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Conserved domains on  [gi|47086907|ref|NP_060309|]
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lysophosphatidylcholine acyltransferase 2 [Homo sapiens]

Protein Classification

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

LPLAT_LPCAT1-like and EFh domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 116-327 5.29e-90

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: 275.25  E-value: 5.29e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 116 RAMFFSMGF-IVAVKGKIASPLEAPVFVAaPHSTFFDGIACVVAGLPSMVSRNENAQVPLIGRLLRAVQPVLVSRVDPDS 194
Cdd:cd07991   2 RVLLFAFGFyVIKVHGKPDPPEAPRIIVA-NHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPKD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 195 RKNTINEIIKRTTSGgEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYTFIQLCMLTF 274
Cdd:cd07991  81 RKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRLL 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 47086907 275 CQLFTKVEVEFMPVQVPNdEEKNDPVLFANKVRNLMAEALGIPVTDHTYEDCR 327
Cdd:cd07991 160 TQPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
377-489 1.76e-14

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 70.59  E-value: 1.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 377 GRIGIEEFAKYLklpvSDVLRQLFALFDRNHDGSIDFREYVIGLAVLCNPSNTEEIIQvAFKLFDVDEDGYITEEEFSTI 456
Cdd:COG5126  20 GVLERDDFEALF----RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARA-AFDLLDTDGDGKISADEFRRL 94

                        90       100       110
                ....*....|....*....|....*....|....*
gi 47086907 457 LQAsLGVPDLDVSGLFKEI-AQGD-SISYEEFKSF 489
Cdd:COG5126  95 LTA-LGVSEEEADELFARLdTDGDgKISFEEFVAA 128
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 116-327 5.29e-90

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: 275.25  E-value: 5.29e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 116 RAMFFSMGF-IVAVKGKIASPLEAPVFVAaPHSTFFDGIACVVAGLPSMVSRNENAQVPLIGRLLRAVQPVLVSRVDPDS 194
Cdd:cd07991   2 RVLLFAFGFyVIKVHGKPDPPEAPRIIVA-NHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPKD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 195 RKNTINEIIKRTTSGgEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYTFIQLCMLTF 274
Cdd:cd07991  81 RKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRLL 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 47086907 275 CQLFTKVEVEFMPVQVPNdEEKNDPVLFANKVRNLMAEALGIPVTDHTYEDCR 327
Cdd:cd07991 160 TQPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 102-315 9.18e-25

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: 102.40  E-value: 9.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 102 WRRKITQTALKFLGRAMFFSMGFIVAVKGKIASPLEAPVFVAAPHSTFFDG--IACVVAGLPSMVSRNENAQVPLIGRLL 179
Cdd:COG0204   7 LLRRFRYRLVRLWARLLLRLLGVRVRVEGLENLPADGPVLIVANHQSWLDIllLLAALPRPVRFVAKKELFKIPLLGWLL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 180 RAVQPVLVSRVDPDSRKNTINEIIKRTTSGGewpQILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPVLLRYpnkld 255
Cdd:COG0204  87 RALGAIPVDRSKRRAALRALRQAVEALKAGE---SLVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG----- 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 256 tvTWTWQGYTFIqlcmltfcQLFTKVEVEFMPVQVPNDEEKNDPVLFANKVRNLMAEALG 315
Cdd:COG0204 159 --TERALPKGFL--------PRPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 142-250 1.49e-20

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: 87.03  E-value: 1.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907    142 VAAPHSTFFDGIACVVA-----GLPSMVSRNENAQVPLIGRLLRAVQPVLVSRVDPDSRKNTINEIIKRTTSGGewpQIL 216
Cdd:smart00563   3 VVANHQSFLDPLVLSALlprklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGE---WLL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 47086907    217 VFPEGTCTNRSCLITFKPGAFI----PGVPVQPVLLRY 250
Cdd:smart00563  80 IFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
377-489 1.76e-14

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 70.59  E-value: 1.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 377 GRIGIEEFAKYLklpvSDVLRQLFALFDRNHDGSIDFREYVIGLAVLCNPSNTEEIIQvAFKLFDVDEDGYITEEEFSTI 456
Cdd:COG5126  20 GVLERDDFEALF----RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARA-AFDLLDTDGDGKISADEFRRL 94

                        90       100       110
                ....*....|....*....|....*....|....*
gi 47086907 457 LQAsLGVPDLDVSGLFKEI-AQGD-SISYEEFKSF 489
Cdd:COG5126  95 LTA-LGVSEEEADELFARLdTDGDgKISFEEFVAA 128
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 126-246 5.27e-14

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: 68.84  E-value: 5.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907   126 VAVKGKIASPLEAPVFVAAPHSTFFDGI--ACVVA---GLPSMVSRNENAQVPLIGRLLRAVQPVLVSRVDPDSRKNTIN 200
Cdd:pfam01553   2 IEVHGLENLPRGGPAIVVANHQSYLDVLllSLALYkrgRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTLE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 47086907   201 EIIKRTTSGGewpQILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPV 246
Cdd:pfam01553  82 YLVELLREGK---LVVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPV 128
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 396-458 4.39e-12

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: 61.02  E-value: 4.39e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47086907 396 LRQLFALFDRNHDGSIDFREYVIGLAVLcNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQ 458
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
394-458 1.26e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 59.96  E-value: 1.26e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47086907   394 DVLRQLFALFDRNHDGSIDFREYVIGLAVLCNPSN-TEEIIQVAFKLFDVDEDGYITEEEFSTILQ 458
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
PTZ00184 PTZ00184
calmodulin; Provisional
 404-486 6.68e-09

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 54.77  E-value: 6.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  404 DRNHDGSIDFREYVIGLAVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILqASLG--VPDLDVSGLFKEI-AQGD- 479
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEVDEMIREAdVDGDg 135


                 ....*..
gi 47086907  480 SISYEEF 486
Cdd:PTZ00184 136 QINYEEF 142
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 123-249 1.84e-08

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: 53.12  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907   123 GFIVAVKGKIASPLEAPVFVAAPHSTFFDGIA--CVVAGLPSMVSRNENAQVPLIGRLLRAVQPVLVSRvdpDSRK--NT 198
Cdd:TIGR00530   1 GLKVEVVGPENLPAKSPVLVVANHQSNLDPLTlsAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFIDR---ENIRaiAT 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 47086907   199 INEIIKRTTSGGEwpQILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPVLLR 249
Cdd:TIGR00530  78 ALKAAIEVLKQGR--SIGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
PLN02833 PLN02833
glycerol acyltransferase family protein
 103-316 2.48e-07

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 52.85  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  103 RRKITQTALKFLGRAMFFSMGFIVAVKGKIASPLEAPVFVAApHSTFFDGIA-CVVAGLPSMVSRNENAQVPLIGRLLRA 181
Cdd:PLN02833 129 RKKIERKLVELICSAFVASWTGVIKYHGPRPSRRPKQVFVAN-HTSMIDFIVlEQMTPFAVIMQKHPGWVGFLQNTILES 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  182 VQPVLVSRVDPDSRkNTINEIIKRTTSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPVLLRYPNKLDTVTWTW 261
Cdd:PLN02833 208 VGCIWFNRTEAKDR-EVVAKKLRDHVQDPDRNPLLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKYNKIFVDAFWNS 286

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 47086907  262 QGYTFIQlcmlTFCQLFTK----VEVEFMPVQVPNDEEknDPVLFANKVRNLMAEALGI 316
Cdd:PLN02833 287 RKQSFTM----HLLRLMTSwavvCDVWYLEPQTLRPGE--TPIEFAERVRDMIAKRAGL 339
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 433-459 2.87e-05

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: 40.82  E-value: 2.87e-05
                           10        20
                   ....*....|....*....|....*..
gi 47086907    433 IQVAFKLFDVDEDGYITEEEFSTILQA 459
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
354-495 2.11e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 42.75  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  354 KLDWDG---VRKhlDEYASIASSSKGGRIGIEefakylklpvsdvLRQLFALFDRNHDGSIDFREYVIGLAVLCNPSNTE 430
Cdd:NF041410  35 KLDSDGdgsVSQ--DELSSALSSKSDDGSLID-------------LSELFSDLDSDGDGSLSSDELAAAAPPPPPPPDQA 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  431 EIIQVAFKLF---DVDEDGYITEEEFSTILQASLGvpDLDVSGLFKEI-AQGD-SISYEEFKSfALKHPE 495
Cdd:NF041410 100 PSTELADDLLsalDTDGDGSISSDELSAGLTSAGS--SADSSQLFSALdSDGDgSVSSDELAA-ALQPPP 166
 
Name Accession Description Interval E-value
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
 116-327 5.29e-90

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: 275.25  E-value: 5.29e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 116 RAMFFSMGF-IVAVKGKIASPLEAPVFVAaPHSTFFDGIACVVAGLPSMVSRNENAQVPLIGRLLRAVQPVLVSRVDPDS 194
Cdd:cd07991   2 RVLLFAFGFyVIKVHGKPDPPEAPRIIVA-NHTSFIDPLILFSDLFPSIVAKKELGKLPFIGTILRALGCIFVDRSEPKD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 195 RKNTINEIIKRTTSGgEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPVLLRYPNKLDTVTWTWQGYTFIQLCMLTF 274
Cdd:cd07991  81 RKKVVEEIKERATDP-NWPPILIFPEGTTTNGKALIMFKKGAFEPGVPVQPVAIRYPNKFVDAFWNSSGYSSLMYLFRLL 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 47086907 275 CQLFTKVEVEFMPVQVPNdEEKNDPVLFANKVRNLMAEALGIPVTDHTYEDCR 327
Cdd:cd07991 160 TQPANVLEVEFLPVYTPS-EEGEDPKEFANRVRLIMANKLGLPATDWTGEDKR 211
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
 102-315 9.18e-25

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: 102.40  E-value: 9.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 102 WRRKITQTALKFLGRAMFFSMGFIVAVKGKIASPLEAPVFVAAPHSTFFDG--IACVVAGLPSMVSRNENAQVPLIGRLL 179
Cdd:COG0204   7 LLRRFRYRLVRLWARLLLRLLGVRVRVEGLENLPADGPVLIVANHQSWLDIllLLAALPRPVRFVAKKELFKIPLLGWLL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 180 RAVQPVLVSRVDPDSRKNTINEIIKRTTSGGewpQILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPVLLRYpnkld 255
Cdd:COG0204  87 RALGAIPVDRSKRRAALRALRQAVEALKAGE---SLVIFPEGTRSPDGRLLPFKTGAARlaleAGVPIVPVAIDG----- 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 256 tvTWTWQGYTFIqlcmltfcQLFTKVEVEFMPVQVPNDEEKNDPVLFANKVRNLMAEALG 315
Cdd:COG0204 159 --TERALPKGFL--------PRPGKVTVRIGPPIDPSDLEGEDRRELAERLRAAIEALLA 208
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
 142-250 1.49e-20

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: 87.03  E-value: 1.49e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907    142 VAAPHSTFFDGIACVVA-----GLPSMVSRNENAQVPLIGRLLRAVQPVLVSRVDPDSRKNTINEIIKRTTSGGewpQIL 216
Cdd:smart00563   3 VVANHQSFLDPLVLSALlprklGRVRFVAKKELFYVPLLGWLLRLLGAIFIDRSNGRKARAALREAVELLKEGE---WLL 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 47086907    217 VFPEGTCTNRSCLITFKPGAFI----PGVPVQPVLLRY 250
Cdd:smart00563  80 IFPEGTRSRPGKLLPFKKGAARlaleAGVPIVPVAIRG 117
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
 116-254 2.09e-19

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: 86.17  E-value: 2.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 116 RAMFFSMGFIVAVKGKIASPLEAPVFVAAPHSTFFDG--IACVVAGLPSMVSRNENAQVPLIGRLLRAVQPVLVSRVDPD 193
Cdd:cd07989   2 RLLLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPlvLGAALPRPIRFVAKKELFKIPFLGWLLRLLGAIPIDRGNGR 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47086907 194 SRKNTINEIIKRTTSGGewpQILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPVLLRYPNKL 254
Cdd:cd07989  82 SAREALREAIEALKEGE---SVVIFPEGTRSRDGELLPFKSGAFRlakeAGVPIVPVAISGTWGS 143
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
377-489 1.76e-14

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 70.59  E-value: 1.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 377 GRIGIEEFAKYLklpvSDVLRQLFALFDRNHDGSIDFREYVIGLAVLCNPSNTEEIIQvAFKLFDVDEDGYITEEEFSTI 456
Cdd:COG5126  20 GVLERDDFEALF----RRLWATLFSEADTDGDGRISREEFVAGMESLFEATVEPFARA-AFDLLDTDGDGKISADEFRRL 94

                        90       100       110
                ....*....|....*....|....*....|....*
gi 47086907 457 LQAsLGVPDLDVSGLFKEI-AQGD-SISYEEFKSF 489
Cdd:COG5126  95 LTA-LGVSEEEADELFARLdTDGDgKISFEEFVAA 128
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
 126-246 5.27e-14

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: 68.84  E-value: 5.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907   126 VAVKGKIASPLEAPVFVAAPHSTFFDGI--ACVVA---GLPSMVSRNENAQVPLIGRLLRAVQPVLVSRVDPDSRKNTIN 200
Cdd:pfam01553   2 IEVHGLENLPRGGPAIVVANHQSYLDVLllSLALYkrgRPLVFVAKKELFDIPLVGWLMRLLGCIFIDRKNRKDAAGTLE 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 47086907   201 EIIKRTTSGGewpQILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPV 246
Cdd:pfam01553  82 YLVELLREGK---LVVIFPEGTRSREGELLPFKKGAFRlaieAGVPIVPV 128
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
 112-252 1.55e-13

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


Pssm-ID: 153244 [Multi-domain]  Cd Length: 187  Bit Score: 68.98  E-value: 1.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 112 KFLGRamFFSMGFIVAVKGKIASPLEAPVFVAAPHSTFFDG---IACVVAGLPS----MVSRNENAQVPLIGRLlravQP 184
Cdd:cd06551   2 RYLLL--NFFGFVRLEVKGPPPPPGGGPVLFVSNHSSWWDGlilFLLLERGLRRdvygLMDEELLERYPFFTRL----GA 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47086907 185 VLVSRVDPDSRKNTINEIIKRTTSGGEWpqILVFPEGTCTNRS-CLITFKPGAFIP----GVPVQPVLLRYPN 252
Cdd:cd06551  76 FSVDRDSPRSAAKSLKYVARLLSKPGSV--VWIFPEGTRTRRDkRPLQFKPGVAHLaekaGVPIVPVALRYTF 146
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 396-458 4.39e-12

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: 61.02  E-value: 4.39e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47086907 396 LRQLFALFDRNHDGSIDFREYVIGLAVLcNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQ 458
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
394-458 1.26e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 59.96  E-value: 1.26e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47086907   394 DVLRQLFALFDRNHDGSIDFREYVIGLAVLCNPSN-TEEIIQVAFKLFDVDEDGYITEEEFSTILQ 458
Cdd:pfam13499   2 EKLKEAFKLLDSDGDGYLDVEELKKLLRKLEEGEPlSDEEVEELFKEFDLDKDGRISFEEFLELYS 67
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
 126-253 4.46e-09

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


Pssm-ID: 153254 [Multi-domain]  Cd Length: 203  Bit Score: 56.50  E-value: 4.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 126 VAVKGKIASPLEAPVFVAAPHS-TFFDG--IACVVAGLPSMVSRNENAQVPLIGRLLRAVQPVLVSRVdPDSRKNTINEI 202
Cdd:cd07992  16 ITVVGRENVPKDGPVIFLGNHPnALIDPllLAATLRRPVRFLAKADLFKNPLIGWLLESFGAIPVYRP-KDLARGGIGKI 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47086907 203 IKRTT--------SGGEWpqILVFPEGTCTNRSCLITFKPGAFI----------PGVPVQPVLLRYPNK 253
Cdd:cd07992  95 SNAAVfdavgealKAGGA--IGIFPEGGSHDRPRLLPLKAGAARmalealeagqKDVKIVPVGLNYEDK 161
PTZ00184 PTZ00184
calmodulin; Provisional
 404-486 6.68e-09

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 54.77  E-value: 6.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  404 DRNHDGSIDFREYVIGLAVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILqASLG--VPDLDVSGLFKEI-AQGD- 479
Cdd:PTZ00184  57 DADGNGTIDFPEFLTLMARKMKDTDSEEEIKEAFKVFDRDGNGFISAAELRHVM-TNLGekLTDEEVDEMIREAdVDGDg 135


                 ....*..
gi 47086907  480 SISYEEF 486
Cdd:PTZ00184 136 QINYEEF 142
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
 123-249 1.84e-08

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: 53.12  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907   123 GFIVAVKGKIASPLEAPVFVAAPHSTFFDGIA--CVVAGLPSMVSRNENAQVPLIGRLLRAVQPVLVSRvdpDSRK--NT 198
Cdd:TIGR00530   1 GLKVEVVGPENLPAKSPVLVVANHQSNLDPLTlsAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFIDR---ENIRaiAT 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 47086907   199 INEIIKRTTSGGEwpQILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPVLLR 249
Cdd:TIGR00530  78 ALKAAIEVLKQGR--SIGVFPEGTRSRGRDILPFKKGAFHiaikAGVPILPVVLS 130
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 433-486 6.14e-08

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: 49.47  E-value: 6.14e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 47086907 433 IQVAFKLFDVDEDGYITEEEFSTILQA-SLGVPDLDVSGLFKEI-AQGD-SISYEEF 486
Cdd:cd00051   2 LREAFRLFDKDGDGTISADELKAALKSlGEGLSEEEIDEMIREVdKDGDgKIDFEEF 58
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 395-489 6.64e-08

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 51.51  E-value: 6.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 395 VLRQLFALFDRNHDGSIDFREyVIGLAVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQASLGVPDLDVsgLFKE 474
Cdd:cd15898   1 WLRRQWIKADKDGDGKLSLKE-IKKLLKRLNIRVSEKELKKLFKEVDTNGDGTLTFDEFEELYKSLTERPELEP--IFKK 77

                        90
                ....*....|....*..
gi 47086907 475 IA--QGDSISYEEFKSF 489
Cdd:cd15898  78 YAgtNRDYMTLEEFIRF 94
EF-hand_7 pfam13499
EF-hand domain pair;
433-491 8.65e-08

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 49.17  E-value: 8.65e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086907   433 IQVAFKLFDVDEDGYITEEEFSTILQA-SLGVP--DLDVSGLFKEIAQ-GD-SISYEEFKSFAL 491
Cdd:pfam13499   4 LKEAFKLLDSDGDGYLDVEELKKLLRKlEEGEPlsDEEVEELFKEFDLdKDgRISFEEFLELYS 67
PTZ00183 PTZ00183
centrin; Provisional
 360-449 2.26e-07

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 50.46  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  360 VRKHLDEYASIASSSKGGRIGIEEFAKYLKL----PVSDVLRQLFALFDRNHDGSIDFREYVIGLAVLCNPSNTEEIIQV 435
Cdd:PTZ00183  15 QKKEIREAFDLFDTDGSGTIDPKELKVAMRSlgfePKKEEIKQMIADVDKDGSGKIDFEEFLDIMTKKLGERDPREEILK 94

                         90
                 ....*....|....
gi 47086907  436 AFKLFDVDEDGYIT 449
Cdd:PTZ00183  95 AFRLFDDDKTGKIS 108
PLN02833 PLN02833
glycerol acyltransferase family protein
 103-316 2.48e-07

glycerol acyltransferase family protein


Pssm-ID: 215447  Cd Length: 376  Bit Score: 52.85  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  103 RRKITQTALKFLGRAMFFSMGFIVAVKGKIASPLEAPVFVAApHSTFFDGIA-CVVAGLPSMVSRNENAQVPLIGRLLRA 181
Cdd:PLN02833 129 RKKIERKLVELICSAFVASWTGVIKYHGPRPSRRPKQVFVAN-HTSMIDFIVlEQMTPFAVIMQKHPGWVGFLQNTILES 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  182 VQPVLVSRVDPDSRkNTINEIIKRTTSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPGVPVQPVLLRYPNKLDTVTWTW 261
Cdd:PLN02833 208 VGCIWFNRTEAKDR-EVVAKKLRDHVQDPDRNPLLIFPEGTCVNNEYTVMFKKGAFELGCTVCPIAIKYNKIFVDAFWNS 286

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 47086907  262 QGYTFIQlcmlTFCQLFTK----VEVEFMPVQVPNDEEknDPVLFANKVRNLMAEALGI 316
Cdd:PLN02833 287 RKQSFTM----HLLRLMTSwavvCDVWYLEPQTLRPGE--TPIEFAERVRDMIAKRAGL 339
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 371-495 2.89e-06

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 46.89  E-value: 2.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 371 ASSSKGGRIGIEEFAKYLKL---PVSDV-LRQLFALFDRNHDGSIDFREYVIGLAVLCNPsntEEIIQVaFKLFDVDEDG 446
Cdd:cd15898   9 ADKDGDGKLSLKEIKKLLKRlniRVSEKeLKKLFKEVDTNGDGTLTFDEFEELYKSLTER---PELEPI-FKKYAGTNRD 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 47086907 447 YITEEEFSTILQASLG--VPDLDVSGLFKEIA---QGDSISYEEFKSFaLKHPE 495
Cdd:cd15898  85 YMTLEEFIRFLREEQGenVSEEECEELIEKYEperENRQLSFEGFTNF-LLSPE 137
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
377-426 3.32e-06

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 46.71  E-value: 3.32e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 47086907 377 GRIGIEEFAKYLK-LPVSD-VLRQLFALFDRNHDGSIDFREYVIGLAVLCNP 426
Cdd:COG5126  84 GKISADEFRRLLTaLGVSEeEADELFARLDTDGDGKISFEEFVAAVRDYYTP 135
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
 396-489 9.89e-06

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 45.30  E-value: 9.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 396 LRQLFALFDRNHDGSIDFREYVIGLAVLcNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQASLGVPDLDvsGLFKEI 475
Cdd:cd16202   2 LKDQFRKADKNGDGKLSFKECKKLLKKL-NVKVDKDYAKKLFQEADTSGEDVLDEEEFVQFYNRLTKRPEIE--ELFKKY 78

                        90
                ....*....|....*
gi 47086907 476 AQGD-SISYEEFKSF 489
Cdd:cd16202  79 SGDDeALTVEELRRF 93
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 430-493 1.93e-05

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: 42.34  E-value: 1.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47086907 430 EEIIQVAFKLFDVDEDGYITEEEFSTILQaSLGVP--DLDVSGLfkeiaqGDSISYEEFKSFALKH 493
Cdd:cd22949   2 EEKFREAFILFDRDGDGELTMYEAVLAMR-SCGIPltNDEKDAL------PASMNWDQFENWAKKK 60
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 433-459 2.87e-05

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: 40.82  E-value: 2.87e-05
                           10        20
                   ....*....|....*....|....*..
gi 47086907    433 IQVAFKLFDVDEDGYITEEEFSTILQA 459
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLKA 28
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 432-459 4.39e-05

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: 40.46  E-value: 4.39e-05
                          10        20
                  ....*....|....*....|....*...
gi 47086907   432 IIQVAFKLFDVDEDGYITEEEFSTILQA 459
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKK 28
S-100 cd00213
S-100: S-100 domain, which represents the largest family within the superfamily of proteins ...
 383-425 6.42e-05

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


Pssm-ID: 238131 [Multi-domain]  Cd Length: 88  Bit Score: 41.71  E-value: 6.42e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 47086907 383 EFAKYLKLPVS-DVLRQLFALFDRNHDGSIDFREY---VIGLAVLCN 425
Cdd:cd00213  39 ELPNFLKNQKDpEAVDKIMKDLDVNKDGKVDFQEFlvlIGKLAVACH 85
EFh_PEF_ALG-2_like cd16185
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ...
 372-460 7.13e-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: 43.36  E-value: 7.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 372 SSSKGGRIGIEEFAKYLKLPVS----DVLRQLFALFDRNHDGSIDFREYVIGLAVLCNpsnteeiIQVAFKLFDVDEDGY 447
Cdd:cd16185  10 DRDRSGSIDVNELQKALAGGGLlfslATAEKLIRMFDRDGNGTIDFEEFAALHQFLSN-------MQNGFEQRDTSRSGR 82

                        90
                ....*....|...
gi 47086907 448 ITEEEFSTILQAS 460
Cdd:cd16185  83 LDANEVHEALAAS 95
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
 121-248 7.58e-05

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


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 43.95  E-value: 7.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  121 SMGFIVAVKGK--IASPLEAPVFVAApHSTFFDGIACVVAGLP-SMVSRNENAQVPLIGRLLRAVQPVLVSRVDPDSRKN 197
Cdd:PLN02901  32 SPFYKIEVEGLenLPSPDEPAVYVSN-HQSFLDIYTLFHLGRPfKFISKTSIFLIPIIGWAMYMTGHIPLKRMDRRSQLE 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 47086907  198 TIN---EIIKRTTSggewpqILVFPEGTCTNRSCLITFKPGAFI----PGVPVQPVLL 248
Cdd:PLN02901 111 CLKrcmELLKKGAS------VFFFPEGTRSKDGKLAAFKKGAFSvaakTGVPVVPITL 162
EF-hand_6 pfam13405
EF-hand domain;
433-459 7.62e-05

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 39.85  E-value: 7.62e-05
                          10        20
                  ....*....|....*....|....*..
gi 47086907   433 IQVAFKLFDVDEDGYITEEEFSTILQA 459
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEELRKALRS 28
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 401-488 1.97e-04

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 40.59  E-value: 1.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 401 ALFDRNHDGSIDFREY--VIGLAvlcnpSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQA-SLGVPDLDVSGLFKEIAQ 477
Cdd:cd16251   7 APSAFRAHGSFNYKKFfeHVGLK-----QKSEDQIKKVFQILDKDKSGFIEEEELKYILKGfSIAGRDLTDEETKALLAA 81

                        90
                ....*....|....*.
gi 47086907 478 GDS-----ISYEEFKS 488
Cdd:cd16251  82 GDTdgdgkIGVEEFAT 97
XopAW NF041410
XopAW family type III secretion system calcium-binding effector;
354-495 2.11e-04

XopAW family type III secretion system calcium-binding effector;


Pssm-ID: 469301 [Multi-domain]  Cd Length: 227  Bit Score: 42.75  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  354 KLDWDG---VRKhlDEYASIASSSKGGRIGIEefakylklpvsdvLRQLFALFDRNHDGSIDFREYVIGLAVLCNPSNTE 430
Cdd:NF041410  35 KLDSDGdgsVSQ--DELSSALSSKSDDGSLID-------------LSELFSDLDSDGDGSLSSDELAAAAPPPPPPPDQA 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907  431 EIIQVAFKLF---DVDEDGYITEEEFSTILQASLGvpDLDVSGLFKEI-AQGD-SISYEEFKSfALKHPE 495
Cdd:NF041410 100 PSTELADDLLsalDTDGDGSISSDELSAGLTSAGS--SADSSQLFSALdSDGDgSVSSDELAA-ALQPPP 166
EF-hand_8 pfam13833
EF-hand domain pair;
407-453 3.28e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 38.84  E-value: 3.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 47086907   407 HDGSIDFREYVIGLAVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEF 453
Cdd:pfam13833   1 EKGVITREELKRALALLGLKDLSEDEVDILFREFDTDGDGYISFDEF 47
EFh_PEF cd15897
The penta-EF hand (PEF) family; The penta-EF hand (PEF) family contains a group of five ...
 313-449 3.56e-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: 41.26  E-value: 3.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 313 ALGIPVTDHTY-----EDCRLMISAGQLTLPMEAGLVEFTKISRKLKlDWDGVRKHLDeyasiasSSKGGRIGIEEFAKY 387
Cdd:cd15897  24 ALSNVGWTHFDlgfslETCRSMIAMMDRDHSGKLNFSEFKGLWNYIK-AWQEIFRTYD-------TDGSGTIDSNELRQA 95

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47086907 388 LKLPVSDVLRQLFAL----FDRNHdGSIDFREYVIGLAVLCNPSNteeiiqvAFKLFDVDEDGYIT 449
Cdd:cd15897  96 LSGAGYRLSEQTYDIiirrYDRGR-GNIDFDDFIQCCVRLQRLTD-------AFRRYDKDQDGQIQ 153
EFh_DMD_DYTN_DTN cd15901
EF-hand-like motif found in the dystrophin/dystrobrevin/dystrotelin family; The dystrophin ...
 399-466 4.09e-04

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: 41.10  E-value: 4.09e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47086907 399 LFALFDRNHDGSIDFREYVIGLAVLCNpSNTEEIIQVAFKLFDvDEDGYITEEEFSTILQASLGVPDL 466
Cdd:cd15901  59 LLNLYDRNRTGCIRLLSVKIALITLCA-ASLLDKYRYLFGQLA-DSSGFISRERLTQFLQDLLQIPDL 124
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 395-493 5.17e-04

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 40.97  E-value: 5.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 395 VLRQLFALFDRNHDGSIDFREYVIGLAVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFstilqaslgvpdldvSGLFKE 474
Cdd:cd16180   1 ELRRIFQAVDRDRSGRISAKELQRALSNGDWTPFSIETVRLMINMFDRDRSGTINFDEF---------------VGLWKY 65

                        90       100       110
                ....*....|....*....|....*....|..
gi 47086907 475 IAQ-------------GdSISYEEFKSfALKH 493
Cdd:cd16180  66 IQDwrrlfrrfdrdrsG-SIDFNELQN-ALSS 95
EH cd00052
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ...
 389-420 7.66e-04

Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.


Pssm-ID: 238009 [Multi-domain]  Cd Length: 67  Bit Score: 37.97  E-value: 7.66e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 47086907 389 KLPvSDVLRQLFALFDRNHDGSIDFREYVIGL 420
Cdd:cd00052  29 GLP-RSVLAQIWDLADTDKDGKLDKEEFAIAM 59
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 396-421 9.82e-04

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


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.59  E-value: 9.82e-04
                           10        20
                   ....*....|....*....|....*.
gi 47086907    396 LRQLFALFDRNHDGSIDFREYVIGLA 421
Cdd:smart00054   2 LKEAFRLFDKDGDGKIDFEEFKDLLK 27
EF-hand_8 pfam13833
EF-hand domain pair;
444-492 2.11e-03

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.52  E-value: 2.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 47086907   444 EDGYITEEEFSTILqASLGVPDL---DVSGLFKEIAQ-GD-SISYEEFKSFALK 492
Cdd:pfam13833   1 EKGVITREELKRAL-ALLGLKDLsedEVDILFREFDTdGDgYISFDEFCVLLER 53
EFh_HEF_CBN cd16179
EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and ...
 399-475 2.23e-03

EF-hand, calcium binding motif, found in Drosophila melanogaster calbindin-32 (CBN) and similar proteins; CBN, the product of the cbn gene, is a Drosophila homolog to vertebrate neuronal six EF-hand calcium binding proteins. It is expressed through most of ontogenesis with a selective distribution in the nervous system and in a few small adult thoracic muscles. Its precise biological role remains unclear. CBN contains six EF-hand motifs, but some of them may not bind calcium ions due to the lack of key residues.


Pssm-ID: 320079 [Multi-domain]  Cd Length: 261  Bit Score: 40.09  E-value: 2.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 399 LFALFDRNHDGSIDFREYVIGLAV----LCNP------SNTEEIIQVAFKLFDVDEDGYITEEEFSTILQ--ASLGVPDL 466
Cdd:cd16179 146 ILQLFDRNKDGKLQLSEMARLLPVkenfLCRPifkgagKLTREDIDRVFALYDRDNNGTIENEELTGFLKdlLELVQEDY 225

                        90
                ....*....|.
gi 47086907 467 DVSGL--FKEI 475
Cdd:cd16179 226 DEQDLeeFKEI 236
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 396-423 2.63e-03

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


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 35.45  E-value: 2.63e-03
                          10        20
                  ....*....|....*....|....*...
gi 47086907   396 LRQLFALFDRNHDGSIDFREYVIGLAVL 423
Cdd:pfam00036   2 LKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_PEF_Group_I cd16180
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ...
 377-449 2.71e-03

Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.


Pssm-ID: 320055 [Multi-domain]  Cd Length: 164  Bit Score: 38.66  E-value: 2.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47086907 377 GRIGIEEFA---KYLKlpvsdVLRQLFALFDRNHDGSIDFRE---------YVIGLAVLC------NPSNTEEI-----I 433
Cdd:cd16180  52 GTINFDEFVglwKYIQ-----DWRRLFRRFDRDRSGSIDFNElqnalssfgYRLSPQFVQllvrkfDRRRRGSIsfddfV 126

                        90       100
                ....*....|....*....|....*
gi 47086907 434 QV---------AFKLFDVDEDGYIT 449
Cdd:cd16180 127 EAcvtlkrltdAFRKYDTNRTGYAT 151
IF2_N pfam04760
Translation initiation factor IF-2, N-terminal region; This conserved feature at the ...
 381-413 3.21e-03

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


Pssm-ID: 428110 [Multi-domain]  Cd Length: 52  Bit Score: 35.90  E-value: 3.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 47086907   381 IEEFAKYLKLPVSDVLRQLFAL-FDRNHDGSIDF 413
Cdd:pfam04760   6 VYELAKELGVSSKELIKKLFKLgIMKSHNSTLDE 39
EFh_PEF_Group_II_CAPN_like cd16182
Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family ...
 397-460 3.43e-03

Penta-EF hand, calcium binding motifs, found in PEF calpain family; The PEF calpain family belongs to the second group of penta-EF hand (PEF) proteins. It includes classical (also called conventional or typical) calpain (referring to a calcium-dependent papain-like enzymes, EC 3.4.22.17) large catalytic subunits (CAPN1, 2, 3, 8, 9, 11, 12, 13, 14) and two calpain small subunits (CAPNS1 and CAPNS2), which are largely confined to animals (metazoans). These PEF-containing are nonlysosomal intracellular calcium-activated intracellular cysteine proteases that play important roles in the degradation or functional modulation in a variety of substrates in response to calcium signalling. The classical mu- and m-calpains are heterodimers consisting of homologous but a distinct (large) L-subunit/chain (CAPN1 or CAPN2) and a common (small) S-subunit/chain (CAPNS1 or CAPNS2). These L-subunits (CAPN1 and CAPN2) and S-subunit CAPNS1 are ubiquitously found in all tissues. Other calpains likely consist of an isolated L-subunit/chain alone. Many of them, such as CAPNS2, CAPN3 (in skeletal muscle, or lens), CAPN8 (in stomach), CAPN9 (in digestive tracts), CAPN11 (in testis), CAPN12 (in follicles), are tissue-specific and have specific functions in distinct organs. The L-subunits of similar structure (called CALPA and B) also have been found in Drosophila melanogaster. The S-subunit seems to have a chaperone-like function for proper folding of the L-subunit. The catalytic L-subunits contain a short N-terminal anchor helix, followed by a calpain cysteine protease (CysPc) domain, a C2-domain-like (C2L) domain, and a C-terminal Ca2+-binding penta-EF-hand (PEF) domain. The S-subunits only have the PEF domain following an N-terminal Gly-rich hydrophobic domain. The calpains undergo a rearrangement of the protein backbone upon Ca2+-binding.


Pssm-ID: 320057 [Multi-domain]  Cd Length: 167  Bit Score: 38.36  E-value: 3.43e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47086907 397 RQLFALFDRNHDGSIDFREYVIGLAVLCNpsnteeiIQVAFKLFDVDEDGYITEEEFSTILQAS 460
Cdd:cd16182  45 RSLIALMDTNGSGRLDLEEFKTLWSDLKK-------WQAIFKKFDTDRSGTLSSYELRKALESA 101
EF-hand_5 pfam13202
EF hand;
433-457 3.98e-03

EF hand;


Pssm-ID: 433035 [Multi-domain]  Cd Length: 25  Bit Score: 34.99  E-value: 3.98e-03
                          10        20
                  ....*....|....*....|....*
gi 47086907   433 IQVAFKLFDVDEDGYITEEEFSTIL 457
Cdd:pfam13202   1 LKDTFRQIDLNGDGKISKEELRRLL 25
EFh_MICU cd15900
EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, ...
 433-459 4.65e-03

EF-hand, calcium binding motif, found in mitochondrial calcium uptake proteins MICU1, MICU2, MICU3, and similar proteins; This family includes mitochondrial calcium uptake protein MICU1 and its two additional paralogs, MICU2 and MICU3. MICU1 localizes to the inner mitochondrial membrane (IMM). It functions as a gatekeeper of the mitochondrial calcium uniporter (MCU) and regulates MCU-mediated mitochondrial Ca2+ uptake, which is essential for maintaining mitochondrial homoeostasis. MICU1 and MICU2 are physically associated within the uniporter complex and are co-expressed across all tissues. They may play non-redundant roles in the regulation of the mitochondrial calcium uniporter. At present, the precise molecular function of MICU2 and MICU3 remain unclear. MICU2 may play possible roles in Ca2+ sensing and regulation of MCU, calcium buffering with a secondary impact on transport or assembly and stabilization of MCU. MICU3 likely has a role in mitochondrial calcium handling. All members in this family contains an N-terminal mitochondrial targeting sequence (MTS) as well as two evolutionarily conserved canonical Ca2+-binding EF-hands separated by a long stretch of residues predicted to form alpha-helices.


Pssm-ID: 320080 [Multi-domain]  Cd Length: 152  Bit Score: 37.98  E-value: 4.65e-03
                        10        20
                ....*....|....*....|....*..
gi 47086907 433 IQVAFKLFDVDEDGYITEEEFSTILQA 459
Cdd:cd15900   2 FEIAFKMFDLDGDGELDKEEFNKVQSI 28
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
433-500 5.53e-03

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 5.53e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47086907 433 IQVAFKLFDVDEDGYITEEEFSTILQAslgvpdlDVSGLFKEI-AQGD-SISYEEFKSFALK------HPEYAKIF 500
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRR-------LWATLFSEAdTDGDgRISREEFVAGMESlfeatvEPFARAAF 75
EF-hand_6 pfam13405
EF-hand domain;
396-415 7.00e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 34.46  E-value: 7.00e-03
                          10        20
                  ....*....|....*....|
gi 47086907   396 LRQLFALFDRNHDGSIDFRE 415
Cdd:pfam13405   2 LREAFKLFDKDGDGKISLEE 21
 
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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