGE-DPKEFANRVRLIMANKLGLPATDWTGEDK 210
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 88-303 5.82e-28

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


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 111.25  E-value: 5.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903  88 LALWRKVVDFLLKAIMRTMWFAGGFhRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPIWG 164
Cdd:COG0204    5 FLLLRRFRYRLVRLWARLLLRLLGV-RVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPrpvRFVAKKELFKIPLLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 165 TLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRYpn 240
Cdd:COG0204   84 WLLRALGAIPVDRSKRRAALRALRQAVEALK-AGES--LVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG-- 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815903 241 kldtiTWTWQGPGALKilwltlcqFQNQVEIEFLPVYCPSEEEKRNPALYASNVRRVMAKALG 303
Cdd:COG0204  159 -----TERALPKGFLP--------RPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 107-299 7.17e-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: 104.42  E-value: 7.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 107 WFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTM-------TMSSIVMKAES-RDIPIWGTLiryiRPVFVSRS 178
Cdd:cd06551    6 LNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLllerglrRDVYGLMDEELlERYPFFTRL----GAFSVDRD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 179 DQDSRRKTVEEIKRRAQSNGKWpqIMIFPEGTCTN-RTCLITFKPGAFIP----GVPVQPVVLRYPNkldtitwtwqgpg 253
Cdd:cd06551   82 SPRSAAKSLKYVARLLSKPGSV--VWIFPEGTRTRrDKRPLQFKPGVAHLaekaGVPIVPVALRYTF------------- 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 110815903 254 alkilWLTLCQFQNQVEIEFLPVYCPSEEEKRNPALYASNVRRVMA 299
Cdd:cd06551  147 -----ELFEQFPEIFVRIGPPIPYAETALGEELAAELANRLTRLLD 187
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 106-257 1.84e-24

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: 100.42  E-value: 1.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 106 MWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDS 182
Cdd:cd07989    3 LLLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALprpIRFVAKKELFKIPFLGWLLRLLGAIPIDRGNGRS 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110815903 183 RRKTVEEIKRRAQsNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRYPNKLDTITWTWQGPGALKI 257
Cdd:cd07989   83 AREALREAIEALK-EGES--VVIFPEGTRSRDGELLPFKSGAFRlakeAGVPIVPVAISGTWGSLPKGKKLPRPGRVTV 158
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 129-238 1.79e-23

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


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 95.50  E-value: 1.79e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903   129 ILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQSNGKwpq 202
Cdd:smart00563   1 ALVVANHQSFLDPLvlsallPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGEW--- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 110815903   203 IMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLRY 238
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 114-236 2.99e-21

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: 89.65  E-value: 2.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903  114 RVAVKGRQALPTEAAILTLAPHSSYFDAI------PVTMTMSSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQDSRRKTV 187
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLllslalYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110815903  188 EEIKRRaQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVL 236
Cdd:pfam01553  81 EYLVEL-LREGKL--VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPVAI 130
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 115-237 7.28e-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: 7.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903  115 VAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTM---SSIVMKAESRDIPIWGTLIRYIRPVFVSRSDQ---DSRRKTVE 188
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFpppIVFIAKKELKWIPFFGIMLWLTGAIFIDRENIraiATALKAAI 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 110815903  189 EIKRRAQSngkwpqIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVLR 237
Cdd:TIGR00530  84 EVLKQGRS------IGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 91-241 9.86e-12

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: 64.21  E-value: 9.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903  91 WRKVVDFLLKaimrtmWFaggFHRVAVKGRQALPTEAAILTLAPHS-SYFDAIPVTMTMS---SIVMKAESRDIPIWGTL 166
Cdd:cd07992    1 VRLLSRVILR------IY---FRRITVVGRENVPKDGPVIFLGNHPnALIDPLLLAATLRrpvRFLAKADLFKNPLIGWL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 167 IRYIRPVFVSRsDQDSRRKTVEEIK--------RRAQSNGKWpqIMIFPEGTCTNRTCLITFKPGAFI----------PG 228
Cdd:cd07992   72 LESFGAIPVYR-PKDLARGGIGKISnaavfdavGEALKAGGA--IGIFPEGGSHDRPRLLPLKAGAARmalealeagqKD 148

                        170
                 ....*....|...
gi 110815903 229 VPVQPVVLRYPNK 241
Cdd:cd07992  149 VKIVPVGLNYEDK 161
EF-hand_8 pfam13833
EF-hand domain pair;
432-483 2.93e-09

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 53.09  E-value: 2.93e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 110815903  432 EDGSIDEANLSCILKTAL--GVSELTVTDLFQAIDQEDKGRITFDDFCGFAEMY 483
Cdd:pfam13833   1 EKGVITREELKRALALLGlkDLSEDEVDILFREFDTDGDGYISFDEFCVLLERR 54
EF-hand_7 pfam13499
EF-hand domain pair;
421-480 2.89e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 50.33  E-value: 2.89e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815903  421 IQLAFKMYGSPEDGSIDEANLSCILKTALGVSELT---VTDLFQAIDQEDKGRITFDDFCGFA 480
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPLSdeeVEELFKEFDLDKDGRISFEEFLELY 66
PLN02833 PLN02833
glycerol acyltransferase family protein
 46-242 7.45e-08

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 54.39  E-value: 7.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903  46 VAFMTLTLFPIRLLFaafmMLLAWpFALLASLGPPD---KEPEQPLALWRKVVDFLLKAimrtmwFAGGFHRVaVKGRQA 122
Cdd:PLN02833  90 VVIRYGILFPVRVLL----LAIGW-IIFLSAFIPVHfllKGHKLRKKIERKLVELICSA------FVASWTGV-IKYHGP 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 123 LPTE-AAILTLAPHSSYFDAIPVT-MTMSSIVMKAEsrdiPIW-----GTLIRYIRPVFVSRSDQDSRRKTVEEIKRRAQ 195
Cdd:PLN02833 158 RPSRrPKQVFVANHTSMIDFIVLEqMTPFAVIMQKH----PGWvgflqNTILESVGCIWFNRTEAKDREVVAKKLRDHVQ 233

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 110815903 196 SNGKWPqIMIFPEGTCTNRTCLITFKPGAFIPGVPVQPVVLRYpNKL 242
Cdd:PLN02833 234 DPDRNP-LLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKY-NKI 278
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
384-494 1.45e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 47.86  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 384 LEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTlATIQLAFKMYGSPEDGSIDEANLSCILkTALGVSELTVTDLFQAI 463
Cdd:COG5126   35 WATLFSEADTDGDGRISREEFVAGMESLFEATVE-PFARAAFDLLDTDGDGKISADEFRRLL-TALGVSEEEADELFARL 112

                         90       100       110
                 ....*....|....*....|....*....|.
gi 110815903 464 DQEDKGRITFDDFCgfaemypDYAEDYLYPD 494
Cdd:COG5126  113 DTDGDGKISFEEFV-------AAVRDYYTPD 136
PTZ00184 PTZ00184
calmodulin; Provisional
 379-477 2.48e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 47.45  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 379 PVSDALEDMFSLFDESGGGEIDLREYVVALSVVCRPSQTLATIQLAFKMYGSPEDGSIDEANLSCILkTALG--VSELTV 456
Cdd:PTZ00184  44 PTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEV 122

                         90       100
                 ....*....|....*....|.
gi 110815903 457 TDLFQAIDQEDKGRITFDDFC 477
Cdd:PTZ00184 123 DEMIREADVDGDGQINYEEFV 143
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 92-237 2.65e-06

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 50.31  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903   92 RKVVDFLLKAIMrtMWFAGGFHRVAVKGRQALPTEAAILTLAPHSSYFDAIPVTMTMS---SIVMKAESRDIPiwgtlir 168
Cdd:PRK08633  408 LLLPDSLLRFLL--LLLMHTRYRLRVEGRENIPAKGGALLLGNHVSWIDWALLQAASPrpiRFVMERSIYEKW------- 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903  169 YIRPVF-------VSrsdQDSRRKTVEEIkRRAQSNGKwpQIMIFPEGTCTNRTCLITFKPG----AFIPGVPVQPVVLR 237
Cdd:PRK08633  479 YLKWFFklfgvipIS---SGGSKESLEFI-RKALDDGE--VVCIFPEGAITRNGQLNEFKRGfeliVKGTDVPIIPFYIR 552
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 385-476 2.15e-05

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: 44.90  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 385 EDMFSLFDESGGGEIDLREYVvALSvvcrpsQTLATIQLAFKMYGSPEDGSIDEANLSCILKTA-LGVSELTVTDLFQAI 463
Cdd:cd16185   39 EKLIRMFDRDGNGTIDFEEFA-ALH------QFLSNMQNGFEQRDTSRSGRLDANEVHEALAASgFQLDPPAFQALFRKF 111

                         90
                 ....*....|...
gi 110815903 464 DQEDKGRITFDDF 476
Cdd:cd16185  112 DPDRGGSLGFDDY 124
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 384-437 2.60e-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: 39.07  E-value: 2.60e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 110815903 384 LEDMFSLFDESGGGEIDLREYVVALSvVCRPSQTLATIQLAFKMYGSPEDGSID 437
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALK-SLGEGLSEEEIDEMIREVDKDGDGKID 54
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 421-477 1.15e-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: 37.53  E-value: 1.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 110815903 421 IQLAFKMYGSPEDGSIDEANLSCILKTA-LGVSELTVTDLFQAIDQEDKGRITFDDFC 477
Cdd:cd00051    2 LREAFRLFDKDGDGTISADELKAALKSLgEGLSEEEIDEMIREVDKDGDGKIDFEEFL 59
LPLAT_LCLAT1-like cd07990
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; ...
 123-210 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: 40.30  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 123 LPTEAAILtLAPHSSYFDAIpVTMTMSS---------IVMKAESRDIPI--WGTLI-RYIrpvFVSRS---DQDSRRKTV 187
Cdd:cd07990   21 LPKERALI-ISNHRSEVDWL-VLWMLADrfgrlgrlkIVLKDSLKYPPLggWGWQLgEFI---FLKRKwekDEKTIKRQL 95

                         90       100
                 ....*....|....*....|...
gi 110815903 188 EEIKRRAQSNgkwpQIMIFPEGT 210
Cdd:cd07990   96 KRLKDSPEPF----WLLIFPEGT 114
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 112-236 1.38e-03

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


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 40.10  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 112 FHRVAVKGRQALPT-EAAILTLAPHSSYFDaIPVTMTMS---SIVMKAESRDIPIWGTLIRYIRPVFVSRSDqdsRRKTV 187
Cdd:PLN02901  34 FYKIEVEGLENLPSpDEPAVYVSNHQSFLD-IYTLFHLGrpfKFISKTSIFLIPIIGWAMYMTGHIPLKRMD---RRSQL 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 110815903 188 EEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFI----PGVPVQPVVL 236
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 ...
 388-476 3.39e-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: 38.28  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 388 FSLFDESGGGEIDLREYVVAL-SVVCRPSQTlaTIQLAFKMYGSPEDGSIDEAN---LSCILKtalgvselTVTDLFQAI 463
Cdd:cd16180   73 FRRFDRDRSGSIDFNELQNALsSFGYRLSPQ--FVQLLVRKFDRRRRGSISFDDfveACVTLK--------RLTDAFRKY 142

                         90
                 ....*....|....*
gi 110815903 464 DQEDKGRIT--FDDF 476
Cdd:cd16180  143 DTNRTGYATisYEDF 157
S-100A1 cd05025
S-100A1: S-100A1 domain found in proteins similar to S100A1. S100A1 is a calcium-binding ...
 350-412 7.24e-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: 7.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815903 350 KDLDKY----SESARMKRGEkirLPEFAAYLEVPvsDALEDMFSLFDESGGGEIDLREYVV---ALSVVC 412
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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