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Conserved domains on  [gi|12853070|dbj|BAB29630|]
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unnamed protein product [Mus musculus]

Protein Classification

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; ...
 111-323 3.80e-82

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: 254.07  E-value: 3.80e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 111 FRLGFFFAGF-LVKVKGKKATREEAPIFVsAPHSTFFDAIAVVVAGLPSVVSDSQLARVPLAGKCILVTQPVLVKREDPN 189
Cdd:cd07991   1 ARVLLFAFGFyVIKVHGKPDPPEAPRIIV-ANHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 190 SRKTTRNEILRRVKSkMKWPQILIFPEGLCTNRSCLVTFKLGAFSPGVPVQPVLLRYPNSLDTVTWTWNGFSGFQVCMLT 269
Cdd:cd07991  80 DRKKVVEEIKERATD-PNWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 12853070 270 LSQLFTRVEVEFMPVYIPSeEEKKDPILFANTVRIKMANALKLPVTDHSLEDCK 323
Cdd:cd07991 159 LTQPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
392-487 2.33e-11

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 2.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 392 LRQLFSLFDRNQDGTIDFREYVIGLTVLCNPSNTEKILQMsFKLFDLDEDGYVTERELTTMLQaAFGVPDLDVSTLFQQM 471
Cdd:COG5126  35 WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAA-FDLLDTDGDGKISADEFRRLLT-ALGVSEEEADELFARL 112

                        90
                ....*....|....*....
gi 12853070 472 agkDSDQ---VSYRTFRRF 487
Cdd:COG5126 113 ---DTDGdgkISFEEFVAA 128
EFh_PEF super family cl25352
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 318-445 3.15e-04

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


The actual alignment was detected with superfamily member cd15897:

Pssm-ID: 355382 [Multi-domain]  Cd Length: 165  Bit Score: 41.65  E-value: 3.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 318 SLEDCKLMISAGALQLPMEAGLVEFTKISQKLKlDWDNIHKHLDQYASFAVSSKGGKIGIEAFSRYLklpiSEPLRQ-LF 396
Cdd:cd15897  38 SLETCRSMIAMMDRDHSGKLNFSEFKGLWNYIK-AWQEIFRTYDTDGSGTIDSNELRQALSGAGYRL----SEQTYDiII 112

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 12853070 397 SLFDRNQdGTIDFREYVIGLTVLCNPSNtekilqmSFKLFDLDEDGYVT 445
Cdd:cd15897 113 RRYDRGR-GNIDFDDFIQCCVRLQRLTD-------AFRRYDKDQDGQIQ 153
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 111-323 3.80e-82

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: 254.07  E-value: 3.80e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 111 FRLGFFFAGF-LVKVKGKKATREEAPIFVsAPHSTFFDAIAVVVAGLPSVVSDSQLARVPLAGKCILVTQPVLVKREDPN 189
Cdd:cd07991   1 ARVLLFAFGFyVIKVHGKPDPPEAPRIIV-ANHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 190 SRKTTRNEILRRVKSkMKWPQILIFPEGLCTNRSCLVTFKLGAFSPGVPVQPVLLRYPNSLDTVTWTWNGFSGFQVCMLT 269
Cdd:cd07991  80 DRKKVVEEIKERATD-PNWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 12853070 270 LSQLFTRVEVEFMPVYIPSeEEKKDPILFANTVRIKMANALKLPVTDHSLEDCK 323
Cdd:cd07991 159 LTQPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 95-311 3.88e-17

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: 80.05  E-value: 3.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070  95 IRRWRKHLIKSALVFLFRLgfffAGFLVKVKGKKATREEAPIFVSAPHSTFFDAIAV--VVAGLPSVVSDSQLARVPLAG 172
Cdd:COG0204   8 LRRFRYRLVRLWARLLLRL----LGVRVRVEGLENLPADGPVLIVANHQSWLDILLLlaALPRPVRFVAKKELFKIPLLG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 173 KCILVTQPVLVKREDPNSRKTTRNEILRRVKSKMkwpQILIFPEGLCTNRSCLVTFKLGAF----SPGVPVQPVLLRYpn 248
Cdd:COG0204  84 WLLRALGAIPVDRSKRRAALRALRQAVEALKAGE---SLVIFPEGTRSPDGRLLPFKTGAArlalEAGVPIVPVAIDG-- 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12853070 249 sldtvTWTWNGFSGFqvcmltlsQLFTRVEVEFMPVYIPSEEEKKDPILFANTVRIKMANALK 311
Cdd:COG0204 159 -----TERALPKGFL--------PRPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 136-246 3.28e-14

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: 68.92  E-value: 3.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070    136 IFVsAPHSTFFDAIAVVVA-----GLPSVVSDSQLARVPLAGKCILVTQPVLVKREDPNSRKTTRNEILRRVKSKMKwpq 210
Cdd:smart00563   2 LVV-ANHQSFLDPLVLSALlprklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGEW--- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 12853070    211 ILIFPEGLCTNRSCLVTFKLGAFS----PGVPVQPVLLRY 246
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
392-487 2.33e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 2.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 392 LRQLFSLFDRNQDGTIDFREYVIGLTVLCNPSNTEKILQMsFKLFDLDEDGYVTERELTTMLQaAFGVPDLDVSTLFQQM 471
Cdd:COG5126  35 WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAA-FDLLDTDGDGKISADEFRRLLT-ALGVSEEEADELFARL 112

                        90
                ....*....|....*....
gi 12853070 472 agkDSDQ---VSYRTFRRF 487
Cdd:COG5126 113 ---DTDGdgkISFEEFVAA 128
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 392-454 5.70e-11

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: 57.94  E-value: 5.70e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12853070 392 LRQLFSLFDRNQDGTIDFREYVIGLTVLcNPSNTEKILQMSFKLFDLDEDGYVTERELTTMLQ 454
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 122-242 2.01e-10

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: 58.44  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070   122 VKVKGKKATREEAPIFVSAPHSTFFD-----AIAVVVAGLPSVVSDSQLARVPLAGKCILVTQPVLVKREDPNSRKTTRN 196
Cdd:pfam01553   2 IEVHGLENLPRGGPAIVVANHQSYLDvlllsLALYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTLE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 12853070   197 EILRRVKSKMKwpqILIFPEGLCTNRSCLVTFKLGAFS----PGVPVQPV 242
Cdd:pfam01553  82 YLVELLREGKL---VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPV 128
PLN02833 PLN02833
glycerol acyltransferase family protein
 51-313 2.50e-07

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 52.85  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070   51 WACTIILG-TVLVPVRvscivFLLILLWPVAVLSAINLPTQPTKPIRRWRKhlIKSALVFLFrLGFFFAGF--LVKVKGK 127
Cdd:PLN02833  86 WCVGVVIRyGILFPVR-----VLLLAIGWIIFLSAFIPVHFLLKGHKLRKK--IERKLVELI-CSAFVASWtgVIKYHGP 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070  128 KATREEAPIFVsAPHSTFFDAIAVVVAGLPSVVSDSQLARVPLAGKCILVTQPVL-VKREDPNSRKTTRNEILRRVKSKM 206
Cdd:PLN02833 158 RPSRRPKQVFV-ANHTSMIDFIVLEQMTPFAVIMQKHPGWVGFLQNTILESVGCIwFNRTEAKDREVVAKKLRDHVQDPD 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070  207 KWPqILIFPEGLCTNRSCLVTFKLGAFSPGVPVQPVLLRYPNSLdtVTWTWNgfSGFQVCMLTLSQLFTR----VEVEFM 282
Cdd:PLN02833 237 RNP-LLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKYNKIF--VDAFWN--SRKQSFTMHLLRLMTSwavvCDVWYL 311

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 12853070  283 -PVYIPSEEekkDPILFANTVR---IKMANALKLP 313
Cdd:PLN02833 312 ePQTLRPGE---TPIEFAERVRdmiAKRAGLKKVP 343
EF-hand_7 pfam13499
EF-hand domain pair;
392-454 4.20e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 4.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12853070   392 LRQLFSLFDRNQDGTIDFREYVIGLTVLCNPSN-TEKILQMSFKLFDLDEDGYVTERELTTMLQ 454
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00183 PTZ00183
centrin; Provisional
 387-449 1.41e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 45.45  E-value: 1.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12853070  387 PISEPLRQLFSLFDRNQDGTIDFREYVIGLTV-LCNPSNTEKILQMsFKLFDLDEDGYVTEREL 449
Cdd:PTZ00183  50 PKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKkLGERDPREEILKA-FRLFDDDKTGKISLKNL 112
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 318-445 3.15e-04

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


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 41.65  E-value: 3.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 318 SLEDCKLMISAGALQLPMEAGLVEFTKISQKLKlDWDNIHKHLDQYASFAVSSKGGKIGIEAFSRYLklpiSEPLRQ-LF 396
Cdd:cd15897  38 SLETCRSMIAMMDRDHSGKLNFSEFKGLWNYIK-AWQEIFRTYDTDGSGTIDSNELRQALSGAGYRL----SEQTYDiII 112

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 12853070 397 SLFDRNQdGTIDFREYVIGLTVLCNPSNtekilqmSFKLFDLDEDGYVT 445
Cdd:cd15897 113 RRYDRGR-GNIDFDDFIQCCVRLQRLTD-------AFRRYDKDQDGQIQ 153
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 392-417 4.17e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.74  E-value: 4.17e-04
                           10        20
                   ....*....|....*....|....*.
gi 12853070    392 LRQLFSLFDRNQDGTIDFREYVIGLT 417
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 111-323 3.80e-82

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: 254.07  E-value: 3.80e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 111 FRLGFFFAGF-LVKVKGKKATREEAPIFVsAPHSTFFDAIAVVVAGLPSVVSDSQLARVPLAGKCILVTQPVLVKREDPN 189
Cdd:cd07991   1 ARVLLFAFGFyVIKVHGKPDPPEAPRIIV-ANHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 190 SRKTTRNEILRRVKSkMKWPQILIFPEGLCTNRSCLVTFKLGAFSPGVPVQPVLLRYPNSLDTVTWTWNGFSGFQVCMLT 269
Cdd:cd07991  80 DRKKVVEEIKERATD-PNWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 12853070 270 LSQLFTRVEVEFMPVYIPSeEEKKDPILFANTVRIKMANALKLPVTDHSLEDCK 323
Cdd:cd07991 159 LTQPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 95-311 3.88e-17

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: 80.05  E-value: 3.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070  95 IRRWRKHLIKSALVFLFRLgfffAGFLVKVKGKKATREEAPIFVSAPHSTFFDAIAV--VVAGLPSVVSDSQLARVPLAG 172
Cdd:COG0204   8 LRRFRYRLVRLWARLLLRL----LGVRVRVEGLENLPADGPVLIVANHQSWLDILLLlaALPRPVRFVAKKELFKIPLLG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 173 KCILVTQPVLVKREDPNSRKTTRNEILRRVKSKMkwpQILIFPEGLCTNRSCLVTFKLGAF----SPGVPVQPVLLRYpn 248
Cdd:COG0204  84 WLLRALGAIPVDRSKRRAALRALRQAVEALKAGE---SLVIFPEGTRSPDGRLLPFKTGAArlalEAGVPIVPVAIDG-- 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12853070 249 sldtvTWTWNGFSGFqvcmltlsQLFTRVEVEFMPVYIPSEEEKKDPILFANTVRIKMANALK 311
Cdd:COG0204 159 -----TERALPKGFL--------PRPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 111-294 2.48e-14

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: 71.15  E-value: 2.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 111 FRLGFFFAGFLVKVKGKKATREEAPIFVSAPHSTFFDAIAVVVAGLPSV--VSDSQLARVPLAGKCILVTQPVLVKREDP 188
Cdd:cd07989   1 LRLLLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALPRPIrfVAKKELFKIPFLGWLLRLLGAIPIDRGNG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 189 NSRKTTRNEILRRVKSKMKwpqILIFPEGLCTNRSCLVTFKLGAFS----PGVPVQPVLLRYpnsldtvTWTWnGFSGFq 264
Cdd:cd07989  81 RSAREALREAIEALKEGES---VVIFPEGTRSRDGELLPFKSGAFRlakeAGVPIVPVAISG-------TWGS-LPKGK- 148

                       170       180       190
                ....*....|....*....|....*....|
gi 12853070 265 vcmltLSQLFTRVEVEFMPVYIPSEEEKKD 294
Cdd:cd07989 149 -----KLPRPGRVTVRIGEPIPPEGLELAE 173
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 136-246 3.28e-14

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: 68.92  E-value: 3.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070    136 IFVsAPHSTFFDAIAVVVA-----GLPSVVSDSQLARVPLAGKCILVTQPVLVKREDPNSRKTTRNEILRRVKSKMKwpq 210
Cdd:smart00563   2 LVV-ANHQSFLDPLVLSALlprklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGEW--- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 12853070    211 ILIFPEGLCTNRSCLVTFKLGAFS----PGVPVQPVLLRY 246
Cdd:smart00563  78 LLIFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
392-487 2.33e-11

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 61.35  E-value: 2.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 392 LRQLFSLFDRNQDGTIDFREYVIGLTVLCNPSNTEKILQMsFKLFDLDEDGYVTERELTTMLQaAFGVPDLDVSTLFQQM 471
Cdd:COG5126  35 WATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAA-FDLLDTDGDGKISADEFRRLLT-ALGVSEEEADELFARL 112

                        90
                ....*....|....*....
gi 12853070 472 agkDSDQ---VSYRTFRRF 487
Cdd:COG5126 113 ---DTDGdgkISFEEFVAA 128
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 392-454 5.70e-11

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: 57.94  E-value: 5.70e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12853070 392 LRQLFSLFDRNQDGTIDFREYVIGLTVLcNPSNTEKILQMSFKLFDLDEDGYVTERELTTMLQ 454
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 122-242 2.01e-10

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: 58.44  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070   122 VKVKGKKATREEAPIFVSAPHSTFFD-----AIAVVVAGLPSVVSDSQLARVPLAGKCILVTQPVLVKREDPNSRKTTRN 196
Cdd:pfam01553   2 IEVHGLENLPRGGPAIVVANHQSYLDvlllsLALYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTLE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 12853070   197 EILRRVKSKMKwpqILIFPEGLCTNRSCLVTFKLGAFS----PGVPVQPV 242
Cdd:pfam01553  82 YLVELLREGKL---VVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPV 128
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 109-254 6.73e-10

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: 58.58  E-value: 6.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 109 FLFRLGFFFAGFLVKVKGKKATREEAPIFVSAPHSTFFDAIAVVVAGLPS-------VVSDSQLARVPLAGKCilvtQPV 181
Cdd:cd06551   1 FRYLLLNFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLILFLLLERGlrrdvygLMDEELLERYPFFTRL----GAF 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12853070 182 LVKREDPNSRKTTRNEILRRVKSkmKWPQILIFPEGLCTNRS-CLVTFKLGAFSP----GVPVQPVLLRYPNSLDTVT 254
Cdd:cd06551  77 SVDRDSPRSAAKSLKYVARLLSK--PGSVVWIFPEGTRTRRDkRPLQFKPGVAHLaekaGVPIVPVALRYTFELFEQF 152
PLN02833 PLN02833
glycerol acyltransferase family protein
 51-313 2.50e-07

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 52.85  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070   51 WACTIILG-TVLVPVRvscivFLLILLWPVAVLSAINLPTQPTKPIRRWRKhlIKSALVFLFrLGFFFAGF--LVKVKGK 127
Cdd:PLN02833  86 WCVGVVIRyGILFPVR-----VLLLAIGWIIFLSAFIPVHFLLKGHKLRKK--IERKLVELI-CSAFVASWtgVIKYHGP 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070  128 KATREEAPIFVsAPHSTFFDAIAVVVAGLPSVVSDSQLARVPLAGKCILVTQPVL-VKREDPNSRKTTRNEILRRVKSKM 206
Cdd:PLN02833 158 RPSRRPKQVFV-ANHTSMIDFIVLEQMTPFAVIMQKHPGWVGFLQNTILESVGCIwFNRTEAKDREVVAKKLRDHVQDPD 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070  207 KWPqILIFPEGLCTNRSCLVTFKLGAFSPGVPVQPVLLRYPNSLdtVTWTWNgfSGFQVCMLTLSQLFTR----VEVEFM 282
Cdd:PLN02833 237 RNP-LLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKYNKIF--VDAFWN--SRKQSFTMHLLRLMTSwavvCDVWYL 311

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 12853070  283 -PVYIPSEEekkDPILFANTVR---IKMANALKLP 313
Cdd:PLN02833 312 ePQTLRPGE---TPIEFAERVRdmiAKRAGLKKVP 343
EF-hand_7 pfam13499
EF-hand domain pair;
392-454 4.20e-07

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 47.25  E-value: 4.20e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12853070   392 LRQLFSLFDRNQDGTIDFREYVIGLTVLCNPSN-TEKILQMSFKLFDLDEDGYVTERELTTMLQ 454
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00183 PTZ00183
centrin; Provisional
 387-449 1.41e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 45.45  E-value: 1.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12853070  387 PISEPLRQLFSLFDRNQDGTIDFREYVIGLTV-LCNPSNTEKILQMsFKLFDLDEDGYVTEREL 449
Cdd:PTZ00183  50 PKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKkLGERDPREEILKA-FRLFDDDKTGKISLKNL 112
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 394-469 2.69e-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: 44.51  E-value: 2.69e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12853070 394 QLFSLFDRNQDGTIDFREYViGLtvlcnpsnTEKILQM--SFKLFDLDEDGYVTERELTTMLQAA-FGVPDLDVSTLFQ 469
Cdd:cd16185  40 KLIRMFDRDGNGTIDFEEFA-AL--------HQFLSNMqnGFEQRDTSRSGRLDANEVHEALAASgFQLDPPAFQALFR 109
PTZ00184 PTZ00184
calmodulin; Provisional
 387-486 5.15e-05

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 43.60  E-value: 5.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070  387 PISEPLRQLFSLFDRNQDGTIDFREYVIGLTVLCNPSNTEKILQMSFKLFDLDEDGYVTERELT-TMLQAAFGVPDLDVS 465
Cdd:PTZ00184  44 PTEAELQDMINEVDADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRhVMTNLGEKLTDEEVD 123

                         90       100
                 ....*....|....*....|..
gi 12853070  466 TLFQQmAGKDSD-QVSYRTFRR 486
Cdd:PTZ00184 124 EMIRE-ADVDGDgQINYEEFVK 144
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 380-421 2.08e-04

S-100: S-100 domain, which represents the largest family within the superfamily of proteins carrying the Ca-binding EF-hand motif. Note that this S-100 hierarchy contains only S-100 EF-hand domains, other EF-hands have been modeled separately. S100 proteins are expressed exclusively in vertebrates, and are implicated in intracellular and extracellular regulatory activities. Intracellularly, S100 proteins act as Ca-signaling or Ca-buffering proteins. The most unusual characteristic of certain S100 proteins is their occurrence in extracellular space, where they act in a cytokine-like manner through RAGE, the receptor for advanced glycation products. Structural data suggest that many S100 members exist within cells as homo- or heterodimers and even oligomers; oligomerization contributes to their functional diversification. Upon binding calcium, most S100 proteins change conformation to a more open structure exposing a hydrophobic cleft. This hydrophobic surface represents the interaction site of S100 proteins with their target proteins. There is experimental evidence showing that many S100 proteins have multiple binding partners with diverse mode of interaction with different targets. In addition to S100 proteins (such as S100A1,-3,-4,-6,-7,-10,-11,and -13), this group includes the ''fused'' gene family, a group of calcium binding S100-related proteins. The ''fused'' gene family includes multifunctional epidermal differentiation proteins - profilaggrin, trichohyalin, repetin, hornerin, and cornulin; functionally these proteins are associated with keratin intermediate filaments and partially crosslinked to the cell envelope. These ''fused'' gene proteins contain N-terminal sequence with two Ca-binding EF-hands motif, which may be associated with calcium signaling in epidermal cells and autoprocessing in a calcium-dependent manner. In contrast to S100 proteins, "fused" gene family proteins contain an extraordinary high number of almost perfect peptide repeats with regular array of polar and charged residues similar to many known cell envelope proteins.


Pssm-ID: 238131 [Multi-domain]  Cd Length: 88  Bit Score: 40.17  E-value: 2.08e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 12853070 380 FSRYLKLPISEP-LRQLFSLFDRNQDGTIDFREY---VIGLTVLCN 421
Cdd:cd00213  40 LPNFLKNQKDPEaVDKIMKDLDVNKDGKVDFQEFlvlIGKLAVACH 85
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 318-445 3.15e-04

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


Pssm-ID: 320054 [Multi-domain]  Cd Length: 165  Bit Score: 41.65  E-value: 3.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 318 SLEDCKLMISAGALQLPMEAGLVEFTKISQKLKlDWDNIHKHLDQYASFAVSSKGGKIGIEAFSRYLklpiSEPLRQ-LF 396
Cdd:cd15897  38 SLETCRSMIAMMDRDHSGKLNFSEFKGLWNYIK-AWQEIFRTYDTDGSGTIDSNELRQALSGAGYRL----SEQTYDiII 112

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 12853070 397 SLFDRNQdGTIDFREYVIGLTVLCNPSNtekilqmSFKLFDLDEDGYVT 445
Cdd:cd15897 113 RRYDRGR-GNIDFDDFIQCCVRLQRLTD-------AFRRYDKDQDGQIQ 153
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 392-417 4.17e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 37.74  E-value: 4.17e-04
                           10        20
                   ....*....|....*....|....*.
gi 12853070    392 LRQLFSLFDRNQDGTIDFREYVIGLT 417
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
PTZ00183 PTZ00183
centrin; Provisional
 390-487 7.70e-04

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 40.06  E-value: 7.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070  390 EPLRQLFSLFDRNQDGTIDFREYVIGLTVLCNPSNTEKILQMsfkLFDLDEDGYvterelttmlqaafGVPD----LDVS 465
Cdd:PTZ00183  17 KEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQM---IADVDKDGS--------------GKIDfeefLDIM 79

                         90       100
                 ....*....|....*....|..
gi 12853070  466 TlfQQMAGKDSDQVSYRTFRRF 487
Cdd:PTZ00183  80 T--KKLGERDPREEILKAFRLF 99
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
373-422 7.70e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.78  E-value: 7.70e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 12853070 373 GKIGIEAFSRYLK-LPISEP-LRQLFSLFDRNQDGTIDFREYVIGLTVLCNP 422
Cdd:COG5126  84 GKISADEFRRLLTaLGVSEEeADELFARLDTDGDGKISFEEFVAAVRDYYTP 135
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 392-419 1.04e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 36.61  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|....*...
gi 12853070   392 LRQLFSLFDRNQDGTIDFREYVIGLTVL 419
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EF-hand_7 pfam13499
EF-hand domain pair;
429-489 1.34e-03

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 37.23  E-value: 1.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12853070   429 LQMSFKLFDLDEDGYVTERELTTMLQA---AFGVPDLDVSTLFqQMAGKDSD-QVSYRTFRRFAL 489
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRKleeGEPLSDEEVEELF-KEFDLDKDgRISFEEFLELYS 67
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 433-495 1.42e-03

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 37.33  E-value: 1.42e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12853070 433 FKLFDLDEDGYVTERELTTMLQAaFGVPdldvstLFQQMAGKDSDQVSYRTFRRFALKHPAYA 495
Cdd:cd22949   9 FILFDRDGDGELTMYEAVLAMRS-CGIP------LTNDEKDALPASMNWDQFENWAKKKLAYS 64
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 429-487 1.47e-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: 37.14  E-value: 1.47e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12853070 429 LQMSFKLFDLDEDGYVTERELTTMLQAA-FGVPDLDVSTLFQQMagkDSD---QVSYRTFRRF 487
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSLgEGLSEEEIDEMIREV---DKDgdgKIDFEEFLEL 61
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 395-462 1.64e-03

EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin/dystrobrevin/dystrotelin family has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. Dystrophin is the founder member of this family. It is a sub-membrane cytoskeletal protein associated with the inner surface membrane. Dystrophin and its close paralog utrophin have a large N-terminal extension of actin-binding CH domains, up to 24 spectrin repeats, and a WW domain. Its further paralog, dystrophin-related protein 2 (DRP-2), retains only two of the spectrin repeats. Dystrophin, utrophin or DRP2 can form the core of a membrane-bound complex consisting of dystroglycan, sarcoglycans and syntrophins, known as the dystrophin-glycoprotein complex (DGC) that plays an important role in brain development and disease, as well as in the prevention of muscle damage. Dystrobrevins, including alpha- and beta-dystrobrevin, lack the large N-terminal extension found in dystrophin, but alpha-dystrobrevin has a characteristic C-terminal extension. Dystrobrevins are part of the DGC. They physically associate with members of the dystrophin family and with the syntrophins through their homologous C-terminal coiled coil motifs. In contrast, dystrotelins lack both the large N-terminal extension found in dystrophin and the obvious syntrophin-binding sites (SBSs). Dystrotelins are not critical for mammalian development. They may be involved in other forms of cytokinesis. Moreover, dystrotelin is unable to heterodimerize with members of the dystrophin or dystrobrevin families, or to homodimerize.


Pssm-ID: 319999  Cd Length: 163  Bit Score: 39.18  E-value: 1.64e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12853070 395 LFSLFDRNQDGTIDFREYVIGLTVLCNPSNTEKiLQMSFKLFDlDEDGYVTERELTTMLQAAFGVPDL 462
Cdd:cd15901  59 LLNLYDRNRTGCIRLLSVKIALITLCAASLLDK-YRYLFGQLA-DSSGFISRERLTQFLQDLLQIPDL 124
EFh_PEF_ALG-2 cd16183
EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar ...
 390-458 1.73e-03

EF-hand, calcium binding motif, found in apoptosis-linked gene 2 protein (ALG-2) and similar proteins; ALG-2, also termed programmed cell death protein 6 (PDCD6), or probable calcium-binding protein ALG-2, is one of the prototypic members of the penta EF-hand protein family. It is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. ALG-2 acts as a pro-apoptotic factor participating in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death, and also serves as a useful molecular marker for the prognosis of cancers. Moreover, ALG-2 functions as a calcium ion sensor at endoplasmic reticulum (ER) exit sites, and modulates ER-stress-stimulated cell death and neuronal apoptosis during organ formation. Furthermore, ALG-2 can mediate the pro-apoptotic activity of cisplatin or tumor necrosis factor alpha (TNFalpha) through the down-regulation of nuclear factor-kappaB (NF-kappaB) expression. It also inhibits angiogenesis through PI3K/mTOR/p70S6K pathway by interacting of vascular endothelial growth factor receptor-2 (VEGFR-2). In addition, nuclear ALG-2 may participate in the post-transcriptional regulation of Inositol Trisphosphate Receptor Type 1 (IP3R1) pre-mRNA at least in part by interacting with CHERP (Ca2+ homeostasis endoplasmic reticulum protein) calcium-dependently. ALG-2 contains five serially repeated EF-hand motifs and interacts with various proteins, including ALG-2-interacting protein X (Alix), Fas, annexin XI, death-associated protein kinase 1 (DAPk1), Tumor susceptibility gene 101 (TSG101), Sec31A, phospholipid scramblase 3 (PLSCR3), the P-body component PATL1, and endosomal sorting complex required for transport (ESCRT)-III-related protein IST1, in a calcium-dependent manner. 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.


Pssm-ID: 320058 [Multi-domain]  Cd Length: 165  Bit Score: 39.16  E-value: 1.73e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12853070 390 EPLRQLFSLFDRNQDGTIDFRE------YVigltvlcnpsnTEkiLQMSFKLFDLDEDGYVTERELTTMLQaAFG 458
Cdd:cd16183  37 ETVRLMIGMFDRDNSGTINFQEfaalwkYI-----------TD--WQNCFRSFDRDNSGNIDKNELKQALT-SFG 97
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 96-244 1.86e-03

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


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 39.71  E-value: 1.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070   96 RRWRKHLIK----SALVFLFrlgfffagFLVKVKGKK-ATREEAPIFVSAPHSTFFDAIAVVVAGLP-SVVSDSQLARVP 169
Cdd:PLN02901  15 RRKAQHFINkvwaTLSTSPF--------YKIEVEGLEnLPSPDEPAVYVSNHQSFLDIYTLFHLGRPfKFISKTSIFLIP 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12853070  170 LAGKCILVTQPVLVKREDPNSRKTTRNEILRRVKskmKWPQILIFPEGLCTNRSCLVTFKLGAFS----PGVPVQPVLL 244
Cdd:PLN02901  87 IIGWAMYMTGHIPLKRMDRRSQLECLKRCMELLK---KGASVFFFPEGTRSKDGKLAAFKKGAFSvaakTGVPVVPITL 162
EF-hand_6 pfam13405
EF-hand domain;
392-419 3.75e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.84  E-value: 3.75e-03
                          10        20
                  ....*....|....*....|....*...
gi 12853070   392 LRQLFSLFDRNQDGTIDFREYVIGLTVL 419
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKALRSL 29
PRK15018 PRK15018
1-acyl-sn-glycerol-3-phosphate acyltransferase; Provisional
 120-242 5.77e-03

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


Pssm-ID: 184979  Cd Length: 245  Bit Score: 38.46  E-value: 5.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070  120 FLVKVKGKKATREEA---PIFVsAPHSTFFDAI-AVVVAGLPSV-VSDSQLARVPLAGKCILVTQPVLVKREDPNSRKTT 194
Cdd:PRK15018  49 FGLKVECRKPADAESygnAIYI-ANHQNNYDMVtASNIVQPPTVtVGKKSLLWIPFFGQLYWLTGNLLIDRNNRTKAHGT 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 12853070  195 RNEILRRVKSKMKwpQILIFPEGLCTNRSCLVTFKLGAF----SPGVPVQPV 242
Cdd:PRK15018 128 IAEVVNHFKKRRI--SIWMFPEGTRSRGRGLLPFKTGAFhaaiAAGVPIIPV 177
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 428-455 7.75e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 33.91  E-value: 7.75e-03
                          10        20
                  ....*....|....*....|....*...
gi 12853070   428 ILQMSFKLFDLDEDGYVTERELTTMLQA 455
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 107-246 8.42e-03

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: 37.63  E-value: 8.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 107 LVFLFRLGFFFAGflVKVKGKKATREEAPIFVSAPHS-TFFDA--IAVVVAGLPSVVSDSQLARVPLAGKCILVTQPVLV 183
Cdd:cd07992   3 LLSRVILRIYFRR--ITVVGRENVPKDGPVIFLGNHPnALIDPllLAATLRRPVRFLAKADLFKNPLIGWLLESFGAIPV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12853070 184 KReDPNSRKTTRNEI--------LRRVKSKMKWpqILIFPEGLCTNRSCLVTFKLGAFS----------PGVPVQPVLLR 245
Cdd:cd07992  81 YR-PKDLARGGIGKIsnaavfdaVGEALKAGGA--IGIFPEGGSHDRPRLLPLKAGAARmalealeagqKDVKIVPVGLN 157


                .
gi 12853070 246 Y 246
Cdd:cd07992 158 Y 158
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 392-445 8.88e-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: 37.12  E-value: 8.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 12853070 392 LRQLFSLFDRNQDGTIDFREYVIGLTVLcnpsnteKILQMSFKLFDLDEDGYVT 445
Cdd:cd16180 105 VQLLVRKFDRRRRGSISFDDFVEACVTL-------KRLTDAFRKYDTNRTGYAT 151
EF-hand_5 pfam13202
EF hand;
392-411 9.61e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 33.83  E-value: 9.61e-03
                          10        20
                  ....*....|....*....|
gi 12853070   392 LRQLFSLFDRNQDGTIDFRE 411
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEE 20
 
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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